ankyrin repeat and SAM domain-containing protein 1A isoform X2 [Mus musculus]
Protein Classification
SAM_AIDA1AB-like_repeat1 and PTB_Anks domain-containing protein( domain architecture ID 13333957)
protein containing domains PHA02791, SAM_AIDA1AB-like_repeat1, SAM_AIDA1AB-like_repeat2, and PTB_Anks
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PTB_Anks | cd01274 | Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ... |
942-1087 | 2.03e-100 | ||||
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. : Pssm-ID: 269972 Cd Length: 146 Bit Score: 313.83 E-value: 2.03e-100
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
68-302 | 5.07e-48 | ||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.22 E-value: 5.07e-48
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| SAM_AIDA1AB-like_repeat1 | cd09499 | SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
713-779 | 3.33e-37 | ||||
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. : Pssm-ID: 188898 Cd Length: 67 Bit Score: 133.96 E-value: 3.33e-37
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| SAM_AIDA1AB-like_repeat2 | cd09500 | SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
784-848 | 1.71e-34 | ||||
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. : Pssm-ID: 188899 Cd Length: 65 Bit Score: 125.88 E-value: 1.71e-34
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| Name | Accession | Description | Interval | E-value | |||||
| PTB_Anks | cd01274 | Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ... |
942-1087 | 2.03e-100 | |||||
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269972 Cd Length: 146 Bit Score: 313.83 E-value: 2.03e-100
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
68-302 | 5.07e-48 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.22 E-value: 5.07e-48
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| SAM_AIDA1AB-like_repeat1 | cd09499 | SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
713-779 | 3.33e-37 | |||||
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. Pssm-ID: 188898 Cd Length: 67 Bit Score: 133.96 E-value: 3.33e-37
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
954-1087 | 3.98e-36 | |||||
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains. Pssm-ID: 214675 Cd Length: 134 Bit Score: 133.21 E-value: 3.98e-36
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| SAM_AIDA1AB-like_repeat2 | cd09500 | SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
784-848 | 1.71e-34 | |||||
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. Pssm-ID: 188899 Cd Length: 65 Bit Score: 125.88 E-value: 1.71e-34
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
203-294 | 3.79e-22 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 3.79e-22
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
66-301 | 1.71e-21 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 99.33 E-value: 1.71e-21
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| PID | pfam00640 | Phosphotyrosine interaction domain (PTB/PID); |
958-1077 | 1.62e-14 | |||||
Phosphotyrosine interaction domain (PTB/PID); Pssm-ID: 395515 Cd Length: 133 Bit Score: 71.63 E-value: 1.62e-14
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
716-775 | 2.19e-14 | |||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 68.86 E-value: 2.19e-14
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
715-775 | 2.08e-13 | |||||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 66.14 E-value: 2.08e-13
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
784-845 | 1.17e-12 | |||||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 63.83 E-value: 1.17e-12
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
783-845 | 4.58e-11 | |||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 59.62 E-value: 4.58e-11
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
112-301 | 1.67e-08 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 58.87 E-value: 1.67e-08
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
76-104 | 5.05e-05 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.42 E-value: 5.05e-05
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
76-241 | 1.69e-04 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 45.84 E-value: 1.69e-04
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| Name | Accession | Description | Interval | E-value | |||||
| PTB_Anks | cd01274 | Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ... |
942-1087 | 2.03e-100 | |||||
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269972 Cd Length: 146 Bit Score: 313.83 E-value: 2.03e-100
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
68-302 | 5.07e-48 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 173.22 E-value: 5.07e-48
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
66-301 | 6.28e-47 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 170.13 E-value: 6.28e-47
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
77-302 | 9.32e-46 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.67 E-value: 9.32e-46
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| SAM_AIDA1AB-like_repeat1 | cd09499 | SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
713-779 | 3.33e-37 | |||||
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. Pssm-ID: 188898 Cd Length: 67 Bit Score: 133.96 E-value: 3.33e-37
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
954-1087 | 3.98e-36 | |||||
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains. Pssm-ID: 214675 Cd Length: 134 Bit Score: 133.21 E-value: 3.98e-36
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| SAM_AIDA1AB-like_repeat2 | cd09500 | SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of ... |
784-848 | 1.71e-34 | |||||
SAM domain of AIDA1AB-like proteins, repeat 2; SAM (sterile alpha motif) domain repeat 2 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of the SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM domains of the AIDA1AB-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. Pssm-ID: 188899 Cd Length: 65 Bit Score: 125.88 E-value: 1.71e-34
