BLNK_HUMAN
ID BLNK_HUMAN Reviewed; 456 AA.
AC Q8WV28; O75498; O75499; Q2MD49;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=B-cell linker protein;
DE AltName: Full=B-cell adapter containing a SH2 domain protein;
DE AltName: Full=B-cell adapter containing a Src homology 2 domain protein;
DE AltName: Full=Cytoplasmic adapter protein;
DE AltName: Full=Src homology 2 domain-containing leukocyte protein of 65 kDa;
DE Short=SLP-65;
GN Name=BLNK; Synonyms=BASH, SLP65;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 7-20;
RP 140-146; 237-248; 250-257; 366-373 AND 392-405, FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH PLCG1; VAV1; GRB2 AND NCK1, ALTERNATIVE
RP SPLICING, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-72; TYR-84; TYR-96 AND
RP TYR-178.
RX PubMed=9697839; DOI=10.1016/s1074-7613(00)80591-9;
RA Fu C., Turck C.W., Kurosaki T., Chan A.C.;
RT "BLNK: a central linker protein in B cell activation.";
RL Immunity 9:93-103(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), FUNCTION IN B-CELL
RP DEVELOPMENT, AND INVOLVEMENT IN AGM4.
RX PubMed=10583958; DOI=10.1126/science.286.5446.1954;
RA Minegishi Y., Rohrer J., Coustan-Smith E., Lederman H.M., Pappu R.,
RA Campana D., Chan A.C., Conley M.E.;
RT "An essential role for BLNK in human B cell development.";
RL Science 286:1954-1957(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=16636677; DOI=10.1038/sj.onc.1209520;
RA Sprangers M., Feldhahn N., Liedtke S., Jumaa H., Siebert R., Muschen M.;
RT "SLP65 deficiency results in perpetual V(D)J recombinase activity in pre-B-
RT lymphoblastic leukemia and B-cell lymphoma cells.";
RL Oncogene 25:5180-5186(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH PLCG1; VAV1; GRB2 AND NCK1.
RX PubMed=9341187; DOI=10.1074/jbc.272.43.27362;
RA Fu C., Chan A.C.;
RT "Identification of two tyrosine phosphoproteins, pp70 and pp68, which
RT interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen
RT receptor activation.";
RL J. Biol. Chem. 272:27362-27368(1997).
RN [7]
RP PHOSPHORYLATION AT TYR-72; TYR-84; TYR-96; TYR-178 AND TYR-189 BY SYK, AND
RP MUTAGENESIS OF TYR-72; TYR-84 AND TYR-96.
RX PubMed=12456653; DOI=10.1093/emboj/cdf658;
RA Chiu C.W., Dalton M., Ishiai M., Kurosaki T., Chan A.C.;
RT "BLNK: molecular scaffolding through 'cis'-mediated organization of
RT signaling proteins.";
RL EMBO J. 21:6461-6472(2002).
RN [8]
RP FUNCTION IN PLCG1 ACTIVATION AND CALCIUM MOBILIZATION.
RX PubMed=15270728; DOI=10.1111/j.1365-2567.2004.01918.x;
RA Taguchi T., Kiyokawa N., Takenouch H., Matsui J., Tang W.-R., Nakajima H.,
RA Suzuki K., Shiozawa Y., Saito M., Katagiri Y.U., Takahashi T.,
RA Karasuyama H., Matsuo Y., Okita H., Fujimoto J.;
RT "Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx
RT induced by the pre-B-cell receptor in human pre-B cells.";
RL Immunology 112:575-582(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH GRB2.
RX PubMed=16912232; DOI=10.1182/blood-2006-02-005397;
RA Grabbe A., Wienands J.;
RT "Human SLP-65 isoforms contribute differently to activation and apoptosis
RT of B lymphocytes.";
RL Blood 108:3761-3768(2006).
RN [10]
RP INTERACTION WITH SYK.
RX PubMed=18369315; DOI=10.1038/emboj.2008.62;
RA Kulathu Y., Hobeika E., Turchinovich G., Reth M.;
RT "The kinase Syk as an adaptor controlling sustained calcium signalling and
RT B-cell development.";
RL EMBO J. 27:1333-1344(2008).
