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Cytoplasmic tyrosine-protein kinase BMX (EC 2.7.10.2) (Bone marrow tyrosine kinase gene in chromosome X protein) (Epithelial and endothelial tyrosine kinase) (ETK) (NTK38)

 BMX_HUMAN               Reviewed;         675 AA.
P51813; A6NIH9; O60564; Q12871;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 190.
RecName: Full=Cytoplasmic tyrosine-protein kinase BMX;
EC=2.7.10.2;
AltName: Full=Bone marrow tyrosine kinase gene in chromosome X protein;
AltName: Full=Epithelial and endothelial tyrosine kinase;
Short=ETK;
AltName: Full=NTK38;
Name=BMX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
PubMed=7970727;
Tamagnone L., Lahtinen I., Mustonen T., Virtaneva K., Francis F.,
Muscatelli F., Alitalo R.P., Smith C.I., Larsson C., Alitalo K.;
"BMX, a novel nonreceptor tyrosine kinase gene of the BTK/ITK/TEC/TXK
family located in chromosome Xp22.2.";
Oncogene 9:3683-3688(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
TISSUE=Prostate;
PubMed=9520419; DOI=10.1073/pnas.95.7.3644;
Qiu Y., Robinson D., Pretlow T., Kung H.-J.;
"Etk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an
effector of phosphatidylinositol 3'-kinase and is involved in
interleukin 6-induced neuroendocrine differentiation of prostate
cancer cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:3644-3649(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 207-220 AND 223-236, AND PHOSPHORYLATION AT
TYR-216 AND TYR-224.
PubMed=12573241; DOI=10.1016/S1570-9639(02)00524-1;
Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A.,
Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.;
"Identification of phosphorylation sites within the SH3 domains of Tec
family tyrosine kinases.";
Biochim. Biophys. Acta 1645:123-132(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 536-599.
TISSUE=Blood;
Fuortes M.;
Thesis (1994), Cornell University, United States.
[8]
PHOSPHORYLATION AT TYR-566, MUTAGENESIS OF TYR-566, FUNCTION, AND
INTERACTION WITH STAT3.
PubMed=10688651; DOI=10.1128/MCB.20.6.2043-2054.2000;
Tsai Y.T., Su Y.H., Fang S.S., Huang T.N., Qiu Y., Jou Y.S.,
Shih H.M., Kung H.J., Chen R.H.;
"Etk, a Btk family tyrosine kinase, mediates cellular transformation
by linking Src to STAT3 activation.";
Mol. Cell. Biol. 20:2043-2054(2000).
[9]
INDUCTION, INTERACTION WITH PTK2/FAK1, ACTIVITY REGULATION, AND
FUNCTION.
PubMed=11331870; DOI=10.1038/35074500;
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H.,
Shimizu Y., Qiu Y.;
"Regulation of the PH-domain-containing tyrosine kinase Etk by focal
adhesion kinase through the FERM domain.";
Nat. Cell Biol. 3:439-444(2001).
[10]
DOMAIN, AND INTERACTION WITH CAV1.
PubMed=11751885; DOI=10.1074/jbc.M108537200;
Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T.,
Smith C.I., Mohamed A.J.;
"Functional interaction of caveolin-1 with Bruton's tyrosine kinase
and Bmx.";
J. Biol. Chem. 277:9351-9357(2002).
[11]
INTERACTION WITH RUFY1 AND RUFY2.
PubMed=11877430; DOI=10.1074/jbc.M111933200;
Yang J., Kim O., Wu J., Qiu Y.;
"Interaction between tyrosine kinase Etk and a RUN-domain and FYVE-
domain containing protein RUFY1. A possible role of Etk in regulation
of vesicle trafficking.";
J. Biol. Chem. 277:30219-30226(2002).
[12]
ACTIVITY REGULATION, PHOSPHORYLATION, FUNCTION, AND INTERACTION WITH
TNFRSF1B.
PubMed=12370298; DOI=10.1128/MCB.22.21.7512-7523.2002;
Pan S., An P., Zhang R., He X., Yin G., Min W.;
"Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase:
role in endothelial cell migration and angiogenesis.";
Mol. Cell. Biol. 22:7512-7523(2002).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BCAR1.
PubMed=12832404; DOI=10.1074/jbc.M306438200;
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.;
"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the
actin cytoskeleton and cell migration.";
J. Biol. Chem. 278:35636-35643(2003).
[14]
FUNCTION.
