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   27-MAR-2024, entry version 228.
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, AND RETRACTED PAPER.
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   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   [28]
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   [29]
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   [30]
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).
RN   [31]
RP   VARIANT CYS-690, AND 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).
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}.
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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   PDB; 8FN7; EM; 2.80 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FND; EM; 3.00 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNG; EM; 2.20 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNH; EM; 2.50 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNJ; EM; 2.40 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNL; EM; 2.80 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNM; EM; 2.80 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNN; EM; 2.70 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNO; EM; 2.50 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNP; EM; 2.20 A; A/B/C/D/G/H/I/J=50-100.
DR   PDB; 8FNQ; EM; 2.80 A; A/B/C/D/G/H/I/J=50-100.
DR   PDBsum; 1GJJ; -.
DR   PDBsum; 1H9E; -.
DR   PDBsum; 1H9F; -.
DR   PDBsum; 8FN7; -.
DR   PDBsum; 8FND; -.
DR   PDBsum; 8FNG; -.
DR   PDBsum; 8FNH; -.
DR   PDBsum; 8FNJ; -.
DR   PDBsum; 8FNL; -.
DR   PDBsum; 8FNM; -.
DR   PDBsum; 8FNN; -.
DR   PDBsum; 8FNO; -.
DR   PDBsum; 8FNP; -.
DR   PDBsum; 8FNQ; -.
DR   AlphaFoldDB; P42166; -.
DR   BMRB; P42166; -.
DR   SMR; P42166; -.
DR   BioGRID; 112967; 754.
DR   IntAct; P42166; 71.
DR   MINT; P42166; -.
DR   STRING; 9606.ENSP00000266732; -.
DR   GlyGen; P42166; 7 sites, 1 O-linked glycan (5 sites).
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; 9606-ENSP00000266732; -.
DR   PeptideAtlas; P42166; -.
DR   ProteomicsDB; 55488; -. [P42166-1]
DR   Pumba; P42166; -.
DR   Antibodypedia; 2387; 456 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   AGR; HGNC:11875; -.
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; 5403043at2759; -.
DR   PhylomeDB; P42166; -.
DR   TreeFam; TF328426; -.
DR   PathwayCommons; P42166; -.
DR   SignaLink; P42166; -.
DR   BioGRID-ORCS; 7112; 21 hits in 1159 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 200 other cell types or tissues.
DR   ExpressionAtlas; P42166; baseline and differential.
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   CDD; cd12940; LEM_LAP2_LEMD1; 1.
DR   CDD; cd12935; LEM_like; 1.
DR   Gene3D; 1.10.287.3160; -; 1.
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   PANTHER; PTHR12019:SF24; LAMINA-ASSOCIATED POLYPEPTIDE 2, ISOFORM ALPHA; 1.
DR   PANTHER; PTHR12019; LAMINA-ASSOCIATED POLYPEPTIDE THYMOPOIETIN; 1.
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; LEM domain; 2.
DR   PROSITE; PS50954; LEM; 1.
DR   PROSITE; PS50955; LEM_LIKE; 1.
DR   Genevisible; P42166; HS.
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                   ECO:0000269|PubMed:27896284"
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
//