RN [11]
RP INTERACTION WITH SCIMP.
RX PubMed=21930792; DOI=10.1128/mcb.05817-11;
RA Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T.,
RA Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.;
RT "SCIMP, a transmembrane adapter protein involved in major
RT histocompatibility complex class II signaling.";
RL Mol. Cell. Biol. 31:4550-4562(2011).
CC -!- FUNCTION: Functions as a central linker protein, downstream of the B-
CC cell receptor (BCR), bridging the SYK kinase to a multitude of
CC signaling pathways and regulating biological outcomes of B-cell
CC function and development. Plays a role in the activation of ERK/EPHB2,
CC MAP kinase p38 and JNK. Modulates AP1 activation. Important for the
CC activation of NF-kappa-B and NFAT. Plays an important role in BCR-
CC mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is
CC required for trafficking of the BCR to late endosomes. However, does
CC not seem to be required for pre-BCR-mediated activation of MAP kinase
CC and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for
CC the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B
CC cell to pre-B cell transition. May play an important role in BCR-
CC induced B-cell apoptosis. {ECO:0000269|PubMed:10583958,
CC ECO:0000269|PubMed:15270728, ECO:0000269|PubMed:16912232,
CC ECO:0000269|PubMed:9697839}.
CC -!- SUBUNIT: Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen
CC receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2.
CC Interacts through its SH2 domain with CD79A. Interacts (via SH2 domain)
CC with SYK; phosphorylated and activated by SYK. Interacts (via SH2
CC domain) with SCIMP; this interaction is dependent on phosphorylation of
CC SCIMP 'Tyr-131' (PubMed:21930792). {ECO:0000269|PubMed:16912232,
CC ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21930792,
CC ECO:0000269|PubMed:9341187, ECO:0000269|PubMed:9697839}.
CC -!- INTERACTION:
CC Q8WV28; P10275: AR; NbExp=2; IntAct=EBI-2623522, EBI-608057;
CC Q8WV28; Q06187: BTK; NbExp=2; IntAct=EBI-2623522, EBI-624835;
CC Q8WV28; Q9Y5K6: CD2AP; NbExp=2; IntAct=EBI-2623522, EBI-298152;
CC Q8WV28; P62993: GRB2; NbExp=4; IntAct=EBI-2623522, EBI-401755;
CC Q8WV28; P10721: KIT; NbExp=2; IntAct=EBI-2623522, EBI-1379503;
CC Q8WV28; Q5ZMQ7: SH3KBP1; Xeno; NbExp=3; IntAct=EBI-2623522, EBI-7061433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9697839}. Cell
CC membrane {ECO:0000269|PubMed:9697839}. Note=BCR activation results in
CC the translocation to membrane fraction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WV28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WV28-2; Sequence=VSP_016178;
CC Name=3;
CC IsoId=Q8WV28-3; Sequence=VSP_045324;
CC -!- TISSUE SPECIFICITY: Expressed in B-cell lineage and fibroblast cell
CC lines (at protein level). Highest levels of expression in the spleen,
CC with lower levels in the liver, kidney, pancreas, small intestines and
CC colon.
CC -!- PTM: Following BCR activation, phosphorylated on tyrosine residues by
CC SYK and LYN. When phosphorylated, serves as a scaffold to assemble
CC downstream targets of antigen activation, including PLCG1, VAV1, GRB2
CC and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates
CC PLCG1 binding. Phosphorylation of Tyr-96 facilitates BTK binding.
CC Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding.
CC Phosphorylation is required for both Ca(2+) and MAPK signaling
CC pathways. {ECO:0000269|PubMed:12456653, ECO:0000269|PubMed:9697839}.
