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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) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65)

 BLNK_HUMAN              Reviewed;         456 AA.
Q8WV28; O75498; O75499; Q2MD49;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 2.
12-SEP-2018, entry version 141.
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=Src homology 2 domain-containing leukocyte protein of 65 kDa;
Short=SLP-65;
Name=BLNK; Synonyms=BASH, SLP65;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
7-20; 140-146; 237-248; 250-257; 366-373 AND 392-405, FUNCTION,
SUBCELLULAR LOCATION, INTERACTION WITH PLCG1; VAV1; GRB2 AND NCK1,
ALTERNATIVE SPLICING, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-72;
TYR-84; TYR-96 AND TYR-178.
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 [GENOMIC DNA] (ISOFORMS 1 AND 2), FUNCTION IN
B-CELL DEVELOPMENT, AND INVOLVEMENT IN AGM4.
PubMed=10583958; DOI=10.1126/science.286.5446.1954;
Minegishi Y., Rohrer J., Coustan-Smith E., Lederman H.M., Pappu R.,
Campana D., Chan A.C., Conley M.E.;
"An essential role for BLNK in human B cell development.";
Science 286:1954-1957(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=16636677; DOI=10.1038/sj.onc.1209520;
Sprangers M., Feldhahn N., Liedtke S., Jumaa H., Siebert R.,
Muschen M.;
"SLP65 deficiency results in perpetual V(D)J recombinase activity in
pre-B-lymphoblastic leukemia and B-cell lymphoma cells.";
Oncogene 25:5180-5186(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
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 PLCG1; VAV1; GRB2 AND NCK1.
PubMed=9341187; DOI=10.1074/jbc.272.43.27362;
Fu C., Chan A.C.;
"Identification of two tyrosine phosphoproteins, pp70 and pp68, which
interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen
receptor activation.";
J. Biol. Chem. 272:27362-27368(1997).
[7]
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.
PubMed=12456653; DOI=10.1093/emboj/cdf658;
Chiu C.W., Dalton M., Ishiai M., Kurosaki T., Chan A.C.;
"BLNK: molecular scaffolding through 'cis'-mediated organization of
signaling proteins.";
EMBO J. 21:6461-6472(2002).
[8]
FUNCTION IN PLCG1 ACTIVATION AND CALCIUM MOBILIZATION.
PubMed=15270728; DOI=10.1111/j.1365-2567.2004.01918.x;
Taguchi T., Kiyokawa N., Takenouch H., Matsui J., Tang W.-R.,
Nakajima H., Suzuki K., Shiozawa Y., Saito M., Katagiri Y.U.,
Takahashi T., Karasuyama H., Matsuo Y., Okita H., Fujimoto J.;
"Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx
induced by the pre-B-cell receptor in human pre-B cells.";
Immunology 112:575-582(2004).
[9]
FUNCTION, AND INTERACTION WITH GRB2.
PubMed=16912232; DOI=10.1182/blood-2006-02-005397;
Grabbe A., Wienands J.;
"Human SLP-65 isoforms contribute differently to activation and
apoptosis of B lymphocytes.";
Blood 108:3761-3768(2006).
[10]
INTERACTION WITH SYK.
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]
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).
-!- 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:10583958,
ECO:0000269|PubMed:15270728, ECO:0000269|PubMed:16912232,
ECO:0000269|PubMed:9697839}.
-!- SUBUNIT: Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen
receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2.
Interacts through its SH2 domain with CD79A. Interacts (via SH2
domain) with SYK; phosphorylated and activated by SYK. Interacts
with SCIMP. {ECO:0000269|PubMed:16912232,
ECO:0000269|PubMed:18369315, ECO:0000269|PubMed:21930792,
ECO:0000269|PubMed:9341187, ECO:0000269|PubMed:9697839}.
-!- INTERACTION:
P10275:AR; NbExp=2; IntAct=EBI-2623522, EBI-608057;
Q06187:BTK; NbExp=2; IntAct=EBI-2623522, EBI-624835;
Q9Y5K6:CD2AP; NbExp=2; IntAct=EBI-2623522, EBI-298152;
P62993:GRB2; NbExp=4; IntAct=EBI-2623522, EBI-401755;
P10721:KIT; NbExp=2; IntAct=EBI-2623522, EBI-1379503;
Q5ZMQ7:SH3KBP1 (xeno); NbExp=3; IntAct=EBI-2623522, EBI-7061433;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9697839}. Cell
membrane {ECO:0000269|PubMed:9697839}. Note=BCR activation results
in the translocation to membrane fraction.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8WV28-1; Sequence=Displayed;
Name=2;
IsoId=Q8WV28-2; Sequence=VSP_016178;
Name=3;
IsoId=Q8WV28-3; Sequence=VSP_045324;
-!- TISSUE SPECIFICITY: Expressed in B-cell lineage and fibroblast
cell lines (at protein level). Highest levels of expression in the
spleen, with lower levels in the liver, kidney, pancreas, small
intestines and colon.