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| PTB | cd00934 | Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ... |
956-1074 | 1.81e-24 | |||||
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. Pssm-ID: 269911 Cd Length: 120 Bit Score: 99.51 E-value: 1.81e-24
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
158-301 | 9.77e-24 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 9.77e-24
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
203-294 | 3.79e-22 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.72 E-value: 3.79e-22
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
66-301 | 1.71e-21 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 99.33 E-value: 1.71e-21
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
170-261 | 3.35e-21 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 89.02 E-value: 3.35e-21
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
66-260 | 1.10e-20 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 96.27 E-value: 1.10e-20
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
65-224 | 6.06e-20 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 93.96 E-value: 6.06e-20
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
80-196 | 1.62e-19 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.40 E-value: 1.62e-19
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| PTB_CED-6 | cd01273 | Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ... |
946-1083 | 7.39e-19 | |||||
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269971 Cd Length: 144 Bit Score: 84.25 E-value: 7.39e-19
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
66-303 | 2.72e-18 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 88.87 E-value: 2.72e-18
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
7-203 | 5.67e-17 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 82.69 E-value: 5.67e-17
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| SAM_Ship2 | cd09491 | SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ... |
710-769 | 1.26e-15 | |||||
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance. Pssm-ID: 188890 Cd Length: 63 Bit Score: 72.17 E-value: 1.26e-15
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
83-321 | 1.79e-15 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 80.04 E-value: 1.79e-15
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| PID | pfam00640 | Phosphotyrosine interaction domain (PTB/PID); |
958-1077 | 1.62e-14 | |||||
Phosphotyrosine interaction domain (PTB/PID); Pssm-ID: 395515 Cd Length: 133 Bit Score: 71.63 E-value: 1.62e-14
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| PTB_TK_HMTK | cd13161 | Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ... |
958-1079 | 1.96e-14 | |||||
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269983 Cd Length: 120 Bit Score: 70.74 E-value: 1.96e-14
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
716-775 | 2.19e-14 | |||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 68.86 E-value: 2.19e-14
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| PTB_LDLRAP-mammal-like | cd13159 | Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ... |
958-1075 | 1.88e-13 | |||||
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges. Pssm-ID: 269981 Cd Length: 123 Bit Score: 68.13 E-value: 1.88e-13
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
715-775 | 2.08e-13 | |||||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 66.14 E-value: 2.08e-13
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
63-139 | 2.26e-13 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 2.26e-13
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| SAM_1 | pfam00536 | SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ... |
784-845 | 1.17e-12 | |||||
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains. Pssm-ID: 425739 Cd Length: 64 Bit Score: 63.83 E-value: 1.17e-12
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
79-301 | 1.31e-12 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.45 E-value: 1.31e-12
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| SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
715-775 | 3.62e-12 | |||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 62.67 E-value: 3.62e-12
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
180-301 | 4.53e-12 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 68.06 E-value: 4.53e-12
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
158-301 | 4.76e-12 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 69.31 E-value: 4.76e-12
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
66-299 | 1.12e-11 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.94 E-value: 1.12e-11
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| SAM_superfamily | cd09487 | SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
716-773 | 1.85e-11 | |||||
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases. Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 60.33 E-value: 1.85e-11
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
180-302 | 2.57e-11 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 67.36 E-value: 2.57e-11
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| PTB_Numb | cd01268 | Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ... |
942-1059 | 3.15e-11 | |||||
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 241298 Cd Length: 135 Bit Score: 61.94 E-value: 3.15e-11
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| SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
783-845 | 4.58e-11 | |||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 59.62 E-value: 4.58e-11
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| PTB_tensin-related | cd13157 | Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal ... |
