ID LAP2B_HUMAN Reviewed; 454 AA. AC P42167; A2T926; Q14861; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Lamina-associated polypeptide 2, isoforms beta/gamma; DE AltName: Full=Thymopoietin, isoforms beta/gamma; DE Short=TP beta/gamma; DE AltName: Full=Thymopoietin-related peptide isoforms beta/gamma; DE Short=TPRP isoforms beta/gamma; 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 [MRNA] (ISOFORM ZETA), AND SUBCELLULAR LOCATION RP (ISOFORM ZETA). RX PubMed=18403046; DOI=10.1016/j.ejcb.2008.01.014; RA Shaklai S., Somech R., Gal-Yam E.N., Deshet-Unger N., RA Moshitch-Moshkovitz S., Hirschberg K., Amariglio N., Simon A.J., RA Rechavi G.; RT "LAP2zeta binds BAF and suppresses LAP2beta-mediated transcriptional RT repression."; RL Eur. J. Cell Biol. 87:267-278(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA). RC TISSUE=Eye; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 AND 313-454 (ISOFORMS BETA AND RP GAMMA). 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 [7] RP INTERACTION WITH LMNB1. RX PubMed=9490046; DOI=10.1046/j.1432-1327.1998.2510729.x; RA Furukawa K., Kondo T.; RT "Identification of the lamina-associated-polypeptide-2-binding domain of B- RT type lamin."; RL Eur. J. Biochem. 251:729-733(1998). RN [8] RP INTERACTION WITH AKAP8L. RX PubMed=12538639; DOI=10.1083/jcb.200210026; RA Martins S., Eikvar S., Furukawa K., Collas P.; RT "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction RT implicated in initiation of DNA replication."; RL J. Cell Biol. 160:177-188(2003). RN [9] RP TOPOLOGY. RX PubMed=10806084; DOI=10.1006/jsbi.2000.4212; RA Dechat T., Vlcek S., Foisner R.; RT "Review: lamina-associated polypeptide 2 isoforms and related proteins in RT cell cycle-dependent nuclear structure dynamics."; RL J. Struct. Biol. 129:335-345(2000). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, 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-306, AND IDENTIFICATION BY RP 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 SER-306, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200; RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling RT network: indicating the involvement of ribonucleoside-diphosphate reductase RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal RT transduction."; RL Mol. Cell. Proteomics 6:1952-1967(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-306 AND SER-315, 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-306, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67; THR-74; RP SER-79; THR-160; THR-164; SER-177; SER-180; SER-306; SER-315; SER-362 AND RP SER-385, AND IDENTIFICATION 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 [18] 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-79; RP THR-154; THR-160; SER-292 AND SER-306, 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-156; THR-160; RP THR-211; SER-265; SER-306; THR-312 AND SER-315, 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 AND THR-74, AND RP 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-180; SER-184; SER-190; SER-222; RP SER-224; SER-250; SER-254; SER-265; SER-306; SER-315; SER-378; SER-385 AND RP SER-402, 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 AND SER-306, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(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). CC -!- FUNCTION: May help direct the assembly of the nuclear lamina and CC thereby help maintain the structural organization of the nuclear CC envelope. Possible receptor for attachment of lamin filaments to the CC inner nuclear membrane. May be involved in the control of initiation of CC DNA replication through its interaction with NAKAP95. CC -!- FUNCTION: Thymopoietin (TP) and Thymopentin (TP5) may play a role in T- CC cell development and function. TP5 is an immunomodulating pentapeptide. CC -!- SUBUNIT: Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and CC chromosomes (By similarity). Isoform Zeta interacts with BANF1/BAF and CC may sequester it in the cytoplasm. {ECO:0000250, CC ECO:0000269|PubMed:12538639, ECO:0000269|PubMed:9490046}. CC -!