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B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65)

 BLNK_MOUSE              Reviewed;         457 AA.
Q9QUN3; O88504;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=B-cell linker protein;
AltName: Full=B-cell adapter containing a SH2 domain protein;
AltName: Full=B-cell adapter containing a Src homology 2 domain protein;
AltName: Full=Cytoplasmic adapter protein;
AltName: Full=Lymphocyte antigen 57;
AltName: Full=Src homology 2 domain-containing leukocyte protein of 65 kDa;
Short=Slp-65;
Name=Blnk; Synonyms=Bash, Ly57, Slp65;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9697839; DOI=10.1016/S1074-7613(00)80591-9;
Fu C., Turck C.W., Kurosaki T., Chan A.C.;
"BLNK: a central linker protein in B cell activation.";
Immunity 9:93-103(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-20; 147-161;
170-186; 356-366 AND 393-412, FUNCTION, TISSUE SPECIFICITY,
PHOSPHORYLATION, AND INTERACTION WITH VAV1 AND GRB2.
STRAIN=BALB/cJ; TISSUE=Lymphoid tissue;
PubMed=9705962; DOI=10.1084/jem.188.4.791;
Wienands J., Schweikert J., Wollschied B., Jumaa H., Nielsen P.J.,
Reth M.;
"SLP-65: a new signaling component in B lymphocytes which requires
expression of the antigen receptor for phosphorylation.";
J. Exp. Med. 188:791-795(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Okamoto N., Hayashi K., Tsuji S., Goitsuka R., Kitamura D.;
"BASH: B lymphocyte adaptor protein containing SH2 domain.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nielsen P.J., Guenet J.-L.;
"The murine SLP-65 gene.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH CD79A, AND MUTAGENESIS OF ARG-373.
PubMed=11449366;
DOI=10.1002/1521-4141(200107)31:7<2126::AID-IMMU2126>3.0.CO;2-O;
Engels N., Wollscheid B., Wienands J.;
"Association of SLP-65/BLNK with the B cell antigen receptor through a
non-ITAM tyrosine of Ig-alpha.";
Eur. J. Immunol. 31:2126-2134(2001).
[7]
INTERACTION WITH CD79A.
PubMed=11859098; DOI=10.4049/jimmunol.168.5.2127;
Siemasko K., Skaggs B.J., Kabak S., Williamson E., Brown B.K.,
Song W., Clark M.R.;
"Receptor-facilitated antigen presentation requires the recruitment of
B cell linker protein to Igalpha.";
J. Immunol. 168:2127-2138(2002).
[8]
INTERACTION WITH CD79A.
PubMed=11909947; DOI=10.1128/MCB.22.8.2524-2535.2002;
Kabak S., Skaggs B.J., Gold M.R., Affolter M., West K.L., Foster M.S.,
Siemasko K., Chan A.C., Aebersold R., Clark M.R.;
"The direct recruitment of BLNK to immunoglobulin alpha couples the B-
cell antigen receptor to distal signaling pathways.";
Mol. Cell. Biol. 22:2524-2535(2002).
[9]
FUNCTION IN PRO-B CELL TO PRE-B CELL TRANSITION, AND MUTAGENESIS OF
TYR-52 AND TYR-96.
PubMed=12761551; DOI=10.1038/nature01608;
Jumaa H., Bossaller L., Portugal K., Storch B., Lotz M., Flemming A.,
Schrappe M., Postila V., Riikonen P., Pelkonen J., Niemeyer C.M.,
Reth M.;
"Deficiency of the adaptor SLP-65 in pre-B-cell acute lymphoblastic
leukaemia.";
Nature 423:452-456(2003).
[10]
FUNCTION IN SYK ACTIVATION, INTERACTION WITH SYK, AND MUTAGENESIS OF
ARG-373.
