P51813 (BMX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	675 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis Cell adhesion Stress response
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	SH2 domain Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 protein autophosphorylation Inferred from direct assay Ref.9. Source: UniProtKB response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome ruffle membrane Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	ATP 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 phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIM1	P11309	4	EBI-696657,EBI-696621

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 675

675

Cytoplasmic tyrosine-protein kinase BMX

PRO_0000088063

Regions

Domain

4 – 111

108

PH

Domain

296 – 392

97

SH2

Domain

417 – 675

259

Protein kinase

Zinc finger

113 – 149

37

Btk-type

Nucleotide binding

423 – 431

9

ATP By similarity

Motif

596 – 603

8

CAV1-binding

Compositional bias

251 – 255

5

Poly-Ser

Compositional bias

282 – 285

4

Poly-Ser

Compositional bias

286 – 289

4

Poly-Glu

Sites

Active site

536

1

Proton acceptor By similarity

Metal binding

121

1

Zinc By similarity

Metal binding

132

1

Zinc By similarity

Metal binding

133

1

Zinc By similarity

Metal binding

143

1

Zinc By similarity

Binding site

445

1

ATP By similarity

Amino acid modifications

Modified residue

216

1

Phosphotyrosine; by autocatalysis Ref.6

Modified residue

224

1

Phosphotyrosine; by autocatalysis Ref.6

Modified residue

566

1

Phosphotyrosine; by SRC and autocatalysis Ref.8

Natural variations

Natural variant

284

1

S → L. Ref.21
Corresponds to variant rs35353387 [ dbSNP | Ensembl ].

VAR_041674

Natural variant

670

1

R → W in a lung large cell carcinoma sample; somatic mutation. Ref.21

VAR_041675

Experimental info

Mutagenesis

566

1

Y → F: Abolishes almost completely the SRC-induced phosphorylation of BMX. Ref.8

Sequence conflict

207

1

P → G AA sequence Ref.6

Sequence conflict

597

1

A → S in AAA17744. Ref.7

Secondary structure

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675

Helix Strand Turn

Details...

Beta strand

129 – 133

5

Beta strand

136 – 139

4

Beta strand

294 – 297

4

Helix

303 – 312

10

Beta strand

318 – 323

6

Beta strand

330 – 334

5

Beta strand

347 – 350

4

Beta strand

359 – 362

4

Helix

370 – 379

10

Beta strand

383 – 385

3

Helix

414 – 416

3

Beta strand

417 – 426

10

Beta strand

429 – 436

8

Turn

437 – 439

3

Beta strand

440 – 447

8

Helix

454 – 466

13

Beta strand

475 – 479

5

Beta strand

481 – 490

10

Helix

497 – 504

8

Helix

505 – 507

3

Helix

510 – 529

20

Beta strand

532 – 536

5

Helix

539 – 541

3

Beta strand

542 – 544

3

Beta strand

550 – 552

3

Turn

555 – 557

3

Beta strand

558 – 560

3

Beta strand

566 – 568

3

Helix

576 – 578

3

Helix

581 – 586

6

Beta strand

587 – 590

4

Helix

593 – 606

14

Turn

607 – 609

3

Turn

612 – 615

4

Helix

618 – 626

9

Helix

639 – 647

9

Helix

653 – 655

3

Helix

659 – 666

8

Helix

667 – 669

3

Sequences

	Sequence		Length	Mass (Da)
	P51813 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CB22382A3BD02599	FASTA	675	78,011
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00020899.

PIR

S60612.

RefSeq

NP_001712.1. NM_001721.6.
NP_975010.1. NM_203281.2.

UniGene

Hs.495731.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EKX	NMR	-	A	291-393	[»]
2YS2	NMR	-	A	113-149	[»]
3SXR	X-ray	2.40	A/B	411-675	[»]
3SXS	X-ray	1.89	A	411-675	[»]

ProteinModelPortal

P51813.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51813. 5 interactions.

MINT

MINT-1433284.

STRING

9606.ENSP00000308774.

PTM databases

PhosphoSite

P51813.

Polymorphism databases

DMDM

1705489.

Proteomic databases

PaxDb

P51813.

PRIDE

P51813.

Protocols and materials databases

DNASU

660.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342014; ENSP00000340082; ENSG00000102010.
ENST00000348343; ENSP00000308774; ENSG00000102010.
ENST00000357607; ENSP00000350224; ENSG00000102010.

GeneID

660.

KEGG

hsa:660.

UCSC

uc004cww.3. human.

Organism-specific databases

CTD

660.

GeneCards

GC0XP015392.

HGNC

HGNC:1079. BMX.

HPA

CAB032495.
HPA001048.

MIM

300101. gene.

neXtProt

NX_P51813.

PharmGKB

PA25389.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233859.

HOVERGEN

HBG008761.

InParanoid

P51813.

KO

K08896.

OMA

SKKNYGS.

OrthoDB

EOG48WC1J.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.

Reactome

REACT_578. Apoptosis.

SignaLink

P51813.

Gene expression databases

Bgee

P51813.

CleanEx

HS_BMX.

Genevestigator

P51813.

GermOnline

ENSG00000102010. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.
3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_cat_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]

Pfam

PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.

SMART

SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50003. 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]

ProtoNet

Search...

Other

BindingDB

P51813.

ChEMBL

CHEMBL3834.

EvolutionaryTrace

P51813.

GenomeRNAi

660.

NextBio

2684.

PMAP-CutDB

P51813.

SOURCE

Search...

Entry information

Entry name

BMX_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.