RHG15_HUMAN
ID RHG15_HUMAN Reviewed; 475 AA.
AC Q53QZ3; Q53R36; Q53RD7; Q53RT6; Q53SX9; Q584N9; Q6PJE6; Q86WP1; Q8IXX1;
AC Q9NRL8; Q9NZ77; Q9NZ91;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rho GTPase-activating protein 15;
DE AltName: Full=ArhGAP15;
DE AltName: Full=Rho-type GTPase-activating protein 15;
GN Name=ARHGAP15; ORFNames=BM-024, BM-030, BM-046;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN PH, AND
RP TISSUE SPECIFICITY.
RX PubMed=12650940; DOI=10.1016/s0014-5793(03)00213-8;
RA Seoh M.L., Ng C.H., Yong J., Lim L., Leung T.;
RT "ArhGAP15, a novel human RacGAP protein with GTPase binding property.";
RL FEBS Lett. 539:131-137(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Lymph;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
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 [6]
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., Buerckstuemmer T.,
RA 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 262-473.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human Rho GTPase activating protein 15 (ARHGAP15).";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Has activity toward RAC1.
CC Overexpression results in an increase in actin stress fibers and cell
CC contraction. {ECO:0000269|PubMed:12650940}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12650940}. Membrane
CC {ECO:0000269|PubMed:12650940}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12650940}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, liver and lymphoid cells.
CC {ECO:0000269|PubMed:12650940}.
CC -!- DOMAIN: The PH domain is required for localization to the membrane.
CC {ECO:0000269|PubMed:12650940}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67618.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF67633.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF87324.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY219338; AAO34684.1; -; mRNA.
DR EMBL; AF212222; AAF87324.1; ALT_FRAME; mRNA.
DR EMBL; AF217507; AAF67618.1; ALT_FRAME; mRNA.
DR EMBL; AF217522; AAF67633.1; ALT_FRAME; mRNA.
DR EMBL; AC013437; AAX93160.1; -; Genomic_DNA.
DR EMBL; AC079584; AAX82009.1; -; Genomic_DNA.
DR EMBL; AC079793; AAY24215.1; -; Genomic_DNA.
DR EMBL; AC092652; AAY14811.1; -; Genomic_DNA.
DR EMBL; AC096558; AAX93158.1; -; Genomic_DNA.
DR EMBL; AC098857; AAX93245.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11590.1; -; Genomic_DNA.
DR EMBL; BC016701; AAH16701.1; -; mRNA.
DR EMBL; BC038976; AAH38976.2; -; mRNA.
DR CCDS; CCDS2184.1; -.
DR RefSeq; NP_060930.3; NM_018460.3.
DR RefSeq; XP_011509781.1; XM_011511479.2.
DR RefSeq; XP_016859988.1; XM_017004499.1.
DR PDB; 3BYI; X-ray; 2.25 A; A/B/C/D=262-473.
DR PDBsum; 3BYI; -.
DR AlphaFoldDB; Q53QZ3; -.
DR SMR; Q53QZ3; -.
DR BioGRID; 120945; 15.
DR IntAct; Q53QZ3; 4.
DR MINT; Q53QZ3; -.
DR STRING; 9606.ENSP00000295095; -.
DR GlyGen; Q53QZ3; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q53QZ3; -.
DR MetOSite; Q53QZ3; -.
DR PhosphoSitePlus; Q53QZ3; -.
DR BioMuta; ARHGAP15; -.
DR DMDM; 166977704; -.
DR EPD; Q53QZ3; -.
DR jPOST; Q53QZ3; -.
DR MassIVE; Q53QZ3; -.
DR MaxQB; Q53QZ3; -.
DR PaxDb; Q53QZ3; -.
DR PeptideAtlas; Q53QZ3; -.
DR PRIDE; Q53QZ3; -.
DR ProteomicsDB; 62513; -.
DR Antibodypedia; 33613; 127 antibodies from 20 providers.
