LAP2A_MOUSE
ID LAP2A_MOUSE Reviewed; 693 AA.
AC Q61033; B2RUB9; Q61028;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Lamina-associated polypeptide 2, isoforms alpha/zeta;
DE AltName: Full=Thymopoietin isoforms alpha/zeta;
DE Short=TP alpha/zeta;
GN Name=Tmpo; Synonyms=Lap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON AND
RP ZETA).
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Thymus;
RX PubMed=8743987; DOI=10.1101/gr.6.5.361;
RA Berger R., Theodor L., Shoham J., Gokkel E., Brok-Simoni F., Avraham K.B.,
RA Copeland N.G., Jenkins N.A., Rechavi G., Simon A.J.;
RT "The characterization and localization of the mouse thymopoietin/lamina-
RT associated polypeptide 2 gene and its alternatively spliced products.";
RL Genome Res. 6:361-370(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; THR-159
RP AND SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-82;
RP THR-153; SER-155; SER-158; THR-159; SER-165; SER-167; SER-420 AND SER-422,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 (ISOFORM ZETA), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-85; ARG-87 AND ARG-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 459-693, IDENTIFICATION BY MASS
RP SPECTROMETRY, DOMAIN, INTERACTION WITH LMNA, AND SUBUNIT.
RX PubMed=17562312; DOI=10.1016/j.str.2007.04.007;
RA Bradley C.M., Jones S., Huang Y., Suzuki Y., Kvaratskhelia M.,
RA Hickman A.B., Craigie R., Dyda F.;
RT "Structural basis for dimerization of LAP2alpha, a component of the nuclear
RT lamina.";
RL Structure 15:643-653(2007).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Interacts with LMNA, BANF1 and RB1 and with
CC chromosomes. Associates directly or indirectly with lamins at specific
CC cell-cycle stages (By similarity). Interacts with CMTM6 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P42166}.
CC -!- INTERACTION:
CC Q61033-1; Q61033-1: Tmpo; NbExp=3; IntAct=EBI-15641551, EBI-15641551;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Expressed diffusely throughout the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Alpha;
CC IsoId=Q61033-1; Sequence=Displayed;
CC Name=Zeta;
CC IsoId=Q61033-2; Sequence=VSP_010128, VSP_010129;
CC Name=Beta;
CC IsoId=Q61029-1; Sequence=External;
CC Name=Delta;
CC IsoId=Q61029-2; Sequence=External;
CC Name=Epsilon;
CC IsoId=Q61029-3; Sequence=External;
CC Name=Gamma;
CC IsoId=Q61029-4; Sequence=External;
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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain forms a four-stranded coiled coil.
CC {ECO:0000269|PubMed:17562312}.
CC -!- PTM: Phosphorylated in a mitose-specific manner. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
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DR EMBL; U39073; AAC52573.1; -; mRNA.
DR EMBL; U39078; AAC52578.1; -; mRNA.
DR EMBL; CH466539; EDL21530.1; -; Genomic_DNA.
DR EMBL; BC141062; AAI41063.1; -; mRNA.
DR CCDS; CCDS24122.1; -. [Q61033-1]
DR RefSeq; NP_035735.2; NM_011605.3. [Q61033-1]
DR PDB; 2V0X; X-ray; 2.20 A; A/B=459-693.
DR PDBsum; 2V0X; -.
DR AlphaFoldDB; Q61033; -.
DR SMR; Q61033; -.
DR BioGRID; 204234; 13.
DR DIP; DIP-29323N; -.
DR IntAct; Q61033; 4.
DR MINT; Q61033; -.
DR STRING; 10090.ENSMUSP00000020123; -.
DR iPTMnet; Q61033; -.
DR SwissPalm; Q61033; -.
DR EPD; Q61033; -.
DR jPOST; Q61033; -.
DR MaxQB; Q61033; -.
DR PaxDb; Q61033; -.
DR PeptideAtlas; Q61033; -.
DR PRIDE; Q61033; -.
DR ProteomicsDB; 264965; -. [Q61033-1]
DR ProteomicsDB; 264966; -. [Q61033-2]
DR Antibodypedia; 2387; 408 antibodies from 37 providers.
DR DNASU; 21917; -.
DR Ensembl; ENSMUST00000020123; ENSMUSP00000020123; ENSMUSG00000019961. [Q61033-1]
DR GeneID; 21917; -.
DR UCSC; uc007gtu.2; mouse. [Q61033-2]
DR UCSC; uc007gtv.2; mouse. [Q61033-1]
DR CTD; 7112; -.
DR MGI; MGI:106920; Tmpo.
DR VEuPathDB; HostDB:ENSMUSG00000019961; -.
