BMX_HUMAN - dbPTM
BMX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BMX_HUMAN
UniProt AC P51813
Protein Name Cytoplasmic tyrosine-protein kinase BMX
Gene Name BMX
Organism Homo sapiens (Human).
Sequence Length 675
Subcellular Localization Cytoplasm . Localizes to the edges of spreading cells when complexed with BCAR1.
Protein Description 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..
Protein Sequence MDTKSILEELLLKRSQQKKKMSPNNYKERLFVLTKTNLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRSQWLKALQKEIRGNPHLLVKYHSGFFVDGKFLCCQQSCKAAPGCTLWEAYANLHTAVNEEKHRVPTFPDRVLKIPRAVPVLKMDAPSSSTTLAQYDNESKKNYGSQPPSSSTSLAQYDSNSKKIYGSQPNFNMQYIPREDFPDWWQVRKLKSSSSSEDVASSNQKERNVNHTTSKISWEFPESSSSEEEENLDDYDWFAGNISRSQSEQLLRQKGKEGAFMVRNSSQVGMYTVSLFSKAVNDKKGTVKHYHVHTNAENKLYLAENYCFDSIPKLIHYHQHNSAGMITRLRHPVSTKANKVPDSVSLGNGIWELKREEITLLKELGSGQFGVVQLGKWKGQYDVAVKMIKEGSMSEDEFFQEAQTMMKLSHPKLVKFYGVCSKEYPIYIVTEYISNGCLLNYLRSHGKGLEPSQLLEMCYDVCEGMAFLESHQFIHRDLAARNCLVDRDLCVKVSDFGMTRYVLDDQYVSSVGTKFPVKWSAPEVFHYFKYSSKSDVWAFGILMWEVFSLGKQPYDLYDNSQVVLKVSQGHRLYRPHLASDTIYQIMYSCWHELPEKRPTFQQLLSSIEPLREKDKH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MDTKSILEEL
-----CCHHHHHHHH		25.9523898821
5Phosphorylation---MDTKSILEELLL
---CCHHHHHHHHHH		34.2023898821
22PhosphorylationSQQKKKMSPNNYKER
HHHCCCCCCCCHHHH		33.1024425749
26PhosphorylationKKMSPNNYKERLFVL
CCCCCCCHHHHEEEE		22.3624425749
34PhosphorylationKERLFVLTKTNLSYY
HHHEEEEECCCCCEE		30.4418785766
40PhosphorylationLTKTNLSYYEYDKMK
EECCCCCEECHHHCC		11.9511331870
120PhosphorylationNPHLLVKYHSGFFVD
CCCEEEEECCCEEEC		8.1723403867
122PhosphorylationHLLVKYHSGFFVDGK
CEEEEECCCEEECCE		33.9223403867
172AcetylationTFPDRVLKIPRAVPV
CCCHHHCCCCCCCCE		48.057493313
181AcetylationPRAVPVLKMDAPSSS
CCCCCEEECCCCCCC		34.667493323
186PhosphorylationVLKMDAPSSSTTLAQ
EEECCCCCCCCCHHH		38.35-
202PhosphorylationDNESKKNYGSQPPSS
CCCCCCCCCCCCCCC		27.3422210691
216PhosphorylationSSTSLAQYDSNSKKI
CCCCCEEECCCCCEE		18.7422817900
224PhosphorylationDSNSKKIYGSQPNFN
CCCCCEEECCCCCCC		21.4312573241
226PhosphorylationNSKKIYGSQPNFNMQ
CCCEEECCCCCCCCE		26.0323403867
251PhosphorylationWQVRKLKSSSSSEDV
HHHCCCCCCCCCHHH		45.9824501219
252PhosphorylationQVRKLKSSSSSEDVA
HHCCCCCCCCCHHHH		32.4323403867
253PhosphorylationVRKLKSSSSSEDVAS
HCCCCCCCCCHHHHH		45.0023403867
254PhosphorylationRKLKSSSSSEDVASS
CCCCCCCCCHHHHHC		39.4323403867
255PhosphorylationKLKSSSSSEDVASSN
CCCCCCCCHHHHHCC		39.5023403867
260PhosphorylationSSSEDVASSNQKERN
CCCHHHHHCCHHHHC		29.66-
261PhosphorylationSSEDVASSNQKERNV
CCHHHHHCCHHHHCC		33.28-
304PhosphorylationFAGNISRSQSEQLLR
HCHHCCHHHHHHHHH		31.1324501219
324PhosphorylationGAFMVRNSSQVGMYT
CCEEEECCCCCEEEE		16.1623403867
325PhosphorylationAFMVRNSSQVGMYTV
CEEEECCCCCEEEEE		32.2223403867
330PhosphorylationNSSQVGMYTVSLFSK
CCCCCEEEEEEHHHH		9.69-
336PhosphorylationMYTVSLFSKAVNDKK
EEEEEHHHHHHCCCC		25.6224719451
