LCP2_HUMAN
ID LCP2_HUMAN Reviewed; 533 AA.
AC Q13094; A8KA25; Q53XV4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 210.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH
RP GRB2.
RC TISSUE=Leukemia;
RX 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 associated
RT with Grb2 in T cells.";
RL J. Biol. Chem. 270:7029-7032(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-410.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH PRAM1.
RX 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., 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 [7]
RP INTERACTION WITH SHB, AND DOMAIN.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic 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 from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP PHOSPHORYLATION BY SYK.
RX PubMed=15388330; DOI=10.1016/j.febslet.2004.07.090;
RA Shim E.K., Moon C.S., Lee G.Y., Ha Y.J., Chae S.K., Lee J.R.;
RT "Association of the Src homology 2 domain-containing leukocyte
RT phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide
RT 3-kinase.";
RL FEBS Lett. 575:35-40(2004).
RN [10]
RP INTERACTION WITH CD6, AND DOMAIN.
RX PubMed=16914752; DOI=10.1128/mcb.00688-06;
RA Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J.,
RA Bomb M., Barclay A.N., Brown M.H.;
RT "CD6 regulates T-cell responses through activation-dependent recruitment of
RT the positive regulator SLP-76.";
RL Mol. Cell. Biol. 26:6727-6738(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
RP PHOSPHORYLATION BY ITK.
RX PubMed=21725281; DOI=10.1038/emboj.2011.213;
RA Sela M., Bogin Y., Beach D., Oellerich T., Lehne J., Smith-Garvin J.E.,
RA Okumura M., Starosvetsky E., Kosoff R., Libman E., Koretzky G.,
RA Kambayashi T., Urlaub H., Wienands J., Chernoff J., Yablonski D.;
RT "Sequential phosphorylation of SLP-76 at tyrosine 173 is required for
RT activation of T and mast cells.";
RL EMBO J. 30:3160-3172(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP INTERACTION WITH CD6.
RX PubMed=24584089; DOI=10.1038/ni.2843;
RA Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
RA Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R., Yamasaki S.,
RA Saito T., Malissen M., Aebersold R., Gstaiger M., Malissen B.;
RT "Quantitative proteomics analysis of signalosome dynamics in primary T
RT cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR
RT signaling hub.";
RL Nat. Immunol. 15:384-392(2014).
RN [16]
RP INTERACTION WITH FYB2 AND FYB1.
RX PubMed=27335501; DOI=10.4049/jimmunol.1501913;
RA Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y., Lee J.R.;
RT "ARAP, a novel adaptor protein, is required for TCR signaling and integrin-
RT mediated adhesion.";
RL J. Immunol. 197:942-952(2016).
RN [17]
RP INVOLVEMENT IN IMD81.
RX PubMed=33231617; DOI=10.1084/jem.20201062;
RA Lev A., Lee Y.N., Sun G., Hallumi E., Simon A.J., Zrihen K.S., Levy S.,
RA Beit Halevi T., Papazian M., Shwartz N., Somekh I., Levy-Mendelovich S.,
RA Wolach B., Gavrieli R., Vernitsky H., Barel O., Javasky E., Stauber T.,
RA Ma C.A., Zhang Y., Amariglio N., Rechavi G., Hendel A., Yablonski D.,
RA Milner J.D., Somech R.;
RT "Inherited SLP76 deficiency in humans causes severe combined
RT immunodeficiency, neutrophil and platelet defects.";
RL J. Exp. Med. 218:0-0(2021).
RN [18]
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 GRB2 (PubMed:7706237). Interacts with SHB
CC (PubMed:12084069). Interacts with PRAM1 (PubMed:11301322). Interacts
CC (via SH2 domain) with CD6 (via tyrosine phosphorylated C-terminus)
CC (PubMed:16914752, PubMed:24584089). Interacts with FYB1 and the
CC phosphorylated form of FYB2 (PubMed:27335501).
