LAP2A_HUMAN
ID LAP2A_HUMAN Reviewed; 694 AA.
AC P42166; P08918; P08919; Q14860; Q16295;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Lamina-associated polypeptide 2, isoform alpha;
DE AltName: Full=Thymopoietin isoform alpha;
DE Short=TP alpha;
DE AltName: Full=Thymopoietin-related peptide isoform alpha;
DE Short=TPRP isoform alpha;
DE Contains:
DE RecName: Full=Thymopoietin;
DE Short=TP;
DE AltName: Full=Splenin;
DE Contains:
DE RecName: Full=Thymopentin;
DE AltName: Full=TP5;
GN Name=TMPO; Synonyms=LAP2;
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] (ISOFORMS ALPHA; BETA AND GAMMA).
RC TISSUE=Thymus;
RX PubMed=7517549; DOI=10.1073/pnas.91.14.6283;
RA Harris C.A., Andryuk P.J., Cline S.W., Chan H.K., Natarajan A.,
RA Siekierka J.J., Goldstein G.;
RT "Three distinct human thymopoietins are derived from alternatively spliced
RT mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6283-6287(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA; BETA AND GAMMA), AND
RP VARIANT GLU-599.
RX PubMed=8530026; DOI=10.1006/geno.1995.1131;
RA Harris C.A., Andryuk P.J., Cline S.W., Siekierka J.J., Goldstein G.;
RT "Structure and mapping of the human thymopoietin (TMPO) gene and
RT relationship of human TMPO beta to rat lamin-associated polypeptide 2.";
RL Genomics 28:198-205(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-526.
RC TISSUE=Thymus;
RX PubMed=7703909;
RA Hara H., Hayashi K., Ohta K., Itoh N., Ohta M.;
RT "A new thymopoietin precursor gene from human thymus.";
RL Biochem. Mol. Biol. Int. 34:927-933(1994).
RN [4]
RP PROTEIN SEQUENCE OF 2-13; 127-139; 254-264; 417-427 AND 526-535, CLEAVAGE
RP OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3473468; DOI=10.1073/pnas.84.11.3545;
RA Audhya T., Schlesinger D.H., Goldstein G.;
RT "Isolation and complete amino acid sequence of human thymopoietin and
RT splenin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3545-3549(1987).
RN [6]
RP ERRATUM OF PUBMED:3473468, AND RETRACTION NOTICE OF PUBMED:3473468.
RX PubMed=8016147; DOI=10.1073/pnas.91.13.6249;
RA Goldstein G., Schlesinger D.H., Audhya T.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:6249-6249(1994).
RN [7]
RP INTERACTION WITH CHROMOSOMES, AND PHOSPHORYLATION.
RX PubMed=9707448; DOI=10.1093/emboj/17.16.4887;
RA Dechat T., Gotzmann J., Stockinger A., Harris C.A., Talle M.A.,
RA Siekierka J.J., Foisner R.;
RT "Detergent-salt resistance of LAP2alpha in interphase nuclei and
RT phosphorylation-dependent association with chromosomes early in nuclear
RT assembly implies functions in nuclear structure dynamics.";
RL EMBO J. 17:4887-4902(1998).
RN [8]
RP INTERACTION WITH LMNA.
RX PubMed=10984438; DOI=10.1242/jcs.113.19.3473;
RA Dechat T., Korbei B., Vaughan O.A., Vlcek S., Hutchison C.J., Foisner R.;
RT "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins.";
RL J. Cell Sci. 113:3473-3484(2000).
RN [9]
RP INTERACTION WITH LMNA AND RB1.
RX PubMed=12475961; DOI=10.1091/mbc.e02-07-0450;
RA Markiewicz E., Dechat T., Foisner R., Quinlan R.A., Hutchison C.J.;
RT "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of
RT retinoblastoma protein.";
RL Mol. Biol. Cell 13:4401-4413(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-351 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74;
RP SER-79; THR-160; THR-164; SER-351; SER-370 AND SER-424, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-79;
RP THR-154; THR-160; SER-351 AND SER-424, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-156; THR-160;
RP SER-351; SER-354; SER-370 AND SER-424, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; THR-74; SER-351 AND
RP SER-354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-79;
RP SER-156; THR-160; THR-164; SER-168; SER-272; SER-351; SER-354; SER-370 AND
RP SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; THR-160;
RP SER-312 AND SER-351, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP LACK OF INVOLVEMENT IN DILATED CARDIOMYOPATHY.
