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Q07960 (RHG01_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 1
Alternative name(s):
CDC42 GTPase-activating protein
GTPase-activating protein rhoOGAP
Rho-related small GTPase protein activator
Rho-type GTPase-activating protein 1
p50-RhoGAP
Gene names
Name:ARHGAP1
Synonyms:CDC42GAP, RHOGAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate.

Subunit structure

Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with BNIPL. Ref.7 Ref.8

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Contains 1 Rho-GAP domain.

Sequence caution

The sequence AAA16142.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Rho GTPase-activating protein 1
PRO_0000056700

Regions

Domain63 – 218156CRAL-TRIO
Domain244 – 431188Rho-GAP
Motif228 – 23811SH3-binding

Sites

Site2821Involved in G-protein binding to GAPs Probable

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.16
Modified residue511Phosphoserine Ref.10 Ref.13 Ref.15
Modified residue651Phosphotyrosine By similarity
Modified residue801N6-acetyllysine Ref.12

Natural variations

Natural variant3691R → C.
Corresponds to variant rs11822837 [ dbSNP | Ensembl ].
VAR_049137

Secondary structure

.................................... 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07960 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4DD0CC4419849C35

FASTA43950,436
        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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain."
Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A., Ashkenazi A.
J. Biol. Chem. 268:26059-26062(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Platelet.
[2]"Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases."
Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E., Hall A.
J. Biol. Chem. 269:1137-1142(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibrosarcoma.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[5]"Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP."
Garrett M.D., Major G.N., Totty N., Hall A.
Biochem. J. 276:833-836(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 213-227.
Tissue: Spleen.
[6]"Bcr encodes a GTPase-activating protein for p21rac."
Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C., Hall C., Lim L., Hall A.
Nature 351:400-402(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 386-416.
[7]"BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis."
Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H., Zhang P., Shen L., Wan D., Gu J.
Biochem. Biophys. Res. Commun. 308:379-385(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BNIPL.
[8]"Exportin 7 defines a novel general nuclear export pathway."
Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35 AND SFN.
[9]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The structure of the GTPase-activating domain from p50rhoGAP."
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.
Nature 385:458-461(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
[18]"Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP."
Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., Gamblin S.J., Smerdon S.J.
Nature 388:693-697(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH CDC42.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02570 mRNA. Translation: AAA16142.1. Different initiation.
Z23024 mRNA. Translation: CAA80560.1.
CH471064 Genomic DNA. Translation: EAW67983.1.
CH471064 Genomic DNA. Translation: EAW67984.1.
BC018118 mRNA. Translation: AAH18118.1.
CCDSCCDS7922.1.
PIRA49678.
RefSeqNP_004299.1. NM_004308.3.
UniGeneHs.138860.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AM4X-ray2.70A/B/C233-431[»]
1GRNX-ray2.10B237-439[»]
1OW3X-ray1.80A198-439[»]
1RGPX-ray2.00A198-439[»]
1TX4X-ray1.65A234-431[»]
2NGRX-ray1.90B206-439[»]
DisProtDP00459.
ProteinModelPortalQ07960.
SMRQ07960. Positions 236-431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106885. 12 interactions.
DIPDIP-6081N.
IntActQ07960. 6 interactions.
MINTMINT-5006067.
STRING9606.ENSP00000310491.

PTM databases

PhosphoSiteQ07960.

Polymorphism databases

DMDM3024550.

2D gel databases

OGPQ07960.

Proteomic databases

MaxQBQ07960.
PaxDbQ07960.
PeptideAtlasQ07960.
PRIDEQ07960.

Protocols and materials databases

DNASU392.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311956; ENSP00000310491; ENSG00000175220.
GeneID392.
KEGGhsa:392.
UCSCuc001ndd.4. human.

Organism-specific databases

CTD392.
GeneCardsGC11M046698.
HGNCHGNC:673. ARHGAP1.
HPAHPA004689.
HPA008285.
MIM602732. gene.
neXtProtNX_Q07960.
PharmGKBPA24956.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260235.
HOGENOMHOG000231442.
HOVERGENHBG054433.
InParanoidQ07960.
OMAFYDIARH.
PhylomeDBQ07960.
TreeFamTF324164.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ07960.
BgeeQ07960.
CleanExHS_ARHGAP1.
GenevestigatorQ07960.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.40.525.10. 1 hit.
InterProIPR001251. CRAL-TRIO_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF13716. CRAL_TRIO_2. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP1. human.
EvolutionaryTraceQ07960.
GeneWikiARHGAP1.
GenomeRNAi392.
NextBio1635.
PROQ07960.
SOURCESearch...

Entry information

Entry nameRHG01_HUMAN
AccessionPrimary (citable) accession number: Q07960
Secondary accession number(s): D3DQQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM