Full text data of ARHGAP1
ARHGAP1
(CDC42GAP, RHOGAP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Rho GTPase-activating protein 1 (CDC42 GTPase-activating protein; GTPase-activating protein rhoOGAP; Rho-related small GTPase protein activator; Rho-type GTPase-activating protein 1; p50-RhoGAP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Rho GTPase-activating protein 1 (CDC42 GTPase-activating protein; GTPase-activating protein rhoOGAP; Rho-related small GTPase protein activator; Rho-type GTPase-activating protein 1; p50-RhoGAP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00020567
IPI00020567 Rho-GTPase-activating protein 1 ubiquitous, 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00020567 Rho-GTPase-activating protein 1 ubiquitous, 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 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q07960
ID RHG01_HUMAN Reviewed; 439 AA.
AC Q07960; D3DQQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Rho GTPase-activating protein 1;
DE AltName: Full=CDC42 GTPase-activating protein;
DE AltName: Full=GTPase-activating protein rhoOGAP;
DE AltName: Full=Rho-related small GTPase protein activator;
DE AltName: Full=Rho-type GTPase-activating protein 1;
DE AltName: Full=p50-RhoGAP;
GN Name=ARHGAP1; Synonyms=CDC42GAP, RHOGAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=8253717;
RA Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A.,
RA Ashkenazi A.;
RT "Cloning and expression of a human CDC42 GTPase-activating protein
RT reveals a functional SH3-binding domain.";
RL J. Biol. Chem. 268:26059-26062(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrosarcoma;
RX PubMed=8288572;
RA Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E.,
RA Hall A.;
RT "Characterization of rhoGAP. A GTPase-activating protein for rho-
RT related small GTPases.";
RL J. Biol. Chem. 269:1137-1142(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 213-227.
RC TISSUE=Spleen;
RX PubMed=1905930;
RA Garrett M.D., Major G.N., Totty N., Hall A.;
RT "Purification and N-terminal sequence of the p21rho GTPase-activating
RT protein, rho GAP.";
RL Biochem. J. 276:833-836(1991).
RN [6]
RP PROTEIN SEQUENCE OF 386-416.
RX PubMed=1903516; DOI=10.1038/351400a0;
RA Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C.,
RA Hall C., Lim L., Hall A.;
RT "Bcr encodes a GTPase-activating protein for p21rac.";
RL Nature 351:400-402(1991).
RN [7]
RP INTERACTION WITH BNIPL.
RX PubMed=12901880; DOI=10.1016/S0006-291X(03)01387-1;
RA Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H.,
RA Zhang P., Shen L., Wan D., Gu J.;
RT "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and
RT Cdc42GAP in apoptosis.";
RL Biochem. Biophys. Res. Commun. 308:379-385(2003).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
RX PubMed=9009196; DOI=10.1038/385458a0;
RA Barrett T., Xiao B., Dodson E.J., Dodson G., Ludbrook S.B.,
RA Nurmahomed K., Gamblin S.J., Musacchio A., Smerdon S.J.,
RA Eccleston J.F.;
RT "The structure of the GTPase-activating domain from p50rhoGAP.";
RL Nature 385:458-461(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH
RP CDC42.
RX PubMed=9262406; DOI=10.1038/41805;
RA Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D.,
RA Laue E., Gamblin S.J., Smerdon S.J.;
RT "Crystal structure of a small G protein in complex with the GTPase-
RT activating protein rhoGAP.";
RL Nature 388:693-697(1997).
CC -!- FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins,
CC converting them to the putatively inactive GDP-bound state. Cdc42
CC seems to be the preferred substrate.
CC -!- SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A,
CC VPS29, VPS35 and SFN. Interacts with BNIPL.
CC -!- INTERACTION:
CC P60953:CDC42; NbExp=2; IntAct=EBI-602762, EBI-81752;
CC P60953-2:CDC42; NbExp=2; IntAct=EBI-602762, EBI-287394;
CC P61586:RHOA; NbExp=2; IntAct=EBI-602762, EBI-446668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16142.1; Type=Erroneous initiation;
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DR EMBL; U02570; AAA16142.1; ALT_INIT; mRNA.
DR EMBL; Z23024; CAA80560.1; -; mRNA.
DR EMBL; CH471064; EAW67983.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW67984.1; -; Genomic_DNA.
