BMX_HUMAN
ID BMX_HUMAN Reviewed; 675 AA.
AC P51813; A6NIH9; O60564; Q12871;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cytoplasmic tyrosine-protein kinase BMX;
DE EC=2.7.10.2;
DE AltName: Full=Bone marrow tyrosine kinase gene in chromosome X protein;
DE AltName: Full=Epithelial and endothelial tyrosine kinase;
DE Short=ETK;
DE AltName: Full=NTK38;
GN Name=BMX;
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].
RC TISSUE=Bone marrow;
RX PubMed=7970727;
RA Tamagnone L., Lahtinen I., Mustonen T., Virtaneva K., Francis F.,
RA Muscatelli F., Alitalo R.P., Smith C.I., Larsson C., Alitalo K.;
RT "BMX, a novel nonreceptor tyrosine kinase gene of the BTK/ITK/TEC/TXK
RT family located in chromosome Xp22.2.";
RL Oncogene 9:3683-3688(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC TISSUE=Prostate;
RX PubMed=9520419; DOI=10.1073/pnas.95.7.3644;
RA Qiu Y., Robinson D., Pretlow T., Kung H.-J.;
RT "Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an
RT effector of phosphatidylinositol 3'-kinase and is involved in interleukin
RT 6-induced neuroendocrine differentiation of prostate cancer cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3644-3649(1998).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP PROTEIN SEQUENCE OF 207-220 AND 223-236, AND PHOSPHORYLATION AT TYR-216 AND
RP TYR-224.
RX PubMed=12573241; DOI=10.1016/s1570-9639(02)00524-1;
RA Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A.,
RA Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.;
RT "Identification of phosphorylation sites within the SH3 domains of Tec
RT family tyrosine kinases.";
RL Biochim. Biophys. Acta 1645:123-132(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 536-599.
RC TISSUE=Blood;
RA Fuortes M.;
RL Thesis (1994), Cornell University, United States.
RN [8]
RP PHOSPHORYLATION AT TYR-566, MUTAGENESIS OF TYR-566, FUNCTION, AND
RP INTERACTION WITH STAT3.
RX PubMed=10688651; DOI=10.1128/mcb.20.6.2043-2054.2000;
RA Tsai Y.T., Su Y.H., Fang S.S., Huang T.N., Qiu Y., Jou Y.S., Shih H.M.,
RA Kung H.J., Chen R.H.;
RT "Etk, a Btk family tyrosine kinase, mediates cellular transformation by
RT linking Src to STAT3 activation.";
RL Mol. Cell. Biol. 20:2043-2054(2000).
RN [9]
RP INDUCTION, INTERACTION WITH PTK2/FAK1, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=11331870; DOI=10.1038/35074500;
RA Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H.,
RA Shimizu Y., Qiu Y.;
RT "Regulation of the PH-domain-containing tyrosine kinase Etk by focal
RT adhesion kinase through the FERM domain.";
RL Nat. Cell Biol. 3:439-444(2001).
RN [10]
RP DOMAIN, AND INTERACTION WITH CAV1.
RX PubMed=11751885; DOI=10.1074/jbc.m108537200;
RA Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T., Smith C.I.,
RA Mohamed A.J.;
RT "Functional interaction of caveolin-1 with Bruton's tyrosine kinase and
RT Bmx.";
RL J. Biol. Chem. 277:9351-9357(2002).
RN [11]
RP INTERACTION WITH RUFY1 AND RUFY2.
RX PubMed=11877430; DOI=10.1074/jbc.m111933200;
RA Yang J., Kim O., Wu J., Qiu Y.;
RT "Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-domain
RT containing protein RUFY1. A possible role of Etk in regulation of vesicle
RT trafficking.";
RL J. Biol. Chem. 277:30219-30226(2002).
RN [12]
RP ACTIVITY REGULATION, PHOSPHORYLATION, FUNCTION, AND INTERACTION WITH
RP TNFRSF1B.
RX PubMed=12370298; DOI=10.1128/mcb.22.21.7512-7523.2002;
RA Pan S., An P., Zhang R., He X., Yin G., Min W.;
RT "Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role
RT in endothelial cell migration and angiogenesis.";
RL Mol. Cell. Biol. 22:7512-7523(2002).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BCAR1.
RX PubMed=12832404; DOI=10.1074/jbc.m306438200;
RA Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.;
RT "p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin
RT cytoskeleton and cell migration.";
RL J. Biol. Chem. 278:35636-35643(2003).
RN [14]
RP FUNCTION.
