ID GEM_MOUSE Reviewed; 295 AA. AC P55041; Q8JZS1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2003, sequence version 2. DT 24-JAN-2024, entry version 173. DE RecName: Full=GTP-binding protein GEM; DE AltName: Full=GTP-binding mitogen-induced T-cell protein; DE AltName: Full=RAS-like protein KIR; GN Name=Gem; Synonyms=Kir; 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 [MRNA]. RX PubMed=7912851; DOI=10.1126/science.7912851; RA Maguire J., Santoro T., Jensen P., Siebenlist U., Yewdell J., Kelly K.; RT "Gem: an induced, immediate early protein belonging to the Ras family."; RL Science 265:241-244(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7809057; DOI=10.1073/pnas.91.26.12448; RA Cohen L., Mohr R., Chen Y.-Y., Huang M., Kato R., Dorin D., Tamanoi F., RA Goga A., Afar D., Rosenberg N., Witte O.; RT "Transcriptional activation of a ras-like gene (kir) by oncogenic tyrosine RT kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12448-12452(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Retina; 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 [4] RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF TRP-269. RX PubMed=8810259; DOI=10.1074/jbc.271.41.25067; RA Fischer R., Wei Y., Anagli J., Berchtold M.W.; RT "Calmodulin binds to and inhibits GTP binding of the ras-like GTPase RT Kir/Gem."; RL J. Biol. Chem. 271:25067-25070(1996). CC -!- FUNCTION: Could be a regulatory protein, possibly participating in CC receptor-mediated signal transduction at the plasma membrane. Has CC guanine nucleotide-binding activity but undetectable intrinsic GTPase CC activity. CC -!- SUBUNIT: Interacts with calmodulin in a Ca(2+)-dependent manner. CC Calmodulin binding significantly decreases GTP binding. Binds ROCK1 (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC P55041; P31946: YWHAB; Xeno; NbExp=3; IntAct=EBI-7082069, EBI-359815; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. CC -!- INDUCTION: By mitogens. CC -!- PTM: Phosphorylated on tyrosine residues. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family. CC {ECO:0000305}. 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; U10551; AAA64912.1; -; mRNA. DR EMBL; U13053; AAC52145.1; -; mRNA. DR EMBL; BC029668; AAH29668.1; -; mRNA. DR CCDS; CCDS17971.1; -. DR PIR; B54575; B54575. DR PIR; I49117; I49117. DR RefSeq; NP_034406.2; NM_010276.4. DR AlphaFoldDB; P55041; -. DR SMR; P55041; -. DR BioGRID; 199898; 1. DR IntAct; P55041; 2. DR MINT; P55041; -. DR STRING; 10090.ENSMUSP00000103939; -. DR iPTMnet; P55041; -. DR PhosphoSitePlus; P55041; -. DR EPD; P55041; -. DR jPOST; P55041; -. DR PaxDb; 10090-ENSMUSP00000103939; -. DR PeptideAtlas; P55041; -. DR ProteomicsDB; 268863; -. DR Antibodypedia; 12852; 199 antibodies from 34 providers. DR DNASU; 14579; -. DR Ensembl; ENSMUST00000029868.7; ENSMUSP00000029868.7; ENSMUSG00000028214.14. DR Ensembl; ENSMUST00000108304.9; ENSMUSP00000103939.3; ENSMUSG00000028214.14. DR GeneID; 14579; -. DR KEGG; mmu:14579; -. DR UCSC; uc008rzv.2; mouse. DR AGR; MGI:99844; -. DR CTD; 2669; -. DR MGI; MGI:99844; Gem. DR VEuPathDB; HostDB:ENSMUSG00000028214; -. DR eggNOG; KOG0395; Eukaryota. DR GeneTree; ENSGT00940000157830; -. DR HOGENOM; CLU_041217_3_2_1; -. DR InParanoid; P55041; -. DR OMA; SNEYNPQ; -. DR OrthoDB; 5473132at2759; -. DR PhylomeDB; P55041; -. DR TreeFam; TF314379; -. DR BioGRID-ORCS; 14579; 3 hits in 79 CRISPR screens. DR ChiTaRS; Gem; mouse. DR PRO; PR:P55041; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P55041; Protein. DR Bgee; ENSMUSG00000028214; Expressed in ascending aorta and 156 other cell types or tissues. DR ExpressionAtlas; P55041; baseline and differential. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI. DR GO; GO:0030496; C:midbody; ISO:MGI. DR GO; GO:0072686; C:mitotic spindle; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051233; C:spindle midzone; ISO:MGI. DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central. DR GO; GO:0019003; F:GDP binding; ISO:MGI. DR GO; GO:0005525; F:GTP binding; ISO:MGI. DR GO; GO:0003924; F:GTPase activity; ISO:MGI. DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI. DR GO; GO:0051276; P:chromosome organization; ISO:MGI. DR GO; GO:0051310; P:metaphase chromosome alignment; ISO:MGI. DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI. DR CDD; cd04148; RGK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR017358; RGK. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR45775:SF4; GTP-BINDING PROTEIN GEM; 1. DR PANTHER; PTHR45775; RAD, GEM/KIR FAMILY MEMBER 2, ISOFORM C; 1. DR Pfam; PF00071; Ras; 1. DR PIRSF; PIRSF038017; GTP-binding_GEM; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51421; RAS; 1. DR Genevisible; P55041; MM. PE 1: Evidence at protein level; KW Cell membrane; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1..295 FT /note="GTP-binding protein GEM" FT /id="PRO_0000122476" FT REGION 39..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 265..284 FT /note="Calmodulin-binding" FT COMPBIAS 39..58 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 81..88 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 190..193 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MUTAGEN 269 FT /note="W->G: No calmodulin binding." FT /evidence="ECO:0000269|PubMed:8810259" FT CONFLICT 23 FT /note="I -> M (in Ref. 1; AAA64912)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="S -> T (in Ref. 1; AAA64912)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="V -> E (in Ref. 1; AAA64912)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="R -> P (in Ref. 1; AAA64912)" FT /evidence="ECO:0000305" FT CONFLICT 282..284 FT /note="FKL -> SSS (in Ref. 1; AAA64912)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="V -> W (in Ref. 2; AAC52145)" FT /evidence="ECO:0000305" SQ SEQUENCE 295 AA; 33725 MW; 4618F225D4FAAFA5 CRC64; MTLNNVTMRQ GTVGMQPQQR WSIPADARHL MVQKDPHPCN LRNRHSTAPE EHCRRSWSSD STDSVISSES GNTYYRVVLI GEQGVGKSTL ANIFAGVHDS MDSDCEVLGE DTYERTLVVD GESATIILLD MWENKGENEW LHDHCMQVGD AYLIVYSITD RASFEKASEL RIQLRRARQT EDIPIILVGN KSDLVRCREV SVSEGRACAV VFDCKFIETS AAVQHNVKEL FEGIVRQVRL RRDSKEKNER RLAYQKRRES IPRKARRFWG KIVAKNNKNM AFKLKSKSCH DLSVL //