ID   GMIP_HUMAN              Reviewed;         970 AA.
AC   Q9P107; A0AVN9; B7ZLZ0;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   10-FEB-2021, entry version 153.
DE   RecName: Full=GEM-interacting protein;
DE            Short=GMIP;
GN   Name=GMIP;
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] (ISOFORM 1), FUNCTION, AND INTERACTION WITH GEM.
RC   TISSUE=Leukemia;
RX   PubMed=12093360; DOI=10.1042/bj20020829;
RA   Aresta S., de Tand-Heim M.-F., Beranger F., de Gunzburg J.;
RT   "A novel Rho GTPase-activating-protein interacts with Gem, a member of the
RT   Ras superfamily of GTPases.";
RL   Biochem. J. 367:57-65(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-243, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8]
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., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP   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   [11]
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   [12]
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., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-234; SER-437;
RP   SER-441; THR-660; SER-885; SER-907; SER-914; SER-919 AND SER-923, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP   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   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 80-357.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the N-terminal domain of the GEM interacting
RT   protein.";
RL   Submitted (MAR-2011) to the PDB data bank.
CC   -!- FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of
CC       RhoA. {ECO:0000269|PubMed:12093360}.
CC   -!- SUBUNIT: Interacts with GEM through its N-terminal.
CC       {ECO:0000269|PubMed:12093360}.
CC   -!- INTERACTION:
CC       Q9P107; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-11603420, EBI-2825900;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9P107-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P107-2; Sequence=VSP_056142;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF132541; AAF61330.1; -; mRNA.
DR   EMBL; AC011458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471106; EAW84839.1; -; Genomic_DNA.
DR   EMBL; BC126436; AAI26437.1; -; mRNA.
DR   EMBL; BC144142; AAI44143.1; -; mRNA.
DR   CCDS; CCDS12408.1; -. [Q9P107-1]
DR   CCDS; CCDS74318.1; -. [Q9P107-2]
DR   PIR; D59435; D59435.
DR   RefSeq; NP_001275927.1; NM_001288998.1.
DR   RefSeq; NP_001275928.1; NM_001288999.1. [Q9P107-2]
DR   RefSeq; NP_057657.2; NM_016573.3. [Q9P107-1]
DR   PDB; 3QWE; X-ray; 2.40 A; A=80-357.
DR   PDBsum; 3QWE; -.
DR   SMR; Q9P107; -.
DR   BioGRID; 119442; 8.
DR   IntAct; Q9P107; 9.
DR   STRING; 9606.ENSP00000203556; -.
DR   iPTMnet; Q9P107; -.
DR   PhosphoSitePlus; Q9P107; -.
DR   BioMuta; GMIP; -.
DR   DMDM; 212286192; -.
DR   EPD; Q9P107; -.
DR   jPOST; Q9P107; -.
DR   MassIVE; Q9P107; -.
DR   MaxQB; Q9P107; -.
DR   PaxDb; Q9P107; -.
DR   PeptideAtlas; Q9P107; -.
DR   PRIDE; Q9P107; -.
DR   ProteomicsDB; 83629; -. [Q9P107-1]
DR   Antibodypedia; 61622; 73 antibodies.
DR   Ensembl; ENST00000203556; ENSP00000203556; ENSG00000089639. [Q9P107-1]
DR   Ensembl; ENST00000587238; ENSP00000467054; ENSG00000089639. [Q9P107-2]
DR   GeneID; 51291; -.
DR   KEGG; hsa:51291; -.
DR   UCSC; uc002nnd.5; human. [Q9P107-1]
DR   CTD; 51291; -.
DR   DisGeNET; 51291; -.
DR   GeneCards; GMIP; -.
DR   HGNC; HGNC:24852; GMIP.
DR   HPA; ENSG00000089639; Tissue enhanced (blood, bone marrow, lymphoid tissue).
DR   MIM; 609694; gene.
DR   neXtProt; NX_Q9P107; -.
DR   OpenTargets; ENSG00000089639; -.
DR   PharmGKB; PA134963566; -.
DR   VEuPathDB; HostDB:ENSG00000089639.10; -.
DR   eggNOG; KOG1453; Eukaryota.
DR   GeneTree; ENSGT00950000183110; -.
DR   HOGENOM; CLU_006236_1_0_1; -.
DR   InParanoid; Q9P107; -.
DR   OMA; HRKCMEV; -.
DR   PhylomeDB; Q9P107; -.
DR   TreeFam; TF351450; -.
