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P51813 (BMX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic tyrosine-protein kinase BMX

EC=2.7.10.2
Alternative name(s):
Bone marrow tyrosine kinase gene in chromosome X protein
Epithelial and endothelial tyrosine kinase
Short name=ETK
NTK38
Gene names
Name:BMX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme 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. Ref.9 Ref.12 Ref.15

Subunit structure

Interacts with BCAR1, CAV1, MYD88, PTK2/FAK1, RUFY1, RUFY2, STAT3, TIRAP and TNFRSF1B. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Cytoplasm. Note: Localizes to the edges of spreading cells when complexed with BCAR1. Ref.13

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. Ref.2 Ref.9 Ref.12 Ref.15

Domain

SH2 domain mediates interaction with RUFY1. Ref.10

Post-translational modification

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. Ref.6 Ref.8 Ref.12 Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.

Contains 1 Btk-type zinc finger.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Sequence caution

The sequence AAC08966.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
Stress response
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainSH2 domain
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

mesoderm development

Traceable author statement Ref.2. Source: ProtInc

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.8Ref.9. Source: GOC

protein autophosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

ruffle membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.8Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB

protein tyrosine kinase activity

Traceable author statement Ref.1. Source: ProtInc

signal transducer activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIM1P113094EBI-696657,EBI-696621

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675Cytoplasmic tyrosine-protein kinase BMX
PRO_0000088063

Regions

Domain4 – 111108PH
Domain296 – 39297SH2
Domain417 – 675259Protein kinase
Zinc finger113 – 14937Btk-type
Nucleotide binding423 – 4319ATP By similarity
Motif596 – 6038CAV1-binding
Compositional bias251 – 2555Poly-Ser
Compositional bias282 – 2854Poly-Ser
Compositional bias286 – 2894Poly-Glu

Sites

Active site5361Proton acceptor By similarity
Metal binding1211Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1331Zinc By similarity
Metal binding1431Zinc By similarity
Binding site4451ATP By similarity

Amino acid modifications

Modified residue2161Phosphotyrosine; by autocatalysis Ref.6
Modified residue2241Phosphotyrosine; by autocatalysis Ref.6
Modified residue5661Phosphotyrosine; by SRC and autocatalysis Ref.8

Natural variations

Natural variant2841S → L. Ref.21
Corresponds to variant rs35353387 [ dbSNP | Ensembl ].
VAR_041674
Natural variant6701R → W in a lung large cell carcinoma sample; somatic mutation. Ref.21
VAR_041675

Experimental info

Mutagenesis5661Y → F: Abolishes almost completely the SRC-induced phosphorylation of BMX. Ref.8
Sequence conflict2071P → G AA sequence Ref.6
Sequence conflict5971A → S in AAA17744. Ref.7

Secondary structure

...................................................................... 675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51813 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CB22382A3BD02599

FASTA67578,011
        10         20         30         40         50         60 
MDTKSILEEL LLKRSQQKKK MSPNNYKERL FVLTKTNLSY YEYDKMKRGS RKGSIEIKKI 

        70         80         90        100        110        120 
RCVEKVNLEE QTPVERQYPF QIVYKDGLLY VYASNEESRS QWLKALQKEI RGNPHLLVKY 

       130        140        150        160        170        180 
HSGFFVDGKF LCCQQSCKAA PGCTLWEAYA NLHTAVNEEK HRVPTFPDRV LKIPRAVPVL 

       190        200        210        220        230        240 
KMDAPSSSTT LAQYDNESKK NYGSQPPSSS TSLAQYDSNS KKIYGSQPNF NMQYIPREDF 

       250        260        270        280        290        300 
PDWWQVRKLK SSSSSEDVAS SNQKERNVNH TTSKISWEFP ESSSSEEEEN LDDYDWFAGN 

       310        320        330        340        350        360 
ISRSQSEQLL RQKGKEGAFM VRNSSQVGMY TVSLFSKAVN DKKGTVKHYH VHTNAENKLY 

       370        380        390        400        410        420 
LAENYCFDSI PKLIHYHQHN SAGMITRLRH PVSTKANKVP DSVSLGNGIW ELKREEITLL 

       430        440        450        460        470        480 
KELGSGQFGV VQLGKWKGQY DVAVKMIKEG SMSEDEFFQE AQTMMKLSHP KLVKFYGVCS 

       490        500        510        520        530        540 
KEYPIYIVTE YISNGCLLNY LRSHGKGLEP SQLLEMCYDV CEGMAFLESH QFIHRDLAAR 

       550        560        570        580        590        600 
NCLVDRDLCV KVSDFGMTRY VLDDQYVSSV GTKFPVKWSA PEVFHYFKYS SKSDVWAFGI 

       610        620        630        640        650        660 
LMWEVFSLGK QPYDLYDNSQ VVLKVSQGHR LYRPHLASDT IYQIMYSCWH ELPEKRPTFQ 

