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 24-JAN-2024, entry version 218. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 51. DR MINT; Q13094; -. DR STRING; 9606.ENSP00000046794; -. DR BindingDB; Q13094; -. 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; 9606-ENSP00000046794; -. DR PeptideAtlas; Q13094; -. DR ProteomicsDB; 59146; -. DR Pumba; Q13094; -. DR Antibodypedia; 3884; 795 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 AGR; HGNC:6529; -. DR CTD; 3937; -. DR DisGeNET; 3937; -. DR GeneCards; LCP2; -. DR HGNC; HGNC:6529; LCP2. DR HPA; ENSG00000043462; Group enriched (bone marrow, lymphoid tissue). DR MalaCards; LCP2; -. 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; GSRNQCM; -. DR OrthoDB; 5351675at2759; -. 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; 21 hits in 1160 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 185 other cell types or tissues. DR ExpressionAtlas; Q13094; baseline and differential. 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 CDD; cd09522; SAM_SLP76; 1. DR CDD; cd09929; SH2_BLNK_SLP-76; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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 PANTHER; PTHR14098:SF1; LYMPHOCYTE CYTOSOLIC PROTEIN 2; 1. DR PANTHER; PTHR14098; SH2 DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF07647; SAM_2; 1. DR Pfam; PF00017; SH2; 1. DR SMART; SM00454; SAM; 1. DR SMART; SM00252; SH2; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR PROSITE; PS50001; SH2; 1. DR Genevisible; Q13094; HS. 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 //