960-1078 | 9.96e-11 | |||||
Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. Pssm-ID: 269979 Cd Length: 129 Bit Score: 60.48 E-value: 9.96e-11
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
168-219 | 1.04e-10 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.05 E-value: 1.04e-10
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| SAM_SASH-like | cd09493 | SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like ... |
715-774 | 2.49e-10 | |||||
SAM (Sterile alpha motif ), SASH1-like; SAM (sterile alpha motif) domain of SASH1-like proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. Proteins of this subfamily are known to be involved in preventing DN thymocytes from premature initiation of programmed cell death and in B cells activation and differentiation. They have been found downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. Pssm-ID: 188892 Cd Length: 60 Bit Score: 57.13 E-value: 2.49e-10
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
66-219 | 3.42e-10 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 63.75 E-value: 3.42e-10
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
146-303 | 9.80e-10 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.35 E-value: 9.80e-10
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| SAM_caskin1,2_repeat2 | cd09498 | SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ... |
785-842 | 1.39e-09 | |||||
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression. Pssm-ID: 188897 Cd Length: 71 Bit Score: 55.38 E-value: 1.39e-09
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
66-241 | 1.76e-09 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 61.43 E-value: 1.76e-09
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| PTB_Shc | cd01209 | Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine ... |
996-1083 | 1.79e-09 | |||||
Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Shc-like subgroup. Pssm-ID: 269920 Cd Length: 170 Bit Score: 57.99 E-value: 1.79e-09
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| SAM_EPH-A2 | cd09543 | SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ... |
784-845 | 1.88e-09 | |||||
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design. Pssm-ID: 188942 Cd Length: 70 Bit Score: 54.84 E-value: 1.88e-09
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| SAM_EPH-R | cd09488 | SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ... |
787-845 | 2.53e-09 | |||||
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy. Pssm-ID: 188887 Cd Length: 61 Bit Score: 54.16 E-value: 2.53e-09
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
68-116 | 2.92e-09 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.89 E-value: 2.92e-09
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| SAM_Samd5 | cd09527 | SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ... |
717-775 | 3.06e-09 | |||||
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown. Pssm-ID: 188926 Cd Length: 63 Bit Score: 53.99 E-value: 3.06e-09
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| SAM_SAMSN1 | cd09561 | SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as ... |
711-775 | 1.00e-08 | |||||
SAM domain of SAMSN1 subfamily; SAM (sterile alpha motif) domain of SAMSN1 (also known as HACS1 or NASH1) proteins is a predicted protein-protein interaction domain. Members of this group are putative signaling/adaptor proteins. They appear to mediate signal transduction in lymphoid tissues. Murine HACS1 protein likely plays a role in B cell activation and differentiation. Potential binding partners of HACS1 are SLAM, DEC205 and PIR-B receptors and also some unidentified tyrosine-phosphorylated proteins. Proteins of this group were found preferentially expressed in normal hematopietic tissues and in some malignancies including lymphoma, myeloid leukemia and myeloma. Pssm-ID: 188960 Cd Length: 66 Bit Score: 52.94 E-value: 1.00e-08
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
76-129 | 1.19e-08 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 1.19e-08
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
112-301 | 1.67e-08 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 58.87 E-value: 1.67e-08
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
138-295 | 3.03e-08 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.37 E-value: 3.03e-08
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| SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
783-847 | 3.88e-08 | |||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 51.12 E-value: 3.88e-08
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
149-206 | 3.99e-08 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 3.99e-08
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
201-252 | 4.61e-08 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.61e-08
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| SAM_SASH1_repeat2 | cd09492 | SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins ... |
716-775 | 6.20e-08 | |||||
SAM domain of SASH1 proteins, repeat 2; SAM (sterile alpha motif) repeat 2 of SASH1 proteins is a protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers if compare to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis. Pssm-ID: 188891 Cd Length: 70 Bit Score: 50.59 E-value: 6.20e-08
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
234-284 | 7.90e-08 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 7.90e-08
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
65-294 | 9.39e-08 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.23 E-value: 9.39e-08
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
73-186 | 1.27e-07 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.03 E-value: 1.27e-07
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| PTB_Dab | cd01215 | Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ... |
958-1051 | 2.75e-07 | |||||