DR EMBL; BC018118; AAH18118.1; -; mRNA.
DR PIR; A49678; A49678.
DR RefSeq; NP_004299.1; NM_004308.3.
DR UniGene; Hs.138860; -.
DR PDB; 1AM4; X-ray; 2.70 A; A/B/C=233-431.
DR PDB; 1GRN; X-ray; 2.10 A; B=237-439.
DR PDB; 1OW3; X-ray; 1.80 A; A=198-439.
DR PDB; 1RGP; X-ray; 2.00 A; A=198-439.
DR PDB; 1TX4; X-ray; 1.65 A; A=234-431.
DR PDB; 2NGR; X-ray; 1.90 A; B=206-439.
DR PDBsum; 1AM4; -.
DR PDBsum; 1GRN; -.
DR PDBsum; 1OW3; -.
DR PDBsum; 1RGP; -.
DR PDBsum; 1TX4; -.
DR PDBsum; 2NGR; -.
DR DisProt; DP00459; -.
DR ProteinModelPortal; Q07960; -.
DR SMR; Q07960; 236-431.
DR DIP; DIP-6081N; -.
DR IntAct; Q07960; 6.
DR MINT; MINT-5006067; -.
DR STRING; 9606.ENSP00000310491; -.
DR PhosphoSite; Q07960; -.
DR DMDM; 3024550; -.
DR OGP; Q07960; -.
DR PaxDb; Q07960; -.
DR PeptideAtlas; Q07960; -.
DR PRIDE; Q07960; -.
DR DNASU; 392; -.
DR Ensembl; ENST00000311956; ENSP00000310491; ENSG00000175220.
DR GeneID; 392; -.
DR KEGG; hsa:392; -.
DR UCSC; uc001ndd.4; human.
DR CTD; 392; -.
DR GeneCards; GC11M046698; -.
DR HGNC; HGNC:673; ARHGAP1.
DR HPA; HPA004689; -.
DR HPA; HPA008285; -.
DR MIM; 602732; gene.
DR neXtProt; NX_Q07960; -.
DR PharmGKB; PA24956; -.
DR eggNOG; NOG260235; -.
DR HOGENOM; HOG000231442; -.
DR HOVERGEN; HBG054433; -.
DR InParanoid; Q07960; -.
DR OMA; FYDIARH; -.
DR PhylomeDB; Q07960; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; ARHGAP1; human.
DR EvolutionaryTrace; Q07960; -.
DR GeneWiki; ARHGAP1; -.
DR GenomeRNAi; 392; -.
DR NextBio; 1635; -.
DR PRO; PR:Q07960; -.
DR ArrayExpress; Q07960; -.
DR Bgee; Q07960; -.
DR CleanEx; HS_ARHGAP1; -.
DR Genevestigator; Q07960; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0030675; F:Rac GTPase activator activity; IEA:Ensembl.
DR GO; GO:0005100; F:Rho GTPase activator activity; IDA:MGI.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Polymorphism; Reference proteome; SH3-binding.
FT CHAIN 1 439 Rho GTPase-activating protein 1.
FT /FTId=PRO_0000056700.
FT DOMAIN 63 218 CRAL-TRIO.
FT DOMAIN 244 431 Rho-GAP.
FT MOTIF 228 238 SH3-binding.
FT SITE 282 282 Involved in G-protein binding to GAPs
FT (Probable).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 65 65 Phosphotyrosine (By similarity).
FT MOD_RES 80 80 N6-acetyllysine.
FT VARIANT 369 369 R -> C (in dbSNP:rs11822837).
FT /FTId=VAR_049137.
FT STRAND 242 244
FT HELIX 246 252
FT HELIX 261 273
FT TURN 278 282
FT HELIX 287 298
FT HELIX 305 307
FT HELIX 312 324
FT STRAND 325 327
FT HELIX 332 334
FT HELIX 335 339
FT HELIX 341 343
FT HELIX 346 348
FT HELIX 349 357
FT HELIX 362 380
FT HELIX 382 385
FT HELIX 389 400
FT HELIX 406 411
FT HELIX 413 425
FT HELIX 427 430
SQ SEQUENCE 439 AA; 50436 MW; 4DD0CC4419849C35 CRC64;
MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPELVTHLKW
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF
KFGQKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ
QFGVSLQHLQ EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV PATLQVLQTL
PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT
KFLLDHQGEL FPSPDPSGL
//
ID RHG01_HUMAN Reviewed; 439 AA.