DR DNASU; 55843; -.
DR Ensembl; ENST00000295095.11; ENSP00000295095.6; ENSG00000075884.14.
DR GeneID; 55843; -.
DR KEGG; hsa:55843; -.
DR MANE-Select; ENST00000295095.11; ENSP00000295095.6; NM_018460.4; NP_060930.3.
DR UCSC; uc002tvm.5; human.
DR CTD; 55843; -.
DR DisGeNET; 55843; -.
DR GeneCards; ARHGAP15; -.
DR HGNC; HGNC:21030; ARHGAP15.
DR HPA; ENSG00000075884; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 610578; gene.
DR neXtProt; NX_Q53QZ3; -.
DR OpenTargets; ENSG00000075884; -.
DR PharmGKB; PA134938065; -.
DR VEuPathDB; HostDB:ENSG00000075884; -.
DR eggNOG; KOG1449; Eukaryota.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_1_0_1; -.
DR InParanoid; Q53QZ3; -.
DR OMA; DHNQWED; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q53QZ3; -.
DR TreeFam; TF329345; -.
DR PathwayCommons; Q53QZ3; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q53QZ3; -.
DR SIGNOR; Q53QZ3; -.
DR BioGRID-ORCS; 55843; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; ARHGAP15; human.
DR EvolutionaryTrace; Q53QZ3; -.
DR GenomeRNAi; 55843; -.
DR Pharos; Q53QZ3; Tbio.
DR PRO; PR:Q53QZ3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53QZ3; protein.
DR Bgee; ENSG00000075884; Expressed in blood and 132 other tissues.
DR ExpressionAtlas; Q53QZ3; baseline and differential.
DR Genevisible; Q53QZ3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..475
FT /note="Rho GTPase-activating protein 15"
FT /id="PRO_0000317574"
FT DOMAIN 79..189
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 281..470
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811M1"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYC5"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYC5"
FT CONFLICT 260
FT /note="T -> P (in Ref. 2; AAF67618)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> P (in Ref. 2; AAF87324)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="G -> A (in Ref. 1; AAO34684)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> G (in Ref. 2; AAF67618)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> Q (in Ref. 1; AAO34684)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="L -> P (in Ref. 4; AAH16701)"
FT /evidence="ECO:0000305"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:3BYI"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:3BYI"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:3BYI"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:3BYI"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 400..418
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 427..439
FT /evidence="ECO:0007829|PDB:3BYI"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 448..464
FT /evidence="ECO:0007829|PDB:3BYI"
FT HELIX 466..470
FT /evidence="ECO:0007829|PDB:3BYI"
SQ SEQUENCE 475 AA; 54544 MW; 35C26B1960694119 CRC64;
MQKSTNSDTS VETLNSTRQG TGAVQMRIKN ANSHHDRLSQ SKSMILTDVG KVTEPISRHR
RNHSQHILKD VIPPLEQLMV EKEGYLQKAK IADGGKKLRK NWSTSWIVLS SRRIEFYKES
KQQALSNMKT GHKPESVDLC GAHIEWAKEK SSRKNVFQIT TVSGNEFLLQ SDIDFIILDW
FHAIKNAIDR LPKDSSCPSR NLELFKIQRS SSTELLSHYD SDIKEQKPEH RKSLMFRLHH
SASDTSDKNR VKSRLKKFIT RRPSLKTLQE KGLIKDQIFG SHLHKVCERE NSTVPWFVKQ
CIEAVEKRGL DVDGIYRVSG NLATIQKLRF IVNQEEKLNL DDSQWEDIHV VTGALKMFFR
ELPEPLFPYS FFEQFVEAIK KQDNNTRIEA VKSLVQKLPP PNRDTMKVLF GHLTKIVAKA
SKNLMSTQSL GIVFGPTLLR AENETGNMAI HMVYQNQIAE LMLSEYSKIF GSEED