CC {ECO:0000250|UniProtKB:Q60787, ECO:0000269|PubMed:11301322,
CC ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:16914752,
CC ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:27335501,
CC ECO:0000269|PubMed:7706237}.
CC -!- INTERACTION:
CC Q13094; P30203: CD6; NbExp=3; IntAct=EBI-346946, EBI-2873748;
CC Q13094; P00533: EGFR; NbExp=3; IntAct=EBI-346946, EBI-297353;
CC Q13094; Q9H5J4: ELOVL6; NbExp=3; IntAct=EBI-346946, EBI-12821617;
CC Q13094; P51116: FXR2; NbExp=7; IntAct=EBI-346946, EBI-740459;
CC Q13094; O15117: FYB1; NbExp=9; IntAct=EBI-346946, EBI-1753267;
CC Q13094; Q08379: GOLGA2; NbExp=6; IntAct=EBI-346946, EBI-618309;
CC Q13094; O75791: GRAP2; NbExp=40; IntAct=EBI-346946, EBI-740418;
CC Q13094; P62993: GRB2; NbExp=18; IntAct=EBI-346946, EBI-401755;
CC Q13094; Q08881: ITK; NbExp=3; IntAct=EBI-346946, EBI-968552;
CC Q13094; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-346946, EBI-739832;
CC Q13094; Q8IVH8: MAP4K3; NbExp=5; IntAct=EBI-346946, EBI-1758170;
CC Q13094; P16333: NCK1; NbExp=21; IntAct=EBI-346946, EBI-389883;
CC Q13094; O43639: NCK2; NbExp=10; IntAct=EBI-346946, EBI-713635;
CC Q13094; P19174: PLCG1; NbExp=3; IntAct=EBI-346946, EBI-79387;
CC Q13094; Q92783: STAM; NbExp=3; IntAct=EBI-346946, EBI-752333;
CC Q13094; O75886: STAM2; NbExp=9; IntAct=EBI-346946, EBI-373258;
CC Q13094; P15498: VAV1; NbExp=9; IntAct=EBI-346946, EBI-625518;
CC Q13094; O89100: Grap2; Xeno; NbExp=4; IntAct=EBI-346946, EBI-642151;
CC Q13094; Q99JP0: Map4k3; Xeno; NbExp=2; IntAct=EBI-346946, EBI-5324222;
CC Q13094; P08487: PLCG1; Xeno; NbExp=5; IntAct=EBI-346946, EBI-8013886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus and peripheral
CC blood leukocytes. Highly expressed also in T-cell and monocytic cell
CC lines, expressed at lower level in B-cell lines. Not detected in
CC fibroblast or neuroblastoma cell lines.
CC -!- DOMAIN: The SH2 domain mediates interaction with phosphorylated CD6
CC (PubMed:16914752). The SH2 domain mediates interaction with SHB
CC (PubMed:12084069). {ECO:0000269|PubMed:12084069,
CC ECO:0000269|PubMed:16914752}.
CC -!- PTM: Phosphorylated after T-cell receptor activation by ZAP70, ITK and
CC TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2.
CC SYK-dependent phosphorylation is required for recruitment of PI3K
CC signaling components. {ECO:0000269|PubMed:15388330,
CC ECO:0000269|PubMed:21725281}.
CC -!- DISEASE: Immunodeficiency 81 (IMD81) [MIM:619374]: An autosomal
CC recessive disorder characterized by recurrent infections, including
CC fungal infections, associated with T cell, neutrophil, and NK cell
CC dysfunction. B cells may also show maturation abnormalities. Other
CC features include autoimmune hemolytic anemia and abnormal platelet
CC aggregation. {ECO:0000269|PubMed:33231617}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
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DR EMBL; U20158; AAC50135.1; -; mRNA.
DR EMBL; BT007273; AAP35937.1; -; mRNA.
DR EMBL; AK292890; BAF85579.1; -; mRNA.
DR EMBL; CH471062; EAW61479.1; -; Genomic_DNA.