DR eggNOG; ENOG502QWCI; Eukaryota.
DR GeneTree; ENSGT00940000154098; -.
DR HOGENOM; CLU_397364_0_0_1; -.
DR InParanoid; Q61033; -.
DR OrthoDB; 323585at2759; -.
DR TreeFam; TF328426; -.
DR BioGRID-ORCS; 21917; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmpo; mouse.
DR EvolutionaryTrace; Q61033; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61033; protein.
DR Bgee; ENSMUSG00000019961; Expressed in ectoderm and 276 other tissues.
DR ExpressionAtlas; Q61033; baseline and differential.
DR Genevisible; Q61033; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.10.720.40; -; 2.
DR InterPro; IPR021623; LAP2alpha_C.
DR InterPro; IPR013146; LEM-like_dom.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR Pfam; PF11560; LAP2alpha; 1.
DR Pfam; PF03020; LEM; 1.
DR Pfam; PF08198; Thymopoietin; 1.
DR SMART; SM00540; LEM; 1.
DR SMART; SM01261; Thymopoietin; 1.
DR SUPFAM; SSF63451; SSF63451; 2.
DR PROSITE; PS50954; LEM; 1.
DR PROSITE; PS50955; LEM_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; Coiled coil;
KW DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..693
FT /note="Lamina-associated polypeptide 2, isoforms
FT alpha/zeta"
FT /id="PRO_0000206145"
FT DOMAIN 5..48
FT /note="LEM-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313,
FT ECO:0000255|PROSITE-ProRule:PRU00314"
FT DOMAIN 108..152
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 48..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..107
FT /note="Linker"
FT REGION 148..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..656
FT MOTIF 190..196
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 92..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 85
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 329
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42166"
FT VAR_SEQ 188..225
FT /note="GKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEI -> DSKIELKLEK
FT REPLKGRAKTPVTLKQRRTEHNQVFVVL (in isoform Zeta)"
FT /evidence="ECO:0000303|PubMed:8743987"
FT /id="VSP_010128"
FT VAR_SEQ 226..693
FT /note="Missing (in isoform Zeta)"
FT /evidence="ECO:0000303|PubMed:8743987"
FT /id="VSP_010129"
FT CONFLICT 72..73
FT /note="EP -> DA (in Ref. 1; AAC52573/AAC52578)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..265
FT /note="KGQT -> RGRP (in Ref. 1; AAC52578)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..281
FT /note="SS -> LC (in Ref. 1; AAC52578)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..324
FT /note="DIV -> EHS (in Ref. 1; AAC52578)"
FT /evidence="ECO:0000305"
FT CONFLICT 393..394
FT /note="GT -> RS (in Ref. 1; AAC52578)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="D -> I (in Ref. 1; AAC52578)"
FT /evidence="ECO:0000305"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:2V0X"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:2V0X"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 524..530
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 537..541
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 558..604
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 610..654
FT /evidence="ECO:0007829|PDB:2V0X"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:2V0X"
FT HELIX 661..669
FT /evidence="ECO:0007829|PDB:2V0X"
FT STRAND 674..678
FT /evidence="ECO:0007829|PDB:2V0X"
FT MOD_RES Q61033-2:206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 693 AA; 75168 MW; 00604F3B66FF63F3 CRC64;
MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK
GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK PRLEDKDDLD VTELSNEELL
DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGTESRSSTP LPTVSSSAEN TRQNGSNDSD
RYSDNDEGKK KEHKKVKSAR DCVPFSELAS TPSGAFFQGI SFPEISTRPP LGRTELQAAK
KVQTTKRDPP RETCTDTALP GKGQTHKLAP GRSLFIPSES SYDRCVEKSS SPSSQREFAA
RLVSAAASPS LIRETTTTYS KDIVENICRG GKSRAQPLRA EEPGVSDQSV FSSEREVLQE
SERSQVISPP LAQAIRDYVN SLLVQGGVGS LPGTSDSVPT LDVENICKRL SQSSYQDSES
LSPPRKVPRL SEKPARGGDS GSCVAFQNTP GSEHRSSFAK SVVSHSLTTL GVEVSKPPPQ
HDKIEASEPS FPLHESILKV VEEEWQQIDR QLPSVACRYP VSSIEAARIL SVPKVDDEIL
GFISEATPRA ATQASSTESC DKHLDLALCR SYEAAASALQ IAAHTAFVAK SLQADISQAA
QIINSDPSDA QQALRILNRT YDAASYLCDA AFDEVRMSAC AMGSSTMGRR YLWLKDCKIS
PASKNKLTVA PFKGGTLFGG EVHKVIKKRG NKQ