RX PubMed=27896284; DOI=10.1002/mgg3.245;
RA Nouhravesh N., Ahlberg G., Ghouse J., Andreasen C., Svendsen J.H.,
RA Haunsoe S., Bundgaard H., Weeke P.E., Olesen M.S.;
RT "Analyses of more than 60,000 exomes questions the role of numerous genes
RT previously associated with dilated cardiomyopathy.";
RL Mol. Genet. Genomic Med. 4:617-623(2016).
RN [28]
RP INTERACTION WITH CMTM6, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28813417; DOI=10.1038/nature23643;
RA Burr M.L., Sparbier C.E., Chan Y.C., Williamson J.C., Woods K.,
RA Beavis P.A., Lam E.Y.N., Henderson M.A., Bell C.C., Stolzenburg S.,
RA Gilan O., Bloor S., Noori T., Morgens D.W., Bassik M.C., Neeson P.J.,
RA Behren A., Darcy P.K., Dawson S.J., Voskoboinik I., Trapani J.A., Cebon J.,
RA Lehner P.J., Dawson M.A.;
RT "CMTM6 maintains the expression of PD-L1 and regulates anti-tumour
RT immunity.";
RL Nature 549:101-105(2017).
RN [29]
RP STRUCTURE BY NMR OF 1-169.
RX PubMed=11500367; DOI=10.1093/emboj/20.16.4399;
RA Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M.;
RT "Solution structure of the constant region of nuclear envelope protein LAP2
RT reveals two LEM-domain structures: one binds BAF and the other binds DNA.";
RL EMBO J. 20:4399-4407(2001).
RN [30]
RP STRUCTURE BY NMR OF 1-57 AND 103-159.
RX PubMed=11435115; DOI=10.1016/s0969-2126(01)00611-6;
RA Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I.,
RA Worman H.J., Zinn-Justin S.;
RT "Structural characterization of the LEM motif common to three human inner
RT nuclear membrane proteins.";
RL Structure 9:503-511(2001).
RN [31]
RP VARIANT CYS-690, AND CHARACTERIZATION OF VARIANT CYS-690.
RX PubMed=16247757; DOI=10.1002/humu.20250;
RA Taylor M.R., Slavov D., Gajewski A., Vlcek S., Ku L., Fain P.R.,
RA Carniel E., Di Lenarda A., Sinagra G., Boucek M.M., Cavanaugh J.,
RA Graw S.L., Ruegg P., Feiger J., Zhu X., Ferguson D.A., Bristow M.R.,
RA Gotzmann J., Foisner R., Mestroni L.;
RT "Thymopoietin (lamina-associated polypeptide 2) gene mutation associated
RT with dilated cardiomyopathy.";
RL Hum. Mutat. 26:566-574(2005).
CC -!- FUNCTION: May be involved in the structural organization of the nucleus
CC and in the post-mitotic nuclear assembly. Plays an important role,
CC together with LMNA, in the nuclear anchorage of RB1.
CC -!- FUNCTION: TP and TP5 may play a role in T-cell development and
CC function. TP5 is an immunomodulating pentapeptide.
CC -!- SUBUNIT: Interacts with LMNA, BANF1 and RB1 and with chromosomes.
CC Associates directly or indirectly with lamins at specific cell-cycle
CC stages. Interacts with CMTM6 (PubMed:28813417).
CC {ECO:0000269|PubMed:10984438, ECO:0000269|PubMed:12475961,
CC ECO:0000269|PubMed:28813417, ECO:0000269|PubMed:9707448}.
CC -!- INTERACTION:
CC P42166; P02545: LMNA; NbExp=4; IntAct=EBI-395393, EBI-351935;
CC P42166; Q8TDX7: NEK7; NbExp=2; IntAct=EBI-395393, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Expressed diffusely
CC throughout the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha;
CC IsoId=P42166-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P42167-1; Sequence=External;
CC Name=Gamma;
CC IsoId=P42167-2; Sequence=External;
CC Name=Zeta;
CC IsoId=P42167-3; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Most abundant in adult
CC thymus and fetal liver.
CC -!- DOMAIN: The N-terminal part contains two structurally independent, non-
CC interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM
CC (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts
CC with BANF1.
