ID   LCP2_HUMAN              Reviewed;         533 AA.
AC   Q13094;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 91.
DE   RecName: Full=Lymphocyte cytosolic protein 2;
DE   AltName: Full=SH2 domain-containing leukocyte protein of 76 kDa;
DE   AltName: Full=SLP-76 tyrosine phosphoprotein;
DE            Short=SLP76;
GN   Name=LCP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Leukemia;
RX   MEDLINE=95221345; PubMed=7706237; DOI=10.1074/jbc.270.13.7029;
RA   Jackman J.K., Motto D.G., Sun Q., Tanemoto M., Turck C.W., Peltz G.A.,
RA   Koretzky G.A., Findell P.R.;
RT   "Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein
RT   associated with Grb2 in T cells.";
RL   J. Biol. Chem. 270:7029-7032(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH PRAM1.
RX   MEDLINE=21303636; PubMed=11301322; DOI=10.1074/jbc.M011683200;
RA   Moog-Lutz C., Peterson E.J., Lutz P.G., Eliason S., Cave-Riant F.,
RA   Singer A., Di Gioia Y., Dmovski S., Kamens J., Cayre Y.E.,
RA   Koretzky G.;
RT   "PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and
RT   promyelocytic leukemia (PML)-RA receptor alpha in acute promyelocytic
RT   leukemia cells.";
RL   J. Biol. Chem. 276:22375-22381(2001).
RN   [4]
RP   INTERACTION WITH SHB.
RX   PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
RA   Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
RT   "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
RL   Eur. J. Biochem. 269:3279-3288(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=15144186; DOI=10.1021/ac035352d;
RA   Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA   Peters E.C.;
RT   "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT   from human T cells using immobilized metal affinity chromatography and
RT   tandem mass spectrometry.";
RL   Anal. Chem. 76:2763-2772(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-173 AND SER-207, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=16094384; DOI=10.1038/nmeth776;
RA   Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,
RA   Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
RT   "Quantitative phosphoproteome analysis using a dendrimer conjugation
RT   chemistry and tandem mass spectrometry.";
RL   Nat. Methods 2:591-598(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   STRUCTURE BY NMR OF 1-83.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal SAM-domain of human lymphocyte
RT   cytosolic protein 2.";
RL   Submitted (FEB-2008) to the PDB data bank.
CC   -!- FUNCTION: Involved in T-cell antigen receptor mediated signaling.
CC   -!- SUBUNIT: Interacts with SLA. Interacts with CBLB (By similarity).
CC       Interacts with the adapter proteins GRB2 and FYB. Interacts with
CC       SHB. Interacts with PRAM1.
CC   -!- INTERACTION:
CC       P08631:HCK; NbExp=1; IntAct=EBI-346946, EBI-346340;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus, and
CC       peripheral blood leukocytes. Highly expressed also in T-cell and
CC       monocytic cell lines, expressed at lower level in B-cell lines.
CC       Not detected in fibroblast or neuroblasatoma cell lines.
CC   -!- DOMAIN: The SH2 domain mediates interaction with SHB.
CC   -!- PTM: Phosphorylated after T-cell receptor activation by ZAP-70.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
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DR   EMBL; U20158; AAC50135.1; -; mRNA.
DR   EMBL; BC016618; AAH16618.1; -; mRNA.
DR   IPI; IPI00297169; -.
DR   PIR; A56110; A56110.
DR   RefSeq; NP_005556.1; -.
DR   UniGene; Hs.304475; -.
DR   PDB; 1H3H; NMR; -; B=232-241.
DR   PDB; 1YWO; X-ray; 1.81 A; P=185-194.
DR   PDB; 2EAP; NMR; -; A=1-83.
DR   PDB; 2ROR; NMR; -; B=122-136.
DR   PDBsum; 1H3H; -.
DR   PDBsum; 1YWO; -.
DR   PDBsum; 2EAP; -.
DR   PDBsum; 2ROR; -.
DR   IntAct; Q13094; 2.
DR   PhosphoSite; Q13094; -.
DR   PRIDE; Q13094; -.
DR   Ensembl; ENSG00000043462; Homo sapiens.
DR   GeneID; 3937; -.
DR   KEGG; hsa:3937; -.
DR   GeneCards; GC05M169607; -.
DR   H-InvDB; HIX0005402; -.
DR   H-InvDB; HIX0005403; -.
DR   HGNC; HGNC:6529; LCP2.
DR   HPA; CAB004574; -.
DR   MIM; 601603; gene.
DR   PharmGKB; PA30313; -.
DR   HOGENOM; Q13094; -.
DR   HOVERGEN; Q13094; -.
DR   Pathway_Interaction_DB; fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
DR   Pathway_Interaction_DB; tcrjnkpathway; JNK signaling in the CD4+ TCR pathway.
DR   Pathway_Interaction_DB; tcrpathway; TCR signaling in naive CD4+ T cells.
DR   Pathway_Interaction_DB; cd8tcrpathway; TCR signaling in naive CD8+ T cells.
DR   Reactome; REACT_6900; Signaling in Immune system.
DR   NextBio; 15461; -.
DR   ArrayExpress; Q13094; -.
DR   Bgee; Q13094; -.
DR   CleanEx; HS_LCP2; -.
DR   GermOnline; ENSG00000043462; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; TAS:ProtInc.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   ProDom; PD000093; SH2; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   SH2 domain.
FT   CHAIN         1    533       Lymphocyte cytosolic protein 2.
FT                                /FTId=PRO_0000084368.
FT   DOMAIN       15     81       SAM.
FT   DOMAIN      422    530       SH2.
FT   COMPBIAS    133    136       Poly-Glu.
FT   COMPBIAS    198    201       Poly-Pro.
FT   MOD_RES      23     23       Phosphotyrosine (By similarity).
FT   MOD_RES     173    173       Phosphotyrosine.
FT   MOD_RES     207    207       Phosphoserine.
FT   STRAND        1      4
FT   HELIX         9     12
FT   TURN         17     19
FT   HELIX        20     26
FT   HELIX        30     38
FT   HELIX        43     47
FT   HELIX        51     54
FT   TURN         59     61
FT   HELIX        62     73
FT   HELIX       237    239
SQ   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
//