-!- 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-96
facilitates BTK binding. Phosphorylation of Tyr-72 facilitates
VAV1 and NCK1 binding. Phosphorylation is required for both Ca(2+)
and MAPK signaling pathways. {ECO:0000269|PubMed:12456653,
ECO:0000269|PubMed:9697839}.
-!- DISEASE: Agammaglobulinemia 4, autosomal recessive (AGM4)
[MIM:613502]: A primary immunodeficiency characterized by
profoundly low or absent serum antibodies and low or absent
circulating B-cells due to an early block of B-cell development.
Affected individuals develop severe infections in the first years
of life. {ECO:0000269|PubMed:10583958}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=BLNKbase; Note=BLNK mutation db;
URL="http://structure.bmc.lu.se/idbase/BLNKbase/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BLNKID804ch10q24.html";
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EMBL; AF068180; AAC39936.1; -; mRNA.
EMBL; AF068181; AAC39937.1; -; mRNA.
EMBL; AF180756; AAF20382.1; -; Genomic_DNA.
EMBL; AF180740; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180741; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180742; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180743; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180744; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180745; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180746; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180747; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180748; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180749; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180750; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180751; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180752; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180753; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180754; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180755; AAF20382.1; JOINED; Genomic_DNA.
EMBL; AF180756; AAF20383.1; -; Genomic_DNA.
EMBL; AF180740; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180741; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180742; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180743; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180744; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180745; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180746; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180748; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180749; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180750; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180751; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180752; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180753; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180754; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AF180755; AAF20383.1; JOINED; Genomic_DNA.
EMBL; AM180337; CAJ55331.1; -; mRNA.
EMBL; AC021037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC018906; AAH18906.1; -; mRNA.
CCDS; CCDS44464.1; -. [Q8WV28-2]
CCDS; CCDS58091.1; -. [Q8WV28-3]
CCDS; CCDS7446.1; -. [Q8WV28-1]
RefSeq; NP_001107566.1; NM_001114094.1. [Q8WV28-2]
RefSeq; NP_001245369.1; NM_001258440.1. [Q8WV28-3]
RefSeq; NP_037446.1; NM_013314.3. [Q8WV28-1]
UniGene; Hs.665244; -.
ProteinModelPortal; Q8WV28; -.
SMR; Q8WV28; -.
BioGrid; 118894; 34.
CORUM; Q8WV28; -.
IntAct; Q8WV28; 22.
MINT; Q8WV28; -.
STRING; 9606.ENSP00000224337; -.
iPTMnet; Q8WV28; -.
PhosphoSitePlus; Q8WV28; -.
BioMuta; BLNK; -.
DMDM; 82592659; -.
MaxQB; Q8WV28; -.
PaxDb; Q8WV28; -.
PeptideAtlas; Q8WV28; -.
PRIDE; Q8WV28; -.
ProteomicsDB; 74740; -.
ProteomicsDB; 74741; -. [Q8WV28-2]
Ensembl; ENST00000224337; ENSP00000224337; ENSG00000095585. [Q8WV28-1]
Ensembl; ENST00000371176; ENSP00000360218; ENSG00000095585. [Q8WV28-2]
Ensembl; ENST00000413476; ENSP00000397487; ENSG00000095585. [Q8WV28-3]
GeneID; 29760; -.
KEGG; hsa:29760; -.
UCSC; uc001kls.5; human. [Q8WV28-1]
CTD; 29760; -.
DisGeNET; 29760; -.
EuPathDB; HostDB:ENSG00000095585.16; -.
GeneCards; BLNK; -.
HGNC; HGNC:14211; BLNK.
HPA; CAB009333; -.
HPA; CAB016291; -.
HPA; HPA038309; -.
HPA; HPA038310; -.
MalaCards; BLNK; -.
MIM; 604515; gene.
MIM; 613502; phenotype.
neXtProt; NX_Q8WV28; -.
OpenTargets; ENSG00000095585; -.
Orphanet; 33110; Autosomal agammaglobulinemia.
PharmGKB; PA25371; -.
eggNOG; ENOG410IGWN; Eukaryota.
eggNOG; ENOG410XYB6; LUCA.
GeneTree; ENSGT00530000063094; -.
HOGENOM; HOG000088646; -.
HOVERGEN; HBG053147; -.
InParanoid; Q8WV28; -.
KO; K07371; -.
OMA; DSEMYVL; -.
OrthoDB; EOG091G053I; -.
PhylomeDB; Q8WV28; -.
TreeFam; TF326567; -.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; Q8WV28; -.
SIGNOR; Q8WV28; -.