PubMed=15788485; DOI=10.1152/ajpcell.00410.2004;
Chau C.H., Clavijo C.A., Deng H.T., Zhang Q., Kim K.J., Qiu Y.,
Le A.D., Ann D.K.;
"Etk/Bmx mediates expression of stress-induced adaptive genes VEGF,
PAI-1, and iNOS via multiple signaling cascades in different cell
systems.";
Am. J. Physiol. 289:C444-C454(2005).
[15]
PHOSPHORYLATION, ACTIVITY REGULATION, FUNCTION, AND INTERACTION WITH
MYD88; PTK2/FAK1 AND TIRAP.
PubMed=18292575; DOI=10.4049/jimmunol.180.5.3485;
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.;
"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the
cross-talk between MyD88 and FAK pathways.";
J. Immunol. 180:3485-3491(2008).
[16]
REVIEW ON FUNCTION.
PubMed=11114746; DOI=10.1038/sj.onc.1203958;
Qiu Y., Kung H.J.;
"Signaling network of the Btk family kinases.";
Oncogene 19:5651-5661(2000).
[17]
REVIEW ON FUNCTION.
PubMed=11340625; DOI=10.1002/bies.1062;
Smith C.I., Islam T.C., Mattsson P.T., Mohamed A.J., Nore B.F.,
Vihinen M.;
"The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx,
Itk, Tec, Txk and homologs in other species.";
Bioessays 23:436-446(2001).
[18]
REVIEW ON FUNCTION.
PubMed=17624943; DOI=10.1111/j.1600-065X.2007.00534.x;
Gomez-Rodriguez J., Readinger J.A., Viorritto I.C., Mueller K.L.,
Houghtling R.A., Schwartzberg P.L.;
"Tec kinases, actin, and cell adhesion.";
Immunol. Rev. 218:45-64(2007).
[19]
STRUCTURE BY NMR OF 112-393.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the human BMX SH2 domain and of the BTK motif
of human cytoplasmic tyrosine-protein kinase BMX.";
Submitted (OCT-2007) to the PDB data bank.
[20]
STRUCTURE BY NMR OF 291-393.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the human bmx SH2 domain.";
Submitted (FEB-2009) to the PDB data bank.
[21]
VARIANTS [LARGE SCALE ANALYSIS] LEU-284 AND TRP-670.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor tyrosine kinase that plays central but
diverse modulatory roles in various signaling processes involved
in the regulation of actin reorganization, cell migration, cell
proliferation and survival, cell adhesion, and apoptosis.
Participates in signal transduction stimulated by growth factor
receptors, cytokine receptors, G-protein coupled receptors,
antigen receptors and integrins. Induces tyrosine phosphorylation
of BCAR1 in response to integrin regulation. Activation of BMX by
integrins is mediated by PTK2/FAK1, a key mediator of integrin
signaling events leading to the regulation of actin cytoskeleton
and cell motility. Plays a critical role in TNF-induced
angiogenesis, and implicated in the signaling of TEK and FLT1
receptors, 2 important receptor families essential for
angiogenesis. Required for the phosphorylation and activation of
STAT3, a transcription factor involved in cell differentiation.
Also involved in interleukin-6 (IL6) induced differentiation.
Plays also a role in programming adaptive cytoprotection against
extracellular stress in different cell systems, salivary
epithelial cells, brain endothelial cells, and dermal fibroblasts.
May be involved in regulation of endocytosis through its
interaction with an endosomal protein RUFY1. May also play a role
in the growth and differentiation of hematopoietic cells; as well
as in signal transduction in endocardial and arterial endothelial
cells. {ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11331870,
ECO:0000269|PubMed:12370298, ECO:0000269|PubMed:12832404,
ECO:0000269|PubMed:15788485, ECO:0000269|PubMed:18292575,
ECO:0000269|PubMed:9520419}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: TEK and vascular endothelial growth factor
receptor 1 (FLT1) stimulate BMX tyrosine kinase activity (By
similarity). Activated by integrins through the mediation of
PTK2/FAK1. Activated by TNF through the mediation of TNFRSF1B.
{ECO:0000250, ECO:0000269|PubMed:11331870,
ECO:0000269|PubMed:12370298, ECO:0000269|PubMed:18292575}.
-!- SUBUNIT: Interacts with BCAR1, CAV1, MYD88, PTK2/FAK1, RUFY1,
RUFY2, STAT3, TIRAP and TNFRSF1B. {ECO:0000269|PubMed:10688651,
ECO:0000269|PubMed:11331870, ECO:0000269|PubMed:11751885,
ECO:0000269|PubMed:11877430, ECO:0000269|PubMed:12370298,
ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:18292575}.