CC -!- DOMAIN: The C-terminal domain forms a four-stranded coiled coil.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated in a mitose-specific manner.
CC {ECO:0000269|PubMed:9707448}.
CC -!- PHARMACEUTICAL: TP5 is available under the names Timunox (Cilag),
CC Sintomodulina (Italofarmaco) and Mepentil (Recordati). Used in primary
CC and secondary immune deficiencies, autoimmunity, infections and cancer.
CC -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
CC -!- CAUTION: TMPO was originally considered a good candidate for dilated
CC cardiomyopathy, and variant Cys-290 has been reported to be a likely
CC pathogenic mutation (PubMed:16247757). However, Cys-290 has a high
CC allele frequency and individuals homozygous for the variant have been
CC reported in ExAC database. Therefore, this variant has been
CC reclassified as a likely benign polymorphism (PubMed:27896284).
CC {ECO:0000269|PubMed:16247757, ECO:0000305|PubMed:27896284}.
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DR EMBL; U09086; AAB60329.1; -; mRNA.
DR EMBL; U18270; AAB60433.1; -; Genomic_DNA.
DR EMBL; U18266; AAB60433.1; JOINED; Genomic_DNA.
DR EMBL; U18267; AAB60433.1; JOINED; Genomic_DNA.
DR EMBL; U18268; AAB60433.1; JOINED; Genomic_DNA.
DR EMBL; S76736; AAB33958.1; -; mRNA.
DR CCDS; CCDS9064.1; -. [P42166-1]
DR PIR; G01161; G01161.
DR RefSeq; NP_003267.1; NM_003276.2. [P42166-1]
DR PDB; 1GJJ; NMR; -; A=1-168.
DR PDB; 1H9E; NMR; -; A=2-57.
DR PDB; 1H9F; NMR; -; A=103-159.
DR PDBsum; 1GJJ; -.
DR PDBsum; 1H9E; -.
DR PDBsum; 1H9F; -.
DR AlphaFoldDB; P42166; -.
DR BMRB; P42166; -.
DR SMR; P42166; -.
DR BioGRID; 112967; 663.
DR IntAct; P42166; 69.
DR MINT; P42166; -.
DR STRING; 9606.ENSP00000266732; -.
DR GlyGen; P42166; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P42166; -.
DR MetOSite; P42166; -.
DR SwissPalm; P42166; -.
DR BioMuta; TMPO; -.
DR DMDM; 1174689; -.
DR CPTAC; CPTAC-949; -.
DR EPD; P42166; -.
DR jPOST; P42166; -.
DR MassIVE; P42166; -.
DR PaxDb; P42166; -.
DR PeptideAtlas; P42166; -.
DR PRIDE; P42166; -.
DR ProteomicsDB; 55488; -. [P42166-1]
DR Antibodypedia; 2387; 408 antibodies from 37 providers.
DR DNASU; 7112; -.
DR Ensembl; ENST00000266732.8; ENSP00000266732.4; ENSG00000120802.14. [P42166-1]
DR GeneID; 7112; -.
DR UCSC; uc001tfh.3; human. [P42166-1]
DR CTD; 7112; -.
DR DisGeNET; 7112; -.
DR GeneCards; TMPO; -.
DR GeneReviews; TMPO; -.
DR HGNC; HGNC:11875; TMPO.
DR HPA; ENSG00000120802; Tissue enhanced (lymphoid).
DR MalaCards; TMPO; -.
DR MIM; 188380; gene.
DR neXtProt; NX_P42166; -.
DR OpenTargets; ENSG00000120802; -.
DR PharmGKB; PA36576; -.
DR VEuPathDB; HostDB:ENSG00000120802; -.
DR eggNOG; ENOG502QWCI; Eukaryota.
DR GeneTree; ENSGT00940000154098; -.
DR HOGENOM; CLU_397364_0_0_1; -.
DR InParanoid; P42166; -.
DR OrthoDB; 323585at2759; -.
DR PhylomeDB; P42166; -.
DR TreeFam; TF328426; -.
DR PathwayCommons; P42166; -.
DR SignaLink; P42166; -.
DR BioGRID-ORCS; 7112; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; TMPO; human.
DR EvolutionaryTrace; P42166; -.
DR GeneWiki; Thymopoietin; -.
DR GenomeRNAi; 7112; -.
