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Q07960

- RHG01_HUMAN

UniProt

Q07960 - RHG01_HUMAN

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Protein
Rho GTPase-activating protein 1
Gene
ARHGAP1, CDC42GAP, RHOGAP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei282 – 2821Involved in G-protein binding to GAPs Inferred

GO - Molecular functioni

  1. Rac GTPase activator activity Source: Ensembl
  2. Rho GTPase activator activity Source: MGI
  3. SH3/SH2 adaptor activity Source: ProtInc
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. Rho protein signal transduction Source: ProtInc
  2. positive regulation of signal transduction Source: GOC
  3. regulation of small GTPase mediated signal transduction Source: Reactome
  4. small GTPase mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ARHGAP1
Synonyms:CDC42GAP, RHOGAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:673. ARHGAP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. plasma membrane Source: Ensembl
  4. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Rho GTPase-activating protein 1
PRO_0000056700Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei51 – 511Phosphoserine3 Publications
Modified residuei65 – 651Phosphotyrosine By similarity
Modified residuei80 – 801N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ07960.
PaxDbiQ07960.
PeptideAtlasiQ07960.
PRIDEiQ07960.

2D gel databases

OGPiQ07960.

PTM databases

PhosphoSiteiQ07960.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ07960.
BgeeiQ07960.
CleanExiHS_ARHGAP1.
GenevestigatoriQ07960.

Organism-specific databases

HPAiHPA004689.
HPA008285.

Interactioni

Subunit structurei

Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with BNIPL.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC42P609532EBI-602762,EBI-81752
CDC42P60953-22EBI-602762,EBI-287394
RHOAP615862EBI-602762,EBI-446668

Protein-protein interaction databases

BioGridi106885. 13 interactions.
DIPiDIP-6081N.
IntActiQ07960. 6 interactions.
MINTiMINT-5006067.
STRINGi9606.ENSP00000310491.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi242 – 2443
Helixi246 – 2527
Helixi261 – 27313
Turni278 – 2825
Helixi287 – 29812
Helixi305 – 3073
Helixi312 – 32413
Beta strandi325 – 3273
Helixi332 – 3343
Helixi335 – 3395
Helixi341 – 3433
Helixi346 – 3483
Helixi349 – 3579
Helixi362 – 38019
Helixi382 – 3854
Helixi389 – 40012
Helixi406 – 4116
Helixi413 – 42513
Helixi427 – 4304

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00459.
ProteinModelPortaliQ07960.
SMRiQ07960. Positions 236-431.

Miscellaneous databases

EvolutionaryTraceiQ07960.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 218156CRAL-TRIO
Add
BLAST
Domaini244 – 431188Rho-GAP
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi228 – 23811SH3-binding
Add
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.
Contains 1 Rho-GAP domain.

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiNOG260235.
HOGENOMiHOG000231442.
HOVERGENiHBG054433.
InParanoidiQ07960.
OMAiFYDIARH.
PhylomeDBiQ07960.
TreeFamiTF324164.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.40.525.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07960-1 [UniParc]FASTAAdd to Basket

« Hide

MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS    50
SPELVTHLKW DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD 100
HSKLLGYLKH TLDQYVESDY TLLYLHHGLT SDNKPSLSWL RDAYREFDRK 150
YKKNIKALYI VHPTMFIKTL LILFKPLISF KFGQKIFYVN YLSELSEHVK 200
LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ QFGVSLQHLQ 250
EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG 300
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV 350
PATLQVLQTL PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL 400
LWAKDAAITL KAINPINTFT KFLLDHQGEL FPSPDPSGL 439
Length:439
Mass (Da):50,436
Last modified:November 1, 1996 - v1
Checksum:i4DD0CC4419849C35
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti369 – 3691R → C.
Corresponds to variant rs11822837 [ dbSNP | Ensembl ].
VAR_049137

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7922.1.
PIRiA49678.
RefSeqiNP_004299.1. NM_004308.3.
UniGeneiHs.138860.

Genome annotation databases

EnsembliENST00000311956; ENSP00000310491; ENSG00000175220.
GeneIDi392.
KEGGihsa:392.
UCSCiuc001ndd.4. human.

Polymorphism databases

DMDMi3024550.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS7922.1.
PIRi A49678.
RefSeqi NP_004299.1. NM_004308.3.
UniGenei Hs.138860.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AM4 X-ray 2.70 A/B/C 233-431 [» ]
1GRN X-ray 2.10 B 237-439 [» ]
1OW3 X-ray 1.80 A 198-439 [» ]
1RGP X-ray 2.00 A 198-439 [» ]
1TX4 X-ray 1.65 A 234-431 [» ]
2NGR X-ray 1.90 B 206-439 [» ]
DisProti DP00459.
ProteinModelPortali Q07960.
SMRi Q07960. Positions 236-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106885. 13 interactions.
DIPi DIP-6081N.
IntActi Q07960. 6 interactions.
MINTi MINT-5006067.
STRINGi 9606.ENSP00000310491.

PTM databases

PhosphoSitei Q07960.

Polymorphism databases

DMDMi 3024550.

2D gel databases

OGPi Q07960.

Proteomic databases

MaxQBi Q07960.
PaxDbi Q07960.
PeptideAtlasi Q07960.
PRIDEi Q07960.

Protocols and materials databases

DNASUi 392.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311956 ; ENSP00000310491 ; ENSG00000175220 .
GeneIDi 392.
KEGGi hsa:392.
UCSCi uc001ndd.4. human.

Organism-specific databases

CTDi 392.
GeneCardsi GC11M046698.
HGNCi HGNC:673. ARHGAP1.
HPAi HPA004689.
HPA008285.
MIMi 602732. gene.
neXtProti NX_Q07960.
PharmGKBi PA24956.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG260235.
HOGENOMi HOG000231442.
HOVERGENi HBG054433.
InParanoidi Q07960.
OMAi FYDIARH.
PhylomeDBi Q07960.
TreeFami TF324164.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSi ARHGAP1. human.
EvolutionaryTracei Q07960.
GeneWikii ARHGAP1.
GenomeRNAii 392.
NextBioi 1635.
PROi Q07960.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q07960.
Bgeei Q07960.
CleanExi HS_ARHGAP1.
Genevestigatori Q07960.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.40.525.10. 1 hit.
InterProi IPR001251. CRAL-TRIO_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view ]
Pfami PF13716. CRAL_TRIO_2. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view ]
SMARTi SM00324. RhoGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEi PS50191. CRAL_TRIO. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. 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. 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. 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.

Entry informationi

Entry nameiRHG01_HUMAN
AccessioniPrimary (citable) accession number: Q07960
Secondary accession number(s): D3DQQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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