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269926 Cd Length: 147 Bit Score: 51.10 E-value: 2.75e-07
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| SAM_EPH-A5 | cd09546 | SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
790-847 | 2.86e-07 | |||||
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression. Pssm-ID: 188945 Cd Length: 66 Bit Score: 48.77 E-value: 2.86e-07
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
251-302 | 2.91e-07 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.11 E-value: 2.91e-07
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| SAM_EPH-A6 | cd09547 | SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
790-845 | 3.18e-07 | |||||
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers. Pssm-ID: 188946 Cd Length: 64 Bit Score: 48.34 E-value: 3.18e-07
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
91-294 | 3.43e-07 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 54.68 E-value: 3.43e-07
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| SAM_caskin1,2_repeat2 | cd09498 | SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ... |
716-775 | 4.70e-07 | |||||
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression. Pssm-ID: 188897 Cd Length: 71 Bit Score: 48.06 E-value: 4.70e-07
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| SAM_SASH1_repeat1 | cd09559 | SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins ... |
715-775 | 6.76e-07 | |||||
SAM domain of SASH1 proteins, repeat 1; SAM (sterile alpha motif) repeat 1 of SASH1 proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative adaptor proteins. They appear to mediate signal transduction. SASH1 can bind 14-3-3 proteins in response to IGF1/phosphatidylinositol 3-kinase signaling. SASH1 was found upregulated in different tissues including thymus, placenta, lungs and downregulated in some breast tumors, liver metastases and colon cancers, relative to corresponding normal tissues. SASH1 is a potential candidate for a tumor suppressor gene in breast cancers. At the same time, downregulation of SASH1 in colon cancer is associated with metastasis and a poor prognosis. Pssm-ID: 188958 Cd Length: 66 Bit Score: 47.71 E-value: 6.76e-07
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
114-220 | 9.40e-07 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 9.40e-07
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| SAM_SASH3 | cd09560 | SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) ... |
711-775 | 1.10e-06 | |||||
SAM domain of SASH3 subfamily; SAM (sterile alpha motif) domain of SAHS3 (also known as SLY) proteins is a predicted protein-protein interaction domain. Members of this subfamily are putative signaling/adaptor proteins. In addition to SAM, they contain SLY and SH3 domains. They appear to mediate signal transduction in lymphoid tissues. Murine SASH3 is involved in preventing DN thymocytes from premature initiation of programmed cell death and in mTOR (mammalian target of rapamycin) activation via signal integration of the Notch receptor and preTCR (T cell receptor) pathways. Pssm-ID: 188959 Cd Length: 68 Bit Score: 47.01 E-value: 1.10e-06
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| PTB_CAPON-like | cd01270 | Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) ... |
958-1088 | 1.52e-06 | |||||
Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269968 Cd Length: 179 Bit Score: 49.59 E-value: 1.52e-06
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
66-135 | 2.34e-06 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 2.34e-06
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| PTB_JIP | cd01212 | JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a ... |
982-1079 | 6.12e-06 | |||||
JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269923 Cd Length: 149 Bit Score: 47.27 E-value: 6.12e-06
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
153-299 | 6.38e-06 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 50.53 E-value: 6.38e-06
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
112-186 | 6.40e-06 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 6.40e-06
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| SAM_DGK-delta-eta | cd09507 | SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ... |
717-775 | 9.59e-06 | |||||
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization. Pssm-ID: 188906 Cd Length: 65 Bit Score: 44.33 E-value: 9.59e-06
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
66-96 | 1.02e-05 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.02e-05
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
65-219 | 1.04e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 1.04e-05
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
184-324 | 1.11e-05 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.87 E-value: 1.11e-05
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| SAM_EPH-A10 | cd09549 | SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 1.48e-05 | |||||
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers. Pssm-ID: 188948 Cd Length: 70 Bit Score: 44.08 E-value: 1.48e-05
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
67-132 | 1.73e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.45 E-value: 1.73e-05
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| SAM_EPH-R | cd09488 | SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH ... |
716-769 | 1.79e-05 | |||||
SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy. Pssm-ID: 188887 Cd Length: 61 Bit Score: 43.37 E-value: 1.79e-05
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| PTB_LOC417372 | cd13168 | uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ... |
957-1074 | 1.87e-05 | |||||
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269989 Cd Length: 125 Bit Score: 45.40 E-value: 1.87e-05
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| SAM_EPH-A1 | cd09542 | SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