DR Pharos; P42166; Tbio.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P42166; protein.
DR Bgee; ENSG00000120802; Expressed in ventricular zone and 198 other tissues.
DR ExpressionAtlas; P42166; baseline and differential.
DR Genevisible; P42166; HS.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005521; F:lamin binding; TAS:ProtInc.
DR Gene3D; 1.10.720.40; -; 2.
DR InterPro; IPR021623; LAP2alpha_C.
DR InterPro; IPR013146; LEM-like_dom.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR Pfam; PF11560; LAP2alpha; 1.
DR Pfam; PF03020; LEM; 1.
DR Pfam; PF08198; Thymopoietin; 1.
DR SMART; SM00540; LEM; 1.
DR SMART; SM01261; Thymopoietin; 1.
DR SUPFAM; SSF63451; SSF63451; 2.
DR PROSITE; PS50954; LEM; 1.
DR PROSITE; PS50955; LEM_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy;
KW Chromosome; Coiled coil; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleus; Pharmaceutical; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..694
FT /note="Lamina-associated polypeptide 2, isoform alpha"
FT /id="PRO_0000017674"
FT PEPTIDE 2..50
FT /note="Thymopoietin"
FT /id="PRO_0000017675"
FT PEPTIDE 33..37
FT /note="Thymopentin"
FT /id="PRO_0000017676"
FT DOMAIN 5..48
FT /note="LEM-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313,
FT ECO:0000255|PROSITE-ProRule:PRU00314"
FT DOMAIN 109..153
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 47..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..108
FT /note="Linker"
FT REGION 150..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..657
FT /evidence="ECO:0000250"
FT MOTIF 190..196
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61033"
FT MOD_RES 88
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61033"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61033"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61033"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 656
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 238
FT /note="L -> R (in dbSNP:rs35998138)"
FT /id="VAR_049773"
FT VARIANT 293
FT /note="S -> A (in dbSNP:rs35645287)"
FT /id="VAR_049774"
FT VARIANT 317
FT /note="T -> S (in dbSNP:rs35969221)"
FT /id="VAR_049775"
FT VARIANT 416
FT /note="K -> E (in dbSNP:rs11838270)"
FT /id="VAR_049776"
FT VARIANT 478
FT /note="K -> N (in dbSNP:rs35761089)"
FT /id="VAR_049777"
FT VARIANT 599
FT /note="Q -> E (in dbSNP:rs17459334)"
FT /evidence="ECO:0000269|PubMed:8530026"
FT /id="VAR_005635"
FT VARIANT 690
FT /note="R -> C (affects the interaction with LMNA;
FT dbSNP:rs17028450)"
FT /evidence="ECO:0000269|PubMed:16247757"
FT /id="VAR_049778"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1GJJ"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1GJJ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1H9E"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:1GJJ"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1GJJ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1GJJ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1GJJ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1GJJ"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:1GJJ"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1GJJ"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1H9F"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1GJJ"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:1GJJ"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:1GJJ"
SQ SEQUENCE 694 AA; 75492 MW; 1B514B0FB61D0D75 CRC64;
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK
GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL
LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS
DRYSDNEEGK KKEHKKVKST RDIVPFSELG TTPSGGGFFQ GISFPEISTR PPLGSTELQA
AKKVHTSKGD LPREPLVATN LPGRGQLQKL ASERNLFISC KSSHDRCLEK SSSSSSQPEH
SAMLVSTAAS PSLIKETTTG YYKDIVENIC GREKSGIQPL CPERSHISDQ SPLSSKRKAL
EESESSQLIS PPLAQAIRDY VNSLLVQGGV GSLPGTSNSM PPLDVENIQK RIDQSKFQET
EFLSPPRKVP RLSEKSVEER DSGSFVAFQN IPGSELMSSF AKTVVSHSLT TLGLEVAKQS
QHDKIDASEL SFPFHESILK VIEEEWQQVD RQLPSLACKY PVSSREATQI LSVPKVDDEI
LGFISEATPL GGIQAASTES CNQQLDLALC RAYEAAASAL QIATHTAFVA KAMQADISQA
AQILSSDPSR THQALGILSK TYDAASYICE AAFDEVKMAA HTMGNATVGR RYLWLKDCKI
NLASKNKLAS TPFKGGTLFG GEVCKVIKKR GNKH