AC Q07960; D3DQQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Rho GTPase-activating protein 1;
DE AltName: Full=CDC42 GTPase-activating protein;
DE AltName: Full=GTPase-activating protein rhoOGAP;
DE AltName: Full=Rho-related small GTPase protein activator;
DE AltName: Full=Rho-type GTPase-activating protein 1;
DE AltName: Full=p50-RhoGAP;
GN Name=ARHGAP1; Synonyms=CDC42GAP, RHOGAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=8253717;
RA Barfod E.T., Zheng Y., Kuang W.-J., Hart M.J., Evans T., Cerione R.A.,
RA Ashkenazi A.;
RT "Cloning and expression of a human CDC42 GTPase-activating protein
RT reveals a functional SH3-binding domain.";
RL J. Biol. Chem. 268:26059-26062(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrosarcoma;
RX PubMed=8288572;
RA Lancaster C.A., Taylor-Harris P.M., Self A.J., Brill S., van Erp H.E.,
RA Hall A.;
RT "Characterization of rhoGAP. A GTPase-activating protein for rho-
RT related small GTPases.";
RL J. Biol. Chem. 269:1137-1142(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 213-227.
RC TISSUE=Spleen;
RX PubMed=1905930;
RA Garrett M.D., Major G.N., Totty N., Hall A.;
RT "Purification and N-terminal sequence of the p21rho GTPase-activating
RT protein, rho GAP.";
RL Biochem. J. 276:833-836(1991).
RN [6]
RP PROTEIN SEQUENCE OF 386-416.
RX PubMed=1903516; DOI=10.1038/351400a0;
RA Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C.,
RA Hall C., Lim L., Hall A.;
RT "Bcr encodes a GTPase-activating protein for p21rac.";
RL Nature 351:400-402(1991).
RN [7]
RP INTERACTION WITH BNIPL.
RX PubMed=12901880; DOI=10.1016/S0006-291X(03)01387-1;
RA Qin W., Hu J., Guo M., Xu J., Li J., Yao G., Zhou X., Jiang H.,
RA Zhang P., Shen L., Wan D., Gu J.;
RT "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and
RT Cdc42GAP in apoptosis.";
RL Biochem. Biophys. Res. Commun. 308:379-385(2003).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH XPO7; EIF4A1; VPS26A; VPS29; VPS35
RP AND SFN.
RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338;
RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.;
RT "Exportin 7 defines a novel general nuclear export pathway.";
RL EMBO J. 23:3227-3236(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 198-439.
RX PubMed=9009196; DOI=10.1038/385458a0;
RA Barrett T., Xiao B., Dodson E.J., Dodson G., Ludbrook S.B.,
RA Nurmahomed K., Gamblin S.J., Musacchio A., Smerdon S.J.,
RA Eccleston J.F.;
RT "The structure of the GTPase-activating domain from p50rhoGAP.";
RL Nature 385:458-461(1997).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 233-431 IN COMPLEX WITH
RP CDC42.
RX PubMed=9262406; DOI=10.1038/41805;
RA Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D.,
RA Laue E., Gamblin S.J., Smerdon S.J.;
RT "Crystal structure of a small G protein in complex with the GTPase-
RT activating protein rhoGAP.";
RL Nature 388:693-697(1997).
CC -!- FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins,
CC converting them to the putatively inactive GDP-bound state. Cdc42
CC seems to be the preferred substrate.
CC -!- SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A,
CC VPS29, VPS35 and SFN. Interacts with BNIPL.
CC -!- INTERACTION:
CC P60953:CDC42; NbExp=2; IntAct=EBI-602762, EBI-81752;
CC P60953-2:CDC42; NbExp=2; IntAct=EBI-602762, EBI-287394;
CC P61586:RHOA; NbExp=2; IntAct=EBI-602762, EBI-446668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16142.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; U02570; AAA16142.1; ALT_INIT; mRNA.
DR EMBL; Z23024; CAA80560.1; -; mRNA.
DR EMBL; CH471064; EAW67983.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW67984.1; -; Genomic_DNA.
DR EMBL; BC018118; AAH18118.1; -; mRNA.