785-845 | 1.90e-05 | |||||
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell. Pssm-ID: 188941 Cd Length: 63 Bit Score: 43.46 E-value: 1.90e-05
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| SAM_EPH-A4 | cd09545 | SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 1.93e-05 | |||||
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy. Pssm-ID: 188944 Cd Length: 71 Bit Score: 43.79 E-value: 1.93e-05
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| SAM_EPH-B3 | cd09553 | SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
784-847 | 2.07e-05 | |||||
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth. Pssm-ID: 188952 Cd Length: 69 Bit Score: 43.48 E-value: 2.07e-05
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
268-301 | 2.17e-05 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.95 E-value: 2.17e-05
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| SAM_EPH-A6 | cd09547 | SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 2.24e-05 | |||||
SAM domain of EPH-A6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A6 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A6 gene is preferentially expressed in the nervous system. EPH-A6 receptors are involved in primate retina vascular and axon guidance, and in neural circuits responsible for learning and memory. EphA6 gene was significantly down regulated in colorectal cancer and in malignant melanomas. It is a potential molecular marker for these cancers. Pssm-ID: 188946 Cd Length: 64 Bit Score: 43.34 E-value: 2.24e-05
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
76-252 | 2.42e-05 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 48.47 E-value: 2.42e-05
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| SAM_SARM1-like_repeat2 | cd09502 | SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like ... |
719-773 | 2.79e-05 | |||||
SAM domain of SARM1-like, repeat 2; SAM (sterile alpha motif) domain repeat 2 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver. Pssm-ID: 188901 Cd Length: 70 Bit Score: 43.05 E-value: 2.79e-05
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
76-100 | 2.86e-05 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.86 E-value: 2.86e-05
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| SAM_EPH-A8 | cd09550 | SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
787-845 | 3.43e-05 | |||||
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions. Pssm-ID: 188949 Cd Length: 65 Bit Score: 42.93 E-value: 3.43e-05
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| SAM_caskin1,2_repeat1 | cd09497 | SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ... |
719-770 | 3.77e-05 | |||||
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression. Pssm-ID: 188896 Cd Length: 66 Bit Score: 42.63 E-value: 3.77e-05
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| SAM_EPH-B4 | cd09554 | SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
790-845 | 3.83e-05 | |||||
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design. Pssm-ID: 188953 Cd Length: 67 Bit Score: 42.54 E-value: 3.83e-05
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
266-302 | 4.10e-05 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 4.10e-05
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| SAM_EPH-B1 | cd09551 | SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
789-845 | 4.86e-05 | |||||
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders. Pssm-ID: 188950 Cd Length: 68 Bit Score: 42.33 E-value: 4.86e-05
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
66-225 | 4.88e-05 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.33 E-value: 4.88e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
76-104 | 5.05e-05 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.42 E-value: 5.05e-05
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| SAM_Ste11_fungal | cd09534 | SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ... |
714-775 | 5.53e-05 | |||||
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator. Pssm-ID: 188933 Cd Length: 62 Bit Score: 42.20 E-value: 5.53e-05
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| SAM_EPH-B2 | cd09552 | SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
784-845 | 6.17e-05 | |||||
SAM domain of EPH-B2 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B2 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B2 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of this subfamily form homodimers/oligomers (in head-to-head/tail-to-tail orientation); apparently such clustering is necessary for signaling. EPH-B2 receptor is involved in regulation of synaptic function; it is needed for normal vestibular function, proper formation of anterior commissure, control of cell positioning, and ordered migration in the intestinal epithelium. EPH-B2 plays a tumor suppressor role in colorectal cancer. It was found to be downregulated in gastric cancer and thus may be a negative biomarker for it. Pssm-ID: 188951 Cd Length: 71 Bit Score: 42.30 E-value: 6.17e-05
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| SAM_liprin-beta1,2_repeat1 | cd09563 | SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
715-774 | 6.66e-05 | |||||
SAM domain of liprin-beta1,2 proteins repeat 1; SAM (sterile alpha motif) domain repeat 1 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta protein contain three copies (repeats) of SAM domain. They may form heterodimers with liprins-alpha through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta is potentially able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity. Pssm-ID: 188962 Cd Length: 64 Bit Score: 41.83 E-value: 6.66e-05
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| SAM_EPH-A5 | cd09546 | SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
715-775 | 6.68e-05 | |||||
