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Protein

Tyrosine-protein kinase Blk

Gene

Blk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 receptor FCGR2. 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.9 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulationi

Antibody-mediated surface engagement of the B-cell antigen receptor (BCR) which results in the phosphorylation of BLK on tyrosine residues, stimulates the enzymatic activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei263 – 2631ATPPROSITE-ProRule annotation
Active sitei354 – 3541Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi241 – 2499ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_271639. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Blk (EC:2.7.10.2)
Alternative name(s):
B lymphocyte kinase
p55-Blk
Gene namesi
Name:Blk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:88169. Blk.

Subcellular locationi

  • Cell membrane By similarity; Lipid-anchor By similarity

  • Note: Present and active in lipid rafts (By similarity). Membrane location is required for the phosphorylation of CD79A and CD79B.By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451R → K: Impairs the interaction with CD79A and CD79B. 1 Publication
Mutagenesisi495 – 4951Y → F: Leads to constitutive activation of BLK. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 499498Tyrosine-protein kinase BlkPRO_0000088062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei383 – 3831Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues after antibody-mediated surface engagement of the B-cell antigen receptor (BCR).
Ubiquitination of activated BLK by the UBE3A ubiquitin protein ligase leads to its degradation by the ubiquitin-proteasome pathway.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP16277.
PaxDbiP16277.
PRIDEiP16277.

PTM databases

PhosphoSiteiP16277.

Expressioni

Tissue specificityi

Specifically expressed in the B-cell lineage.2 Publications

Inductioni

Expression increases during B-cell differentiation and is under the control of the B-cell specific transcription factors PAX5 and NF-kappa-B.3 Publications

Gene expression databases

BgeeiP16277.
CleanExiMM_BLK.
GenevisibleiP16277. MM.

Interactioni

Subunit structurei

Interacts with CBL (via SH2 domain) (By similarity). Interacts with CD79A and CD79B (via SH2 domain).By similarity2 Publications

Protein-protein interaction databases

IntActiP16277. 3 interactions.
STRINGi10090.ENSMUSP00000014597.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi116 – 1194Combined sources
Helixi125 – 1328Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi160 – 1623Combined sources
Turni163 – 1653Combined sources
Beta strandi171 – 1766Combined sources
Turni177 – 1793Combined sources
Beta strandi180 – 1845Combined sources
Beta strandi187 – 1915Combined sources
Helixi192 – 20110Combined sources
Beta strandi204 – 2085Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLJNMR-A107-218[»]
1BLKNMR-A107-218[»]
ProteinModelPortaliP16277.
SMRiP16277. Positions 57-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16277.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 11261SH3PROSITE-ProRule annotationAdd
BLAST
Domaini118 – 21497SH2PROSITE-ProRule annotationAdd
BLAST
Domaini235 – 488254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP16277.
KOiK08890.
OMAiQMNSIHR.
OrthoDBiEOG7GTT2V.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLSSKRQV SEKGKGWSPV KIRTQDKAPP PLPPLVVFNH LAPPSPNQDP
60 70 80 90 100
DEEERFVVAL FDYAAVNDRD LQVLKGEKLQ VLRSTGDWWL ARSLVTGREG
110 120 130 140 150
YVPSNFVAPV ETLEVEKWFF RTISRKDAER QLLAPMNKAG SFLIRESESN
160 170 180 190 200
KGAFSLSVKD ITTQGEVVKH YKIRSLDNGG YYISPRITFP TLQALVQHYS
210 220 230 240 250
KKGDGLCQKL TLPCVNLAPK NLWAQDEWEI PRQSLKLVRK LGSGQFGEVW
260 270 280 290 300
MGYYKNNMKV AIKTLKEGTM SPEAFLGEAN VMKTLQHERL VRLYAVVTRE
310 320 330 340 350
PIYIVTEYMA RGCLLDFLKT DEGSRLSLPR LIDMSAQVAE GMAYIERMNS
360 370 380 390 400
IHRDLRAANI LVSETLCCKI ADFGLARIID SEYTAQEGAK FPIKWTAPEA
410 420 430 440 450
IHFGVFTIKA DVWSFGVLLM EIVTYGRVPY PGMSNPEVIR SLEHGYRMPC
460 470 480 490
PETCPPELYN DIITECWRGR PEERPTFEFL QSVLEDFYTA TEGQYELQP
Length:499
Mass (Da):56,674
Last modified:July 27, 2011 - v4
Checksum:i14C607564BB4E66D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti421 – 4211E → V in AAA40453 (PubMed:2404338).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30903 mRNA. Translation: AAA40453.1.
AK089888 mRNA. Translation: BAC40986.1.
CT010240 mRNA. Translation: CAJ18448.1.
AC090496 Genomic DNA. No translation available.
BC030668 mRNA. Translation: AAH30668.1.
CCDSiCCDS27200.1.
PIRiA40092.
RefSeqiNP_031575.2. NM_007549.2.
UniGeneiMm.3962.

