Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51813

- BMX_HUMAN

UniProt

P51813 - BMX_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cytoplasmic tyrosine-protein kinase BMX

Gene

BMX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

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.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211ZincBy similarity
Metal bindingi132 – 1321ZincBy similarity
Metal bindingi133 – 1331ZincBy similarity
Metal bindingi143 – 1431ZincBy similarity
Binding sitei445 – 4451ATPPROSITE-ProRule annotation
Active sitei536 – 5361Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi423 – 4319ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. protein tyrosine kinase activity Source: ProtInc
  5. signal transducer activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. cell adhesion Source: UniProtKB-KW
  3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  4. intracellular signal transduction Source: InterPro
  5. mesoderm development Source: ProtInc
  6. peptidyl-tyrosine phosphorylation Source: GOC
  7. protein autophosphorylation Source: UniProtKB
  8. protein phosphorylation Source: ProtInc
  9. response to stress Source: UniProtKB-KW
  10. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Cell adhesion, Stress response

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
SignaLinkiP51813.

Names & Taxonomyi

Protein namesi
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 namesi
Name:BMX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:1079. BMX.

Subcellular locationi

Cytoplasm 1 Publication
Note: Localizes to the edges of spreading cells when complexed with BCAR1.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi566 – 5661Y → F: Abolishes almost completely the SRC-induced phosphorylation of BMX. 1 Publication

Organism-specific databases

PharmGKBiPA25389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 675675Cytoplasmic tyrosine-protein kinase BMXPRO_0000088063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161Phosphotyrosine; by autocatalysis1 Publication
Modified residuei224 – 2241Phosphotyrosine; by autocatalysis1 Publication
Modified residuei566 – 5661Phosphotyrosine; by SRC and autocatalysis1 Publication

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP51813.
PRIDEiP51813.

PTM databases

PhosphoSiteiP51813.

Miscellaneous databases

PMAP-CutDBP51813.

Expressioni

Tissue specificityi

Highly expressed in cells with great migratory potential, including endothelial cells and metastatic carcinoma cell lines.

Inductioni

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.2 Publications

Gene expression databases

BgeeiP51813.
CleanExiHS_BMX.
GenevestigatoriP51813.

Organism-specific databases

HPAiCAB032495.
HPA001048.

Interactioni

Subunit structurei

Interacts with BCAR1, CAV1, MYD88, PTK2/FAK1, RUFY1, RUFY2, STAT3, TIRAP and TNFRSF1B.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIM1P113094EBI-696657,EBI-696621

Protein-protein interaction databases

BioGridi107128. 28 interactions.
IntActiP51813. 8 interactions.
MINTiMINT-1433284.
STRINGi9606.ENSP00000308774.

Structurei

Secondary structure

1
675
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi129 – 1335Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi294 – 2974Combined sources
Helixi303 – 31210Combined sources
Beta strandi318 – 3236Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi347 – 3504Combined sources
Beta strandi359 – 3624Combined sources
Helixi370 – 37910Combined sources
Beta strandi383 – 3853Combined sources
Helixi414 – 4163Combined sources
Beta strandi417 – 42610Combined sources
Beta strandi429 – 4368Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 4478Combined sources
Helixi454 – 46613Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi481 – 49010Combined sources
Helixi497 – 5048Combined sources
Helixi505 – 5073Combined sources
Helixi510 – 52920Combined sources
Beta strandi532 – 5365Combined sources
Helixi539 – 5413Combined sources
Beta strandi542 – 5443Combined sources
Beta strandi550 – 5523Combined sources
Turni555 – 5573Combined sources
Beta strandi558 – 5603Combined sources
Beta strandi566 – 5683Combined sources
Helixi576 – 5783Combined sources
Helixi581 – 5866Combined sources
Beta strandi587 – 5904Combined sources
Helixi593 – 60614Combined sources
Turni607 – 6093Combined sources
Turni612 – 6154Combined sources
Helixi618 – 6269Combined sources
Helixi639 – 6479Combined sources
Helixi653 – 6553Combined sources
Helixi659 – 6668Combined sources
Helixi667 – 6693Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKXNMR-A291-393[»]
2YS2NMR-A113-149[»]
3SXRX-ray2.40A/B411-675[»]
3SXSX-ray1.89A411-675[»]
ProteinModelPortaliP51813.
SMRiP51813. Positions 6-150, 233-671.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PHPROSITE-ProRule annotationAdd
BLAST
Domaini296 – 39297SH2PROSITE-ProRule annotationAdd
BLAST
Domaini417 – 675259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi596 – 6038CAV1-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 2555Poly-Ser
Compositional biasi282 – 2854Poly-Ser
Compositional biasi286 – 2894Poly-Glu

Domaini

SH2 domain mediates interaction with RUFY1.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

SH2 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP51813.
KOiK08896.
OMAiAVNEEKH.
OrthoDBiEOG7KM5SC.
PhylomeDBiP51813.
TreeFamiTF351634.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR028840. BMX.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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]
PANTHERiPTHR24418:SF91. PTHR24418:SF91. 1 hit.
PfamiPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTiSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. 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]

Sequencei

Sequence statusi: Complete.