- INTERACTION: CC P42167; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-455283, EBI-712073; CC P42167; Q8WZ60: KLHL6; NbExp=3; IntAct=EBI-455283, EBI-6426464; CC P42167; P16333: NCK1; NbExp=2; IntAct=EBI-455283, EBI-389883; CC P42167; P27105: STOM; NbExp=3; IntAct=EBI-455283, EBI-1211440; CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II CC membrane protein. Note=Tightly associated with the nuclear lamina. CC -!- SUBCELLULAR LOCATION: [Isoform Zeta]: Cytoplasm CC {ECO:0000269|PubMed:18403046}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=Beta; CC IsoId=P42167-1; Sequence=Displayed; CC Name=Alpha; CC IsoId=P42166-1; Sequence=External; CC Name=Gamma; CC IsoId=P42167-2; Sequence=VSP_004456; CC Name=Zeta; CC IsoId=P42167-3; Sequence=VSP_056162, VSP_056163; CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Most abundant in adult CC thymus and fetal liver. CC -!- DOMAIN: Has two structurally independent, non-interacting domains: LEM- CC like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C or LEM- CC B). LEM-like binds DNA while LEM interacts with BANF1. CC -!- PTM: Mitosis-specific phosphorylation specifically abolishes its CC binding to lamin B and chromosomes. {ECO:0000250}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}. 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 -!- MISCELLANEOUS: [Isoform Zeta]: Inhibits LAP2beta-mediated repression. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}. 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; U09087; AAB60330.1; -; mRNA. DR EMBL; U09088; AAB60331.1; -; mRNA. DR EMBL; EF028063; ABL61272.1; -; mRNA. DR EMBL; AF070631; AAC25390.1; -; mRNA. DR EMBL; BC053675; AAH53675.1; -; mRNA. DR EMBL; U18269; AAB60434.1; -; Genomic_DNA. DR EMBL; U18266; AAB60434.1; JOINED; Genomic_DNA. DR EMBL; U18267; AAB60434.1; JOINED; Genomic_DNA. DR EMBL; U18268; AAB60434.1; JOINED; Genomic_DNA. DR EMBL; U18270; AAB60434.1; JOINED; Genomic_DNA. DR EMBL; U18271; AAB60435.1; -; Genomic_DNA. DR CCDS; CCDS31879.1; -. [P42167-1] DR CCDS; CCDS31880.1; -. [P42167-2] DR PIR; B55741; B55741. DR PIR; C55741; C55741. DR RefSeq; NP_001027454.1; NM_001032283.2. [P42167-1] DR RefSeq; NP_001027455.1; NM_001032284.2. [P42167-2] DR RefSeq; NP_001294904.1; NM_001307975.1. DR AlphaFoldDB; P42167; -. DR BMRB; P42167; -. DR SMR; P42167; -. DR BioGRID; 112967; 754. DR CORUM; P42167; -. DR DIP; DIP-43686N; -. DR IntAct; P42167; 78. DR MINT; P42167; -. DR iPTMnet; P42167; -. DR MetOSite; P42167; -. DR PhosphoSitePlus; P42167; -. DR SwissPalm; P42167; -. DR BioMuta; TMPO; -. DR DMDM; 1174690; -. DR EPD; P42167; -. DR jPOST; P42167; -. DR MassIVE; P42167; -. DR MaxQB; P42167; -. DR PeptideAtlas; P42167; -. DR ProteomicsDB; 55489; -. [P42167-1] DR ProteomicsDB; 55490; -. [P42167-2] DR Pumba; P42167; -. DR TopDownProteomics; P42167-1; -. [P42167-1] DR TopDownProteomics; P42167-2; -. [P42167-2] DR Antibodypedia; 2387; 456 antibodies from 37 providers. DR DNASU; 7112; -. DR Ensembl; ENST00000261210.9; ENSP00000261210.5; ENSG00000120802.14. [P42167-3] DR Ensembl; ENST00000393053.6; ENSP00000376773.2; ENSG00000120802.14. [P42167-2] DR Ensembl; ENST00000556029.6; ENSP00000450627.1; ENSG00000120802.14. [P42167-1] DR GeneID; 7112; -. DR KEGG; hsa:7112; -. DR MANE-Select; ENST00000556029.6; ENSP00000450627.1; NM_001032283.3; NP_001027454.1. DR UCSC; uc001tfi.3; human. [P42167-1] 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_P42167; -. DR OpenTargets; ENSG00000120802; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR PharmGKB; PA36576; -. DR VEuPathDB; HostDB:ENSG00000120802; -. DR GeneTree; ENSGT00940000154098; -. DR HOGENOM; CLU_097968_0_0_1; -. DR OMA; TETLWTS; -. DR OrthoDB; 5403043at2759; -. DR PathwayCommons; P42167; -. DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown. [P42167-1] DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation. [P42167-1] DR Reactome; R-HSA-4419969; Depolymerization of the Nuclear Lamina. [P42167-1] DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013106; RHOC GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013405; RHOD GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR SignaLink; P42167; -. DR BioGRID-ORCS; 7112; 21 hits in 1159 CRISPR screens. DR ChiTaRS; TMPO; human. DR GenomeRNAi; 7112; -. DR Pharos; P42167; Tbio. