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Lymphocyte cytosolic protein 2 (SH2 domain-containing leukocyte protein of 76 kDa) (SLP-76 tyrosine phosphoprotein) (SLP76)

 LCP2_HUMAN              Reviewed;         533 AA.
Q13094; A8KA25; Q53XV4;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 181.
RecName: Full=Lymphocyte cytosolic protein 2;
AltName: Full=SH2 domain-containing leukocyte protein of 76 kDa;
AltName: Full=SLP-76 tyrosine phosphoprotein;
Short=SLP76;
Name=LCP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION
WITH GRB2.
TISSUE=Leukemia;
PubMed=7706237; DOI=10.1074/jbc.270.13.7029;
Jackman J.K., Motto D.G., Sun Q., Tanemoto M., Turck C.W., Peltz G.A.,
Koretzky G.A., Findell P.R.;
"Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein
associated with Grb2 in T cells.";
J. Biol. Chem. 270:7029-7032(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-410.
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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 PRAM1.
PubMed=11301322; DOI=10.1074/jbc.M011683200;
Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F.,
Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E.,
Koretzky G.;
"PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and
promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic
leukemia cells.";
J. Biol. Chem. 276:22375-22381(2001).
[7]
INTERACTION WITH SHB, AND DOMAIN.
PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
Eur. J. Biochem. 269:3279-3288(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
PHOSPHORYLATION BY SYK.
PubMed=15388330; DOI=10.1016/j.febslet.2004.07.090;
Shim E.K., Moon C.S., Lee G.Y., Ha Y.J., Chae S.K., Lee J.R.;
"Association of the Src homology 2 domain-containing leukocyte
phosphoprotein of 76 kD (SLP-76) with the p85 subunit of
phosphoinositide 3-kinase.";
FEBS Lett. 575:35-40(2004).
[10]
INTERACTION WITH CD6, AND DOMAIN.
PubMed=16914752; DOI=10.1128/MCB.00688-06;
Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J.,
Bomb M., Barclay A.N., Brown M.H.;
"CD6 regulates T-cell responses through activation-dependent
recruitment of the positive regulator SLP-76.";
Mol. Cell. Biol. 26:6727-6738(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION BY ITK.
PubMed=21725281; DOI=10.1038/emboj.2011.213;
Sela M., Bogin Y., Beach D., Oellerich T., Lehne J.,
Smith-Garvin J.E., Okumura M., Starosvetsky E., Kosoff R., Libman E.,
Koretzky G., Kambayashi T., Urlaub H., Wienands J., Chernoff J.,
Yablonski D.;
"Sequential phosphorylation of SLP-76 at tyrosine 173 is required for
activation of T and mast cells.";
EMBO J. 30:3160-3172(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-410, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
INTERACTION WITH CD6.
PubMed=24584089; DOI=10.1038/ni.2843;
Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R.,
Yamasaki S., Saito T., Malissen M., Aebersold R., Gstaiger M.,
Malissen B.;
"Quantitative proteomics analysis of signalosome dynamics in primary T
cells identifies the surface receptor CD6 as a Lat adaptor-independent
TCR signaling hub.";
Nat. Immunol. 15:384-392(2014).
[16]
INTERACTION WITH FYB2 AND FYB1.
PubMed=27335501; DOI=10.4049/jimmunol.1501913;
Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y.,
Lee J.R.;
"ARAP, a novel adaptor protein, is required for TCR signaling and
integrin-mediated adhesion.";
J. Immunol. 197:942-952(2016).
[17]
STRUCTURE BY NMR OF 1-83.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the N-terminal SAM-domain of human lymphocyte
cytosolic protein 2.";
Submitted (FEB-2008) to the PDB data bank.
-!- FUNCTION: Involved in T-cell antigen receptor mediated signaling.
-!- SUBUNIT: Interacts with SLA. Interacts with CBLB (By similarity).
Interacts with GRB2 (PubMed:7706237). Interacts with SHB
(PubMed:12084069). Interacts with PRAM1 (PubMed:11301322).
Interacts (via SH2 domain) with CD6 (via tyrosine phosphorylated
C-terminus) (PubMed:16914752, PubMed:24584089). Interacts with
FYB1 and the phosphorylated form of FYB2 (PubMed:27335501).
{ECO:0000250|UniProtKB:Q60787, ECO:0000269|PubMed:11301322,
ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:16914752,
ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:27335501,
ECO:0000269|PubMed:7706237}.