       670 
QLLSSIEPLR EKDKH 

« Hide

References

« Hide 'large scale' references
[1]"BMX, a novel nonreceptor tyrosine kinase gene of the BTK/ITK/TEC/TXK family located in chromosome Xp22.2."
Tamagnone L., Lahtinen I., Mustonen T., Virtaneva K., Francis F., Muscatelli F., Alitalo R.P., Smith C.I., Larsson C., Alitalo K.
Oncogene 9:3683-3688(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[2]"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."
Qiu Y., Robinson D., Pretlow T., Kung H.-J.
Proc. Natl. Acad. Sci. U.S.A. 95:3644-3649(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
Tissue: Prostate.
[3]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[6]"Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases."
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.
Biochim. Biophys. Acta 1645:123-132(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 207-220 AND 223-236, PHOSPHORYLATION AT TYR-216 AND TYR-224.
[7]Fuortes M.
Thesis (1994), Cornell University, United States
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 536-599.
Tissue: Blood.
[8]"Etk, a Btk family tyrosine kinase, mediates cellular transformation by linking Src to STAT3 activation."
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.
Mol. Cell. Biol. 20:2043-2054(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-566, MUTAGENESIS OF TYR-566, FUNCTION, INTERACTION WITH STAT3.
[9]"Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain."
Chen R., Kim O., Li M., Xiong X., Guan J.L., Kung H.J., Chen H., Shimizu Y., Qiu Y.
Nat. Cell Biol. 3:439-444(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, INTERACTION WITH PTK2/FAK1, ENZYME REGULATION, FUNCTION.
[10]"Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx."
Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T., Smith C.I., Mohamed A.J.
J. Biol. Chem. 277:9351-9357(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH CAV1.
[11]"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."
Yang J., Kim O., Wu J., Qiu Y.
J. Biol. Chem. 277:30219-30226(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RUFY1 AND RUFY2.
[12]"Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase: role in endothelial cell migration and angiogenesis."
Pan S., An P., Zhang R., He X., Yin G., Min W.
Mol. Cell. Biol. 22:7512-7523(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, PHOSPHORYLATION, FUNCTION, INTERACTION WITH TNFRSF1B.
[13]"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration."
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.
J. Biol. Chem. 278:35636-35643(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCAR1.
[14]"Etk/Bmx mediates expression of stress-induced adaptive genes VEGF, PAI-1, and iNOS via multiple signaling cascades in different cell systems."
Chau C.H., Clavijo C.A., Deng H.T., Zhang Q., Kim K.J., Qiu Y., Le A.D., Ann D.K.
Am. J. Physiol. 289:C444-C454(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Etk/BMX, a Btk family tyrosine kinase, and Mal contribute to the cross-talk between MyD88 and FAK pathways."
Semaan N., Alsaleh G., Gottenberg J.E., Wachsmann D., Sibilia J.
J. Immunol. 180:3485-3491(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, ENZYME REGULATION, FUNCTION, INTERACTION WITH MYD88; PTK2/FAK1 AND TIRAP.
[16]"Signaling network of the Btk family kinases."
Qiu Y., Kung H.J.
Oncogene 19:5651-5661(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[17]"The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species."
Smith C.I., Islam T.C., Mattsson P.T., Mohamed A.J., Nore B.F., Vihinen M.
Bioessays 23:436-446(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[18]"Tec kinases, actin, and cell adhesion."
Gomez-Rodriguez J., Readinger J.A., Viorritto I.C., Mueller K.L., Houghtling R.A., Schwartzberg P.L.
Immunol. Rev. 218:45-64(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[19]"Solution structure of the human BMX SH2 domain and of the BTK motif of human cytoplasmic tyrosine-protein kinase BMX."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 112-393.
[20]"Solution structure of the human bmx SH2 domain."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 291-393.
[21]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-284 AND TRP-670.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83107 mRNA. Translation: CAA58169.1.
AF045459 mRNA. Translation: AAC08966.1. Different initiation.
AC097625 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98889.1.
BC016652 mRNA. Translation: AAH16652.1.
U08341 mRNA. Translation: AAA17744.1.
CCDSCCDS14168.1.
PIRS60612.
RefSeqNP_001712.1. NM_001721.6.
NP_975010.1. NM_203281.2.
UniGeneHs.495731.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKXNMR-A291-393[»]
2YS2NMR-A113-149[»]
3SXRX-ray2.40A/B411-675[»]
3SXSX-ray1.89A411-675[»]
ProteinModelPortalP51813.
SMRP51813. Positions 6-150, 233-671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107128. 28 interactions.
IntActP51813. 7 interactions.
MINTMINT-1433284.
STRING9606.ENSP00000308774.

Chemistry

BindingDBP51813.
ChEMBLCHEMBL3834.
GuidetoPHARMACOLOGY1942.

PTM databases

PhosphoSiteP51813.

Polymorphism databases

DMDM1705489.

Proteomic databases

PaxDbP51813.
PRIDEP51813.

Protocols and materials databases

DNASU660.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342014; ENSP00000340082; ENSG00000102010.
ENST00000348343; ENSP00000308774; ENSG00000102010.
ENST00000357607; ENSP00000350224; ENSG00000102010.
GeneID660.
KEGGhsa:660.
UCSCuc004cww.3. human.

Organism-specific databases

CTD660.
GeneCardsGC0XP015392.
HGNCHGNC:1079. BMX.
HPACAB032495.
HPA001048.
MIM300101. gene.
neXtProtNX_P51813.
PharmGKBPA25389.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233859.
HOVERGENHBG008761.
InParanoidP51813.
KOK08896.
OMAAVNEEKH.
OrthoDBEOG7KM5SC.
PhylomeDBP51813.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_578. Apoptosis.
SignaLinkP51813.

Gene expression databases

BgeeP51813.
CleanExHS_BMX.
GenevestigatorP51813.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR028840. BMX.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view]
PANTHERPTHR24418:SF91. PTHR24418:SF91. 1 hit.
PfamPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51813.
GeneWikiBMX_(gene).
GenomeRNAi660.
NextBio2684.
PMAP-CutDBP51813.
PROP51813.
SOURCESearch...

Entry information

Entry nameBMX_HUMAN
AccessionPrimary (citable) accession number: P51813
Secondary accession number(s): A6NIH9, O60564, Q12871
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM