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Lamina-associated polypeptide 2, isoforms beta/gamma (Thymopoietin, isoforms beta/gamma) (TP beta/gamma) (Thymopoietin-related peptide isoforms beta/gamma) (TPRP isoforms beta/gamma) [Cleaved into: Thymopoietin (TP) (Splenin); Thymopentin (TP5)]

 LAP2B_HUMAN             Reviewed;         454 AA.
P42167; A2T926; Q14861;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 191.
RecName: Full=Lamina-associated polypeptide 2, isoforms beta/gamma;
AltName: Full=Thymopoietin, isoforms beta/gamma;
Short=TP beta/gamma;
AltName: Full=Thymopoietin-related peptide isoforms beta/gamma;
Short=TPRP isoforms beta/gamma;
Contains:
RecName: Full=Thymopoietin;
Short=TP;
AltName: Full=Splenin;
Contains:
RecName: Full=Thymopentin;
AltName: Full=TP5;
Name=TMPO; Synonyms=LAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
TISSUE=Thymus;
PubMed=7517549; DOI=10.1073/pnas.91.14.6283;
Harris C.A., Andryuk P.J., Cline S.W., Chan H.K., Natarajan A.,
Siekierka J.J., Goldstein G.;
"Three distinct human thymopoietins are derived from alternatively
spliced mRNAs.";
Proc. Natl. Acad. Sci. U.S.A. 91:6283-6287(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA), AND SUBCELLULAR LOCATION
(ISOFORM ZETA).
PubMed=18403046; DOI=10.1016/j.ejcb.2008.01.014;
Shaklai S., Somech R., Gal-Yam E.N., Deshet-Unger N.,
Moshitch-Moshkovitz S., Hirschberg K., Amariglio N., Simon A.J.,
Rechavi G.;
"LAP2zeta binds BAF and suppresses LAP2beta-mediated transcriptional
repression.";
Eur. J. Cell Biol. 87:267-278(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA).
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-237 AND 313-454 (ISOFORMS BETA
AND GAMMA).
PubMed=8530026; DOI=10.1006/geno.1995.1131;
Harris C.A., Andryuk P.J., Cline S.W., Siekierka J.J., Goldstein G.;
"Structure and mapping of the human thymopoietin (TMPO) gene and
relationship of human TMPO beta to rat lamin-associated polypeptide
2.";
Genomics 28:198-205(1995).
[7]
INTERACTION WITH LMNB1.
PubMed=9490046; DOI=10.1046/j.1432-1327.1998.2510729.x;
Furukawa K., Kondo T.;
"Identification of the lamina-associated-polypeptide-2-binding domain
of B-type lamin.";
Eur. J. Biochem. 251:729-733(1998).
[8]
INTERACTION WITH AKAP8L.
PubMed=12538639; DOI=10.1083/jcb.200210026;
Martins S., Eikvar S., Furukawa K., Collas P.;
"HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope
interaction implicated in initiation of DNA replication.";
J. Cell Biol. 160:177-188(2003).
[9]
TOPOLOGY.
PubMed=10806084; DOI=10.1006/jsbi.2000.4212;
Dechat T., Vlcek S., Foisner R.;
"Review: lamina-associated polypeptide 2 isoforms and related proteins
in cell cycle-dependent nuclear structure dynamics.";
J. Struct. Biol. 129:335-345(2000).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-306 AND SER-315,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-306, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-66; SER-67;
THR-74; SER-79; THR-160; THR-164; SER-177; SER-180; SER-306; SER-315;
SER-362 AND SER-385, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74;
SER-79; THR-154; THR-160; SER-292 AND SER-306, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-156; THR-160;
THR-211; SER-265; SER-306; THR-312 AND SER-315, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND THR-74, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74;
SER-79; SER-156; THR-160; THR-164; SER-168; SER-180; SER-184; SER-190;
SER-222; SER-224; SER-250; SER-254; SER-265; SER-306; SER-315;
SER-378; SER-385 AND SER-402, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74;
THR-160 AND SER-306, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
STRUCTURE BY NMR OF 1-169.
PubMed=11500367; DOI=10.1093/emboj/20.16.4399;
Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M.;
"Solution structure of the constant region of nuclear envelope protein
LAP2 reveals two LEM-domain structures: one binds BAF and the other
binds DNA.";
EMBO J. 20:4399-4407(2001).
[29]
STRUCTURE BY NMR OF 1-57 AND 103-159.