SAM domain of EPH-A5 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A5 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A5 receptors and appears to mediate cell-cell initiated signal transduction. Eph-A5 gene is almost exclusively expressed in the nervous system. Murine EPH-A5 receptors participate in axon guidance during embryogenesis and play a role in the adult synaptic plasticity, particularly in neuron-target interactions in multiple neural circuits. Additionally EPH-A5 receptors and its ligand ephrin A5 regulate dopaminergic axon outgrowth and influence the formation of the midbrain dopaminergic pathways. EphA5 gene expression was found decreased in a few different breast cancer cell lines, thus it might be a potential molecular marker for breast cancer carcinogenesis and progression. Pssm-ID: 188945 Cd Length: 66 Bit Score: 41.84 E-value: 6.68e-05
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| SAM_EPH-B1 | cd09551 | SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 8.77e-05 | |||||
SAM domain of EPH-B1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B1 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH- B1 receptors. In human vascular endothelial cells it appears to mediate cell-cell initiated signal transduction via the binding of the adaptor protein GRB10 (growth factor) through its SH2 domain to a conserved tyrosine that is phosphorylated. EPH-B1 receptors play a role in neurogenesis, in particular in regulation of proliferation and migration of neural progenitors in the hippocampus and in corneal neovascularization; they are involved in converting the crossed retinal projection to ipsilateral retinal projection. They may be potential targets in angiogenesis-related disorders. Pssm-ID: 188950 Cd Length: 68 Bit Score: 41.56 E-value: 8.77e-05
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
165-197 | 8.77e-05 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 8.77e-05
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
166-301 | 8.86e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.52 E-value: 8.86e-05
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| PTB_X11 | cd01208 | X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is ... |
960-1084 | 9.13e-05 | |||||
X11-like Phosphotyrosine-binding (PTB) domain; The function of the neuronal protein X11 is unknown to date. X11 has a PTB domain followed by two PDZ domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269919 Cd Length: 161 Bit Score: 44.20 E-value: 9.13e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
233-260 | 1.06e-04 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.06e-04
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| SAM_EPH-B4 | cd09554 | SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 1.16e-04 | |||||
SAM domain of EPH-B4 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B4 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B4 protein kinase performs kinase-dependent and kinase-independent functions. These receptors play a role in the regular vascular system development during embryogenesis. They were found overexpressed in a variety of cancers, including carcinoma of the head and neck, ovarian cancer, bladder cancer, and downregulated in bone myeloma. Thus, EphB4 is a potential biomarker and a target for drug design. Pssm-ID: 188953 Cd Length: 67 Bit Score: 41.39 E-value: 1.16e-04
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| SAM_Samd5 | cd09527 | SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a ... |
788-841 | 1.19e-04 | |||||
SAM domain of Samd5 subfamily; SAM (sterile alpha motif) domain of Samd5 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. The exact function of proteins belonging to this subfamily is unknown. Pssm-ID: 188926 Cd Length: 63 Bit Score: 41.28 E-value: 1.19e-04
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| SAM_EPH-A2 | cd09543 | SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of ... |
715-768 | 1.34e-04 | |||||
SAM domain of EPH-A2 family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A2 subfamily of receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A2 receptors and appears to mediate cell-cell initiated signal transduction. For example, SAM domain of EPH-A2 receptors interacts with SAM domain of Ship2 proteins (SH2 containing phosphoinositide 5-phosphotase-2) forming heterodimers; such recruitment of Ship2 by EPH-A2 attenuates the positive signal for receptor endocytosis. Eph-A2 is found overexpressed in many types of human cancer, including breast, prostate, lung and colon cancer. High level of expression could induce cancer progression by a variety of mechanisms and could be used as a novel tag for cancer immunotherapy. EPH-A2 receptors are attractive targets for drag design. Pssm-ID: 188942 Cd Length: 70 Bit Score: 41.36 E-value: 1.34e-04
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| SAM_EPH-A7 | cd09548 | SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
784-845 | 1.38e-04 | |||||
SAM domain of EPH-A7 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A7 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A7 receptors and appears to mediate cell-cell initiated signal transduction. EphA7 was found expressed in human embryonic stem (ES) cells, neural tissues, kidney vasculature. EphA7 knockout mice show decrease in cortical progenitor cell death at mid-neurogenesis and significant increase in cortical size. EphA7 may be involved in the pathogenesis and development of different cancers; in particular, EphA7 was found upregulated in glioblastoma and downregulated in colorectal cancer and gastric cancer. Thus, it is a potential molecular marker and/or therapy target for these types of cancers. Pssm-ID: 188947 Cd Length: 70 Bit Score: 41.17 E-value: 1.38e-04
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
76-241 | 1.69e-04 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 45.84 E-value: 1.69e-04
