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UniProtKB/Swiss-Prot entry Q07960


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RHG01_HUMAN
Primary accession number Q07960
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 94)
Name and origin of the protein
Protein name Rho GTPase-activating protein 1
Synonyms Rho-type GTPase-activating protein 1
Rho-related small GTPase protein activator
GTPase-activating protein rhoOGAP
p50-RhoGAP
CDC42 GTPase-activating protein
Gene name
Name: ARHGAP1
Synonyms: CDC42GAP, RHOGAP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Platelet;
PubMed=8253717 [NCBI, ExPASy, EBI, Israel, Japan]
Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A., Ashkenazi A.;
"Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain.";
J. Biol. Chem. 268:26059-26062(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibrosarcoma;
PubMed=8288572 [NCBI, ExPASy, EBI, Israel, Japan]
Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E., Hall A.;
"Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases.";
J. Biol. Chem. 269:1137-1142(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 213-227.
TISSUE=Spleen;
PubMed=1905930 [NCBI, ExPASy, EBI, Israel, Japan]
Garrett M.D., Major G.N., Totty N., Hall A.;
"Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP.";
Biochem. J. 276:833-836(1991).
[5]
PROTEIN SEQUENCE OF 386-416.
DOI=10.1038/351400a0; PubMed=1903516 [NCBI, ExPASy, EBI, Israel, Japan]
Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C., Hall C., Lim L., Hall A.;
"Bcr encodes a GTPase-activating protein for p21rac.";
Nature 351:400-402(1991).
[6]
INTERACTION WITH BNIPL.
DOI=10.1016/S0006-291X(03)01387-1; PubMed=12901880 [NCBI, ExPASy, EBI, Israel, Japan]
Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P., Shen L., Wan D., Gu J.;
"BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis.";
Biochem. Biophys. Res. Commun. 308:379-385(2003).
[7]
IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35 AND SFN.
DOI=10.1038/sj.emboj.7600338; PubMed=15282546 [NCBI, ExPASy, EBI, Israel, Japan]
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
"Exportin 7 defines a novel general nuclear export pathway.";
EMBO J. 23:3227-3236(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
DOI=10.1038/385458a0; PubMed=9009196 [NCBI, ExPASy, EBI, Israel, Japan]
Barrett T., Xiao B., Dodson E.J., Dodson G., Ludbrook S.B., Nurmahomed K., Gamblin S.J., Musacchio A., Smerdon S.J., Eccleston J.F.;
"The structure of the GTPase-activating domain from p50rhoGAP.";
Nature 385:458-461(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH CDC42.
DOI=10.1038/41805; PubMed=9262406 [NCBI, ExPASy, EBI, Israel, Japan]
Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., Gamblin S.J., Smerdon S.J.;
"Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP.";
Nature 388:693-697(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U02570; AAA16142.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z23024; CAA80560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018118; AAH18118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A49678; A49678.
RefSeq NP_004299.1; -.
UniGene Hs.138860
3D structure databases
PDB
1AM4; X-ray; 2.70 A; A/B/C=233-431.[ExPASy / RCSB / EBI]
1GRN; X-ray; 2.10 A; B=237-439.[ExPASy / RCSB / EBI]
1OW3; X-ray; 1.80 A; A=198-439.[ExPASy / RCSB / EBI]
1RGP; X-ray; 2.00 A; A=198-439.[ExPASy / RCSB / EBI]
1TX4; X-ray; 1.65 A; A=234-431.[ExPASy / RCSB / EBI]
2NGR; X-ray; 1.90 A; B=206-439.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AM4; -.
1GRN; -.
1OW3; -.
1RGP; -.
1TX4; -.
2NGR; -.
DisProt DP00459; -.
ModBase Q07960.
Protein-protein interaction databases
DIP DIP:6081N; -.
IntAct Q07960; -.
PTM databases
PhosphoSite Q07960; -.
Enzyme and pathway databases
Reactome REACT_11044; Signaling by Rho GTPases.
2D gel databases
OGP Q07960; -.
Organism-specific databases
H-InvDB HIX0009605; -.
HGNC HGNC:673; ARHGAP1.
GenAtlas ARHGAP1.
HPA HPA004689; -.
HPA008285; -.
MIM 602732; gene. [NCBI / EBI]
PharmGKB PA24956; -.
GeneCards Q07960.
Gene expression databases
ArrayExpress Q07960; -.
CleanEx HS_ARHGAP1; -.
GermOnline ENSG00000175220; Homo sapiens.
Ontologies
GO
GO:0005100; Molecular function: Rho GTPase activator activity (inferred from direct assay from MGI).
GO:0005070; Molecular function: SH3/SH2 adaptor activity (traceable author statement from ProtInc).
GO:0007266; Biological process: Rho protein signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001251; CRAL_bd_TRIO_C.
IPR000198; RhoGAP.
Graphical view of domain structure.
Gene3D G3DSA:1.10.555.10; RhoGAP; 1.
Pfam PF00620; RhoGAP; 1.
Pfam graphical view of domain structure.
SMART SM00324; RhoGAP; 1.
SM00516; SEC14; 1.
SMART graphical view of domain structure.
PROSITE PS50191; CRAL_TRIO; 1.
PS50238; RHOGAP; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q07960.
Proteomic databases
PeptideAtlas Q07960; -.
Genome annotation databases
Ensembl ENSG00000175220; Homo sapiens. [Contig view]
GeneID 392; -.
KEGG hsa:392; -.
Phylogenomic databases
HOGENOM Q07960; -.
HOVERGEN Q07960; -.
Other
LinkHub Q07960; -.
SOURCE ARHGAP1; Homo sapiens.
ProtoNet Q07960.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; GTPase activation; Phosphoprotein; SH3-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   439  439     Rho GTPase-activating protein 1. PRO_0000056700
DOMAIN   63   218  156     CRAL-TRIO. 
DOMAIN   244   431  188     Rho-GAP. 
MOTIF   228   238  11     SH3-binding. 
SITE   282   282  1     Involved in G-protein binding to GAPs (Probable). 
MOD_RES   51    51        Phosphoserine. 
MOD_RES   65    65        Phosphotyrosine (By similarity). 
HELIX   246   251  6      
HELIX   261   273  13      
TURN   278   282  5      
HELIX   287   299  13      
HELIX   305   308  4      
HELIX   312   323  12      
STRAND   325   327  3      
HELIX   332   334  3      
HELIX   335   339  5      
HELIX   341   343  3      
TURN   346   348  3      
HELIX   349   357  9      
HELIX   362   380  19      
HELIX   382   385  4      
HELIX   389   400  12      
HELIX   406   411  6      
HELIX   413   425  13      
HELIX   427   430  4      
Sequence information
Length: 439 AA [This is the length of the unprocessed precursor] Molecular weight: 50436 Da [This is the MW of the unprocessed precursor] CRC64: 4DD0CC4419849C35 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPELVTHLKW 

        70         80         90        100        110        120 
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY 

       130        140        150        160        170        180 
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF 

       190        200        210        220        230        240 
KFGQKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ 

       250        260        270        280        290        300 
QFGVSLQHLQ EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG 

       310        320        330        340        350        360 
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV PATLQVLQTL 

       370        380        390        400        410        420 
PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT 

       430 
KFLLDHQGEL FPSPDPSGL 

Q07960 in FASTA format

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