GMIP_MOUSE
ID GMIP_MOUSE Reviewed; 971 AA.
AC Q6PGG2; Q6P9S3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GEM-interacting protein;
DE Short=GMIP;
GN Name=Gmip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; 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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-436 AND SER-440, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-436 AND SER-440, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of
CC RhoA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GEM through its N-terminal. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGG2-2; Sequence=VSP_013190, VSP_013191;
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DR EMBL; BC057037; AAH57037.1; -; mRNA.
DR EMBL; BC060628; AAH60628.1; -; mRNA.
DR CCDS; CCDS22350.1; -. [Q6PGG2-1]
DR RefSeq; NP_932769.1; NM_198101.1. [Q6PGG2-1]
DR AlphaFoldDB; Q6PGG2; -.
DR SMR; Q6PGG2; -.
DR BioGRID; 219655; 2.
DR STRING; 10090.ENSMUSP00000045676; -.
DR iPTMnet; Q6PGG2; -.
DR PhosphoSitePlus; Q6PGG2; -.
DR EPD; Q6PGG2; -.
DR jPOST; Q6PGG2; -.
DR MaxQB; Q6PGG2; -.
DR PaxDb; Q6PGG2; -.
DR PeptideAtlas; Q6PGG2; -.
DR PRIDE; Q6PGG2; -.
DR ProteomicsDB; 271405; -. [Q6PGG2-1]
DR ProteomicsDB; 271406; -. [Q6PGG2-2]
DR Antibodypedia; 61622; 82 antibodies from 17 providers.
DR DNASU; 78816; -.
DR Ensembl; ENSMUST00000036074; ENSMUSP00000045676; ENSMUSG00000036246. [Q6PGG2-1]
DR Ensembl; ENSMUST00000123453; ENSMUSP00000116542; ENSMUSG00000036246. [Q6PGG2-2]
DR GeneID; 78816; -.
DR KEGG; mmu:78816; -.
DR UCSC; uc009lxs.1; mouse. [Q6PGG2-2]
DR UCSC; uc009lxt.1; mouse. [Q6PGG2-1]
DR CTD; 51291; -.
DR MGI; MGI:1926066; Gmip.
DR VEuPathDB; HostDB:ENSMUSG00000036246; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_1_0_1; -.
DR InParanoid; Q6PGG2; -.
DR OMA; QYMLGLD; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q6PGG2; -.
DR TreeFam; TF351450; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 78816; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Gmip; mouse.
DR PRO; PR:Q6PGG2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PGG2; protein.
DR Bgee; ENSMUSG00000036246; Expressed in granulocyte and 154 other tissues.
DR ExpressionAtlas; Q6PGG2; baseline and differential.
DR Genevisible; Q6PGG2; MM.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_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 SUPFAM; SSF57889; SSF57889; 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 Alternative splicing; Coiled coil; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..971
FT /note="GEM-interacting protein"
FT /id="PRO_0000056726"
FT DOMAIN 85..348
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 553..756
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 492..536
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 41..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P107"
FT VAR_SEQ 824..839
FT /note="LATLQRDQREEEVEDT -> VGISLPCRCGEGPVCV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013190"
FT VAR_SEQ 840..971
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013191"
SQ SEQUENCE 971 AA; 107545 MW; 0ACA8B6048BD97F2 CRC64;
MDSAETELTP APEGRKRYSD IFQSLDNLEI SLGNVTFDPL AGDPVRREDL EPDKADTATV
VTEENSEASS WRDLSPEGPA PLTEEELDLR LIRTKGGVDA ALEYAKAWSR YAKELLAWTD
KRANYELEFA KSIMKLAEAG KVSILQQSQM PLQYIYTLFL EHDLSLGALA LETVAQQKRD
YYQPLAAKRM EIEKWRKEFK EQWLKEQKRM NEAVQALRRS ELQYIQRRED LRARSQGSPE
DPPSQASPGS NKQQERRRRS REEAQAKAHE AEALYQACVR EANSRQQDLE TTKRRIVSHV
RKLVLQGDEV LRRVTLGLFE LRGAQAERGP RSFSALAECC VPFEPGQRYQ EFVRTLQPGA
PPPPSPAFCF QEFTAVVHSF PQDTKKKFSG PLPPRLEEEG SPEPGPWEVA SLGSQGIPGS
DVDSVGGGSE SRSLDSPTSS PGAGARRLVK ASSTGTESSD DFEERDPDLG DGIENGVGSP
FRKWTLSTAA QTHRLRRLRG PAKCRECEAF MVSGTECEEC FLTCHKRCLE TLLILCGHRR
LPARMSLFGV DFLQLPRDFP EEVPFVITRC TAEIEHRALG LQGIYRVSGS RVRVERLCQA
FENGRALVEL SGNSPHDITS VLKRFLQELT DPVVPFHLYD AFISLAKTLH ADPGDDPGTP
NPSPEIIRSL KTLLVQLPDS NYSTLRHLVA HLFRVAARFE ENKMSANNLG IVFGPTLLRP
PDGPRATGAS PVACLLDSGH QAQLVEFLIV HYEQIFGMDE LPLASEPLTQ DPGLAPACLE
SSPQHPASLL AQDTQPLTIA LDSSPDPKHH SALEKCPEVT PPELATLQRD QREEEVEDTR
DGAGDGSSHC PEDLALGAQS RGHFSRQPVK YSRGGVRPVT HQLSSLALVA SKLCEETPVT
VSAVHRGSLR VRGLGPAAAC PEGSPLRRNP LPKHFEITQE TARLLSKLNS DAVSRTTCCA
DPEPEESEEH L