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| SAM_Ste50-like_fungal | cd09533 | SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ... |
717-771 | 1.73e-04 | |||||
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity. Pssm-ID: 188932 Cd Length: 58 Bit Score: 40.38 E-value: 1.73e-04
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| SAM_KIF24-like | cd09541 | SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ... |
719-775 | 1.81e-04 | |||||
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization. Pssm-ID: 188940 Cd Length: 60 Bit Score: 40.36 E-value: 1.81e-04
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
158-297 | 1.83e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.34 E-value: 1.83e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
76-106 | 1.89e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 1.89e-04
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
191-239 | 1.94e-04 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.94e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
266-295 | 2.17e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 2.17e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
165-194 | 2.27e-04 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.49 E-value: 2.27e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
233-263 | 2.44e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 2.44e-04
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| PTB_Rab6GAP | cd01211 | GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ... |
962-1057 | 3.15e-04 | |||||
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269922 Cd Length: 129 Bit Score: 41.85 E-value: 3.15e-04
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| SAM_EPH-A1 | cd09542 | SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
715-769 | 3.58e-04 | |||||
SAM domain of EPH-A1 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A1 subfamily of the receptor tyrosine kinases is a C-terminal protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A1 receptors and appears to mediate cell-cell initiated signal transduction. Activation of these receptors leads to inhibition of cell spreading and migration in a RhoA-ROCK-dependent manner. EPH-A1 receptors are known to bind ILK (integrin-linked kinase) which is the mediator of interactions between integrin and the actin cytoskeleton. However SAM is not sufficient for this interaction; it rather plays an ancillary role. SAM domains of Eph-A1 receptors do not form homo/hetero dimers/oligomers. EphA1 gene was found expressed widely in differentiated epithelial cells. In a number of different malignant tumors EphA1 genes are downregulated. In breast carcinoma the downregulation is associated with invasive behavior of the cell. Pssm-ID: 188941 Cd Length: 63 Bit Score: 39.99 E-value: 3.58e-04
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| SAM_EPH-B3 | cd09553 | SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-775 | 4.35e-04 | |||||
SAM domain of EPH-B3 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B3 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B3 receptors and appears to mediate cell-cell initiated signal transduction. EPH-B3 receptor protein kinase performs kinase-dependent and kinase-independent functions. It is known to be involved in thymus morphogenesis, in regulation of cell adhesion and migration. Also EphB3 controls cell positioning and ordered migration in the intestinal epithelium and plays a role in the regulation of adult retinal ganglion cell axon plasticity after optic nerve injury. In some experimental models overexpression of EphB3 enhances cell/cell contacts and suppresses colon tumor growth. Pssm-ID: 188952 Cd Length: 69 Bit Score: 39.63 E-value: 4.35e-04
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
234-259 | 5.55e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 5.55e-04
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| SAM_Arap1,2,3 | cd09490 | SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ... |
716-769 | 8.14e-04 | |||||
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia. Pssm-ID: 188889 Cd Length: 63 Bit Score: 38.82 E-value: 8.14e-04
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
83-266 | 9.44e-04 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.32 E-value: 9.44e-04
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| SAM_AIDA1AB-like_repeat1 | cd09499 | SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of ... |
788-842 | 1.09e-03 | |||||
SAM domain of AIDA1AB-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of AIDA1AB-like proteins is a protein-protein interaction domain. AIDA1AB-like proteins have two tandem SAM domains. They may form an intramolecular head-to-tail homodimer. One of two basic motifs of the nuclear localization signal (NLS) is located within helix 5 of SAM2 (motif HKRK). This signal plays a role in decoupling of SAM2 from SAM1, thus facilitating translocation of this type proteins into the nucleus. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. SAM domains of the AIDA1-like subfamily can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor. Additionally AIDA1AB-like proteins may participate in the regulation of nucleoplasmic coilin protein interactions. Pssm-ID: 188898 Cd Length: 67 Bit Score: 38.43 E-value: 1.09e-03
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| SAM_EPH-A8 | cd09550 | SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
716-774 | 1.38e-03 | |||||
SAM domain of EPH-A8 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A8 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A8 receptors and appears to mediate cell-cell initiated signal transduction. EPH-A8 receptors are involved in ligand dependent (ephirin A2, A3, A5) regulation of cell adhesion and migration, and in ligand independent regulation of neurite outgrowth in neuronal cells. They perform signaling in kinase dependent and kinase independent manner. EPH-A8 receptors are known to interact with a number of different proteins including PI 3-kinase and AIDA1-like subfamily SAM repeat domain containing proteins. However other domains (not SAM) of EPH-A8 receptors are involved in these interactions. Pssm-ID: 188949 Cd Length: 65 Bit Score: 38.31 E-value: 1.38e-03