CC -!- DISEASE: Agammaglobulinemia 4, autosomal recessive (AGM4) [MIM:613502]:
CC A primary immunodeficiency characterized by profoundly low or absent
CC serum antibodies and low or absent circulating B-cells due to an early
CC block of B-cell development. Affected individuals develop severe
CC infections in the first years of life. {ECO:0000269|PubMed:10583958}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- WEB RESOURCE: Name=BLNKbase; Note=BLNK mutation db;
CC URL="http://structure.bmc.lu.se/idbase/BLNKbase/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BLNKID804ch10q24.html";
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DR EMBL; AF068180; AAC39936.1; -; mRNA.
DR EMBL; AF068181; AAC39937.1; -; mRNA.
DR EMBL; AF180756; AAF20382.1; -; Genomic_DNA.
DR EMBL; AF180740; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180741; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180742; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180743; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180744; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180745; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180746; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180747; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180748; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180749; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180750; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180751; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180752; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180753; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180754; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180755; AAF20382.1; JOINED; Genomic_DNA.
DR EMBL; AF180756; AAF20383.1; -; Genomic_DNA.
DR EMBL; AF180740; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180741; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180742; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180743; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180744; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180745; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180746; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180748; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180749; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180750; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180751; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180752; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180753; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180754; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AF180755; AAF20383.1; JOINED; Genomic_DNA.
DR EMBL; AM180337; CAJ55331.1; -; mRNA.
DR EMBL; AC021037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018906; AAH18906.1; -; mRNA.
DR CCDS; CCDS44464.1; -. [Q8WV28-2]
DR CCDS; CCDS58091.1; -. [Q8WV28-3]
DR CCDS; CCDS7446.1; -. [Q8WV28-1]
DR RefSeq; NP_001107566.1; NM_001114094.1. [Q8WV28-2]
DR RefSeq; NP_001245369.1; NM_001258440.1. [Q8WV28-3]
DR RefSeq; NP_037446.1; NM_013314.3. [Q8WV28-1]
DR PDB; 6YLU; X-ray; 1.88 A; B=147-158.
DR PDBsum; 6YLU; -.
DR AlphaFoldDB; Q8WV28; -.
DR SMR; Q8WV28; -.
DR BioGRID; 118894; 39.
DR CORUM; Q8WV28; -.
DR IntAct; Q8WV28; 23.
DR MINT; Q8WV28; -.
DR STRING; 9606.ENSP00000224337; -.
DR iPTMnet; Q8WV28; -.
DR PhosphoSitePlus; Q8WV28; -.
DR BioMuta; BLNK; -.
DR DMDM; 82592659; -.
DR EPD; Q8WV28; -.
DR jPOST; Q8WV28; -.
DR MassIVE; Q8WV28; -.
DR MaxQB; Q8WV28; -.
DR PaxDb; Q8WV28; -.
DR PeptideAtlas; Q8WV28; -.
DR PRIDE; Q8WV28; -.
DR ProteomicsDB; 74740; -. [Q8WV28-1]
DR ProteomicsDB; 74741; -. [Q8WV28-2]
DR Antibodypedia; 3990; 761 antibodies from 42 providers.
DR DNASU; 29760; -.
DR Ensembl; ENST00000224337.10; ENSP00000224337.6; ENSG00000095585.17. [Q8WV28-1]
DR Ensembl; ENST00000371176.6; ENSP00000360218.2; ENSG00000095585.17. [Q8WV28-2]
DR Ensembl; ENST00000413476.6; ENSP00000397487.2; ENSG00000095585.17. [Q8WV28-3]
DR GeneID; 29760; -.
DR KEGG; hsa:29760; -.
DR MANE-Select; ENST00000224337.10; ENSP00000224337.6; NM_013314.4; NP_037446.1.
DR UCSC; uc001kls.5; human. [Q8WV28-1]
DR CTD; 29760; -.
DR DisGeNET; 29760; -.
DR GeneCards; BLNK; -.
DR HGNC; HGNC:14211; BLNK.
DR HPA; ENSG00000095585; Tissue enhanced (lymphoid).
DR MalaCards; BLNK; -.
DR MIM; 604515; gene.
DR MIM; 613502; phenotype.
DR neXtProt; NX_Q8WV28; -.
DR OpenTargets; ENSG00000095585; -.