-!- INTERACTION:
P30203:CD6; NbExp=3; IntAct=EBI-346946, EBI-2873748;
P00533:EGFR; NbExp=2; IntAct=EBI-346946, EBI-297353;
P51116:FXR2; NbExp=5; IntAct=EBI-346946, EBI-740459;
O15117:FYB1; NbExp=11; IntAct=EBI-346946, EBI-1753267;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-346946, EBI-618309;
O75791:GRAP2; NbExp=20; IntAct=EBI-346946, EBI-740418;
O89100:Grap2 (xeno); NbExp=7; IntAct=EBI-346946, EBI-642151;
P62993:GRB2; NbExp=14; IntAct=EBI-346946, EBI-401755;
P62994:Grb2 (xeno); NbExp=3; IntAct=EBI-346946, EBI-401775;
Q08881:ITK; NbExp=4; IntAct=EBI-346946, EBI-968552;
Q03526:Itk (xeno); NbExp=2; IntAct=EBI-346946, EBI-647969;
P06239:LCK; NbExp=2; IntAct=EBI-346946, EBI-1348;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-346946, EBI-739832;
Q8IVH8:MAP4K3; NbExp=5; IntAct=EBI-346946, EBI-1758170;
Q99JP0:Map4k3 (xeno); NbExp=2; IntAct=EBI-346946, EBI-5324222;
P16333:NCK1; NbExp=14; IntAct=EBI-346946, EBI-389883;
O43639:NCK2; NbExp=9; IntAct=EBI-346946, EBI-713635;
P08487:PLCG1 (xeno); NbExp=5; IntAct=EBI-346946, EBI-8013886;
P19174:PLCG1; NbExp=3; IntAct=EBI-346946, EBI-79387;
Q92783:STAM; NbExp=3; IntAct=EBI-346946, EBI-752333;
O75886:STAM2; NbExp=8; IntAct=EBI-346946, EBI-373258;
P15498:VAV1; NbExp=9; IntAct=EBI-346946, EBI-625518;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus and
peripheral blood leukocytes. Highly expressed also in T-cell and
monocytic cell lines, expressed at lower level in B-cell lines.
Not detected in fibroblast or neuroblastoma cell lines.
-!- DOMAIN: The SH2 domain mediates interaction with phosphorylated
CD6 (PubMed:16914752). The SH2 domain mediates interaction with
SHB (PubMed:12084069). {ECO:0000269|PubMed:12084069,
ECO:0000269|PubMed:16914752}.
-!- PTM: Phosphorylated after T-cell receptor activation by ZAP70, ITK
and TXK, which leads to the up-regulation of Th1 preferred
cytokine IL-2. SYK-dependent phosphorylation is required for
recruitment of PI3K signaling components.
{ECO:0000269|PubMed:15388330, ECO:0000269|PubMed:21725281}.
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EMBL; U20158; AAC50135.1; -; mRNA.
EMBL; BT007273; AAP35937.1; -; mRNA.
EMBL; AK292890; BAF85579.1; -; mRNA.
EMBL; CH471062; EAW61479.1; -; Genomic_DNA.
EMBL; BC016618; AAH16618.1; -; mRNA.
CCDS; CCDS47339.1; -.
PIR; A56110; A56110.
RefSeq; NP_005556.1; NM_005565.4.
UniGene; Hs.304475; -.
UniGene; Hs.660173; -.
PDB; 1H3H; NMR; -; B=232-241.
PDB; 1YWO; X-ray; 1.81 A; P=185-194.
PDB; 2EAP; NMR; -; A=1-83.
PDB; 2ROR; NMR; -; B=122-136.
PDBsum; 1H3H; -.
PDBsum; 1YWO; -.
PDBsum; 2EAP; -.
PDBsum; 2ROR; -.
ProteinModelPortal; Q13094; -.
SMR; Q13094; -.
BioGrid; 110129; 32.
CORUM; Q13094; -.
DIP; DIP-31812N; -.
IntAct; Q13094; 43.
MINT; Q13094; -.
STRING; 9606.ENSP00000046794; -.
iPTMnet; Q13094; -.
PhosphoSitePlus; Q13094; -.
BioMuta; LCP2; -.
DMDM; 10720065; -.
EPD; Q13094; -.
MaxQB; Q13094; -.
PaxDb; Q13094; -.
PeptideAtlas; Q13094; -.
PRIDE; Q13094; -.
DNASU; 3937; -.
Ensembl; ENST00000046794; ENSP00000046794; ENSG00000043462.
GeneID; 3937; -.
KEGG; hsa:3937; -.
UCSC; uc003man.2; human.
CTD; 3937; -.
DisGeNET; 3937; -.
EuPathDB; HostDB:ENSG00000043462.11; -.
GeneCards; LCP2; -.
H-InvDB; HIX0005402; -.
HGNC; HGNC:6529; LCP2.
HPA; CAB004574; -.
HPA; HPA036396; -.
HPA; HPA036397; -.
MIM; 601603; gene.
neXtProt; NX_Q13094; -.
OpenTargets; ENSG00000043462; -.
PharmGKB; PA30313; -.
eggNOG; ENOG410IFFN; Eukaryota.
eggNOG; ENOG4111KZ2; LUCA.
GeneTree; ENSGT00530000063094; -.
HOGENOM; HOG000049173; -.
HOVERGEN; HBG006247; -.
InParanoid; Q13094; -.
KO; K07361; -.
OMA; MSSNTFP; -.
PhylomeDB; Q13094; -.
TreeFam; TF326567; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
SignaLink; Q13094; -.
SIGNOR; Q13094; -.
