GRRE1_HUMAN
ID GRRE1_HUMAN Reviewed; 1070 AA.
AC O15063; Q2M3W4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Granule associated Rac and RHOG effector protein 1 {ECO:0000305};
DE Short=GARRE1 {ECO:0000305};
GN Name=GARRE1 {ECO:0000312|HGNC:HGNC:29016}; Synonyms=KIAA0355;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION BY
RP 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 [5]
RP INTERACTION WITH TNRC6A AND AGO2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29395067; DOI=10.1016/j.molcel.2017.12.020;
RA Youn J.Y., Dunham W.H., Hong S.J., Knight J.D.R., Bashkurov M., Chen G.I.,
RA Bagci H., Rathod B., MacLeod G., Eng S.W.M., Angers S., Morris Q.,
RA Fabian M., Cote J.F., Gingras A.C.;
RT "High-Density Proximity Mapping Reveals the Subcellular Organization of
RT mRNA-Associated Granules and Bodies.";
RL Mol. Cell 69:517.e11-532.e11(2018).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAC1.
RX PubMed=31871319; DOI=10.1038/s41556-019-0438-7;
RA Bagci H., Sriskandarajah N., Robert A., Boulais J., Elkholi I.E., Tran V.,
RA Lin Z.Y., Thibault M.P., Dube N., Faubert D., Hipfner D.R., Gingras A.C.,
RA Cote J.F.;
RT "Mapping the proximity interaction network of the Rho-family GTPases
RT reveals signalling pathways and regulatory mechanisms.";
RL Nat. Cell Biol. 22:120-134(2020).
RN [7]
RP CORRECTION OF PUBMED:31871319.
RX PubMed=32042180; DOI=10.1038/s41556-020-0479-y;
RA Bagci H., Sriskandarajah N., Robert A., Boulais J., Elkholi I.E., Tran V.,
RA Lin Z.Y., Thibault M.P., Dube N., Faubert D., Hipfner D.R., Gingras A.C.,
RA Cote J.F.;
RT "Author Correction: Mapping the proximity interaction network of the Rho-
RT family GTPases reveals signalling pathways and regulatory mechanisms.";
RL Nat. Cell Biol. 22:353-353(2020).
CC -!- FUNCTION: Acts as an effector of RAC1 (PubMed:31871319). Associates
CC with CCR4-NOT complex which is one of the major cellular mRNA
CC deadenylases and is linked to various cellular processes including bulk
CC mRNA degradation, miRNA-mediated repression, translational repression
CC during translational initiation and general transcription regulation
CC (PubMed:29395067). May also play a role in miRNA silencing machinery
CC (PubMed:29395067). {ECO:0000269|PubMed:29395067,
CC ECO:0000269|PubMed:31871319}.
CC -!- SUBUNIT: Interacts with AGO2 and TNRC6A. {ECO:0000269|PubMed:29395067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000305|PubMed:29395067}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20812.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002353; BAA20812.2; ALT_INIT; mRNA.
DR EMBL; BC104761; AAI04762.1; -; mRNA.
DR EMBL; BC104763; AAI04764.1; -; mRNA.
DR CCDS; CCDS12436.1; -.
DR RefSeq; NP_055501.2; NM_014686.3.
DR RefSeq; XP_005259501.1; XM_005259444.1.
DR AlphaFoldDB; O15063; -.
DR BioGRID; 115061; 159.
DR IntAct; O15063; 16.
DR STRING; 9606.ENSP00000299505; -.
DR iPTMnet; O15063; -.
DR PhosphoSitePlus; O15063; -.
DR BioMuta; KIAA0355; -.
DR EPD; O15063; -.
DR jPOST; O15063; -.
DR MassIVE; O15063; -.
DR MaxQB; O15063; -.
DR PaxDb; O15063; -.
DR PeptideAtlas; O15063; -.
DR PRIDE; O15063; -.
DR ProteomicsDB; 48415; -.
DR Antibodypedia; 2909; 27 antibodies from 13 providers.
DR DNASU; 9710; -.
DR Ensembl; ENST00000299505.8; ENSP00000299505.4; ENSG00000166398.14.
DR GeneID; 9710; -.
DR KEGG; hsa:9710; -.
DR MANE-Select; ENST00000299505.8; ENSP00000299505.4; NM_014686.5; NP_055501.2.
DR UCSC; uc002nvd.5; human.
DR CTD; 9710; -.
