BLNK_HUMAN - dbPTM
BLNK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLNK_HUMAN
UniProt AC Q8WV28
Protein Name B-cell linker protein
Gene Name BLNK
Organism Homo sapiens (Human).
Sequence Length 456
Subcellular Localization Cytoplasm . Cell membrane . BCR activation results in the translocation to membrane fraction.
Protein Description Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis..
Protein Sequence MDKLNKITVPASQKLRQLQKMVHDIKNNEGGIMNKIKKLKVKAPPSVPRRDYASESPADEEEQWSDDFDSDYENPDEHSDSEMYVMPAEENADDSYEPPPVEQETRPVHPALPFARGEYIDNRSSQRHSPPFSKTLPSKPSWPSEKARLTSTLPALTALQKPQVPPKPKGLLEDEADYVVPVEDNDENYIHPTESSSPPPEKAPMVNRSTKPNSSTPASPPGTASGRNSGAWETKSPPPAAPSPLPRAGKKPTTPLKTTPVASQQNASSVCEEKPIPAERHRGSSHRQEAVQSPVFPPAQKQIHQKPIPLPRFTEGGNPTVDGPLPSFSSNSTISEQEAGVLCKPWYAGACDRKSAEEALHRSNKDGSFLIRKSSGHDSKQPYTLVVFFNKRVYNIPVRFIEATKQYALGRKKNGEEYFGSVAEIIRNHQHSPLVLIDSQNNTKDSTRLKYAVKVS
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
8PhosphorylationMDKLNKITVPASQKL
CCCCCCCCCCHHHHH		23.2629083192
12PhosphorylationNKITVPASQKLRQLQ
CCCCCCHHHHHHHHH		23.0629083192
46PhosphorylationLKVKAPPSVPRRDYA
CCCCCCCCCCCCCCC		43.6329396449
72PhosphorylationSDDFDSDYENPDEHS
CCCCCCCCCCCCCCC		22.8912456653
84PhosphorylationEHSDSEMYVMPAEEN
CCCCCEEEEEECHHC		6.9112456653
96PhosphorylationEENADDSYEPPPVEQ
HHCCCCCCCCCCCCC		39.1812456653
119PhosphorylationLPFARGEYIDNRSSQ
CCCCCCCCCCCCCCC		19.1927155012
124PhosphorylationGEYIDNRSSQRHSPP
CCCCCCCCCCCCCCC		36.7628348404
125PhosphorylationEYIDNRSSQRHSPPF
CCCCCCCCCCCCCCC		28.1723403867
129PhosphorylationNRSSQRHSPPFSKTL
CCCCCCCCCCCCCCC		36.1426657352
133PhosphorylationQRHSPPFSKTLPSKP
CCCCCCCCCCCCCCC		30.4224275569
135PhosphorylationHSPPFSKTLPSKPSW
CCCCCCCCCCCCCCC		42.5828348404
138PhosphorylationPFSKTLPSKPSWPSE
CCCCCCCCCCCCCCH		61.3824719451
141PhosphorylationKTLPSKPSWPSEKAR
CCCCCCCCCCCHHHH		56.1928857561
144PhosphorylationPSKPSWPSEKARLTS
CCCCCCCCHHHHHHC		45.5328857561
150PhosphorylationPSEKARLTSTLPALT
CCHHHHHHCHHHHHH		17.7028348404
151PhosphorylationSEKARLTSTLPALTA
CHHHHHHCHHHHHHH		32.3228348404
152PhosphorylationEKARLTSTLPALTAL
HHHHHHCHHHHHHHH		31.3728348404
178PhosphorylationLLEDEADYVVPVEDN
CCCCCCCEEEECCCC		15.4712456653
189PhosphorylationVEDNDENYIHPTESS
CCCCCCCEECCCCCC		9.8816636677
193PhosphorylationDENYIHPTESSSPPP
CCCEECCCCCCCCCC		34.0428450419
195PhosphorylationNYIHPTESSSPPPEK
CEECCCCCCCCCCCC		38.3026657352
196PhosphorylationYIHPTESSSPPPEKA
EECCCCCCCCCCCCC		40.4026657352
197PhosphorylationIHPTESSSPPPEKAP
ECCCCCCCCCCCCCC		51.1828450419
206PhosphorylationPPEKAPMVNRSTKPN
CCCCCCCCCCCCCCC		5.3927251275
209PhosphorylationKAPMVNRSTKPNSST
CCCCCCCCCCCCCCC		35.2628102081
210PhosphorylationAPMVNRSTKPNSSTP
CCCCCCCCCCCCCCC		47.4828102081
214PhosphorylationNRSTKPNSSTPASPP
CCCCCCCCCCCCCCC		44.0828102081
215PhosphorylationRSTKPNSSTPASPPG
CCCCCCCCCCCCCCC		45.0824275569
216PhosphorylationSTKPNSSTPASPPGT
CCCCCCCCCCCCCCC		23.7730108239
219PhosphorylationPNSSTPASPPGTASG
CCCCCCCCCCCCCCC		32.6026657352
223PhosphorylationTPASPPGTASGRNSG
CCCCCCCCCCCCCCC		24.3528102081
225PhosphorylationASPPGTASGRNSGAW
CCCCCCCCCCCCCCC		37.8228102081