Genome annotation databases

EnsembliENSMUST00000014597; ENSMUSP00000014597; ENSMUSG00000014453.
GeneIDi12143.
KEGGimmu:12143.
UCSCiuc007uhq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30903 mRNA. Translation: AAA40453.1.
AK089888 mRNA. Translation: BAC40986.1.
CT010240 mRNA. Translation: CAJ18448.1.
AC090496 Genomic DNA. No translation available.
BC030668 mRNA. Translation: AAH30668.1.
CCDSiCCDS27200.1.
PIRiA40092.
RefSeqiNP_031575.2. NM_007549.2.
UniGeneiMm.3962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLJNMR-A107-218[»]
1BLKNMR-A107-218[»]
ProteinModelPortaliP16277.
SMRiP16277. Positions 57-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16277. 3 interactions.
STRINGi10090.ENSMUSP00000014597.

Chemistry

BindingDBiP16277.
ChEMBLiCHEMBL3343.

PTM databases

PhosphoSiteiP16277.

Proteomic databases

MaxQBiP16277.
PaxDbiP16277.
PRIDEiP16277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014597; ENSMUSP00000014597; ENSMUSG00000014453.
GeneIDi12143.
KEGGimmu:12143.
UCSCiuc007uhq.1. mouse.

Organism-specific databases

CTDi640.
MGIiMGI:88169. Blk.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP16277.
KOiK08890.
OMAiQMNSIHR.
OrthoDBiEOG7GTT2V.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_271639. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP16277.
NextBioi280469.
PROiP16277.
SOURCEiSearch...

Gene expression databases

BgeeiP16277.
CleanExiMM_BLK.
GenevisibleiP16277. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Specific expression of a tyrosine kinase gene, blk, in B lymphoid cells."
    Dymecki S.M., Niederhuber J.E., Desiderio S.V.
    Science 247:332-336(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: B-cell.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  6. "Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases."
    Burkhardt A.L., Brunswick M., Bolen J.B., Mond J.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:7410-7414(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. "Structure and developmental regulation of the B-lymphoid tyrosine kinase gene blk."
    Dymecki S.M., Zwollo P., Zeller K., Kuhajda F.P., Desiderio S.V.
    J. Biol. Chem. 267:4815-4823(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple src family protein tyrosine kinases."
    Lin J., Justement L.B.
    J. Immunol. 149:1548-1555(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD79A AND CD79B.
  9. "Antisense oligodeoxynucleotides to the blk tyrosine kinase prevent anti-mu-chain-mediated growth inhibition and apoptosis in a B-cell lymphoma."
    Yao X.R., Scott D.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:7946-7950(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Specific recognition of the blk promoter by the B-lymphoid transcription factor B-cell-specific activator protein."
    Zwollo P., Desiderio S.
    J. Biol. Chem. 269:15310-15317(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PAX5.
  11. "Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement."
    Saouaf S.J., Mahajan S., Rowley R.B., Kut S.A., Fargnoli J., Burkhardt A.L., Tsukada S., Witte O.N., Bolen J.B.
    Proc. Natl. Acad. Sci. U.S.A. 91:9524-9528(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. "Differential expression of the blk and ret tyrosine kinases during B lineage development is dependent on Ig rearrangement."
    Wasserman R., Li Y.S., Hardy R.R.
    J. Immunol. 155:644-651(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  13. "Reconstitution of the B cell antigen receptor signaling components in COS cells."
    Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S.
    J. Biol. Chem. 270:27072-27078(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CD79A AND CD79B, INTERACTION WITH CD79A AND CD79B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-145.
  14. "Src family protein tyrosine kinases induce autoactivation of Bruton's tyrosine kinase."
    Mahajan S., Fargnoli J., Burkhardt A.L., Kut S.A., Saouaf S.J., Bolen J.B.
    Mol. Cell. Biol. 15:5304-5311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF BTK ACTIVITY.
  15. "Palmitylation of Src family tyrosine kinases regulates functional interaction with a B cell substrate."
    Saouaf S.J., Wolven A., Resh M.D., Bolen J.B.
    Biochem. Biophys. Res. Commun. 234:325-329(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CD79A.
  16. "The transcription factor NF-kappaB/p50 interacts with the blk gene during B cell activation."
    Zwollo P., Rao S., Wallin J.J., Gackstetter E.R., Koshland M.E.
    J. Biol. Chem. 273:18647-18655(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  17. "Malignant transformation of early lymphoid progenitors in mice expressing an activated Blk tyrosine kinase."
    Malek S.N., Dordai D.I., Reim J., Dintzis H., Desiderio S.
    Proc. Natl. Acad. Sci. U.S.A. 95:7351-7356(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-495.
  18. "Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination."
    Oda H., Kumar S., Howley P.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:9557-9562(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  19. "Mimicry of pre-B-cell receptor signaling by activation of the tyrosine kinase Blk."
    Tretter T., Ross A.E., Dordai D.I., Desiderio S.
    J. Exp. Med. 198:1863-1873(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-495.
  20. "Essential role of Src-family protein tyrosine kinases in NF-kappaB activation during B cell development."
    Saijo K., Schmedt C., Su I.H., Karasuyama H., Lowell C.A., Reth M., Adachi T., Patke A., Santana A., Tarakhovsky A.
    Nat. Immunol. 4:274-279(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "The three-dimensional solution structure of the SH2 domain from p55blk kinase."
    Metzler W.J., Leiting B., Pryor K., Mueller L., Farmer B.T. II
    Biochemistry 35:6201-6211(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.

Entry informationi

Entry nameiBLK_MOUSE
AccessioniPrimary (citable) accession number: P16277
Secondary accession number(s): Q8K2M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.