PubMed=11435115; DOI=10.1016/S0969-2126(01)00611-6;
Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K.,
Callebaut I., Worman H.J., Zinn-Justin S.;
"Structural characterization of the LEM motif common to three human
inner nuclear membrane proteins.";
Structure 9:503-511(2001).
-!- FUNCTION: May help direct the assembly of the nuclear lamina and
thereby help maintain the structural organization of the nuclear
envelope. Possible receptor for attachment of lamin filaments to
the inner nuclear membrane. May be involved in the control of
initiation of DNA replication through its interaction with
NAKAP95.
-!- FUNCTION: Thymopoietin (TP) and Thymopentin (TP5) may play a role
in T-cell development and function. TP5 is an immunomodulating
pentapeptide.
-!- SUBUNIT: Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and
chromosomes (By similarity). Isoform Zeta interacts with BANF1/BAF
and may sequester it in the cytoplasm. {ECO:0000250,
ECO:0000269|PubMed:12538639, ECO:0000269|PubMed:9490046}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-455283, EBI-389883;
-!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II
membrane protein. Note=Tightly associated with the nuclear lamina.
-!- SUBCELLULAR LOCATION: Isoform Zeta: Cytoplasm
{ECO:0000269|PubMed:18403046}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=Beta;
IsoId=P42167-1; Sequence=Displayed;
Name=Alpha;
IsoId=P42166-1; Sequence=External;
Name=Gamma;
IsoId=P42167-2; Sequence=VSP_004456;
Name=Zeta;
IsoId=P42167-3; Sequence=VSP_056162, VSP_056163;
Note=Inhibits LAP2beta-mediated repression.;
-!- TISSUE SPECIFICITY: Expressed in many tissues. Most abundant in
adult thymus and fetal liver.
-!- DOMAIN: Has two structurally independent, non-interacting domains:
LEM-like (also called LAP2-N or LEM-D) and LEM (also called LAP2-C
or LEM-B). LEM-like binds DNA while LEM interacts with BANF1.
-!- PTM: Mitosis-specific phosphorylation specifically abolishes its
binding to lamin B and chromosomes. {ECO:0000250}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- PHARMACEUTICAL: TP5 is available under the names Timunox (Cilag),
Sintomodulina (Italofarmaco) and Mepentil (Recordati). Used in
primary and secondary immune deficiencies, autoimmunity,
infections and cancer.
-!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
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EMBL; U09087; AAB60330.1; -; mRNA.
EMBL; U09088; AAB60331.1; -; mRNA.
EMBL; EF028063; ABL61272.1; -; mRNA.
EMBL; AF070631; AAC25390.1; -; mRNA.
EMBL; BC053675; AAH53675.1; -; mRNA.
EMBL; U18269; AAB60434.1; -; Genomic_DNA.
EMBL; U18266; AAB60434.1; JOINED; Genomic_DNA.
EMBL; U18267; AAB60434.1; JOINED; Genomic_DNA.
EMBL; U18268; AAB60434.1; JOINED; Genomic_DNA.
EMBL; U18270; AAB60434.1; JOINED; Genomic_DNA.
EMBL; U18271; AAB60435.1; -; Genomic_DNA.
CCDS; CCDS31879.1; -. [P42167-1]
CCDS; CCDS31880.1; -. [P42167-2]
PIR; B55741; B55741.
PIR; C55741; C55741.
RefSeq; NP_001027454.1; NM_001032283.2. [P42167-1]
RefSeq; NP_001027455.1; NM_001032284.2. [P42167-2]
RefSeq; NP_001294904.1; NM_001307975.1.
UniGene; Hs.11355; -.
ProteinModelPortal; P42167; -.
BioGrid; 112967; 117.
CORUM; P42167; -.
DIP; DIP-43686N; -.
IntAct; P42167; 57.
MINT; P42167; -.
iPTMnet; P42167; -.
PhosphoSitePlus; P42167; -.
SwissPalm; P42167; -.
BioMuta; PLCE1; -.
DMDM; 1174690; -.
EPD; P42167; -.
MaxQB; P42167; -.
PeptideAtlas; P42167; -.
PRIDE; P42167; -.
ProteomicsDB; 55489; -.
ProteomicsDB; 55490; -. [P42167-2]
TopDownProteomics; P42167-1; -. [P42167-1]
TopDownProteomics; P42167-2; -. [P42167-2]
DNASU; 7112; -.