RX PubMed=15788485; DOI=10.1152/ajpcell.00410.2004;
RA Chau C.H., Clavijo C.A., Deng H.T., Zhang Q., Kim K.J., Qiu Y., Le A.D.,
RA Ann D.K.;
RT "Etk/Bmx mediates expression of stress-induced adaptive genes VEGF, PAI-1,
RT and iNOS via multiple signaling cascades in different cell systems.";
RL Am. J. Physiol. 289:C444-C454(2005).
RN [15]
RP PHOSPHORYLATION, ACTIVITY REGULATION, FUNCTION, AND INTERACTION WITH MYD88;
RP PTK2/FAK1 AND TIRAP.
RX PubMed=18292575; DOI=10.4049/jimmunol.180.5.3485;
RA Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.;
RT "Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-
RT talk between MyD88 and FAK pathways.";
RL J. Immunol. 180:3485-3491(2008).
RN [16]
RP REVIEW ON FUNCTION.
RX PubMed=11114746; DOI=10.1038/sj.onc.1203958;
RA Qiu Y., Kung H.J.;
RT "Signaling network of the Btk family kinases.";
RL Oncogene 19:5651-5661(2000).
RN [17]
RP REVIEW ON FUNCTION.
RX PubMed=11340625; DOI=10.1002/bies.1062;
RA Smith C.I., Islam T.C., Mattsson P.T., Mohamed A.J., Nore B.F., Vihinen M.;
RT "The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk,
RT Tec, Txk and homologs in other species.";
RL Bioessays 23:436-446(2001).
RN [18]
RP REVIEW ON FUNCTION.
RX PubMed=17624943; DOI=10.1111/j.1600-065x.2007.00534.x;
RA Gomez-Rodriguez J., Readinger J.A., Viorritto I.C., Mueller K.L.,
RA Houghtling R.A., Schwartzberg P.L.;
RT "Tec kinases, actin, and cell adhesion.";
RL Immunol. Rev. 218:45-64(2007).
RN [19]
RP STRUCTURE BY NMR OF 112-393.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the human BMX SH2 domain and of the BTK motif of
RT human cytoplasmic tyrosine-protein kinase BMX.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [20]
RP STRUCTURE BY NMR OF 291-393.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the human bmx SH2 domain.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [21]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-284 AND TRP-670.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Non-receptor tyrosine kinase that plays central but diverse
CC modulatory roles in various signaling processes involved in the
CC regulation of actin reorganization, cell migration, cell proliferation
CC and survival, cell adhesion, and apoptosis. Participates in signal
CC transduction stimulated by growth factor receptors, cytokine receptors,
CC G-protein coupled receptors, antigen receptors and integrins. Induces
CC tyrosine phosphorylation of BCAR1 in response to integrin regulation.
CC Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator
CC of integrin signaling events leading to the regulation of actin
CC cytoskeleton and cell motility. Plays a critical role in TNF-induced
CC angiogenesis, and implicated in the signaling of TEK and FLT1
CC receptors, 2 important receptor families essential for angiogenesis.
CC Required for the phosphorylation and activation of STAT3, a
CC transcription factor involved in cell differentiation. Also involved in
CC interleukin-6 (IL6) induced differentiation. Also plays a role in
CC programming adaptive cytoprotection against extracellular stress in
CC different cell systems, salivary epithelial cells, brain endothelial
CC cells, and dermal fibroblasts. May be involved in regulation of
CC endocytosis through its interaction with an endosomal protein RUFY1.
CC May also play a role in the growth and differentiation of hematopoietic
CC cells; as well as in signal transduction in endocardial and arterial
CC endothelial cells. {ECO:0000269|PubMed:10688651,
CC ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:12370298,
CC ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:15788485,
CC ECO:0000269|PubMed:18292575, ECO:0000269|PubMed:9520419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: TEK and vascular endothelial growth factor
CC receptor 1 (FLT1) stimulate BMX tyrosine kinase activity (By
CC similarity). Activated by integrins through the mediation of PTK2/FAK1.
CC Activated by TNF through the mediation of TNFRSF1B. {ECO:0000250,
CC ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:12370298,
CC ECO:0000269|PubMed:18292575}.
CC -!- SUBUNIT: Interacts with BCAR1, CAV1, MYD88, PTK2/FAK1, RUFY1, RUFY2,
CC STAT3, TIRAP and TNFRSF1B. {ECO:0000269|PubMed:10688651,
CC ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11751885,
CC ECO:0000269|PubMed:11877430, ECO:0000269|PubMed:12370298,
CC ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:18292575}.