DR PIR; A49678; A49678.
DR RefSeq; NP_004299.1; NM_004308.3.
DR UniGene; Hs.138860; -.
DR PDB; 1AM4; X-ray; 2.70 A; A/B/C=233-431.
DR PDB; 1GRN; X-ray; 2.10 A; B=237-439.
DR PDB; 1OW3; X-ray; 1.80 A; A=198-439.
DR PDB; 1RGP; X-ray; 2.00 A; A=198-439.
DR PDB; 1TX4; X-ray; 1.65 A; A=234-431.
DR PDB; 2NGR; X-ray; 1.90 A; B=206-439.
DR PDBsum; 1AM4; -.
DR PDBsum; 1GRN; -.
DR PDBsum; 1OW3; -.
DR PDBsum; 1RGP; -.
DR PDBsum; 1TX4; -.
DR PDBsum; 2NGR; -.
DR DisProt; DP00459; -.
DR ProteinModelPortal; Q07960; -.
DR SMR; Q07960; 236-431.
DR DIP; DIP-6081N; -.
DR IntAct; Q07960; 6.
DR MINT; MINT-5006067; -.
DR STRING; 9606.ENSP00000310491; -.
DR PhosphoSite; Q07960; -.
DR DMDM; 3024550; -.
DR OGP; Q07960; -.
DR PaxDb; Q07960; -.
DR PeptideAtlas; Q07960; -.
DR PRIDE; Q07960; -.
DR DNASU; 392; -.
DR Ensembl; ENST00000311956; ENSP00000310491; ENSG00000175220.
DR GeneID; 392; -.
DR KEGG; hsa:392; -.
DR UCSC; uc001ndd.4; human.
DR CTD; 392; -.
DR GeneCards; GC11M046698; -.
DR HGNC; HGNC:673; ARHGAP1.
DR HPA; HPA004689; -.
DR HPA; HPA008285; -.
DR MIM; 602732; gene.
DR neXtProt; NX_Q07960; -.
DR PharmGKB; PA24956; -.
DR eggNOG; NOG260235; -.
DR HOGENOM; HOG000231442; -.
DR HOVERGEN; HBG054433; -.
DR InParanoid; Q07960; -.
DR OMA; FYDIARH; -.
DR PhylomeDB; Q07960; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; ARHGAP1; human.
DR EvolutionaryTrace; Q07960; -.
DR GeneWiki; ARHGAP1; -.
DR GenomeRNAi; 392; -.
DR NextBio; 1635; -.
DR PRO; PR:Q07960; -.
DR ArrayExpress; Q07960; -.
DR Bgee; Q07960; -.
DR CleanEx; HS_ARHGAP1; -.
DR Genevestigator; Q07960; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0030675; F:Rac GTPase activator activity; IEA:Ensembl.
DR GO; GO:0005100; F:Rho GTPase activator activity; IDA:MGI.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Polymorphism; Reference proteome; SH3-binding.
FT CHAIN 1 439 Rho GTPase-activating protein 1.
FT /FTId=PRO_0000056700.
FT DOMAIN 63 218 CRAL-TRIO.
FT DOMAIN 244 431 Rho-GAP.
FT MOTIF 228 238 SH3-binding.
FT SITE 282 282 Involved in G-protein binding to GAPs
FT (Probable).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 65 65 Phosphotyrosine (By similarity).
FT MOD_RES 80 80 N6-acetyllysine.
FT VARIANT 369 369 R -> C (in dbSNP:rs11822837).
FT /FTId=VAR_049137.
FT STRAND 242 244
FT HELIX 246 252
FT HELIX 261 273
FT TURN 278 282
FT HELIX 287 298
FT HELIX 305 307
FT HELIX 312 324
FT STRAND 325 327
FT HELIX 332 334
FT HELIX 335 339
FT HELIX 341 343
FT HELIX 346 348
FT HELIX 349 357
FT HELIX 362 380
FT HELIX 382 385
FT HELIX 389 400
FT HELIX 406 411
FT HELIX 413 425
FT HELIX 427 430
SQ SEQUENCE 439 AA; 50436 MW; 4DD0CC4419849C35 CRC64;
MDPLSELQDD LTLDDTSEAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPELVTHLKW
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF
KFGQKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ
QFGVSLQHLQ EKNPEQEPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV PATLQVLQTL
PEENYQVLRF LTAFLVQISA HSDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT
KFLLDHQGEL FPSPDPSGL
//
MIM
602732
*RECORD*
*FIELD* NO
602732
*FIELD* TI
*602732 RHO GTPase-ACTIVATING PROTEIN 1; ARHGAP1
;;GTPase-ACTIVATING PROTEIN, RHO, 1;;
read moreRHOGAP1;;
RHOGAP;;
CDC42GAP
*FIELD* TX
CLONING
The Rho family of GTP-binding proteins modulates cytoskeletal changes.