229PhosphorylationGTASGRNSGAWETKS
CCCCCCCCCCCCCCC		28.6428857561
234PhosphorylationRNSGAWETKSPPPAA
CCCCCCCCCCCCCCC		26.5630576142
236PhosphorylationSGAWETKSPPPAAPS
CCCCCCCCCCCCCCC		50.4930108239
243PhosphorylationSPPPAAPSPLPRAGK
CCCCCCCCCCCCCCC		34.0528857561
253PhosphorylationPRAGKKPTTPLKTTP
CCCCCCCCCCCCCCC		50.3428857561
254PhosphorylationRAGKKPTTPLKTTPV
CCCCCCCCCCCCCCC		34.8428857561
293PhosphorylationHRQEAVQSPVFPPAQ
HHHHHHHCCCCCHHH		19.2126657352
355PhosphorylationAGACDRKSAEEALHR
CCCCCHHHHHHHHHH		41.6328842319
405AcetylationVRFIEATKQYALGRK
HHHHHHHHHHHHCCC		48.65156781
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
72YPhosphorylationKinaseSYKP43405
Uniprot
72YPhosphorylationKinaseSYKQ15046
PhosphoELM
84YPhosphorylationKinaseSYKP43405
Uniprot
84YPhosphorylationKinaseSYKQ15046
PhosphoELM
96YPhosphorylationKinaseSYKP43405
Uniprot
96YPhosphorylationKinaseSYKQ15046
PhosphoELM
178YPhosphorylationKinaseSYKP43405
Uniprot
178YPhosphorylationKinaseSYKQ15046
PhosphoELM
189YPhosphorylationKinaseSYKP43405
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLNK_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 BLNK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCK1_HUMANNCK1physical
9697839
VAV_HUMANVAV1physical
9697839
GRB2_HUMANGRB2physical
9697839
M4K1_HUMANMAP4K1physical
11514608
SH3K1_HUMANSH3KBP1physical
11071869
GRB2_HUMANGRB2physical
11449366
CD79A_HUMANCD79Aphysical
11449366
CD79A_HUMANCD79Aphysical
11909947
GRB2_HUMANGRB2physical
10820378
BTK_HUMANBTKphysical
10498607
SH3K1_HUMANSH3KBP1physical
22262777
GRB2_HUMANGRB2physical
21822214
SH3K1_HUMANSH3KBP1physical
21822214
CD2AP_HUMANCD2APphysical
21822214
CAZA1_HUMANCAPZA1physical
21822214
CAZA2_HUMANCAPZA2physical
21822214
CAPZB_HUMANCAPZBphysical
21822214
HSP74_HUMANHSPA4physical
21822214
HS105_HUMANHSPH1physical
21822214
MYPC3_HUMANMYBPC3physical
21822214
CD79A_HUMANCD79Aphysical
21822214
CL17A_HUMANCLEC17Aphysical
21822214
DOK3_HUMANDOK3physical
21822214
NCK2_HUMANNCK2physical
21822214
TLN1_HUMANTLN1physical
21822214
LYN_HUMANLYNphysical
21822214
KSYK_HUMANSYKphysical
21822214
BTK_HUMANBTKphysical
21822214
PLCG2_HUMANPLCG2physical
21822214
VAV3_HUMANVAV3physical
21822214
MP2K4_HUMANMAP2K4physical
21822214
2ABG_HUMANPPP2R2Cphysical
21822214
AIFM1_HUMANAIFM1physical
21822214
WDR81_HUMANWDR81physical
21822214
CBL_HUMANCBLphysical
10684856
GRAP2_HUMANGRAP2physical
12176364
BTK_HUMANBTKphysical
21482705
KSYK_HUMANSYKphysical
21482705
Drug and Disease Associations
Kegg Disease
H00085 Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
OMIM Disease
613502Agammaglobulinemia 4, autosomal recessive (AGM4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLNK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"BLNK: molecular scaffolding through 'cis'-mediated organization ofsignaling proteins.";
Chiu C.W., Dalton M., Ishiai M., Kurosaki T., Chan A.C.;
EMBO J. 21:6461-6472(2002).
Cited for: PHOSPHORYLATION AT TYR-72; TYR-84; TYR-96; TYR-178 AND TYR-189 BY SYK,AND MUTAGENESIS OF TYR-72; TYR-84 AND TYR-96.

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