CC -!- INTERACTION:
CC P51813; Q13490: BIRC2; NbExp=3; IntAct=EBI-696657, EBI-514538;
CC P51813; P08238: HSP90AB1; NbExp=3; IntAct=EBI-696657, EBI-352572;
CC P51813; P11309: PIM1; NbExp=2; IntAct=EBI-696657, EBI-696621;
CC P51813; P11309-2: PIM1; NbExp=6; IntAct=EBI-696657, EBI-1018633;
CC P51813; Q16825: PTPN21; NbExp=3; IntAct=EBI-696657, EBI-2860264;
CC P51813; P40763: STAT3; NbExp=8; IntAct=EBI-696657, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12832404}.
CC Note=Localizes to the edges of spreading cells when complexed with
CC BCAR1.
CC -!- TISSUE SPECIFICITY: Highly expressed in cells with great migratory
CC potential, including endothelial cells and metastatic carcinoma cell
CC lines.
CC -!- INDUCTION: Activated by IL6/interleukin-6 through phosphatidylinositol
CC 3-kinase (PI3-kinase) pathway. It is likely that activation occurs
CC through binding of phosphoinositides to the PH domain.
CC {ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:9520419}.
CC -!- DOMAIN: SH2 domain mediates interaction with RUFY1.
CC {ECO:0000269|PubMed:11751885}.
CC -!- PTM: Phosphorylated in response to protein I/II and to LPS.
CC Phosphorylation at Tyr-566 by SRC and by autocatalysis leads to
CC activation and is required for STAT3 phosphorylation by BMX.
CC {ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12370298,
CC ECO:0000269|PubMed:12573241, ECO:0000269|PubMed:18292575}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. TEC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08966.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X83107; CAA58169.1; -; mRNA.
DR EMBL; AF045459; AAC08966.1; ALT_INIT; mRNA.
DR EMBL; AC097625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98889.1; -; Genomic_DNA.
DR EMBL; BC016652; AAH16652.1; -; mRNA.
DR EMBL; U08341; AAA17744.1; -; mRNA.
DR CCDS; CCDS14168.1; -.
DR PIR; S60612; S60612.
DR RefSeq; NP_001307795.1; NM_001320866.1.
DR RefSeq; NP_001712.1; NM_001721.6.
DR RefSeq; NP_975010.1; NM_203281.2.
DR PDB; 2EKX; NMR; -; A=291-393.
DR PDB; 2YS2; NMR; -; A=113-149.
DR PDB; 3SXR; X-ray; 2.40 A; A/B=411-675.
DR PDB; 3SXS; X-ray; 1.89 A; A=411-675.
DR PDB; 6I99; X-ray; 2.00 A; A/B=411-675.
DR PDBsum; 2EKX; -.
DR PDBsum; 2YS2; -.
DR PDBsum; 3SXR; -.
DR PDBsum; 3SXS; -.
DR PDBsum; 6I99; -.
DR AlphaFoldDB; P51813; -.
DR SMR; P51813; -.
DR BioGRID; 107128; 72.
DR IntAct; P51813; 77.
DR MINT; P51813; -.
DR STRING; 9606.ENSP00000350224; -.
DR BindingDB; P51813; -.
DR ChEMBL; CHEMBL3834; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB15035; Zanubrutinib.
DR DrugCentral; P51813; -.
DR GuidetoPHARMACOLOGY; 1942; -.
DR iPTMnet; P51813; -.
DR PhosphoSitePlus; P51813; -.
DR BioMuta; BMX; -.
DR DMDM; 1705489; -.
DR EPD; P51813; -.
DR jPOST; P51813; -.
DR MassIVE; P51813; -.
DR MaxQB; P51813; -.
DR PaxDb; P51813; -.
DR PeptideAtlas; P51813; -.
DR PRIDE; P51813; -.
DR ProteomicsDB; 56409; -.
DR Antibodypedia; 412; 655 antibodies from 34 providers.
DR DNASU; 660; -.
DR Ensembl; ENST00000342014.6; ENSP00000340082.6; ENSG00000102010.15.
DR Ensembl; ENST00000348343.11; ENSP00000308774.6; ENSG00000102010.15.
DR Ensembl; ENST00000357607.6; ENSP00000350224.2; ENSG00000102010.15.
DR GeneID; 660; -.
DR KEGG; hsa:660; -.
DR MANE-Select; ENST00000348343.11; ENSP00000308774.6; NM_203281.3; NP_975010.1.
DR UCSC; uc004cww.3; human.
DR CTD; 660; -.
DR DisGeNET; 660; -.
DR GeneCards; BMX; -.
DR HGNC; HGNC:1079; BMX.
DR HPA; ENSG00000102010; Tissue enriched (epididymis).
DR MIM; 300101; gene.
DR neXtProt; NX_P51813; -.
DR OpenTargets; ENSG00000102010; -.
DR PharmGKB; PA25389; -.