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| SAM_Arap1,2,3 | cd09490 | SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) ... |
789-845 | 1.40e-03 | |||||
SAM domain of Arap1,2,3 (angiotensin receptor-associated protein); SAM (sterile alpha motif) domain of Arap1,2,3 subfamily proteins (angiotensin receptor-associated) is a protein-protein interaction domain. Arap1,2,3 proteins are phosphatidylinositol-3,4,5-trisphosphate-dependent GTPase-activating proteins. They are involved in phosphatidylinositol-3 kinase (PI3K) signaling pathways. In addition to SAM domain, Arap1,2,3 proteins contain ArfGap, PH-like, RhoGAP and UBQ domains. SAM domain of Arap3 protein was shown to interact with SAM domain of Ship2 phosphatidylinositol-trisphosphate phosphatase proteins. Such interaction apparently plays a role in inhibition of PI3K regulated pathways since Ship2 converts PI(3,4,5)P3 into PI(3,4)P2. Proteins of this subfamily participate in regulation of signaling and trafficking associated with a number of different receptors (including EGFR, TRAIL-R1/DR4, TRAIL-R2/DR5) in normal and cancer cells; they are involved in regulation of actin cytoskeleton remodeling, cell spreading and formation of lamellipodia. Pssm-ID: 188889 Cd Length: 63 Bit Score: 38.05 E-value: 1.40e-03
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| SAM_caskin1,2_repeat1 | cd09497 | SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ... |
793-846 | 1.55e-03 | |||||
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression. Pssm-ID: 188896 Cd Length: 66 Bit Score: 38.01 E-value: 1.55e-03
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
68-285 | 1.61e-03 | |||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.76 E-value: 1.61e-03
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
239-301 | 1.70e-03 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.55 E-value: 1.70e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
108-142 | 2.53e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 2.53e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
108-134 | 2.54e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 2.54e-03
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| SAM_Ship2 | cd09491 | SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 ... |
788-847 | 2.76e-03 | |||||
SAM domain of Ship2 lipid phosphatase proteins; SAM (sterile alpha motif) domain of Ship2 subfamily is a protein-protein interaction domain. Ship2 proteins are lipid phosphatases (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2) containing an N-terminal SH2 domain, a central phosphatase domain and a C-terminal SAM domain. Ship2 is involved in a number of PI3K signaling pathways. For example, it plays a role in regulation of the actin cytoskeleton remodeling, in insulin signaling pathways, and in EphA2 receptor endocytosis. SAM domain of Ship2 can interact with SAM domain of other proteins in these pathways, thus participating in signal transduction. In particular, SAM of Ship2 is known to form heterodimers with SAM domain of Eph-A2 receptor tyrosine kinase during receptor endocytosis as well as with SAM domain of PI3K effector protein Arap3 in the actin cytoskeleton signaling network. Since Ship2 plays a role in negatively regulating insulin signaling, it has been suggested that inhibition of its expression or function may contribute in treating type 2 diabetes and obesity-induced insulin resistance. Pssm-ID: 188890 Cd Length: 63 Bit Score: 37.50 E-value: 2.76e-03
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
247-347 | 4.11e-03 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.20 E-value: 4.11e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
165-187 | 4.46e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 4.46e-03
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
215-284 | 4.54e-03 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 4.54e-03
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| SAM_Shank1,2,3 | cd09506 | SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ... |
715-775 | 5.77e-03 | |||||
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen. Pssm-ID: 188905 Cd Length: 66 Bit Score: 36.53 E-value: 5.77e-03
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| PHA02791 | PHA02791 | ankyrin-like protein; Provisional |
73-264 | 6.40e-03 | |||||
ankyrin-like protein; Provisional Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 6.40e-03
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| SAM_EPH-A10 | cd09549 | SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain ... |
790-845 | 6.86e-03 | |||||
SAM domain of EPH-A10 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-A10 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A10 receptors and appears to mediate cell-cell initiated signal transduction. It was found preferentially expressed in the testis. EphA10 may be involved in the pathogenesis and development of prostate carcinoma and lymphocytic leukemia. It is a potential molecular marker and/or therapy target for these types of cancers. Pssm-ID: 188948 Cd Length: 70 Bit Score: 36.38 E-value: 6.86e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
266-292 | 7.51e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.93 E-value: 7.51e-03
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| SAM_BICC1 | cd09520 | SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ... |
719-777 | 8.91e-03 | |||||
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates. Pssm-ID: 188919 Cd Length: 65 Bit Score: 35.73 E-value: 8.91e-03
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