Garrett et al. (1991) purified a 29-kD cytoplasmic GTPase-activating
protein (GAP), called RHOGAP by them, from human spleen extracts. RHOGAP
stimulated the GTPase activity of p21-Rho but not other small molecular
mass GTP-binding proteins. Diekmann et al. (1991) reported a partial
amino acid sequence of RHOGAP. Using PCR with primers based on the
RHOGAP protein sequence, Lancaster et al. (1994) isolated a human
fibrosarcoma cell line cDNA encoding RHOGAP. Northern blot analysis
revealed that RHOGAP is expressed as a 3.6-kb mRNA. The RHOGAP cDNA
encodes a predicted 439-amino acid protein with a calculated molecular
mass of 50 kD. Since antibodies against RHOGAP detected a 50-kD protein
on Western blots of cell extracts, Lancaster et al. (1994) suggested
that the previously observed 29-kD protein was a C-terminal proteolytic
fragment of RHOGAP that was generated during protein purification.
Barfod et al. (1993) cloned human platelet-precursor cell cDNAs encoding
CDC42GAP, a protein that inactivates CDC42 by stimulating GTP
hydrolysis. They found that CDC42GAP contains a functional SH3-binding
domain.
GENE FUNCTION
Lancaster et al. (1994) found that the Rho family members Rho, RAC, and
CDC42 (116952) were substrates for RHOGAP, with CDC42 the preferred
substrate.
Shen et al. (2008) showed that Nudel (NDEL1; 607538) colocalized with
Cdc42gap at the leading edge of migrating NIH3T3 mouse fibroblasts. This
localization of Nudel required its phosphorylation by Erk1 (MAPK3;
601795)/Erk2 (MAPK1; 176948). Shen et al. (2008) found that Nudel
competed with Cdc42 for binding Cdc42gap. Consequently, Nudel inhibited
Cdc42gap-mediated inactivation of Cdc42 in a dose-dependent manner.
Depletion of Nudel by RNA interference or overexpression of a
nonphosphorylatable Nudel mutant abolished Cdc42 activation and cell
migration. Shen et al. (2008) concluded that NUDEL facilitates cell
migration by sequestering CDC42GAP at the leading edge to stabilize
active CDC42 in response to extracellular stimuli.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RHOGAP1
gene to chromosome 11 (TMAP RH79109).
*FIELD* SA
Wildenberg et al. (2006)
*FIELD* RF
1. 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. 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 p21-rac. Nature 351: 400-402, 1991.
3. Garrett, M. D.; Major, G. N.; Totty, N.; Hall, A.: Purification
and N-terminal sequence of the p21-rho GTPase-activating protein,
rho GAP. Biochem. J. 276: 833-836, 1991.
4. 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.
5. Shen, Y.; Li, N.; Wu, S.; Zhou, Y.; Shan, Y.; Zhang, Q.; Ding,
C.; Yuan, Q.; Zhao, F.; Zeng, R.; Zhu, X.: Nudel binds Cdc42GAP to
modulate Cdc42 activity at the leading edge of migrating cells. Dev.
Cell 14: 342-353, 2008.
6. Wildenberg, G. A.; Dohn, M. R.; Carnahan, R. H.; Davis, M. A.;
Lobdell, N. A.; Settleman, J.; Reynolds, A. B.: p120-catenin and
p190RhoGAP regulate cell-cell adhesion by coordinating antagonism
between Rac and Rho. Cell 127: 1027-1039, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 4/28/2008
*FIELD* CD
Rebekah S. Rasooly: 6/18/1998
*FIELD* ED
mgross: 05/04/2009
terry: 4/30/2009
mgross: 4/28/2008
carol: 10/16/2006
wwang: 3/8/2005
terry: 3/1/2005
psherman: 6/19/1998
*RECORD*
*FIELD* NO
602732
*FIELD* TI
*602732 RHO GTPase-ACTIVATING PROTEIN 1; ARHGAP1
;;GTPase-ACTIVATING PROTEIN, RHO, 1;;
read moreRHOGAP1;;
RHOGAP;;
CDC42GAP
*FIELD* TX
CLONING
The Rho family of GTP-binding proteins modulates cytoskeletal changes.