P51813-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDTKSILEEL LLKRSQQKKK MSPNNYKERL FVLTKTNLSY YEYDKMKRGS
60 70 80 90 100
RKGSIEIKKI RCVEKVNLEE QTPVERQYPF QIVYKDGLLY VYASNEESRS
110 120 130 140 150
QWLKALQKEI RGNPHLLVKY HSGFFVDGKF LCCQQSCKAA PGCTLWEAYA
160 170 180 190 200
NLHTAVNEEK HRVPTFPDRV LKIPRAVPVL KMDAPSSSTT LAQYDNESKK
210 220 230 240 250
NYGSQPPSSS TSLAQYDSNS KKIYGSQPNF NMQYIPREDF PDWWQVRKLK
260 270 280 290 300
SSSSSEDVAS SNQKERNVNH TTSKISWEFP ESSSSEEEEN LDDYDWFAGN
310 320 330 340 350
ISRSQSEQLL RQKGKEGAFM VRNSSQVGMY TVSLFSKAVN DKKGTVKHYH
360 370 380 390 400
VHTNAENKLY LAENYCFDSI PKLIHYHQHN SAGMITRLRH PVSTKANKVP
410 420 430 440 450
DSVSLGNGIW ELKREEITLL KELGSGQFGV VQLGKWKGQY DVAVKMIKEG
460 470 480 490 500
SMSEDEFFQE AQTMMKLSHP KLVKFYGVCS KEYPIYIVTE YISNGCLLNY
510 520 530 540 550
LRSHGKGLEP SQLLEMCYDV CEGMAFLESH QFIHRDLAAR NCLVDRDLCV
560 570 580 590 600
KVSDFGMTRY VLDDQYVSSV GTKFPVKWSA PEVFHYFKYS SKSDVWAFGI
610 620 630 640 650
LMWEVFSLGK QPYDLYDNSQ VVLKVSQGHR LYRPHLASDT IYQIMYSCWH
660 670
ELPEKRPTFQ QLLSSIEPLR EKDKH
Length:675
Mass (Da):78,011
Last modified:October 1, 1996 - v1
Checksum:iCB22382A3BD02599
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071P → G AA sequence (PubMed:12573241)Curated
Sequence conflicti597 – 5971A → S in AAA17744. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti284 – 2841S → L.1 Publication
Corresponds to variant rs35353387 [ dbSNP | Ensembl ].
VAR_041674
Natural varianti670 – 6701R → W in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_041675

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14168.1.
PIRiS60612.
RefSeqiNP_001712.1. NM_001721.6.
NP_975010.1. NM_203281.2.
UniGeneiHs.495731.

Genome annotation databases

EnsembliENST00000342014; ENSP00000340082; ENSG00000102010.
ENST00000348343; ENSP00000308774; ENSG00000102010.
ENST00000357607; ENSP00000350224; ENSG00000102010.
GeneIDi660.
KEGGihsa:660.
UCSCiuc004cww.3. human.

Polymorphism databases

DMDMi1705489.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14168.1.
PIRi S60612.
RefSeqi NP_001712.1. NM_001721.6.
NP_975010.1. NM_203281.2.
UniGenei Hs.495731.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P51813.
SMRi P51813. Positions 6-150, 233-671.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107128. 28 interactions.
IntActi P51813. 8 interactions.
MINTi MINT-1433284.
STRINGi 9606.ENSP00000308774.

Chemistry

BindingDBi P51813.
ChEMBLi CHEMBL3834.
GuidetoPHARMACOLOGYi 1942.

PTM databases

PhosphoSitei P51813.

Polymorphism databases

DMDMi 1705489.

Proteomic databases

PaxDbi P51813.
PRIDEi P51813.

Protocols and materials databases

DNASUi 660.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342014 ; ENSP00000340082 ; ENSG00000102010 .
ENST00000348343 ; ENSP00000308774 ; ENSG00000102010 .
ENST00000357607 ; ENSP00000350224 ; ENSG00000102010 .
GeneIDi 660.
KEGGi hsa:660.
UCSCi uc004cww.3. human.

Organism-specific databases

CTDi 660.
GeneCardsi GC0XP015392.
HGNCi HGNC:1079. BMX.
HPAi CAB032495.
HPA001048.
MIMi 300101. gene.
neXtProti NX_P51813.
PharmGKBi PA25389.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi P51813.
KOi K08896.
OMAi AVNEEKH.
OrthoDBi EOG7KM5SC.
PhylomeDBi P51813.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
SignaLinki P51813.

Miscellaneous databases

EvolutionaryTracei P51813.
GeneWikii BMX_(gene).
GenomeRNAii 660.
NextBioi 2684.
PMAP-CutDB P51813.
PROi P51813.
SOURCEi Search...

Gene expression databases

Bgeei P51813.
CleanExi HS_BMX.
Genevestigatori P51813.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR028840. BMX.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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 ]
PANTHERi PTHR24418:SF91. PTHR24418:SF91. 1 hit.
Pfami PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTi SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiBMX_HUMAN
AccessioniPrimary (citable) accession number: P51813
Secondary accession number(s): A6NIH9, O60564, Q12871
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3