DR   PathwayCommons; Q9P107; -.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   SIGNOR; Q9P107; -.
DR   BioGRID-ORCS; 51291; 11 hits in 877 CRISPR screens.
DR   ChiTaRS; GMIP; human.
DR   EvolutionaryTrace; Q9P107; -.
DR   GenomeRNAi; 51291; -.
DR   Pharos; Q9P107; Tbio.
DR   PRO; PR:Q9P107; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9P107; protein.
DR   Bgee; ENSG00000089639; Expressed in blood and 189 other tissues.
DR   ExpressionAtlas; Q9P107; baseline and differential.
DR   Genevisible; Q9P107; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:HGNC-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC-UCL.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; IDA:BHF-UCL.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; GTPase activation;
KW   Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..970
FT                   /note="GEM-interacting protein"
FT                   /id="PRO_0000056725"
FT   DOMAIN          81..344
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          554..757
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   ZN_FING         493..537
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   COMPBIAS        252..257
FT                   /note="Poly-Arg"
FT   COMPBIAS        354..419
FT                   /note="Pro-rich"
FT   COMPBIAS        763..828
FT                   /note="Pro-rich"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6PGG2"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         660
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         885
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         907
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         914
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         919
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         923
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         442..467
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056142"
FT   VARIANT         641
FT                   /note="D -> N (in dbSNP:rs12003)"
FT                   /id="VAR_044518"
FT   CONFLICT        666
FT                   /note="E -> D (in Ref. 1; AAF61330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        773
FT                   /note="S -> F (in Ref. 1; AAF61330)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        870
FT                   /note="V -> C (in Ref. 1; AAF61330)"
FT                   /evidence="ECO:0000305"
FT   HELIX           81..89
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           93..140
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           149..176
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           178..229
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           248..322
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           324..335
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   TURN            336..338
FT                   /evidence="ECO:0000244|PDB:3QWE"
FT   HELIX           343..351
FT                   /evidence="ECO:0000244|PDB:3QWE"
SQ   SEQUENCE   970 AA;  106683 MW;  8163EF62F85EB2EE CRC64;
     MDAAEPGLPP GPEGRKRYSD IFRSLDNLEI SLGNVTLEML AGDPLLSEDP EPDKTPTATV
     TNEASCWSGP SPEGPVPLTG EELDLRLIRT KGGVDAALEY AKTWSRYAKE LLAWTEKRAS
     YELEFAKSTM KIAEAGKVSI QQQSHMPLQY IYTLFLEHDL SLGTLAMETV AQQKRDYYQP
     LAAKRTEIEK WRKEFKEQWM KEQKRMNEAV QALRRAQLQY VQRSEDLRAR SQGSPEDSAP
     QASPGPSKQQ ERRRRSREEA QAKAQEAEAL YQACVREANA RQQDLEIAKQ RIVSHVRKLV
     FQGDEVLRRV TLSLFGLRGA QAERGPRAFA ALAECCAPFE PGQRYQEFVR ALRPEAPPPP
     PPAFSFQEFL PSLNSSPLDI RKKLSGPLPP RLDENSAEPG PWEDPGTGWR WQGTPGPTPG
     SDVDSVGGGS ESRSLDSPTS SPGAGTRQLV KASSTGTESS DDFEERDPDL GDGLENGLGS
     PFGKWTLSSA AQTHQLRRLR GPAKCRECEA FMVSGTECEE CFLTCHKRCL ETLLILCGHR
     RLPARTPLFG VDFLQLPRDF PEEVPFVVTK CTAEIEHRAL DVQGIYRVSG SRVRVERLCQ
     AFENGRALVE LSGNSPHDVS SVLKRFLQEL TEPVIPFHLY DAFISLAKTL HADPGDDPGT
     PSPSPEVIRS LKTLLVQLPD SNYNTLRHLV AHLFRVAARF MENKMSANNL GIVFGPTLLR
     PPDGPRAASA IPVTCLLDSG HQAQLVEFLI VHYEQIFGMD ELPQATEPPP QDSSPAPGPL
     TTSSQPPPPH LDPDSQPPVL ASDPGPDPQH HSTLEQHPTA TPTEIPTPQS DQREDVAEDT
     KDGGGEVSSQ GPEDSLLGTQ SRGHFSRQPV KYPRGGVRPV THQLSSLALV ASKLCEETPI
     TSVPRGSLRG RGPSPAAASP EGSPLRRTPL PKHFEITQET ARLLSKLDSE AVPRATCCPD
     VQPEEAEDHL
//