DR EMBL; BC016618; AAH16618.1; -; mRNA.
DR CCDS; CCDS47339.1; -.
DR PIR; A56110; A56110.
DR RefSeq; NP_005556.1; NM_005565.4.
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 PDB; 6ZCJ; X-ray; 1.53 A; P=371-380.
DR PDBsum; 1H3H; -.
DR PDBsum; 1YWO; -.
DR PDBsum; 2EAP; -.
DR PDBsum; 2ROR; -.
DR PDBsum; 6ZCJ; -.
DR AlphaFoldDB; Q13094; -.
DR SMR; Q13094; -.
DR BioGRID; 110129; 45.
DR CORUM; Q13094; -.
DR DIP; DIP-31812N; -.
DR IntAct; Q13094; 50.
DR MINT; Q13094; -.
DR STRING; 9606.ENSP00000046794; -.
DR GlyGen; Q13094; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13094; -.
DR PhosphoSitePlus; Q13094; -.
DR BioMuta; LCP2; -.
DR DMDM; 10720065; -.
DR EPD; Q13094; -.
DR jPOST; Q13094; -.
DR MassIVE; Q13094; -.
DR MaxQB; Q13094; -.
DR PaxDb; Q13094; -.
DR PeptideAtlas; Q13094; -.
DR PRIDE; Q13094; -.
DR ProteomicsDB; 59146; -.
DR Antibodypedia; 3884; 723 antibodies from 45 providers.
DR DNASU; 3937; -.
DR Ensembl; ENST00000046794.10; ENSP00000046794.5; ENSG00000043462.13.
DR GeneID; 3937; -.
DR KEGG; hsa:3937; -.
DR MANE-Select; ENST00000046794.10; ENSP00000046794.5; NM_005565.5; NP_005556.1.
DR UCSC; uc003man.2; human.
DR CTD; 3937; -.
DR DisGeNET; 3937; -.
DR GeneCards; LCP2; -.
DR HGNC; HGNC:6529; LCP2.
DR HPA; ENSG00000043462; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 601603; gene.
DR MIM; 619374; phenotype.
DR neXtProt; NX_Q13094; -.
DR OpenTargets; ENSG00000043462; -.
DR PharmGKB; PA30313; -.
DR VEuPathDB; HostDB:ENSG00000043462; -.
DR eggNOG; ENOG502QV3T; Eukaryota.
DR GeneTree; ENSGT00940000156835; -.
DR HOGENOM; CLU_040430_0_0_1; -.
DR InParanoid; Q13094; -.
DR OMA; AHHNVIF; -.
DR OrthoDB; 744111at2759; -.
DR PhylomeDB; Q13094; -.
DR TreeFam; TF326567; -.
DR PathwayCommons; Q13094; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR SignaLink; Q13094; -.
DR SIGNOR; Q13094; -.
DR BioGRID-ORCS; 3937; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; LCP2; human.
DR EvolutionaryTrace; Q13094; -.
DR GeneWiki; Lymphocyte_cytosolic_protein_2; -.
DR GenomeRNAi; 3937; -.
DR Pharos; Q13094; Tbio.
DR PRO; PR:Q13094; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13094; protein.
DR Bgee; ENSG00000043462; Expressed in monocyte and 183 other tissues.
DR ExpressionAtlas; Q13094; baseline and differential.
DR Genevisible; Q13094; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0036398; C:TCR signalosome; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045576; P:mast cell activation; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEP:CACAO.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID00318; -.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT CHAIN 1..533
FT /note="Lymphocyte cytosolic protein 2"
FT /id="PRO_0000084368"
FT DOMAIN 15..81
FT /note="SAM"
FT DOMAIN 422..530
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 78..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60787"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 410
FT /note="S -> C (in dbSNP:rs34192428)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070803"
FT CONFLICT 19
FT /note="S -> G (in Ref. 3; BAF85579)"
FT /evidence="ECO:0000305"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:2EAP"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:2EAP"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:2EAP"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1H3H"
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
