BLK_HUMAN - dbPTM
BLK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLK_HUMAN
UniProt AC P51451
Protein Name Tyrosine-protein kinase Blk
Gene Name BLK
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cell membrane
Lipid-anchor. Present and active in lipid rafts. Membrane location is required for the phosphorylation of CD79A and CD79B (By similarity)..
Protein Description Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207'. Phosphorylates also the immunoglobulin G receptors FCGR2A, FCGR2B and FCGR2C. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation. Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation. In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose..
Protein Sequence MGLVSSKKPDKEKPIKEKDKGQWSPLKVSAQDKDAPPLPPLVVFNHLTPPPPDEHLDEDKHFVVALYDYTAMNDRDLQMLKGEKLQVLKGTGDWWLARSLVTGREGYVPSNFVARVESLEMERWFFRSQGRKEAERQLLAPINKAGSFLIRESETNKGAFSLSVKDVTTQGELIKHYKIRCLDEGGYYISPRITFPSLQALVQHYSKKGDGLCQRLTLPCVRPAPQNPWAQDEWEIPRQSLRLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKALQHERLVRLYAVVTKEPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQIAEGMAYIERMNSIHRDLRAANILVSEALCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWSFGVLLMEVVTYGRVPYPGMSNPEVIRNLERGYRMPRPDTCPPELYRGVIAECWRSRPEERPTFEFLQSVLEDFYTATERQYELQP
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
2Myristoylation------MGLVSSKKP
------CCCCCCCCC		34.48-
5Phosphorylation---MGLVSSKKPDKE
---CCCCCCCCCCCC		41.2924505115
6Phosphorylation--MGLVSSKKPDKEK
--CCCCCCCCCCCCC		36.9024505115
16AcetylationPDKEKPIKEKDKGQW
CCCCCCCCCCCCCCC		68.2121339330
24PhosphorylationEKDKGQWSPLKVSAQ
CCCCCCCCCCCCCCC		16.6830108239
102PhosphorylationWLARSLVTGREGYVP
HHHHHHHHCCCCCCC		35.5024719451
107PhosphorylationLVTGREGYVPSNFVA
HHHCCCCCCCCCCEE		12.39-
144UbiquitinationQLLAPINKAGSFLIR
HHHHCHHHCCCEEEE		55.64-
157UbiquitinationIRESETNKGAFSLSV
EEECCCCCCCEEEEE		60.06-
161PhosphorylationETNKGAFSLSVKDVT
CCCCCCEEEEEEECC		21.1424719451
163PhosphorylationNKGAFSLSVKDVTTQ
CCCCEEEEEEECCCC		26.3920860994
165UbiquitinationGAFSLSVKDVTTQGE
CCEEEEEEECCCCCC		43.00-
175UbiquitinationTTQGELIKHYKIRCL
CCCCCEEEEEEEEEE		54.21-
187PhosphorylationRCLDEGGYYISPRIT
EEECCCCEEECCCCC		14.4220090780
188PhosphorylationCLDEGGYYISPRITF
EECCCCEEECCCCCC		9.7420090780
190PhosphorylationDEGGYYISPRITFPS
CCCCEEECCCCCCHH		7.6326074081
197PhosphorylationSPRITFPSLQALVQH
CCCCCCHHHHHHHHH		28.99-
205PhosphorylationLQALVQHYSKKGDGL
HHHHHHHHHHCCCCC		12.7019702290
206PhosphorylationQALVQHYSKKGDGLC
HHHHHHHHHCCCCCC		26.2628634298
208UbiquitinationLVQHYSKKGDGLCQR
HHHHHHHCCCCCCHH		57.18-
259PhosphorylationFGEVWMGYYKNNMKV
CCCEEEEEECCCEEE		8.6524043423
260PhosphorylationGEVWMGYYKNNMKVA
CCEEEEEECCCEEEE		11.0824043423
272UbiquitinationKVAIKTLKEGTMSPE
EEEEEHHHCCCCCHH		60.37-
305UbiquitinationRLYAVVTKEPIYIVT
HHEEEECCCCCCHHH		50.30-
309PhosphorylationVVTKEPIYIVTEYMA
EECCCCCCHHHHHHH		10.47-
314PhosphorylationPIYIVTEYMARGCLL
CCCHHHHHHHCCCHH		6.16-
325UbiquitinationGCLLDFLKTDEGSRL
CCHHHHHHCCCCCCC		54.66-
333PhosphorylationTDEGSRLSLPRLIDM
CCCCCCCCHHHHHHH		34.9124719451
341PhosphorylationLPRLIDMSAQIAEGM
HHHHHHHHHHHHHHH		17.1820873877
350PhosphorylationQIAEGMAYIERMNSI
HHHHHHHHHHHHHHH		8.4020873877
356PhosphorylationAYIERMNSIHRDLRA
HHHHHHHHHCHHHHH		15.49-
375UbiquitinationVSEALCCKIADFGLA
HHHHHHHHHHHHHHH		39.67-
387PhosphorylationGLARIIDSEYTAQEG
HHHEEECCCCCCCCC		23.3028796482
389PhosphorylationARIIDSEYTAQEGAK
HEEECCCCCCCCCCC		16.0128796482
390PhosphorylationRIIDSEYTAQEGAKF
EEECCCCCCCCCCCC		20.1528796482
396UbiquitinationYTAQEGAKFPIKWTA
CCCCCCCCCCCEECC		63.63-
494PhosphorylationQSVLEDFYTATERQY
HHHHHHHHHHHHHHH		14.0522817900
501PhosphorylationYTATERQYELQP---
HHHHHHHHCCCC---		25.4824927040
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
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLK_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 BLK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE3A_HUMANUBE3Aphysical
10449731
BCL2_HUMANBCL2physical
9525867
B2CL1_HUMANBCL2L1physical
9525867
PLCG2_HUMANPLCG2physical
8395016
CD79A_HUMANCD79Aphysical
7592958
CD79B_HUMANCD79Bphysical
7592958
SPF27_MOUSEBcas2physical
12406557
STAT3_HUMANSTAT3physical
25416956
EFS_HUMANEFSphysical
25416956
CCD33_HUMANCCDC33physical
25416956
ANR54_HUMANANKRD54physical
25852190
ATPA_HUMANATP5A1physical
25852190
ATPB_HUMANATP5Bphysical
25852190
ATPG_HUMANATP5C1physical
25852190
ATPD_HUMANATP5Dphysical
25852190
ATP5E_HUMANATP5Ephysical
25852190
AT5F1_HUMANATP5F1physical
25852190
ATP5H_HUMANATP5Hphysical
25852190
ATP5I_HUMANATP5Iphysical
25852190
ATP5J_HUMANATP5Jphysical
25852190
ATPK_HUMANATP5J2physical
25852190
ATP5L_HUMANATP5Lphysical
25852190
ATPO_HUMANATP5Ophysical
25852190
ATIF1_HUMANATPIF1physical
25852190
YBOX3_HUMANYBX3physical
25852190
MCA3_HUMANEEF1E1physical
25852190
EF2_HUMANEEF2physical
25852190
G3P_HUMANGAPDHphysical
25852190
GBG12_HUMANGNG12physical
25852190
ENPL_HUMANHSP90B1physical
25852190
PHB2_HUMANPHB2physical
25852190
SMD1_HUMANSNRPD1physical
25852190
USMG5_HUMANUSMG5physical
25852190
Drug and Disease Associations
Kegg Disease
H00410 Maturity onset diabetes of the young (MODY)
OMIM Disease
613375Maturity-onset diabetes of the young 11 (MODY11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLK_HUMAN

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Related Literatures of Post-Translational Modification

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