DR VEuPathDB; HostDB:ENSG00000102010; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000161172; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; P51813; -.
DR OMA; VPILRMD; -.
DR PhylomeDB; P51813; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; P51813; -.
DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; P51813; -.
DR SIGNOR; P51813; -.
DR BioGRID-ORCS; 660; 11 hits in 714 CRISPR screens.
DR ChiTaRS; BMX; human.
DR EvolutionaryTrace; P51813; -.
DR GeneWiki; BMX_(gene); -.
DR GenomeRNAi; 660; -.
DR Pharos; P51813; Tchem.
DR PRO; PR:P51813; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51813; protein.
DR Bgee; ENSG00000102010; Expressed in corpus epididymis and 106 other tissues.
DR Genevisible; P51813; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR CDD; cd10399; SH2_Tec_Bmx; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR028840; BMX.
DR InterPro; IPR035875; BMX_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR24418:SF91; PTHR24418:SF91; 2.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; ATP-binding; Cell adhesion; Cytoplasm;
KW Direct protein sequencing; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; SH2 domain; Stress response;
KW Transferase; Tyrosine-protein kinase; Zinc; Zinc-finger.
FT CHAIN 1..675
FT /note="Cytoplasmic tyrosine-protein kinase BMX"
FT /id="PRO_0000088063"
FT DOMAIN 4..111
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 296..392
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 417..675
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 113..149
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT MOTIF 596..603
FT /note="CAV1-binding"
FT ACT_SITE 536
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 423..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 216
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12573241"
FT MOD_RES 224
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12573241"
FT MOD_RES 566
FT /note="Phosphotyrosine; by SRC and autocatalysis"
FT /evidence="ECO:0000269|PubMed:10688651"
FT VARIANT 284
FT /note="S -> L (in dbSNP:rs35353387)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041674"
FT VARIANT 670
FT /note="R -> W (in a lung large cell carcinoma sample;
FT somatic mutation; dbSNP:rs1029888196)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041675"
FT MUTAGEN 566
FT /note="Y->F: Abolishes almost completely the SRC-induced
FT phosphorylation of BMX."
FT /evidence="ECO:0000269|PubMed:10688651"
FT CONFLICT 207
FT /note="P -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="A -> S (in Ref. 7; AAA17744)"
FT /evidence="ECO:0000305"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2YS2"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2YS2"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2EKX"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:2EKX"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:2EKX"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:2EKX"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2EKX"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:2EKX"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:2EKX"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2EKX"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:3SXS"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 454..466
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 497..504
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 510..529
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:3SXS"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:3SXR"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 581..586
FT /evidence="ECO:0007829|PDB:3SXS"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 593..606
FT /evidence="ECO:0007829|PDB:3SXS"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:3SXS"
FT TURN 612..615
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 618..626
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 639..647
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 659..666
FT /evidence="ECO:0007829|PDB:3SXS"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:3SXS"
SQ SEQUENCE 675 AA; 78011 MW; CB22382A3BD02599 CRC64;
MDTKSILEEL LLKRSQQKKK MSPNNYKERL FVLTKTNLSY YEYDKMKRGS RKGSIEIKKI
RCVEKVNLEE QTPVERQYPF QIVYKDGLLY VYASNEESRS QWLKALQKEI RGNPHLLVKY
HSGFFVDGKF LCCQQSCKAA PGCTLWEAYA NLHTAVNEEK HRVPTFPDRV LKIPRAVPVL
KMDAPSSSTT LAQYDNESKK NYGSQPPSSS TSLAQYDSNS KKIYGSQPNF NMQYIPREDF
PDWWQVRKLK SSSSSEDVAS SNQKERNVNH TTSKISWEFP ESSSSEEEEN LDDYDWFAGN
ISRSQSEQLL RQKGKEGAFM VRNSSQVGMY TVSLFSKAVN DKKGTVKHYH VHTNAENKLY
LAENYCFDSI PKLIHYHQHN SAGMITRLRH PVSTKANKVP DSVSLGNGIW ELKREEITLL
KELGSGQFGV VQLGKWKGQY DVAVKMIKEG SMSEDEFFQE AQTMMKLSHP KLVKFYGVCS
KEYPIYIVTE YISNGCLLNY LRSHGKGLEP SQLLEMCYDV CEGMAFLESH QFIHRDLAAR
NCLVDRDLCV KVSDFGMTRY VLDDQYVSSV GTKFPVKWSA PEVFHYFKYS SKSDVWAFGI
LMWEVFSLGK QPYDLYDNSQ VVLKVSQGHR LYRPHLASDT IYQIMYSCWH ELPEKRPTFQ
QLLSSIEPLR EKDKH
