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Database: UniProt
Entry: A0A0A0MSK6_HUMAN
LinkDB: A0A0A0MSK6_HUMAN
Original site: A0A0A0MSK6_HUMAN 
ID   A0A0A0MSK6_HUMAN        Unreviewed;      1498 AA.
AC   A0A0A0MSK6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   31-JUL-2019, entry version 47.
DE   SubName: Full=Rho GTPase-activating protein 5 {ECO:0000313|Ensembl:ENSP00000393307};
GN   Name=ARHGAP5 {ECO:0000313|Ensembl:ENSP00000393307};
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 {ECO:0000313|Ensembl:ENSP00000393307, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000393307, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [2] {ECO:0000213|PubMed:16777052}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA   Zhan X., Desiderio D.M.;
RT   "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT   nitrotyrosine affinity column and tandem mass spectrometry.";
RL   Anal. Biochem. 354:279-289(2006).
RN   [3] {ECO:0000213|PubMed:18691976}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [4] {ECO:0000213|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [5] {ECO:0000213|PubMed:19413330}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [6] {ECO:0000213|PubMed:19690332}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [7] {ECO:0000213|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8] {ECO:0000213|PubMed:21269460}
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   Burckstummer 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   [9] {ECO:0000213|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [10] {ECO:0000213|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12] {ECO:0000313|Ensembl:ENSP00000393307}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2014) to UniProtKB.
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DR   EMBL; AL161665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   jPOST; A0A0A0MSK6; -.
DR   PeptideAtlas; A0A0A0MSK6; -.
DR   Ensembl; ENST00000432921; ENSP00000393307; ENSG00000100852.
DR   UCSC; uc059apr.1; human.
DR   HGNC; HGNC:675; ARHGAP5.
DR   OpenTargets; ENSG00000100852; -.
DR   eggNOG; KOG4271; Eukaryota.
DR   eggNOG; ENOG410XR4E; LUCA.
DR   GeneTree; ENSGT00940000154553; -.
DR   ChiTaRS; ARHGAP5; human.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000100852; Expressed in 229 organ(s), highest expression level in corpus callosum.
DR   ExpressionAtlas; A0A0A0MSK6; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.10.440; -; 3.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039007; pG1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR032835; RhoGAP-FF1.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR039006; RhoGAP_pG2.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF16512; RhoGAP-FF1; 1.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81698; SSF81698; 1.
DR   PROSITE; PS51676; FF; 4.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Proteomics identification {ECO:0000213|EPD:A0A0A0MSK6,
KW   ECO:0000213|MaxQB:A0A0A0MSK6, ECO:0000213|PeptideAtlas:A0A0A0MSK6,
KW   ECO:0000213|ProteomicsDB:A0A0A0MSK6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN      267    325       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      366    420       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      427    481       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      482    548       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      590    763       PG1 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51852}.
FT   DOMAIN      779    944       PG2 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51853}.
FT   DOMAIN     1259   1445       Rho-GAP. {ECO:0000259|PROSITE:PS50238}.
FT   REGION      975   1004       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1022   1050       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1069   1089       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1189   1251       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      309    329       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1024   1038       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1498 AA;  171685 MW;  4E28BB21B125E9E1 CRC64;
     MMAKNKEPRP PSYTISIVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI
     DFGGRVVNND HFLYWGDIIQ NSEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA
     ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV
     NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT
     ALVQMLDKTR SKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
     PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIN TLPRAFNTLL PNLEEIEHLN
     WSEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH
     LISEKRRVEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAYKYITEAD SKEVYGRHQR
     EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES
     LLLKHIGFVY HPTKETCLSG QNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI
     LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYFLSQLWT AAFKPHGCFC
     VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL ANQRDSISKN LPILRHQGQQ
     LANKLQCPFV DVPAGTYPRK FNETQIKQAL RGVLESVKHN LDVVSPIPAN KDLSEADLRI
     VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI
     GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
     MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ
     SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP
     IHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA
     HPEDMDPSDN YAEPIDTIFK QKGYSDEIYV VPDDSQNRIK IRNSFVNNTQ GDEENGFSDR
     PQKVMGNGGL QNTNINLKPC LVKPSHTIEE HIQMPVMMRL SPLLKQRKGR HRGSEEDPLL
     SPVETWKGGI DNPAITSDQE LDDKKMKKKT HKVKEDKKKK TKNFNPPTRR NWESNYFGMP
     LQDLVTAEKP IPLFVEKCVE FIEDTGLCTE GLYRVSGNKT DQDNIQKQFD QDHNINLVSM
     EVTVNAVAGA LKAFFADLPD PLIPYSLHPE LLEAAKIPDK TERLHALKEI VKKFHPVNYD
     VFRYVITHLN RVSQQHKINL MTADNLSICF WPTLMRPDLK IEFLSTTKIH QSVVETFIQQ
     CQFFFYNGEI VETTNIVAPP PPSNPGQLVE PMVPLQLPPP LQPQLIQPQL QTDPLGII
//
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