| Tag |
Content |
LipidDB ID |
LipidDB-9606-00893 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
7.98 |
Molecular Weight |
57706.5 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Tyrosine-protein kinase Blk |
Protein Synonyms/Alias |
2.7.10.2; B lymphocyte kinase; p55-Blk; |
Gene Name |
BLK |
Gene Synonyms/Alias |
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Created Date |
01-OCT-1996 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGLVSSKKP | [1] | N-Myristoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Johnson DR, Bhatnagar RS, Knoll LJ, Gordon JI. Genetic and biochemical studiesof protein N-myristoylation. Annu Rev Biochem. 1994;63:869-914. Review. PubMedPMID: 7979256.[ PMID:7979256]
|
Functional 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. |
Sequence Annotation |
Domain: 58 118 SH3.
Domain: 124 220 SH2.
Domain: 241 494 Protein kinase.
Nucleotide-binding: 247 255 ATP.
Active site: 360 360 Proton acceptor.
Binding site: 269 269 ATP.
Modified residue: 389 389 Phosphotyrosine; by autocatalysis.
|
Protein Length |
505 AA. |
Protein Sequence
(Canonical) |
MGLVSSKKPD KEKPIKEKDK GQWSPLKVSA QDKDAPPLPP LVVFNHLTPP PPDEHLDEDK 60
HFVVALYDYT AMNDRDLQML KGEKLQVLKG TGDWWLARSL VTGREGYVPS NFVARVESLE 120
MERWFFRSQG RKEAERQLLA PINKAGSFLI RESETNKGAF SLSVKDVTTQ GELIKHYKIR 180
CLDEGGYYIS PRITFPSLQA LVQHYSKKGD GLCQRLTLPC VRPAPQNPWA QDEWEIPRQS 240
LRLVRKLGSG QFGEVWMGYY KNNMKVAIKT LKEGTMSPEA FLGEANVMKA LQHERLVRLY 300
AVVTKEPIYI VTEYMARGCL LDFLKTDEGS RLSLPRLIDM SAQIAEGMAY IERMNSIHRD 360
LRAANILVSE ALCCKIADFG LARIIDSEYT AQEGAKFPIK WTAPEAIHFG VFTIKADVWS 420
FGVLLMEVVT YGRVPYPGMS NPEVIRNLER GYRMPRPDTC PPELYRGVIA ECWRSRPEER 480
PTFEFLQSVL EDFYTATERQ YELQP 505
|
FASTA
(Canonical) |
>LipidDB-9606-00893|P51451
MGLVSSKKPDKEKPIKEKDKGQWSPLKVSAQDKDAPPLPPLVVFNHLTPPPPDEHLDEDK
HFVVALYDYTAMNDRDLQMLKGEKLQVLKGTGDWWLARSLVTGREGYVPSNFVARVESLE
MERWFFRSQGRKEAERQLLAPINKAGSFLIRESETNKGAFSLSVKDVTTQGELIKHYKIR
CLDEGGYYISPRITFPSLQALVQHYSKKGDGLCQRLTLPCVRPAPQNPWAQDEWEIPRQS
LRLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKALQHERLVRLY
AVVTKEPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQIAEGMAYIERMNSIHRD
LRAANILVSEALCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWS
FGVLLMEVVTYGRVPYPGMSNPEVIRNLERGYRMPRPDTCPPELYRGVIAECWRSRPEER
PTFEFLQSVLEDFYTATERQYELQP
|
Gene Ontology |
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW GO:0005524; F:ATP binding; IEA:UniProtKB-KW GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB GO:0035556; P:intracellular signal transduction; TAS:ProtInc GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:GOC GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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