-!- INTERACTION:
P11309:PIM1; NbExp=4; IntAct=EBI-696657, EBI-696621;
P40763:STAT3; NbExp=6; IntAct=EBI-696657, EBI-518675;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12832404}.
Note=Localizes to the edges of spreading cells when complexed with
BCAR1.
-!- TISSUE SPECIFICITY: Highly expressed in cells with great migratory
potential, including endothelial cells and metastatic carcinoma
cell lines.
-!- INDUCTION: Activated by IL6/interleukin-6 through
phosphatidylinositol 3-kinase (PI3-kinase) pathway. It is likely
that activation occurs through binding of phosphoinositides to the
PH domain. {ECO:0000269|PubMed:11331870,
ECO:0000269|PubMed:9520419}.
-!- DOMAIN: SH2 domain mediates interaction with RUFY1.
{ECO:0000269|PubMed:11751885}.
-!- PTM: Phosphorylated in response to protein I/II and to LPS.
Phosphorylation at Tyr-566 by SRC and by autocatalysis leads to
activation and is required for STAT3 phosphorylation by BMX.
{ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12370298,
ECO:0000269|PubMed:12573241, ECO:0000269|PubMed:18292575}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAC08966.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X83107; CAA58169.1; -; mRNA.
EMBL; AF045459; AAC08966.1; ALT_INIT; mRNA.
EMBL; AC097625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471074; EAW98889.1; -; Genomic_DNA.
EMBL; BC016652; AAH16652.1; -; mRNA.
EMBL; U08341; AAA17744.1; -; mRNA.
CCDS; CCDS14168.1; -.
PIR; S60612; S60612.
RefSeq; NP_001307795.1; NM_001320866.1.
RefSeq; NP_001712.1; NM_001721.6.
RefSeq; NP_975010.1; NM_203281.2.
UniGene; Hs.495731; -.
PDB; 2EKX; NMR; -; A=291-393.
PDB; 2YS2; NMR; -; A=113-149.
PDB; 3SXR; X-ray; 2.40 A; A/B=411-675.
PDB; 3SXS; X-ray; 1.89 A; A=411-675.
PDBsum; 2EKX; -.
PDBsum; 2YS2; -.
PDBsum; 3SXR; -.
PDBsum; 3SXS; -.
ProteinModelPortal; P51813; -.
SMR; P51813; -.
BioGrid; 107128; 27.
IntAct; P51813; 13.
MINT; P51813; -.
STRING; 9606.ENSP00000308774; -.
BindingDB; P51813; -.
ChEMBL; CHEMBL3834; -.
GuidetoPHARMACOLOGY; 1942; -.
iPTMnet; P51813; -.
PhosphoSitePlus; P51813; -.
BioMuta; BMX; -.
DMDM; 1705489; -.
EPD; P51813; -.
MaxQB; P51813; -.
PaxDb; P51813; -.
PeptideAtlas; P51813; -.
PRIDE; P51813; -.
ProteomicsDB; 56409; -.
DNASU; 660; -.
Ensembl; ENST00000342014; ENSP00000340082; ENSG00000102010.
Ensembl; ENST00000348343; ENSP00000308774; ENSG00000102010.
Ensembl; ENST00000357607; ENSP00000350224; ENSG00000102010.
GeneID; 660; -.
KEGG; hsa:660; -.
UCSC; uc004cww.3; human.
CTD; 660; -.
DisGeNET; 660; -.
EuPathDB; HostDB:ENSG00000102010.14; -.
GeneCards; BMX; -.
HGNC; HGNC:1079; BMX.
HPA; CAB032495; -.
HPA; HPA001048; -.
MIM; 300101; gene.
neXtProt; NX_P51813; -.
OpenTargets; ENSG00000102010; -.
PharmGKB; PA25389; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000161172; -.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; P51813; -.
KO; K08896; -.
OMA; ISWGFPE; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P51813; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
SignaLink; P51813; -.
SIGNOR; P51813; -.
ChiTaRS; BMX; human.
EvolutionaryTrace; P51813; -.
GeneWiki; BMX_(gene); -.
GenomeRNAi; 660; -.
PMAP-CutDB; P51813; -.
PRO; PR:P51813; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102010; Expressed in 109 organ(s), highest expression level in corpus epididymis.
CleanEx; HS_BMX; -.
Genevisible; P51813; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
CDD; cd10399; SH2_Tec_Bmx; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR028840; BMX.
InterPro; IPR035875; BMX_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001562; Znf_Btk_motif.
PANTHER; PTHR24418:SF91; PTHR24418:SF91; 2.
Pfam; PF00779; BTK; 1.
