GAB3_MOUSE
ID GAB3_MOUSE Reviewed; 595 AA.
AC Q8BSM5; Q684I9; Q8VH53;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GRB2-associated-binding protein 3;
DE AltName: Full=GRB2-associated binder 3;
DE AltName: Full=Growth factor receptor bound protein 2-associated protein 3;
GN Name=Gab3;
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], INTERACTION WITH PIK3R AND SHP2, INDUCTION BY
RP M-CSF, AND PHOSPHORYLATION.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=11739737; DOI=10.1128/mcb.22.1.231-244.2002;
RA Wolf I., Jenkins B.J., Liu Y., Seiffert M., Custodio J.M., Young P.,
RA Rohrschneider L.R.;
RT "Gab3, a new DOS/Gab family member, facilitates macrophage
RT differentiation.";
RL Mol. Cell. Biol. 22:231-244(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 330-579.
RC STRAIN=NMRI; TISSUE=Brain, and Heart;
RX PubMed=16503986; DOI=10.1186/1471-2164-7-29;
RA Kolb-Kokocinski A., Mehrle A., Bechtel S., Simpson J.C., Kioschis P.,
RA Wiemann S., Wellenreuther R., Poustka A.;
RT "The systematic functional characterisation of Xq28 genes prioritises
RT candidate disease genes.";
RL BMC Genomics 7:29-29(2006).
RN [5]
RP INTERACTION WITH GRAP2.
RX PubMed=11997510; DOI=10.1128/mcb.22.11.3744-3756.2002;
RA Bourgin C., Bourette R.P., Arnaud S., Liu Y., Rohrschneider L.R.,
RA Mouchiroud G.;
RT "Induced expression and association of the Mona/Gads adapter and Gab3
RT scaffolding protein during monocyte/macrophage differentiation.";
RL Mol. Cell. Biol. 22:3744-3756(2002).
RN [6]
RP FUNCTION.
RX PubMed=12640125; DOI=10.1128/mcb.23.7.2415-2424.2003;
RA Seiffert M., Custodio J.M., Wolf I., Harkey M., Liu Y., Blattman J.N.,
RA Greenberg P.D., Rohrschneider L.R.;
RT "Gab3-deficient mice exhibit normal development and hematopoiesis and are
RT immunocompetent.";
RL Mol. Cell. Biol. 23:2415-2424(2003).
CC -!- SUBUNIT: Interacts with PIK3R/p85, SHP2 and GRAP2/MONA. May interact
CC with Grb2. {ECO:0000269|PubMed:11739737, ECO:0000269|PubMed:11997510}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus and weakly in
CC brain, heart, lung, kidney, uterus, and embryonic stem cells. Also
CC expressed in myeloid and macrophage cell lines.
CC -!- PTM: Phosphorylated on tyrosine residue(s) after macrophage colony-
CC stimulating factor (M-CSF) receptor stimulation.
CC {ECO:0000269|PubMed:11739737}.
CC -!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}.
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DR EMBL; AY057988; AAL25824.1; -; mRNA.
DR EMBL; AK031227; BAC27308.1; -; mRNA.
DR EMBL; AL808110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ748654; CAG38688.1; -; mRNA.
DR CCDS; CCDS30235.1; -.
DR RefSeq; NP_853615.1; NM_181584.4.
DR AlphaFoldDB; Q8BSM5; -.
DR SMR; Q8BSM5; -.
DR STRING; 10090.ENSMUSP00000041951; -.
DR iPTMnet; Q8BSM5; -.
DR PhosphoSitePlus; Q8BSM5; -.
DR PaxDb; Q8BSM5; -.
DR PRIDE; Q8BSM5; -.
DR ProteomicsDB; 271822; -.
DR Antibodypedia; 535; 130 antibodies from 25 providers.
DR DNASU; 210710; -.
DR Ensembl; ENSMUST00000037374; ENSMUSP00000041951; ENSMUSG00000032750.
DR GeneID; 210710; -.
DR KEGG; mmu:210710; -.
DR UCSC; uc009tpn.2; mouse.
DR CTD; 139716; -.
DR MGI; MGI:2387324; Gab3.
DR VEuPathDB; HostDB:ENSMUSG00000032750; -.
DR eggNOG; ENOG502QU11; Eukaryota.
DR GeneTree; ENSGT00940000159803; -.
DR InParanoid; Q8BSM5; -.
DR OMA; SQCETGS; -.
DR OrthoDB; 1153633at2759; -.
DR PhylomeDB; Q8BSM5; -.
DR TreeFam; TF329487; -.
DR BioGRID-ORCS; 210710; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Gab3; mouse.
DR PRO; PR:Q8BSM5; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BSM5; protein.
DR Bgee; ENSMUSG00000032750; Expressed in animal zygote and 69 other tissues.
DR ExpressionAtlas; Q8BSM5; baseline and differential.
DR Genevisible; Q8BSM5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0030225; P:macrophage differentiation; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046355; Gab1-4-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR45960; PTHR45960; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..595
FT /note="GRB2-associated-binding protein 3"
FT /id="PRO_0000318940"
FT DOMAIN 5..117
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 295..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW8"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWW8"
FT CONFLICT 161
FT /note="R -> G (in Ref. 1; AAL25824)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="T -> I (in Ref. 1; AAL25824)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="E -> A (in Ref. 1; AAL25824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 67840 MW; 59850B7B55276F30 CRC64;
MSTGDTVCMG WLIKSPPERK LQRYAWRKRW FVLRRGRMSG NPDVLEYYRN KHSNKPIRVI
DLSECTVWKH AGPGFIRKEF QKNFVFIVKT TSRTFYLVAK TEEEMQVWVH SISQVCNFSH
LEDGADSMES LSHMPSSFQP SPASSLHTVH VANSALLKDD RNTNSVVTEE TRRESEFLFL
PDYLILSNCE TGRLHHASLP TRCDSWSNSN HSLAQTSFDD VFLDGLQPFI SNNLVHPLHH
GKVSQDFPSI RPQASLIWNR EINGPSRNLM SSSPLLESSL NPTVHVEEKQ VSLPSGVKEL
NIMSNTPPPR PPKPSYLSEQ RQDQPLLTGH SSNKKPGYTM VPRRISLSGL DHVGSWKGDV
QSQSLRHRDK RLSLNLPCKF SPIYPTASPS AEDSYVPMSP KGTASELRPH CSQDDYIPMS
SSMLPELPAD LEPPPVNRNL KPQRKSRPPP LDSRNLSTIQ EHTSLTRTYT VPCNRTSFLS
PQRNGINCAR LFSTPSEEEE EEEEEEEEEE EEEKYIQMEE YGTVSSLSRS ALSWTKKFSL
DYLALDFNST SPAPVQKKLL LSEEQRVDYV QVDEQKTQAL RSTKQEWTDE RQSKV