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000120802; Expressed in ventricular zone and 200 other cell types or tissues. DR ExpressionAtlas; P42167; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL. DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. 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; 1.10.720.40; -; 2. DR InterPro; IPR013146; LEM-like_dom. DR InterPro; IPR011015; LEM/LEM-like_dom_sf. DR InterPro; IPR003887; LEM_dom. DR PANTHER; PTHR12019:SF23; LAMINA-ASSOCIATED POLYPEPTIDE 2, ISOFORM BETA; 1. DR PANTHER; PTHR12019; LAMINA-ASSOCIATED POLYPEPTIDE THYMOPOIETIN; 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; P42167; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Citrullination; Cytoplasm; DNA-binding; KW Isopeptide bond; Membrane; Methylation; Nucleus; Pharmaceutical; KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1..454 FT /note="Lamina-associated polypeptide 2, isoforms FT beta/gamma" FT /id="PRO_0000045841" FT PEPTIDE 1..50 FT /note="Thymopoietin" FT /id="PRO_0000017677" FT PEPTIDE 33..37 FT /note="Thymopentin" FT /id="PRO_0000017678" FT TRANSMEM 411..434 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 435..454 FT /note="Lumenal" FT /evidence="ECO:0000255" 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 1..410 FT /note="Nucleoplasmic" FT /evidence="ECO:0000255" FT REGION 47..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 49..108 FT /note="Linker" FT REGION 138..243 FT /note="NAKAP95-binding N" FT REGION 149..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..371 FT /note="Binds lamins B" FT REGION 300..374 FT /note="NAKAP95-binding C" 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..214 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..251 FT /note="Polar 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:Q61029" FT MOD_RES 88 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q61029" 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:Q61029" 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:Q61029" FT MOD_RES 168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 207 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61029" FT MOD_RES 211 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 254 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 306 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17693683, 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 ECO:0007744|PubMed:24275569" FT MOD_RES 312 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 315 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 320 FT /note="Citrulline" FT /evidence="ECO:0000250" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 389 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q61029" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 401 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 222..330 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:7517549, ECO:0000303|Ref.3" FT /id="VSP_004456" FT VAR_SEQ 222..248 FT /note="SYSQAGITETEWTSGSSKGGPLQALTR -> VSLVLLPPCTGINNLLTTLIH FT VLAFNG (in isoform Zeta)" FT /evidence="ECO:0000303|PubMed:18403046" FT /id="VSP_056162" FT VAR_SEQ 249..454 FT /note="Missing (in isoform Zeta)" FT /evidence="ECO:0000303|PubMed:18403046" FT /id="VSP_056163" FT VARIANT 287 FT /note="A -> P (in dbSNP:rs7133258)" FT /id="VAR_049779" FT VARIANT 427 FT /note="L -> F (in dbSNP:rs1058288)" FT /id="VAR_014786" SQ SEQUENCE 454 AA; 50670 MW; 03277C5723117909 CRC64; MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLPAGTNSK GPPDFSSDEE REPTPVLGSG AAAAGRSRAA VGRKATKKTD KPRQEDKDDL DVTELTNEDL LDQLVKYGVN PGPIVGTTRK LYEKKLLKLR EQGTESRSST PLPTISSSAE NTRQNGSNDS DRYSDNEEDS KIELKLEKRE PLKGRAKTPV TLKQRRVEHN QSYSQAGITE TEWTSGSSKG GPLQALTRES TRGSRRTPRK RVETSEHFRI DGPVISESTP IAETIMASSN ESLVVNRVTG NFKHASPILP ITEFSDIPRR APKKPLTRAE VGEKTEERRV ERDILKEMFP YEASTPTGIS ASCRRPIKGA AGRPLELSDF RMEESFSSKY VPKYVPLADV KSEKTKKGRS IPVWIKILLF VVVAVFLFLV YQAMETNQVN PFSNFLHVDP RKSN //