Ensembl; ENST00000261210; ENSP00000261210; ENSG00000120802. [P42167-3]
Ensembl; ENST00000393053; ENSP00000376773; ENSG00000120802. [P42167-2]
Ensembl; ENST00000556029; ENSP00000450627; ENSG00000120802. [P42167-1]
GeneID; 7112; -.
KEGG; hsa:7112; -.
UCSC; uc001tfi.3; human. [P42167-1]
CTD; 7112; -.
DisGeNET; 7112; -.
EuPathDB; HostDB:ENSG00000120802.13; -.
GeneCards; TMPO; -.
GeneReviews; TMPO; -.
HGNC; HGNC:11875; TMPO.
HPA; CAB009847; -.
HPA; HPA008150; -.
MalaCards; TMPO; -.
MIM; 188380; gene.
neXtProt; NX_P42167; -.
OpenTargets; ENSG00000120802; -.
PharmGKB; PA36576; -.
eggNOG; ENOG410IT7C; Eukaryota.
eggNOG; ENOG4111J0N; LUCA.
GeneTree; ENSGT00510000048934; -.
HOGENOM; HOG000113280; -.
HOVERGEN; HBG000166; -.
OMA; TNQGNPF; -.
Reactome; R-HSA-2993913; Clearance of Nuclear Envelope Membranes from Chromatin.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope Reformation.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
ChiTaRS; TMPO; human.
GenomeRNAi; 7112; -.
PMAP-CutDB; P42167; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000120802; Expressed in 223 organ(s), highest expression level in intestine.
CleanEx; HS_TMPO; -.
ExpressionAtlas; P42167; baseline and differential.
Genevisible; P42167; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0005521; F:lamin binding; TAS:ProtInc.
Gene3D; 1.10.720.40; -; 2.
InterPro; IPR013146; LEM-like_dom.
InterPro; IPR011015; LEM/LEM-like_dom_sf.
InterPro; IPR003887; LEM_dom.
Pfam; PF03020; LEM; 1.
Pfam; PF08198; Thymopoietin; 1.
SMART; SM00540; LEM; 1.
SMART; SM01261; Thymopoietin; 1.
SUPFAM; SSF63451; SSF63451; 2.
PROSITE; PS50954; LEM; 1.
PROSITE; PS50955; LEM_LIKE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Citrullination; Complete proteome;
Cytoplasm; DNA-binding; Isopeptide bond; Membrane; Methylation;
Nucleus; Pharmaceutical; Phosphoprotein; Polymorphism;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 454 Lamina-associated polypeptide 2, isoforms
beta/gamma.
/FTId=PRO_0000045841.
PEPTIDE 1 50 Thymopoietin.
/FTId=PRO_0000017677.
PEPTIDE 33 37 Thymopentin.
/FTId=PRO_0000017678.
TRANSMEM 411 434 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 435 454 Lumenal. {ECO:0000255}.
DOMAIN 5 48 LEM-like. {ECO:0000255|PROSITE-
ProRule:PRU00313, ECO:0000255|PROSITE-
ProRule:PRU00314}.
DOMAIN 109 153 LEM. {ECO:0000255|PROSITE-
ProRule:PRU00313}.
REGION 1 410 Nucleoplasmic. {ECO:0000255}.
REGION 49 108 Linker.
REGION 138 243 NAKAP95-binding N.
REGION 299 371 Binds lamins B.
REGION 300 374 NAKAP95-binding C.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 86 86 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 88 88 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 154 154 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 160 160 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 164 164 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 207 207 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 312 312 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 320 320 Citrulline. {ECO:0000250}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 389 389 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61029}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 222 330 Missing (in isoform Gamma).
{ECO:0000303|PubMed:7517549,
ECO:0000303|Ref.3}.
/FTId=VSP_004456.
VAR_SEQ 222 248 SYSQAGITETEWTSGSSKGGPLQALTR -> VSLVLLPPCT
GINNLLTTLIHVLAFNG (in isoform Zeta).
{ECO:0000303|PubMed:18403046}.
/FTId=VSP_056162.
VAR_SEQ 249 454 Missing (in isoform Zeta).
{ECO:0000303|PubMed:18403046}.
/FTId=VSP_056163.
VARIANT 287 287 A -> P (in dbSNP:rs7133258).
/FTId=VAR_049779.
VARIANT 427 427 L -> F (in dbSNP:rs1058288).
/FTId=VAR_014786.
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


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