Garrett et al. (1991) purified a 29-kD cytoplasmic GTPase-activating
protein (GAP), called RHOGAP by them, from human spleen extracts. RHOGAP
stimulated the GTPase activity of p21-Rho but not other small molecular
mass GTP-binding proteins. Diekmann et al. (1991) reported a partial
amino acid sequence of RHOGAP. Using PCR with primers based on the
RHOGAP protein sequence, Lancaster et al. (1994) isolated a human
fibrosarcoma cell line cDNA encoding RHOGAP. Northern blot analysis
revealed that RHOGAP is expressed as a 3.6-kb mRNA. The RHOGAP cDNA
encodes a predicted 439-amino acid protein with a calculated molecular
mass of 50 kD. Since antibodies against RHOGAP detected a 50-kD protein
on Western blots of cell extracts, Lancaster et al. (1994) suggested
that the previously observed 29-kD protein was a C-terminal proteolytic
fragment of RHOGAP that was generated during protein purification.
Barfod et al. (1993) cloned human platelet-precursor cell cDNAs encoding
CDC42GAP, a protein that inactivates CDC42 by stimulating GTP
hydrolysis. They found that CDC42GAP contains a functional SH3-binding
domain.
GENE FUNCTION
Lancaster et al. (1994) found that the Rho family members Rho, RAC, and
CDC42 (116952) were substrates for RHOGAP, with CDC42 the preferred
substrate.
Shen et al. (2008) showed that Nudel (NDEL1; 607538) colocalized with
Cdc42gap at the leading edge of migrating NIH3T3 mouse fibroblasts. This
localization of Nudel required its phosphorylation by Erk1 (MAPK3;
601795)/Erk2 (MAPK1; 176948). Shen et al. (2008) found that Nudel
competed with Cdc42 for binding Cdc42gap. Consequently, Nudel inhibited
Cdc42gap-mediated inactivation of Cdc42 in a dose-dependent manner.
Depletion of Nudel by RNA interference or overexpression of a
nonphosphorylatable Nudel mutant abolished Cdc42 activation and cell
migration. Shen et al. (2008) concluded that NUDEL facilitates cell
migration by sequestering CDC42GAP at the leading edge to stabilize
active CDC42 in response to extracellular stimuli.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RHOGAP1
gene to chromosome 11 (TMAP RH79109).
*FIELD* SA
Wildenberg et al. (2006)
*FIELD* RF
1. 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. 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 p21-rac. Nature 351: 400-402, 1991.
3. Garrett, M. D.; Major, G. N.; Totty, N.; Hall, A.: Purification
and N-terminal sequence of the p21-rho GTPase-activating protein,
rho GAP. Biochem. J. 276: 833-836, 1991.
4. 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.
5. Shen, Y.; Li, N.; Wu, S.; Zhou, Y.; Shan, Y.; Zhang, Q.; Ding,
C.; Yuan, Q.; Zhao, F.; Zeng, R.; Zhu, X.: Nudel binds Cdc42GAP to
modulate Cdc42 activity at the leading edge of migrating cells. Dev.
Cell 14: 342-353, 2008.
6. Wildenberg, G. A.; Dohn, M. R.; Carnahan, R. H.; Davis, M. A.;
Lobdell, N. A.; Settleman, J.; Reynolds, A. B.: p120-catenin and
p190RhoGAP regulate cell-cell adhesion by coordinating antagonism
between Rac and Rho. Cell 127: 1027-1039, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 4/28/2008
*FIELD* CD
Rebekah S. Rasooly: 6/18/1998
*FIELD* ED
mgross: 05/04/2009
terry: 4/30/2009
mgross: 4/28/2008
carol: 10/16/2006
wwang: 3/8/2005
terry: 3/1/2005
psherman: 6/19/1998