ID GAB3_HUMAN Reviewed; 586 AA. AC Q8WWW8; A6NHF8; E9PB44; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 24-JUL-2024, entry version 151. 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 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). RC TISSUE=Dendritic cell, and Eosinophil; 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] (ISOFORMS 2 AND 3). RC TISSUE=Thalamus, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-482, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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). CC -!- SUBUNIT: Interacts with PIK3R/p85, SHP2 and GRAP2/MONA (By similarity). CC May interact with Grb2. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WWW8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWW8-2; Sequence=VSP_045033; CC Name=3; CC IsoId=Q8WWW8-3; Sequence=VSP_045033, VSP_055259; CC -!- PTM: Phosphorylated on tyrosine residue(s) after macrophage colony- CC stimulating factor (M-CSF) receptor stimulation. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GAB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AK307927; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={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; AY057989; AAL25825.1; -; mRNA. DR EMBL; AK126283; BAG54302.1; -; mRNA. DR EMBL; AK307927; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC107450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109993; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72665.1; -; Genomic_DNA. DR EMBL; CH471172; EAW72667.1; -; Genomic_DNA. DR CCDS; CCDS14760.1; -. [Q8WWW8-1] DR CCDS; CCDS48198.1; -. [Q8WWW8-2] DR CCDS; CCDS65357.1; -. [Q8WWW8-3] DR RefSeq; NP_001075042.1; NM_001081573.2. [Q8WWW8-2] DR RefSeq; NP_001269212.1; NM_001282283.1. [Q8WWW8-3] DR RefSeq; NP_542179.1; NM_080612.3. [Q8WWW8-1] DR RefSeq; XP_005274705.1; XM_005274648.1. [Q8WWW8-2] DR RefSeq; XP_006724867.1; XM_006724804.1. [Q8WWW8-2] DR AlphaFoldDB; Q8WWW8; -. DR SMR; Q8WWW8; -. DR BioGRID; 126581; 10. DR ELM; Q8WWW8; -. DR IntAct; Q8WWW8; 1. DR MINT; Q8WWW8; -. DR STRING; 9606.ENSP00000399588; -. DR iPTMnet; Q8WWW8; -. DR PhosphoSitePlus; Q8WWW8; -. DR BioMuta; GAB3; -. DR DMDM; 74716251; -. DR MassIVE; Q8WWW8; -. DR PaxDb; 9606-ENSP00000399588; -. DR PeptideAtlas; Q8WWW8; -. DR ProteomicsDB; 1194; -. DR ProteomicsDB; 19139; -. DR ProteomicsDB; 74948; -. [Q8WWW8-1] DR Antibodypedia; 535; 130 antibodies from 25 providers. DR DNASU; 139716; -. DR Ensembl; ENST00000369568.8; ENSP00000358581.4; ENSG00000160219.12. [Q8WWW8-3] DR Ensembl; ENST00000369575.7; ENSP00000358588.3; ENSG00000160219.12. [Q8WWW8-1] DR Ensembl; ENST00000424127.3; ENSP00000399588.2; ENSG00000160219.12. [Q8WWW8-2] DR GeneID; 139716; -. DR KEGG; hsa:139716; -. DR MANE-Select; ENST00000424127.3; ENSP00000399588.2; NM_001081573.3; NP_001075042.1. [Q8WWW8-2] DR UCSC; uc004fmj.3; human. [Q8WWW8-1] DR AGR; HGNC:17515; -. DR CTD; 139716; -. DR DisGeNET; 139716; -. DR GeneCards; GAB3; -. DR HGNC; HGNC:17515; GAB3. DR HPA; ENSG00000160219; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 300482; gene. DR neXtProt; NX_Q8WWW8; -. DR OpenTargets; ENSG00000160219; -. DR PharmGKB; PA28479; -. DR VEuPathDB; HostDB:ENSG00000160219; -. DR eggNOG; ENOG502QU11; Eukaryota. DR GeneTree; ENSGT00940000159803; -. DR HOGENOM; CLU_028652_1_0_1; -. DR InParanoid; Q8WWW8; -. DR OMA; GRMCGNP; -. DR OrthoDB; 2904117at2759; -. DR PhylomeDB; Q8WWW8; -. DR TreeFam; TF329487; -. DR PathwayCommons; Q8WWW8; -. DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells. DR SignaLink; Q8WWW8; -. DR BioGRID-ORCS; 139716; 18 hits in 772 CRISPR screens. DR ChiTaRS; GAB3; human. DR GenomeRNAi; 139716; -. DR Pharos; Q8WWW8; Tbio. DR PRO; PR:Q8WWW8; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8WWW8; Protein. DR Bgee; ENSG00000160219; Expressed in left ventricle myocardium and 122 other cell types or tissues. DR ExpressionAtlas; Q8WWW8; baseline and differential. 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; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd13385; PH_Gab3; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR046355; Gab1-4-like. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR45960; GRB2-ASSOCIATED-BINDING PROTEIN; 1. DR PANTHER; PTHR45960:SF3; GRB2-ASSOCIATED-BINDING PROTEIN 3; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Phosphoprotein; Reference proteome. FT CHAIN 1..586 FT /note="GRB2-associated-binding protein 3" FT /id="PRO_0000318939" FT DOMAIN 5..117 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 149..171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 401..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..330 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 482 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 125 FT /note="A -> AA (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045033" FT VAR_SEQ 510..548 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055259" FT VARIANT 237 FT /note="P -> S (in dbSNP:rs17281349)" FT /id="VAR_038917" SQ SEQUENCE 586 AA; 65589 MW; 9DE0223C34AD8FFE CRC64; MSAGDAVCTG WLVKSPPERK LQRYAWRKRW FVLRRGRMSG NPDVLEYYRN KHSSKPIRVI DLSECAVWKH VGPSFVRKEF QNNFVFIVKT TSRTFYLVAK TEQEMQVWVH SISQVCNLGH LEDGADSMES LSYTPSSLQP SSASSLLTAH AASSSLPRDD PNTNAVATEE TRSESELLFL PDYLVLSNCE TGRLHHTSLP TRCDSWSNSD RSLEQASFDD VFVDCLQPLP SSHLVHPSCH GSGAQEVPSS RPQAALIWSR EINGPPRDHL SSSPLLESSL SSTIQVDKNQ GSLPCGAKEL DIMSNTPPPR PPKPSHLSER RQEEWSTHSG SKKPECTLVP RRISLSGLDN MRTWKADVEG QSLRHRDKRL SLNLPCRFSP MYPTASASIE DSYVPMSPQA GASGLGPHCS PDDYIPMNSG SISSPLPELP ANLEPPPVNR DLKPQRKSRP PPLDLRNLSI IREHASLTRT RTVPCSRTSF LSPERNGINS ARFFANPVSR EDEESYIEME EHRTASSLSS GALTWTKKFS LDYLALDFNS ASPAPMQQKL LLSEEQRVDY VQVDEQKTQA LQSTKQEWTD ERQSKV //