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Protein Page:
ARHGAP5 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ARHGAP5 a GTPase activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of p120GAP. Negatively regulates RHO GTPases, a family which may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Note: This description may include information from UniProtKB.
Protein type: GAPs, Rac/Rho; Motility/polarity/chemotaxis; GAPs
Cellular Component: membrane; cytoplasm; cytosol
Molecular Function: GTPase activity; protein binding; GTP binding; Rho GTPase activator activity; SH2 domain binding
Biological Process: regulation of small GTPase mediated signal transduction; mammary gland development; GTP catabolic process; small GTPase mediated signal transduction; positive regulation of mesenchymal cell proliferation; cell adhesion; regulation of cell size; Rho protein signal transduction; positive regulation of Rho GTPase activity; positive regulation of cell migration
Reference #:  Q13017 (UniProtKB)
Alt. Names/Synonyms: ARHGAP5; GFI2; growth factor independent 2; p100 RasGAP-associated p105 protein; p105 RhoGAP; p190-B; p190BRhoGAP; RHG05; Rho GTPase activating protein 5; Rho GTPase-activating protein 5; Rho-type GTPase-activating protein 5; RHOGAP5
Gene Symbols: ARHGAP5
Molecular weight: 172,460 Da
Basal Isoelectric point: 6.18  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ARHGAP5

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  RCSB PDB  |  Phospho3D  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cell differentiation, altered: Y306‑p
cell growth, altered: Y1109‑p
cell motility, altered: Y1109‑p
activity, induced: Y1109‑p
intracellular localization: Y306‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T199-p KPVIIAAtKCDECVD
0 1 K278 TATDKFEKLVQTVRD
0 1 T289 TVRDYHATWKTVSNK
1 0 Y306-p NHPDYEEyINLEGTR
0 1 K333 LKQEHIRKRREEYIN
0 3 S590-p RLRLYHDsTNIDKVN
0 1 Y630-p YALDGKIyELDLRPV
0 5 S765-p KHNLDVVsPIPANKD
0 1 Y836-p IQITILSyHSSIGVR
0 1 S951-p MIENSYLsDNTREST
0 1 T954 NSYLsDNTRESTHQS
0 3 S968-p SEDVFLPsPRDCFPY
0 1 S981 PYNNYPDSDDDTEAP
0 1 T985 YPDSDDDTEAPPPYS
0 12 Y1019-p LDLEGNEyPIHSTPN
0 1 K1060 KLDPNLLKTIEAGIG
1 110 Y1091-p DMDPSDNyAEPIDTI
0 1 K1100 EPIDTIFKQKGySDE
0 1 K1102 IDTIFKQKGySDEIy
0 5 Y1104-p TIFKQKGySDEIyVV
2 175 Y1109-p KGySDEIyVVPDDsQ
0 2 S1115-p IyVVPDDsQNRIKIR
0 22 S1124-p NRIKIRNsFVNNtQG
0 5 T1129-p RNsFVNNtQGDEENG
0 1 S1138-p GDEENGFsDRTSKSH
0 2 T1171-p AKSYYRRtHsDAsDD
0 21 S1173-p SYYRRtHsDAsDDEA
0 23 S1176-p RRtHsDAsDDEAFTT
0 17 S1195-p RKGRHRGsEEDPLLs
0 18 S1202-p sEEDPLLsPVEtWKG
0 1 T1206-p PLLsPVEtWKGGIDN
0 1 K1208 LsPVEtWKGGIDNPA
0 22 S1218-p IDNPAITsDQELDDK
0 1 Y1259 RRNWESNYFGMPLQD
  mouse

