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Conserved domains on  [gi|2462553995|ref|XP_054171470|]
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rho guanine nucleotide exchange factor 15 isoform X2 [Homo sapiens]

Protein Classification

PH domain-containing RhoGEF family protein( domain architecture ID 10646143)

PH domain-containing RhoGEF (rho guanine nucleotide exchange factor) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of RhoGEFs that accelerate the intrinsic exchange activity of Rho GTPases to stimulate formation of Rho-GTP

CATH:  1.20.900.10|2.30.29.30
Gene Ontology:  GO:0005085|GO:0005515
PubMed:  11738596|23303910|22728242
SCOP:  4001108|4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 422-613 1.13e-31

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


:

Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 121.64  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  422 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISD-LCDVVHAH 499
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  500 AVGpFSVYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLqghraggpvtlp 579
Cdd:smart00325  82 EEF-FKIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLL------------ 147

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462553995  580 pcpQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:smart00325 148 ---KELLKHTPEDHEDREDLKKALKAIKELANQV 178
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 637-699 8.86e-07

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01221:

Pssm-ID: 473070  Cd Length: 131  Bit Score: 48.79  E-value: 8.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462553995 637 KVKALPLVSWSRRLEFQGELTELGCRRGGVLFASRPRFTPLCLLLFSDLLLITQPKRPSRFRI 699
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYLV 63
 
Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 422-613 1.13e-31

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 121.64  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  422 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISD-LCDVVHAH 499
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  500 AVGpFSVYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLqghraggpvtlp 579
Cdd:smart00325  82 EEF-FKIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLL------------ 147

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462553995  580 pcpQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:smart00325 148 ---KELLKHTPEDHEDREDLKKALKAIKELANQV 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 422-613 2.53e-30

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 117.79  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 422 LFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQGVSERFLatLLSRVRSSPHISDLCDVVHAHAV 501
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQRIGDIFLKFAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 502 GpFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLqghraggpvtlppc 581
Cdd:pfam00621  80 G-FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL-------------- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462553995 582 pQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:pfam00621 145 -KELLKHTPPDHPDYEDLKKALEAIKEVAKQI 175
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 418-613 2.88e-27

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 108.92  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 418 MQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDT-LTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISD-LCDV 495
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPrIGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 496 VHAHAvGPFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSlpKCERLPLPSFLLLPFQRITRLRMLLqghraggp 575
Cdd:cd00160    81 FLKLA-PFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLL-------- 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462553995 576 vtlppcpQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:cd00160   150 -------KELLKHTPDGHEDREDLKKALEAIKEVASQV 180
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 407-656 8.61e-10

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 62.60  E-value: 8.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  407 LLDTLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVlSQALRDTLTPRDH-----HTLFSNVQRVQGVSERFLATLLS 481
Cdd:COG5422    474 VWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWI-KPLEESNIIPENArrnfiKHVFANINEIYAVNSKLLKALTN 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  482 RVRSSPHISDLCDVVHAHaVGPFSVYVDYVRNQQYQEETYSRLMDTN---VRFSAELRRLQSlpkcerlplpsflllpfq 558
Cdd:COG5422    553 RQCLSPIVNGIADIFLDY-VPKFEPFIKYGASQPYAKYEFEREKSVNpnfARFDHEVERLDE------------------ 613

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  559 ritRLRMLLQGHRAGGPVTLPPCP---QNILRQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRF 635
Cdd:COG5422    614 ---SRKLELDGYLTKPTTRLARYPlllEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFHLNQQLLF 690

                          250       260
                   ....*....|....*....|..
gi 2462553995  636 HKVKA-LPLVSWSRRLEFQGEL 656
Cdd:COG5422    691 KPEYVnLGLNDEYRKIIFKGVL 712
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
 637-699 8.86e-07

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269929  Cd Length: 131  Bit Score: 48.79  E-value: 8.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462553995 637 KVKALPLVSWSRRLEFQGELTELGCRRGGVLFASRPRFTPLCLLLFSDLLLITQPKRPSRFRI 699
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYLV 63
 
Name Accession Description Interval E-value
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 422-613 1.13e-31

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 121.64  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  422 LFEVVTSEASYLRSLRLLTDTFVLS-QALRDTLTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISD-LCDVVHAH 499
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPlKKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVErIGDVFLKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  500 AVGpFSVYVDYVRNQQYQEETYSRLMDtNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLqghraggpvtlp 579
Cdd:smart00325  82 EEF-FKIYSEYCSNHPDALELLKKLKK-NPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLL------------ 147

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462553995  580 pcpQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:smart00325 148 ---KELLKHTPEDHEDREDLKKALKAIKELANQV 178
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 422-613 2.53e-30

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 117.79  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 422 LFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQGVSERFLatLLSRVRSSPHISDLCDVVHAHAV 501
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQRIGDIFLKFAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 502 GpFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLqghraggpvtlppc 581
Cdd:pfam00621  80 G-FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL-------------- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462553995 582 pQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:pfam00621 145 -KELLKHTPPDHPDYEDLKKALEAIKEVAKQI 175
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 418-613 2.88e-27

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 108.92  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 418 MQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDT-LTPRDHHTLFSNVQRVQGVSERFLATLLSRVRSSPHISD-LCDV 495
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPrIGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995 496 VHAHAvGPFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSlpKCERLPLPSFLLLPFQRITRLRMLLqghraggp 575
Cdd:cd00160    81 FLKLA-PFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLL-------- 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462553995 576 vtlppcpQNILRQTEEGSSRQENAQKALGAVSKIIERC 613
Cdd:cd00160   150 -------KELLKHTPDGHEDREDLKKALEAIKEVASQV 180
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 407-656 8.61e-10

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 62.60  E-value: 8.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  407 LLDTLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVlSQALRDTLTPRDH-----HTLFSNVQRVQGVSERFLATLLS 481
Cdd:COG5422    474 VWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWI-KPLEESNIIPENArrnfiKHVFANINEIYAVNSKLLKALTN 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  482 RVRSSPHISDLCDVVHAHaVGPFSVYVDYVRNQQYQEETYSRLMDTN---VRFSAELRRLQSlpkcerlplpsflllpfq 558
Cdd:COG5422    553 RQCLSPIVNGIADIFLDY-VPKFEPFIKYGASQPYAKYEFEREKSVNpnfARFDHEVERLDE------------------ 613

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553995  559 ritRLRMLLQGHRAGGPVTLPPCP---QNILRQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRF 635
Cdd:COG5422    614 ---SRKLELDGYLTKPTTRLARYPlllEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFHLNQQLLF 690

                          250       260
                   ....*....|....*....|..
gi 2462553995  636 HKVKA-LPLVSWSRRLEFQGEL 656
Cdd:COG5422    691 KPEYVnLGLNDEYRKIIFKGVL 712
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
 637-699 8.86e-07

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269929  Cd Length: 131  Bit Score: 48.79  E-value: 8.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462553995 637 KVKALPLVSWSRRLEFQGELTELGCRRGGVLFASRPRFTPLCLLLFSDLLLITQPKRPSRFRI 699
Cdd:cd01221     1 KIKAFPLISSSRWLVKRGELTELVEDGGSLTFRKKFSKTPVYLFLFNDLLLITKKKSEERYLV 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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