PubMed=18369315; DOI=10.1038/emboj.2008.62;
Kulathu Y., Hobeika E., Turchinovich G., Reth M.;
"The kinase Syk as an adaptor controlling sustained calcium signalling
and B-cell development.";
EMBO J. 27:1333-1344(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
INTERACTION WITH SCIMP.
PubMed=21930792; DOI=10.1128/MCB.05817-11;
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M.,
Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A.,
Brdicka T.;
"SCIMP, a transmembrane adapter protein involved in major
histocompatibility complex class II signaling.";
Mol. Cell. Biol. 31:4550-4562(2011).
[13]
STRUCTURE BY NMR OF 328-457.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH2 domain from mouse B-cell linker protein
BLNK.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000269|PubMed:12761551,
ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:9705962}.
-!- SUBUNIT: Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen
receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2
(By similarity). Interacts through its SH2 domain with CD79A.
Interacts (via SH2 domain) with SYK; phosphorylated and activated
by SYK. Interacts with SCIMP. {ECO:0000250,
ECO:0000269|PubMed:11449366, ECO:0000269|PubMed:11859098,
ECO:0000269|PubMed:11909947, ECO:0000269|PubMed:18369315,
ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:9705962}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=BCR activation results in the translocation to
membrane fraction. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the spleen and weakly in thymus,
no expression was seen in liver, testis, or brain. Expressed in B-
cell lines representing different developmental stages from the
pre-B to the plasma cell stage, but not in a T-cell or a
fibroblast cell line. {ECO:0000269|PubMed:9705962}.
-!- PTM: Following BCR activation, phosphorylated on tyrosine residues
by SYK and LYN. When phosphorylated, serves as a scaffold to
assemble downstream targets of antigen activation, including
PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and
Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72
facilitates VAV1 and NCK1 binding. Phosphorylation is required for
both Ca(2+) and MAPK signaling pathways (By similarity).
Phosphorylation of Tyr-96 is required for the binding of BTK.
{ECO:0000250, ECO:0000269|PubMed:9705962}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF068182; AAC40206.1; -; mRNA.
EMBL; Y17159; CAA76666.1; -; mRNA.
EMBL; AB015290; BAA34944.1; -; mRNA.
EMBL; AJ298054; CAC18565.1; -; Genomic_DNA.
EMBL; BC059785; AAH59785.1; -; mRNA.
CCDS; CCDS37983.1; -.
RefSeq; NP_032554.2; NM_008528.4.
UniGene; Mm.9749; -.
PDB; 2EO6; NMR; -; A=330-457.
PDBsum; 2EO6; -.
ProteinModelPortal; Q9QUN3; -.
SMR; Q9QUN3; -.
BioGrid; 201236; 5.
CORUM; Q9QUN3; -.
IntAct; Q9QUN3; 6.
MINT; MINT-110328; -.
STRING; 10090.ENSMUSP00000057844; -.
iPTMnet; Q9QUN3; -.
PhosphoSitePlus; Q9QUN3; -.
MaxQB; Q9QUN3; -.
PaxDb; Q9QUN3; -.
PeptideAtlas; Q9QUN3; -.
PRIDE; Q9QUN3; -.
Ensembl; ENSMUST00000054769; ENSMUSP00000057844; ENSMUSG00000061132.
GeneID; 17060; -.
KEGG; mmu:17060; -.
UCSC; uc008hll.1; mouse.
CTD; 29760; -.
MGI; MGI:96878; Blnk.
eggNOG; ENOG410IGWN; Eukaryota.
eggNOG; ENOG410XYB6; LUCA.
GeneTree; ENSGT00530000063094; -.
HOGENOM; HOG000088646; -.
HOVERGEN; HBG053147; -.
InParanoid; Q9QUN3; -.
KO; K07371; -.
OMA; DSEMYVL; -.
OrthoDB; EOG091G053I; -.
PhylomeDB; Q9QUN3; -.
TreeFam; TF326567; -.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; Q9QUN3; -.