Pfam; PF00169; PH; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00402; TECBTKDOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00107; BTK; 1.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS51113; ZF_BTK; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; ATP-binding; Cell adhesion;
Complete proteome; Cytoplasm; Direct protein sequencing; Kinase;
Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; SH2 domain; Stress response; Transferase;
Tyrosine-protein kinase; Zinc; Zinc-finger.
CHAIN 1 675 Cytoplasmic tyrosine-protein kinase BMX.
/FTId=PRO_0000088063.
DOMAIN 4 111 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 296 392 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 417 675 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 113 149 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
NP_BIND 423 431 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 596 603 CAV1-binding.
COMPBIAS 251 255 Poly-Ser.
COMPBIAS 282 285 Poly-Ser.
COMPBIAS 286 289 Poly-Glu.
ACT_SITE 536 536 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 132 132 Zinc. {ECO:0000250}.
METAL 133 133 Zinc. {ECO:0000250}.
METAL 143 143 Zinc. {ECO:0000250}.
BINDING 445 445 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 216 216 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12573241}.
MOD_RES 224 224 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12573241}.
MOD_RES 566 566 Phosphotyrosine; by SRC and
autocatalysis.
{ECO:0000269|PubMed:10688651}.
VARIANT 284 284 S -> L (in dbSNP:rs35353387).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041674.
VARIANT 670 670 R -> W (in a lung large cell carcinoma
sample; somatic mutation;
dbSNP:rs1029888196).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041675.
MUTAGEN 566 566 Y->F: Abolishes almost completely the
SRC-induced phosphorylation of BMX.
{ECO:0000269|PubMed:10688651}.
CONFLICT 207 207 P -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 597 597 A -> S (in Ref. 7; AAA17744).
{ECO:0000305}.
STRAND 129 133 {ECO:0000244|PDB:2YS2}.
STRAND 136 139 {ECO:0000244|PDB:2YS2}.
STRAND 294 297 {ECO:0000244|PDB:2EKX}.
HELIX 303 312 {ECO:0000244|PDB:2EKX}.
STRAND 318 323 {ECO:0000244|PDB:2EKX}.
STRAND 330 334 {ECO:0000244|PDB:2EKX}.
STRAND 347 350 {ECO:0000244|PDB:2EKX}.
STRAND 359 362 {ECO:0000244|PDB:2EKX}.
HELIX 370 379 {ECO:0000244|PDB:2EKX}.
STRAND 383 385 {ECO:0000244|PDB:2EKX}.
HELIX 414 416 {ECO:0000244|PDB:3SXS}.
STRAND 417 426 {ECO:0000244|PDB:3SXS}.
STRAND 429 436 {ECO:0000244|PDB:3SXS}.
TURN 437 439 {ECO:0000244|PDB:3SXS}.
STRAND 440 447 {ECO:0000244|PDB:3SXS}.
HELIX 454 466 {ECO:0000244|PDB:3SXS}.
STRAND 475 479 {ECO:0000244|PDB:3SXS}.
STRAND 481 490 {ECO:0000244|PDB:3SXS}.
HELIX 497 504 {ECO:0000244|PDB:3SXS}.
HELIX 505 507 {ECO:0000244|PDB:3SXS}.
HELIX 510 529 {ECO:0000244|PDB:3SXS}.
STRAND 532 536 {ECO:0000244|PDB:3SXS}.
HELIX 539 541 {ECO:0000244|PDB:3SXS}.
STRAND 542 544 {ECO:0000244|PDB:3SXS}.
STRAND 550 552 {ECO:0000244|PDB:3SXS}.
TURN 555 557 {ECO:0000244|PDB:3SXR}.
STRAND 558 560 {ECO:0000244|PDB:3SXS}.
STRAND 566 568 {ECO:0000244|PDB:3SXS}.
HELIX 576 578 {ECO:0000244|PDB:3SXS}.
HELIX 581 586 {ECO:0000244|PDB:3SXS}.
STRAND 587 590 {ECO:0000244|PDB:3SXS}.
HELIX 593 606 {ECO:0000244|PDB:3SXS}.
TURN 607 609 {ECO:0000244|PDB:3SXS}.
TURN 612 615 {ECO:0000244|PDB:3SXS}.
HELIX 618 626 {ECO:0000244|PDB:3SXS}.
HELIX 639 647 {ECO:0000244|PDB:3SXS}.
HELIX 653 655 {ECO:0000244|PDB:3SXS}.
HELIX 659 666 {ECO:0000244|PDB:3SXS}.
HELIX 667 669 {ECO:0000244|PDB:3SXS}.
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


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