SubmitCancel

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.

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi121 – 1211Zinc By similarity
Metal bindingi132 – 1321Zinc By similarity
Metal bindingi133 – 1331Zinc By similarity
Metal bindingi143 – 1431Zinc By similarity
Binding sitei445 – 4451ATP By similarity
Active sitei536 – 5361Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 14937Btk-typeAdd
BLAST
Nucleotide bindingi423 – 4319ATP By similarity

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 binding Source: UniProtKB
  5. protein tyrosine kinase activity Source: ProtInc
  6. 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
Note: Localizes to the edges of spreading cells when complexed with BCAR1.1 Publication

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.4 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. 7 interactions.
MINTiMINT-1433284.
STRINGi9606.ENSP00000308774.

Structurei

Secondary structure

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

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.

Miscellaneous databases

EvolutionaryTraceiP51813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 111108PHAdd
BLAST
Domaini296 – 39297SH2Add
BLAST
Domaini417 – 675259Protein kinaseAdd
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

Contains 1 PH domain.
Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
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

MDTKSILEEL LLKRSQQKKK MSPNNYKERL FVLTKTNLSY YEYDKMKRGS    50
RKGSIEIKKI RCVEKVNLEE QTPVERQYPF QIVYKDGLLY VYASNEESRS 100
QWLKALQKEI RGNPHLLVKY HSGFFVDGKF LCCQQSCKAA PGCTLWEAYA 150
NLHTAVNEEK HRVPTFPDRV LKIPRAVPVL KMDAPSSSTT LAQYDNESKK 200
NYGSQPPSSS TSLAQYDSNS KKIYGSQPNF NMQYIPREDF PDWWQVRKLK 250
SSSSSEDVAS SNQKERNVNH TTSKISWEFP ESSSSEEEEN LDDYDWFAGN 300
ISRSQSEQLL RQKGKEGAFM VRNSSQVGMY TVSLFSKAVN DKKGTVKHYH 350
VHTNAENKLY LAENYCFDSI PKLIHYHQHN SAGMITRLRH PVSTKANKVP 400
DSVSLGNGIW ELKREEITLL KELGSGQFGV VQLGKWKGQY DVAVKMIKEG 450
SMSEDEFFQE AQTMMKLSHP KLVKFYGVCS KEYPIYIVTE YISNGCLLNY 500
LRSHGKGLEP SQLLEMCYDV CEGMAFLESH QFIHRDLAAR NCLVDRDLCV 550
KVSDFGMTRY VLDDQYVSSV GTKFPVKWSA PEVFHYFKYS SKSDVWAFGI 600
LMWEVFSLGK QPYDLYDNSQ VVLKVSQGHR LYRPHLASDT IYQIMYSCWH 650
ELPEKRPTFQ QLLSSIEPLR EKDKH 675
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.

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 conflict

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

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. 7 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.
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: September 3, 2014
This is version 152 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

Similar proteinsi