PRO; PR:Q9QUN3; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000061132; -.
CleanEx; MM_BLNK; -.
ExpressionAtlas; Q9QUN3; baseline and differential.
Genevisible; Q9QUN3; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005070; F:SH3/SH2 adaptor activity; ISO:MGI.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF00017; SH2; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; B-cell activation; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; Membrane; Phosphoprotein;
Reference proteome; SH2 domain.
CHAIN 1 457 B-cell linker protein.
/FTId=PRO_0000064941.
DOMAIN 347 454 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COMPBIAS 130 330 Pro-rich.
MOD_RES 72 72 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:Q8WV28}.
MOD_RES 84 84 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:Q8WV28}.
MOD_RES 96 96 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:Q8WV28}.
MOD_RES 178 178 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:Q8WV28}.
MOD_RES 189 189 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:Q8WV28}.
MUTAGEN 52 52 Y->F: No effect on pre-BCR down-
regulation.
{ECO:0000269|PubMed:12761551}.
MUTAGEN 96 96 Y->F: Fails to induce pre-BCR down-
regulation, leading to splenomegaly and
leukemia. {ECO:0000269|PubMed:12761551}.
MUTAGEN 373 373 R->L: Abolishes binding to CD79A and SYK.
{ECO:0000269|PubMed:11449366,
ECO:0000269|PubMed:18369315}.
CONFLICT 333 333 S -> L (in Ref. 1; AAC40206).
{ECO:0000305}.
CONFLICT 340 340 A -> G (in Ref. 1; AAC40206).
{ECO:0000305}.
CONFLICT 356 356 S -> F (in Ref. 1; AAC40206).
{ECO:0000305}.
CONFLICT 376 376 S -> F (in Ref. 1; AAC40206).
{ECO:0000305}.
HELIX 334 340 {ECO:0000244|PDB:2EO6}.
TURN 341 344 {ECO:0000244|PDB:2EO6}.
STRAND 346 351 {ECO:0000244|PDB:2EO6}.
HELIX 354 364 {ECO:0000244|PDB:2EO6}.
STRAND 372 374 {ECO:0000244|PDB:2EO6}.
STRAND 383 390 {ECO:0000244|PDB:2EO6}.
STRAND 393 399 {ECO:0000244|PDB:2EO6}.
TURN 403 406 {ECO:0000244|PDB:2EO6}.
STRAND 410 412 {ECO:0000244|PDB:2EO6}.
STRAND 420 422 {ECO:0000244|PDB:2EO6}.
HELIX 423 432 {ECO:0000244|PDB:2EO6}.
STRAND 440 442 {ECO:0000244|PDB:2EO6}.
SEQUENCE 457 AA; 50671 MW; 66C93D4FDDF9D260 CRC64;
MDKLNKITVP ASQKLRQLQK MVHDIKNNEG GIMDKIKKLK VKGPPSVPRR DYALDSPADE
EEQWSDDFDS DYENPDEHSD SEMYVMPAEE TGDDSYEPPP AEQQTRVVHP ALPFTRGEYV
DNRSSQRHSP PFSKTLPSKP SWPSAKARLA STLPAPNSLQ KPQVPPKPKD LLEDEADYVV
PVEDNDENYI HPRESSPPPA EKAPMVNRST KPNSSSKHMS PPGTVAGRNS GVWDSKSSLP
AAPSPLPRAG KKPATPLKTT PVPPLPNASN VCEEKPVPAE RHRGSSHRQD TVQSPVFPPT
QKPVHQKPVP LPRFPEAGSP AADGPFHSFP FNSTFADQEA ELLGKPWYAG ACDRKSAEEA
LHRSNKDGSF LIRKSSGHDS KQPYTLVAFF NKRVYNIPVR FIEATKQYAL GKKKNGEEYF
GSVVEIVNSH QHNPLVLIDS QNNTKDSTRL KYAVKVS


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