ChiTaRS; BLNK; human.
GeneWiki; B-cell_linker; -.
GenomeRNAi; 29760; -.
PRO; PR:Q8WV28; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000095585; Expressed in 193 organ(s), highest expression level in mouth mucosa.
CleanEx; HS_BLNK; -.
ExpressionAtlas; Q8WV28; baseline and differential.
Genevisible; Q8WV28; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:UniProtKB.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:ProtInc.
GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
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;
Alternative splicing; B-cell activation; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing; Membrane;
Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1 456 B-cell linker protein.
/FTId=PRO_0000064940.
DOMAIN 346 453 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COMPBIAS 98 260 Pro-rich.
MOD_RES 72 72 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12456653}.
MOD_RES 84 84 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12456653}.
MOD_RES 96 96 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12456653}.
MOD_RES 178 178 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12456653}.
MOD_RES 189 189 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12456653}.
VAR_SEQ 203 225 Missing (in isoform 2).
{ECO:0000303|PubMed:9697839}.
/FTId=VSP_016178.
VAR_SEQ 366 417 Missing (in isoform 3).
{ECO:0000303|PubMed:16636677}.
/FTId=VSP_045324.
MUTAGEN 72 72 Y->F: Significant phosphorylation
reduction; when associated with F-84; F-
96 and F-178.
{ECO:0000269|PubMed:12456653,
ECO:0000269|PubMed:9697839}.
MUTAGEN 84 84 Y->F: Significant phosphorylation
reduction; when associated with F-72; F-
96 and F-178.
{ECO:0000269|PubMed:12456653,
ECO:0000269|PubMed:9697839}.
MUTAGEN 96 96 Y->F: Significant phosphorylation
reduction; when associated with F-72; F-
84 and F-178.
{ECO:0000269|PubMed:12456653,
ECO:0000269|PubMed:9697839}.
MUTAGEN 178 178 Y->F: Significant phosphorylation
reduction; when associated with F-72; F-
84 and F-96.
{ECO:0000269|PubMed:9697839}.
CONFLICT 62 62 E -> Q (in Ref. 5; AAH18906).
{ECO:0000305}.
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


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18-783-78531 GOAT ANTI HUMAN APS - SH2 and PH domain-containing adapter protein APS; Adapter protein with pleckstrin homology and Src homology 2 domains Polyclonal 0.1 mg
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EIAAB31262 FAPP1,FAPP-1,Homo sapiens,Human,PH domain-containing family A member 3,Phosphatidylinositol-four-phosphate adapter protein 1,Phosphoinositol 4-phosphate adapter protein 1,Pleckstrin homology domain-co
EIAAB31273 Fapp2,FAPP-2,Mouse,Mus musculus,PH domain-containing family A member 8,Phosphatidylinositol-four-phosphate adapter protein 2,Phosphoinositol 4-phosphate adapter protein 2,Pleckstrin homology domain-co
EIAAB31263 Fapp1,FAPP-1,Mouse,Mus musculus,PH domain-containing family A member 3,Phosphatidylinositol-four-phosphate adapter protein 1,Phosphoinositol 4-phosphate adapter protein 1,Pleckstrin homology domain-co
EIAAB42483 Adaptor protein Wyatt,Homo sapiens,Human,MAL,MyD88 adapter-like protein,TIR domain-containing adapter protein,TIRAP,Toll_interleukin-1 receptor domain-containing adapter protein
EIAAB41674 Mouse,Mus musculus,Ticam1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-containing adapter protein inducing IFN-beta,Toll-interleukin-1 receptor domain-containing adapter protein inducin
EIAAB42482 Adaptor protein Wyatt,Mal,Mouse,Mus musculus,MyD88 adapter-like protein,TIR domain-containing adapter protein,Tirap,Toll_interleukin-1 receptor domain-containing adapter protein
18-661-15155 Toll-interleukin 1 receptor domain-containing adapter protein - TIR domain-containing adapter protein; MyD88 adapter-like protein; Adaptor protein Wyatt Polyclonal 0.1 mg
18-661-15156 Toll-interleukin 1 receptor domain-containing adapter protein - TIR domain-containing adapter protein; MyD88 adapter-like protein; Adaptor protein Wyatt Polyclonal 0.1 mg
EIAAB41675 Bos taurus,Bovine,TICAM1,TICAM-1,TIR domain-containing adapter molecule 1,TIR domain-containing adapter protein inducing IFN-beta,Toll-interleukin-1 receptor domain-containing adapter protein inducing
EIAAB31272 FAPP2,FAPP-2,hFAPP2,Homo sapiens,Human,PH domain-containing family A member 8,Phosphatidylinositol-four-phosphate adapter protein 2,Phosphoinositol 4-phosphate adapter protein 2,Pleckstrin homology do


 

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