DR Orphanet; 33110; Autosomal agammaglobulinemia.
DR PharmGKB; PA25371; -.
DR VEuPathDB; HostDB:ENSG00000095585; -.
DR eggNOG; ENOG502QUXR; Eukaryota.
DR GeneTree; ENSGT00940000155715; -.
DR HOGENOM; CLU_043673_0_0_1; -.
DR InParanoid; Q8WV28; -.
DR OMA; QEADLHC; -.
DR OrthoDB; 556782at2759; -.
DR PhylomeDB; Q8WV28; -.
DR TreeFam; TF326567; -.
DR PathwayCommons; Q8WV28; -.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q8WV28; -.
DR SIGNOR; Q8WV28; -.
DR BioGRID-ORCS; 29760; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; BLNK; human.
DR GeneWiki; B-cell_linker; -.
DR GenomeRNAi; 29760; -.
DR Pharos; Q8WV28; Tbio.
DR PRO; PR:Q8WV28; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8WV28; protein.
DR Bgee; ENSG00000095585; Expressed in tongue squamous epithelium and 171 other tissues.
DR ExpressionAtlas; Q8WV28; baseline and differential.
DR Genevisible; Q8WV28; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0043274; F:phospholipase binding; IPI:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:ProtInc.
DR GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR DisProt; DP01544; -.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; B-cell activation; Cell membrane;
KW Cytoplasm; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..456
FT /note="B-cell linker protein"
FT /id="PRO_0000064940"
FT DOMAIN 346..453
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 36..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12456653"
FT MOD_RES 84
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12456653"
FT MOD_RES 96
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12456653"
FT MOD_RES 178
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12456653"
FT MOD_RES 189
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12456653"
FT VAR_SEQ 203..225
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9697839"
FT /id="VSP_016178"
FT VAR_SEQ 366..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16636677"
FT /id="VSP_045324"
FT MUTAGEN 72
FT /note="Y->F: Significant phosphorylation reduction; when
FT associated with F-84; F-96 and F-178."
FT /evidence="ECO:0000269|PubMed:12456653,
FT ECO:0000269|PubMed:9697839"
FT MUTAGEN 84
FT /note="Y->F: Significant phosphorylation reduction; when
FT associated with F-72; F-96 and F-178."
FT /evidence="ECO:0000269|PubMed:12456653,
FT ECO:0000269|PubMed:9697839"
FT MUTAGEN 96
FT /note="Y->F: Significant phosphorylation reduction; when
FT associated with F-72; F-84 and F-178."
FT /evidence="ECO:0000269|PubMed:12456653,
FT ECO:0000269|PubMed:9697839"
FT MUTAGEN 178
FT /note="Y->F: Significant phosphorylation reduction; when
FT associated with F-72; F-84 and F-96."
FT /evidence="ECO:0000269|PubMed:9697839"
FT CONFLICT 62
FT /note="E -> Q (in Ref. 5; AAH18906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50466 MW; 95F1D5485D03D397 CRC64;
MDKLNKITVP ASQKLRQLQK MVHDIKNNEG GIMNKIKKLK VKAPPSVPRR DYASESPADE
EEQWSDDFDS DYENPDEHSD SEMYVMPAEE NADDSYEPPP VEQETRPVHP ALPFARGEYI
DNRSSQRHSP PFSKTLPSKP SWPSEKARLT STLPALTALQ KPQVPPKPKG LLEDEADYVV
PVEDNDENYI HPTESSSPPP EKAPMVNRST KPNSSTPASP PGTASGRNSG AWETKSPPPA
APSPLPRAGK KPTTPLKTTP VASQQNASSV CEEKPIPAER HRGSSHRQEA VQSPVFPPAQ
KQIHQKPIPL PRFTEGGNPT VDGPLPSFSS NSTISEQEAG VLCKPWYAGA CDRKSAEEAL
HRSNKDGSFL IRKSSGHDSK QPYTLVVFFN KRVYNIPVRF IEATKQYALG RKKNGEEYFG
SVAEIIRNHQ HSPLVLIDSQ NNTKDSTRLK YAVKVS
