kinase suppressor of Ras 2 isoform X5 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
C1 super family | cl00040 | protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
408-464 | 1.65e-31 | ||
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme. The actual alignment was detected with superfamily member cd20873: Pssm-ID: 412127 Cd Length: 57 Bit Score: 116.33 E-value: 1.65e-31
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SAM_KSR1_N | pfam20406 | Kinase suppressor RAS 1 N-terminal helical hairpin; |
24-77 | 2.08e-25 | ||
Kinase suppressor RAS 1 N-terminal helical hairpin; : Pssm-ID: 466555 Cd Length: 54 Bit Score: 99.09 E-value: 2.08e-25
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SAM_KSR1 super family | cl16297 | SAM like domain present in kinase suppressor RAS 1; |
85-152 | 3.87e-16 | ||
SAM like domain present in kinase suppressor RAS 1; The actual alignment was detected with superfamily member pfam13543: Pssm-ID: 463916 Cd Length: 70 Bit Score: 73.17 E-value: 3.87e-16
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Name | Accession | Description | Interval | E-value | ||
C1_KSR2 | cd20873 | protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ... |
408-464 | 1.65e-31 | ||
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410423 Cd Length: 57 Bit Score: 116.33 E-value: 1.65e-31
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SAM_KSR1_N | pfam20406 | Kinase suppressor RAS 1 N-terminal helical hairpin; |
24-77 | 2.08e-25 | ||
Kinase suppressor RAS 1 N-terminal helical hairpin; Pssm-ID: 466555 Cd Length: 54 Bit Score: 99.09 E-value: 2.08e-25
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SAM_KSR1 | pfam13543 | SAM like domain present in kinase suppressor RAS 1; |
85-152 | 3.87e-16 | ||
SAM like domain present in kinase suppressor RAS 1; Pssm-ID: 463916 Cd Length: 70 Bit Score: 73.17 E-value: 3.87e-16
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C1 | smart00109 | Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
413-455 | 4.15e-05 | ||
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains. Pssm-ID: 197519 Cd Length: 50 Bit Score: 41.30 E-value: 4.15e-05
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C1_1 | pfam00130 | Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
413-456 | 4.91e-05 | ||
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain. Pssm-ID: 395079 Cd Length: 53 Bit Score: 41.27 E-value: 4.91e-05
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Name | Accession | Description | Interval | E-value | ||
C1_KSR2 | cd20873 | protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and ... |
408-464 | 1.65e-31 | ||
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 2 (KSR2) and similar proteins; KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410423 Cd Length: 57 Bit Score: 116.33 E-value: 1.65e-31
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SAM_KSR1_N | pfam20406 | Kinase suppressor RAS 1 N-terminal helical hairpin; |
24-77 | 2.08e-25 | ||
Kinase suppressor RAS 1 N-terminal helical hairpin; Pssm-ID: 466555 Cd Length: 54 Bit Score: 99.09 E-value: 2.08e-25
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C1_KSR1 | cd20872 | protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and ... |
411-456 | 4.61e-21 | ||
protein kinase C conserved region 1 (C1 domain) found in kinase suppressor of Ras 1 (KSR1) and similar proteins; KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410422 Cd Length: 47 Bit Score: 86.64 E-value: 4.61e-21
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C1_KSR | cd20812 | protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
411-455 | 2.68e-20 | ||
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410362 Cd Length: 48 Bit Score: 84.30 E-value: 2.68e-20
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SAM_KSR1 | pfam13543 | SAM like domain present in kinase suppressor RAS 1; |
85-152 | 3.87e-16 | ||
SAM like domain present in kinase suppressor RAS 1; Pssm-ID: 463916 Cd Length: 70 Bit Score: 73.17 E-value: 3.87e-16
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C1_MgcRacGAP | cd20821 | protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ... |
411-456 | 2.42e-09 | ||
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410371 Cd Length: 55 Bit Score: 53.56 E-value: 2.42e-09
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C1 | cd00029 | protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
413-456 | 1.17e-06 | ||
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme. Pssm-ID: 410341 Cd Length: 50 Bit Score: 45.59 E-value: 1.17e-06
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C1_nPKC_theta-like_rpt2 | cd20837 | second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
413-454 | 2.97e-05 | ||
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410387 Cd Length: 50 Bit Score: 41.65 E-value: 2.97e-05
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C1 | smart00109 | Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
413-455 | 4.15e-05 | ||
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains. Pssm-ID: 197519 Cd Length: 50 Bit Score: 41.30 E-value: 4.15e-05
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C1_1 | pfam00130 | Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
413-456 | 4.91e-05 | ||
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain. Pssm-ID: 395079 Cd Length: 53 Bit Score: 41.27 E-value: 4.91e-05
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C1_Raf | cd20811 | protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ... |
411-455 | 9.53e-05 | ||
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410361 Cd Length: 49 Bit Score: 40.36 E-value: 9.53e-05
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C1_Stac | cd20817 | protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ... |
425-456 | 2.24e-04 | ||
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410367 Cd Length: 51 Bit Score: 39.23 E-value: 2.24e-04
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CRIK | cd20814 | protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ... |
409-454 | 2.24e-04 | ||
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410364 Cd Length: 56 Bit Score: 39.54 E-value: 2.24e-04
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C1_Myosin-IX | cd20818 | protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ... |
413-456 | 6.01e-04 | ||
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410368 Cd Length: 56 Bit Score: 38.05 E-value: 6.01e-04
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C1_cPKC_nPKC_rpt2 | cd20793 | second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ... |
413-456 | 7.81e-04 | ||
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410343 Cd Length: 50 Bit Score: 37.64 E-value: 7.81e-04
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C1_MRCK | cd20809 | protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ... |
413-455 | 2.05e-03 | ||
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410359 Cd Length: 53 Bit Score: 36.48 E-value: 2.05e-03
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C1_ScPKC1-like_rpt1 | cd20822 | first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
413-449 | 2.48e-03 | ||
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410372 Cd Length: 52 Bit Score: 36.50 E-value: 2.48e-03
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C1_PDZD8 | cd20825 | protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ... |
412-451 | 2.82e-03 | ||
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410375 Cd Length: 55 Bit Score: 36.10 E-value: 2.82e-03
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C1_RASSF5 | cd20886 | protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ... |
413-449 | 3.09e-03 | ||
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410436 Cd Length: 50 Bit Score: 35.82 E-value: 3.09e-03
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C1_CeDKF1-like_rpt1 | cd20797 | first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ... |
410-454 | 3.57e-03 | ||
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410347 Cd Length: 56 Bit Score: 35.91 E-value: 3.57e-03
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C1_nPKC_epsilon-like_rpt2 | cd20838 | second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
411-455 | 8.06e-03 | ||
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410388 Cd Length: 55 Bit Score: 34.94 E-value: 8.06e-03
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C1_Munc13-1 | cd20858 | protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ... |
408-449 | 9.23e-03 | ||
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410408 Cd Length: 60 Bit Score: 35.06 E-value: 9.23e-03
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C1_VAV | cd20810 | protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ... |
424-457 | 9.76e-03 | ||
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410360 Cd Length: 52 Bit Score: 34.54 E-value: 9.76e-03
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Blast search parameters | ||||
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