337AcetylationYTVSLFSKAVNDKKG
EEEEHHHHHHCCCCC		49.3630588605
343AcetylationSKAVNDKKGTVKHYH
HHHHCCCCCCEEEEE		63.7830588611
347AcetylationNDKKGTVKHYHVHTN
CCCCCCEEEEEEEEC		37.9830588617
365PhosphorylationKLYLAENYCFDSIPK
CEEEEHHHCCCCHHH		5.9922817900
394PhosphorylationRLRHPVSTKANKVPD
ECCCCCCCCCCCCCC		34.1223911959
395AcetylationLRHPVSTKANKVPDS
CCCCCCCCCCCCCCC		42.3219821499
412UbiquitinationLGNGIWELKREEITL
CCCCHHHCHHHEEHH		3.6822817900
413UbiquitinationGNGIWELKREEITLL
CCCHHHCHHHEEHHH		46.3722817900
425PhosphorylationTLLKELGSGQFGVVQ
HHHHHHCCCCCEEEE		41.88-
440PhosphorylationLGKWKGQYDVAVKMI
EECCCCCEEEEEEEH		22.51-
553PhosphorylationRDLCVKVSDFGMTRY
CCCEEEEHHCCCEEE		22.8523879269
558PhosphorylationKVSDFGMTRYVLDDQ
EEHHCCCEEEEECCC		21.1623879269
560PhosphorylationSDFGMTRYVLDDQYV
HHCCCEEEEECCCCC		9.0123879269
566PhosphorylationRYVLDDQYVSSVGTK
EEEECCCCCCCCCCC		14.8610688651
568PhosphorylationVLDDQYVSSVGTKFP
EECCCCCCCCCCCCC		17.86-
569PhosphorylationLDDQYVSSVGTKFPV
ECCCCCCCCCCCCCC		17.9623879269
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
216YPhosphorylationKinaseBMXP51813
GPS
216YPhosphorylationKinaseBTKQ06187
PSP
216YPhosphorylationKinaseITKQ08881
PSP
216YPhosphorylationKinaseTECP42680
PSP
224YPhosphorylationKinaseBMXP51813
GPS
224YPhosphorylationKinaseBTKQ06187
PhosphoELM
224YPhosphorylationKinaseTECP42680
PhosphoELM
566YPhosphorylationKinaseBMXP51813
GPS
566YPhosphorylationKinaseSRCP12931
Uniprot
566YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BMX_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BMX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN21_HUMANPTPN21physical
11013262
CAV1_HUMANCAV1physical
11751885
FAK1_HUMANPTK2physical
11331870
RUFY1_HUMANRUFY1physical
11877430
RUFY2_HUMANRUFY2physical
11877430
SRC_HUMANSRCphysical
10688651
STAT3_HUMANSTAT3physical
10688651
PAK1_HUMANPAK1physical
11382770
A4_HUMANAPPphysical
21832049
CL045_HUMANC12orf45physical
21988832
STAT3_HUMANSTAT3physical
25416956
STAT3_HUMANSTAT3physical
21516116
C2D1B_HUMANCC2D1Bphysical
28514442
UBP24_HUMANUSP24physical
28514442
ARI2_HUMANARIH2physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
PDD2L_HUMANPDCD2Lphysical
28514442
CSN8_HUMANCOPS8physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BMX_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Etk, a Btk family tyrosine kinase, mediates cellular transformationby 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).
Cited for: PHOSPHORYLATION AT TYR-566, MUTAGENESIS OF TYR-566, FUNCTION, ANDINTERACTION WITH STAT3.
"Identification of phosphorylation sites within the SH3 domains of Tecfamily 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).
Cited for: PROTEIN SEQUENCE OF 207-220 AND 223-236, AND PHOSPHORYLATION ATTYR-216 AND TYR-224.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory