LAP2B_HUMAN
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 03-AUG-2022, entry version 215.
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}.
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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 BioGRID; 112967; 663.
DR CORUM; P42167; -.
DR DIP; DIP-43686N; -.
DR IntAct; P42167; 72.
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 PRIDE; P42167; -.
DR ProteomicsDB; 55489; -. [P42167-1]
DR ProteomicsDB; 55490; -. [P42167-2]
DR TopDownProteomics; P42167-1; -. [P42167-1]
DR TopDownProteomics; P42167-2; -. [P42167-2]
DR Antibodypedia; 2387; 408 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 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; METTSIN; -.
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; Depolymerisation 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; 17 hits in 1077 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 198 other tissues.
DR ExpressionAtlas; P42167; baseline and differential.
DR Genevisible; P42167; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 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 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