EvolutionaryTrace; Q13094; -.
GeneWiki; Lymphocyte_cytosolic_protein_2; -.
GenomeRNAi; 3937; -.
PRO; PR:Q13094; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000043462; -.
CleanEx; HS_LCP2; -.
ExpressionAtlas; Q13094; baseline and differential.
Genevisible; Q13094; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0036398; C:TCR signalosome; IDA:UniProtKB.
GO; GO:0050663; P:cytokine secretion; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0045576; P:mast cell activation; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEP:CACAO.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
Pfam; PF07647; SAM_2; 1.
Pfam; PF00017; SH2; 1.
SMART; SM00454; SAM; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain.
CHAIN 1 533 Lymphocyte cytosolic protein 2.
/FTId=PRO_0000084368.
DOMAIN 15 81 SAM.
DOMAIN 422 530 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COMPBIAS 133 136 Poly-Glu.
COMPBIAS 198 201 Poly-Pro.
MOD_RES 23 23 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q60787}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 410 410 S -> C (in dbSNP:rs34192428).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_070803.
CONFLICT 19 19 S -> G (in Ref. 3; BAF85579).
{ECO:0000305}.
STRAND 1 4 {ECO:0000244|PDB:2EAP}.
HELIX 9 12 {ECO:0000244|PDB:2EAP}.
TURN 17 19 {ECO:0000244|PDB:2EAP}.
HELIX 20 26 {ECO:0000244|PDB:2EAP}.
HELIX 30 38 {ECO:0000244|PDB:2EAP}.
HELIX 43 47 {ECO:0000244|PDB:2EAP}.
HELIX 51 54 {ECO:0000244|PDB:2EAP}.
TURN 59 61 {ECO:0000244|PDB:2EAP}.
HELIX 62 73 {ECO:0000244|PDB:2EAP}.
HELIX 237 239 {ECO:0000244|PDB:1H3H}.
SEQUENCE 533 AA; 60188 MW; C5D22F31D36200C8 CRC64;
MALRNVPFRS EVLGWDPDSL ADYFKKLNYK DCEKAVKKYH IDGARFLNLT ENDIQKFPKL
RVPILSKLSQ EINKNEERRS IFTRKPQVPR FPEETESHEE DNGGWSSFEE DDYESPNDDQ
DGEDDGDYES PNEEEEAPVE DDADYEPPPS NDEEALQNSI LPAKPFPNSN SMYIDRPPSG
KTPQQPPVPP QRPMAALPPP PAGRNHSPLP PPQTNHEEPS RSRNHKTAKL PAPSIDRSTK
PPLDRSLAPF DREPFTLGKK PPFSDKPSIP AGRSLGEHLP KIQKPPLPPT TERHERSSPL
PGKKPPVPKH GWGPDRREND EDDVHQRPLP QPALLPMSSN TFPSRSTKPS PMNPLPSSHM
PGAFSESNSS FPQSASLPPY FSQGPSNRPP IRAEGRNFPL PLPNKPRPPS PAEEENSLNE
EWYVSYITRP EAEAALRKIN QDGTFLVRDS SKKTTTNPYV LMVLYKDKVY NIQIRYQKES
QVYLLGTGLR GKEDFLSVSD IIDYFRKMPL LLIDGKNRGS RYQCTLTHAA GYP


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18-003-43968 KH domain-containing. RNA-binding. signal transduction-associated protein 1 - p21 Ras GTPase-activating protein-associated p62; GAP-associated tyrosine phosphoprotein p62; Src-associated in mitosis 68 0.1 mg Protein A
EIAAB37261 Mouse,Mus musculus,SAM domain, SH3 domain and nuclear localization signals protein 1,SAM domain-containing protein SAMSN-1,Samsn1,SH3 protein expressed in lymphocytes 2,SH3-lymphocyte protein 2,SLy2
U1030m CLIA L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030m ELISA kit L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
E1030m ELISA L-CA,Leukocyte common antigen,Ly-5,Ly-5,Lymphocyte antigen 5,Mouse,Mus musculus,Ptprc,Receptor-type tyrosine-protein phosphatase C,T200 96T
LF-PA41504 anti-Leukocyte Protein Tyrosine Kinase, Rabbit polyclonal to Leukocyte Protein Tyrosine Kinase, Isotype IgG, Host Rabbit 100 ul
32-186 Lck(lymphocyte-specific protein tyrosine kinase), with 509-amino acid protein (about 56kDa), belongs to the Src non-receptor tyrosine kinases family. By virtue of common structural motifs, the Src fam 0.1 mL
EIAAB33112 LAR-PTP2,Leukocyte common antigen-related protein-tyrosine phosphatase 2,Ptprs,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase S,Receptor-type tyrosine-protein phosphatase sigma,R-PTP
EIAAB32305 B lymphocyte-induced maturation protein 1,Beta-interferon gene positive regulatory domain I-binding factor,Blimp1,Blimp-1,Mouse,Mus musculus,PR domain zinc finger protein 1,PR domain-containing protei


 

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