► Hide Isoforms
 
T199 KPVIIAATKCDECVD
K278-u TATDKFEkLVQTVRD
T289-p TVRDYHAtWKTVSNK
Y306 NHPDYEEYINLEGTR
K333-u LKQEHIRkRREEYIS
S590 RVRLYHDSTNIDKVN
Y630 YALDGKIYELDLRPV
S765-p KHNLDVVsPVPINKD
Y836 IQITILSYHSSIGVR
S951 MIENSYLSDNtREST
T954-p NSYLSDNtRESTHQS
S968-p SEDVFLPsPRDCFPY
S981-p PYNNYPDsDDDtEAP
T985-p YPDsDDDtEAPPPYS
Y1019 LDLEGNEYPVHSTPN
K1060-u KLDPNLLkTIEAGIG
Y1091 DMDSSDNYVEPLDTI
K1100-u EPLDTIFkQkGYSDE
K1102-u LDTIFkQkGYSDEIy
Y1104 TIFkQkGYSDEIyVV
Y1109-p kGYSDEIyVVPDDSQ
S1115 IyVVPDDSQNRIIKI
S1125 RIIKIRNSFVNNTQG
T1130 RNSFVNNTQGDEENG
S1139 GDEENGFSDPQKVME
- gap
- gap
- gap
S1194-p RKGRHRGsEEDPLLs
S1201-p sEEDPLLsPVETWkG
T1205 PLLsPVETWkGGIDN
K1207-u LsPVETWkGGIDNPA
S1217-p IDNPAITsDQEVDDK
Y1258-p RRNWESNyFGMPLQD
  ARHGAP5 iso3  
T199 KPVIIAATKCDECVD
K278 TATDKFEKLVQTVRD
T289 TVRDYHATWKTVSNK
Y306 NHPDYEEYINLEGTR
K333 LKQEHIRKRREEYIS
S590 RVRLYHDSTNIDKVN
Y630 YALDGKIYELDLRPV
S765 KHNLDVVSPVPINKD
Y836 IQITILSYHSSIGVR
S951 MIENSYLSDNTREST
T954 NSYLSDNTRESTHQS
S968 SEDVFLPSPRDCFPY
S981 PYNNYPDSDDDTEAP
T985 YPDSDDDTEAPPPYS
Y1019 LDLEGNEYPVHSTPN
K1060 KLDPNLLKTIEAGIG
Y1091 DMDSSDNYVEPLDTI
K1100 EPLDTIFKQKGYSDE
K1102 LDTIFKQKGYSDEIY
Y1104 TIFKQKGYSDEIYVV
Y1109 KGYSDEIYVVPDDSQ
S1115 IYVVPDDSQNRIIKI
S1125 RIIKIRNSFVNNTQG
T1130 RNSFVNNTQGDEENG
S1139 GDEENGFSDRTSKGH
T1172 AKSYYRRTHsDAsDD
S1174-p SYYRRTHsDAsDDEA
S1177-p RRTHsDAsDDEAFTT
S1196 RKGRHRGSEEDPLLS
S1203 SEEDPLLSPVETWKG
T1207 PLLSPVETWKGGIDN
K1209 LSPVETWKGGIDNPA
S1219 IDNPAITSDQEVDDK
Y1260 RRNWESNYFGMPLQD
  rat

 
T198 KPVIIAATKCDECVD
K277 TATDKFEKLVQTVRD
T288 TVRDYHATWKTVSNK
Y305 NHPDYEEYINLEGTR
K332 LKQEHIRKRREEYIS
S589 RSRLYHDSTNIDKVN
Y629 YALDGKIYELDLRPV
S764 KHNLDVVSPVPINKD
Y835 IQITILSYHSSIGVR
S950 MIENSYLSDNTREST
T953 NSYLSDNTRESTHQS
S967 SEDVFLPSPRDCFPY
S980 PYNNYPDSDDDTEAP
T984 YPDSDDDTEAPPPYS
Y1018 LDLEGNEYPVHSTPN
K1059 KLDPNLLKTIEAGIG
Y1090 DMDSSDNYAEPLDTI
K1099 EPLDTIFKQKGYPDE
K1101 LDTIFKQKGYPDEIy
Y1103 TIFKQKGYPDEIyVV
Y1108-p KGYPDEIyVVPDDSQ
S1114 IyVVPDDSQNRIIKI
S1124 RIIKIRNSFVNNTQG
T1129 RNSFVNNTQGDEENG
S1138 GDEENGFSDRTSKGH
T1171 AKSYYRRTHSDAsDD
S1173 SYYRRTHSDAsDDEA
S1176-p RRTHSDAsDDEAFPT
S1195 RKGRHRGSEEDPLLS
S1202 SEEDPLLSPVETWKG
T1206 PLLSPVETWKGGIDN
K1208 LSPVETWKGGIDNPA
S1218 IDNPAITSDQEVDDK
- gap
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