Q07960 (RHG01_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ARHGAP1
Synonyms:	CDC42GAP, RHOGAP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	SH3-binding
Molecular function	GTPase activation
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytosol Traceable author statement. Source: Reactome intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW SH3/SH2 adaptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953	2	EBI-602762,EBI-81752
CDC42	P60953-2	2	EBI-602762,EBI-287394
RHOA	P61586	2	EBI-602762,EBI-446668

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 439

439

Rho GTPase-activating protein 1

PRO_0000056700

Regions

Domain

63 – 218

156

CRAL-TRIO

Domain

244 – 431

188

Rho-GAP

Motif

228 – 238

11

SH3-binding

Sites

Site

282

1

Involved in G-protein binding to GAPs Probable

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.12

Modified residue

51

1

Phosphoserine Ref.9 Ref.10 Ref.11

Modified residue

65

1

Phosphotyrosine By similarity

Modified residue

80

1

N6-acetyllysine Ref.13

Modified residue

212

1

N6-acetyllysine Ref.13

Natural variations

Natural variant

369

1

R → C.
Corresponds to variant rs11822837 [ dbSNP | Ensembl ].

VAR_049137

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

439

Helix Strand Turn

Details...

Helix

246 – 251

6

Helix

261 – 273

13

Turn

278 – 282

5

Helix

287 – 299

13

Helix

305 – 308

4

Helix

312 – 323

12

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Q07960 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4DD0CC4419849C35	FASTA	439	50,436
	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

References

	« Hide 'large scale' referencesShow '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: 8253717] [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: 8288572] [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. , 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: 15489334] [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: 1905930] [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: 1903516] [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: 12901880] [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: 15282546] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35 AND SFN.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Platelet.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 AND LYS-212, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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: 9009196] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
[16]	"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: 9262406] [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.

IPI

IPI00020567.

PIR

A49678.

RefSeq

NP_004299.1. NM_004308.2.

UniGene

Hs.138860.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q07960.

SMR

Q07960. Positions 236-431.

DisProt

DP00459.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6081N.

IntAct

Q07960. 6 interactions.

MINT

MINT-5006067.

STRING

Q07960.

PTM databases

PhosphoSite

Q07960.

Polymorphism databases

DMDM

3024550.

2D gel databases

OGP

Q07960.

Proteomic databases

PeptideAtlas

Q07960.

PRIDE

Q07960.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311956; ENSP00000310491; ENSG00000175220.

GeneID

392.

KEGG

hsa:392.

UCSC

uc001ndd.1. human.

Organism-specific databases

CTD

392.

GeneCards

GC11M046655.

H-InvDB

HIX0009605.

HGNC

HGNC:673. ARHGAP1.

HPA

HPA004689.
HPA008285.

MIM

602732. gene.

neXtProt

NX_Q07960.

PharmGKB

PA24956.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12643.

GeneTree

ENSGT00600000084084.

HOVERGEN

HBG054433.

InParanoid

Q07960.

PhylomeDB

Q07960.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q07960.

Bgee

Q07960.

CleanEx

HS_ARHGAP1.

Genevestigator

Q07960.

GermOnline

ENSG00000175220. Homo sapiens.

Family and domain databases

InterPro

IPR001251. CRAL-TRIO_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Gene3D

G3DSA:3.40.525.10. CRAL_bd_TRIO_C. 1 hit.
G3DSA:1.10.555.10. RhoGAP. 1 hit.

Pfam

PF00650. CRAL_TRIO. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00324. RhoGAP. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]

SUPFAM

SSF52087. CRAL_TRIO_C. 1 hit.
SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50191. CRAL_TRIO. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1635.

SOURCE

Search...

Entry information

Entry name

RHG01_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.