DR DisGeNET; 9710; -.
DR GeneCards; GARRE1; -.
DR HGNC; HGNC:29016; GARRE1.
DR HPA; ENSG00000166398; Low tissue specificity.
DR MIM; 619335; gene.
DR neXtProt; NX_O15063; -.
DR OpenTargets; ENSG00000166398; -.
DR VEuPathDB; HostDB:ENSG00000166398; -.
DR eggNOG; ENOG502QR1K; Eukaryota.
DR GeneTree; ENSGT00390000003210; -.
DR HOGENOM; CLU_010313_0_0_1; -.
DR InParanoid; O15063; -.
DR OMA; HKQINKG; -.
DR OrthoDB; 1533370at2759; -.
DR PhylomeDB; O15063; -.
DR TreeFam; TF328377; -.
DR PathwayCommons; O15063; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; O15063; -.
DR BioGRID-ORCS; 9710; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; KIAA0355; human.
DR GenomeRNAi; 9710; -.
DR Pharos; O15063; Tdark.
DR PRO; PR:O15063; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O15063; protein.
DR Bgee; ENSG00000166398; Expressed in placenta and 104 other tissues.
DR ExpressionAtlas; O15063; baseline and differential.
DR Genevisible; O15063; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB.
DR InterPro; IPR031813; DUF4745.
DR InterPro; IPR043385; GARRE1.
DR PANTHER; PTHR15703; PTHR15703; 1.
DR Pfam; PF15923; DUF4745; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1070
FT /note="Granule associated Rac and RHOG effector protein 1"
FT /id="PRO_0000050748"
FT REGION 681..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 127
FT /note="A -> V (in Ref. 1; BAA20812)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1070 AA; 116020 MW; F8A0D57717F1D89C CRC64;
MYCCSAQDSK MDYKRRFLLG GSKQKVQQHQ QYPMPELGRA LSAPLASTAT TAPLGSLTAA
GSCHHAMPHT TPIADIQQGI SKYLDALNVF CRASTFLTDL FSTVFRNSHY SKAATQLKDV
QEHVMEAASR LTSAIKPEIA KMLMELSAGA ANFTDQKEFS LQDIEVLGRC FLTVVQVHFQ
FLTHALQKVQ PVAHSCFAEV IVPEKKNSGS GGGLSGMGHT PEVEEAVRSW RGAAEATSRL
RERGCDGCLA GIEVQQLFCS QSAAIPEHQL KELNIKIDSA LQAYKIALES LGHCEYAMKA
GFHLNPKAIE ASLQGCCSEA EAQQTGRRQT PPQPMQCELP TVPVQIGSHF LKGVSFNESA
ADNLKLKTHT MLQLMKEAGC YNGITSRDDF PVTEVLNQVC PSTWRGACKT AVQLLFGQAG
LVVVDTAQIE NKEAYAPQIS LEGSRIVVQV PSTWCLKEDP ATMSLLQRSL DPEKTLGLVD
VLYTAVLDLN RWRAGREQAL PCIQIQLQRE ICDFGNQADL PSGNGNKSSG GLQKTFSKLT
SRFTKKASCT SSSSSTNYSI QNTPSKNIFI AGCSEEKAKM PGNIDTRLQS ILNIGNFPRT
TDPSQSAQNS SNTVANGFLM ERRENFLHGD DGKDEKGMNL PTDQEMQEVI DFLSGFNMGQ
SHQGSPLVTR HNSAATAMVT EQKAGAMQPQ QPSLPVPPPP RAPQAGAHTP LTPQPGLAPQ
QQSPKQQQPQ VQYYQHLLQP IGPQQPPPQP RAPGKWVHGS SQQPAQAVGA GLSPLGQWPG
ISDLSSDLYS LGLVSSYMDN VMSEVLGQKP QGPRNNTWPN RDQSDGVFGM LGEILPFDPA
VGSDPEFARY VAGVSQAMQQ KRQAQHGRRP GNPRGNWPPM DDAHRTWPFP EFFTEGDGLH
GGWSGAQGDS ASSSDETSSA NGDSLFSMFS GPDLVAAVKQ RRKHSSGEQD TSTLPSPPLL
TTVEDVNQDN KTKTWPPKAP WQHPSPLPST LPSPSAPLYA VTSPGSQWND TMQMLQSPVW
AATNDCSAAA FSYVQTPPQP PPPPAHKAAP KGFKAFPGKG ERRPAYLPQY
