ID   LAP2B_MOUSE             Reviewed;         452 AA.
AC   Q61029; Q3UCI5; Q61030; Q61031; Q61032;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Lamina-associated polypeptide 2, isoforms beta/delta/epsilon/gamma;
DE   AltName: Full=Thymopoietin isoforms beta/delta/epsilon/gamma;
DE            Short=TP beta/delta/epsilon/gamma;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 61-85 AND 173-194 (ISOFORM BETA), PHOSPHORYLATION AT
RP   THR-74; THR-159; SER-176 AND SER-179, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=10413518; DOI=10.1021/bi990645f;
RA   Dreger M., Otto H., Neubauer G., Mann M., Hucho F.;
RT   "Identification of phosphorylation sites in native lamina-associated
RT   polypeptide 2 beta.";
RL   Biochemistry 38:9426-9434(1999).
RN   [5]
RP   INTERACTION WITH BANF1.
RX   PubMed=10393804; DOI=10.1242/jcs.112.15.2485;
RA   Furukawa K.;
RT   "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-
RT   chromatin interaction.";
RL   J. Cell Sci. 112:2485-2492(1999).
RN   [6]
RP   INTERACTION WITH GMCL.
RX   PubMed=11591818; DOI=10.1242/jcs.114.18.3297;
RA   Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Berger R., Shaklai S., Amariglio N., Brok-Simoni F.,
RA   Simon A.J., Rechavi G.;
RT   "Nuclear membrane protein LAP2beta mediates transcriptional repression
RT   alone and together with its binding partner GCL (germ-cell-less).";
RL   J. Cell Sci. 114:3297-3307(2001).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74 AND
RP   THR-159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [9]
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   [10]
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   [11]
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-305; SER-306 AND
RP   SER-361, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-388, 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   [13]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-85 AND ARG-87, AND IDENTIFICATION
RP   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   [14]
RP   CITRULLINATION AT ARG-319.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LMNB1, LMNB2, BANF1, AKAP8L, GMCL and
CC       chromosomes. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q61029; Q64321: Zbtb7b; NbExp=2; IntAct=EBI-6172136, EBI-642868;
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Tightly associated with the nuclear lamina. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=Beta;
CC         IsoId=Q61029-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=Q61033-1; Sequence=External;
CC       Name=Zeta;
CC         IsoId=Q61033-2; Sequence=External;
CC       Name=Delta;
CC         IsoId=Q61029-2; Sequence=VSP_010131;
CC       Name=Epsilon;
CC         IsoId=Q61029-3; Sequence=VSP_010130;
CC       Name=Gamma;
CC         IsoId=Q61029-4; Sequence=VSP_010132;
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Mitosis-specific phosphorylation specifically abolishes its
CC       binding to lamin B and chromosomes. {ECO:0000250}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC   -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
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DR   EMBL; U39074; AAC52574.1; -; mRNA.
DR   EMBL; U39075; AAC52575.1; -; mRNA.
DR   EMBL; U39076; AAC52576.1; -; mRNA.
DR   EMBL; U39077; AAC52577.1; -; mRNA.
DR   EMBL; AK150305; BAE29455.1; -; mRNA.
DR   EMBL; AK150515; BAE29627.1; -; mRNA.
DR   EMBL; AK153281; BAE31865.1; -; mRNA.
DR   EMBL; AK165851; BAE38413.1; -; mRNA.
DR   EMBL; CH466539; EDL21533.1; -; Genomic_DNA.
DR   CCDS; CCDS36032.1; -. [Q61029-4]
DR   CCDS; CCDS36033.1; -. [Q61029-2]
DR   CCDS; CCDS36034.1; -. [Q61029-3]
DR   CCDS; CCDS36035.1; -. [Q61029-1]
DR   RefSeq; NP_001073598.1; NM_001080129.2. [Q61029-1]
DR   RefSeq; NP_001073600.1; NM_001080131.2. [Q61029-2]
DR   RefSeq; NP_001073601.1; NM_001080132.2. [Q61029-4]
DR   AlphaFoldDB; Q61029; -.
DR   BioGRID; 204234; 15.
DR   IntAct; Q61029; 4.
DR   ChEMBL; CHEMBL4879470; -.
DR   iPTMnet; Q61029; -.
DR   PhosphoSitePlus; Q61029; -.
DR   SwissPalm; Q61029; -.
DR   EPD; Q61029; -.
DR   jPOST; Q61029; -.
DR   MaxQB; Q61029; -.
DR   PeptideAtlas; Q61029; -.
DR   ProteomicsDB; 264967; -. [Q61029-1]
DR   ProteomicsDB; 264968; -. [Q61029-2]
DR   ProteomicsDB; 264969; -. [Q61029-3]
DR   ProteomicsDB; 264970; -. [Q61029-4]
DR   Pumba; Q61029; -.
DR   TopDownProteomics; Q61029-1; -. [Q61029-1]
DR   Antibodypedia; 2387; 456 antibodies from 37 providers.
DR   DNASU; 21917; -.
DR   Ensembl; ENSMUST00000072239.14; ENSMUSP00000072092.8; ENSMUSG00000019961.18. [Q61029-1]
DR   Ensembl; ENSMUST00000092219.14; ENSMUSP00000089864.7; ENSMUSG00000019961.18. [Q61029-3]
DR   Ensembl; ENSMUST00000099355.12; ENSMUSP00000096956.5; ENSMUSG00000019961.18. [Q61029-2]
DR   Ensembl; ENSMUST00000105293.11; ENSMUSP00000100930.4; ENSMUSG00000019961.18. [Q61029-4]
DR   GeneID; 21917; -.
DR   KEGG; mmu:21917; -.
DR   UCSC; uc007gtq.2; mouse. [Q61029-1]
DR   UCSC; uc007gts.2; mouse. [Q61029-2]
DR   UCSC; uc007gtt.2; mouse. [Q61029-4]
DR   AGR; MGI:106920; -.
DR   CTD; 7112; -.
DR   MGI; MGI:106920; Tmpo.
DR   VEuPathDB; HostDB:ENSMUSG00000019961; -.
DR   GeneTree; ENSGT00940000154098; -.
DR   HOGENOM; CLU_032534_1_0_1; -.
DR   OMA; TETLWTS; -.
DR   OrthoDB; 5403043at2759; -.
DR   BioGRID-ORCS; 21917; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Tmpo; mouse.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000019961; Expressed in ectoderm and 279 other cell types or tissues.
DR   ExpressionAtlas; Q61029; baseline and differential.
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:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
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; Q61029; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; Citrullination;
KW   Direct protein sequencing; DNA-binding; Isopeptide bond; Membrane;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..452
FT                   /note="Lamina-associated polypeptide 2, isoforms
FT                   beta/delta/epsilon/gamma"
FT                   /id="PRO_0000206146"
FT   TRANSMEM        410..430
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..452
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..409
FT                   /note="Nucleoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          48..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..108
FT                   /note="Linker"
FT   REGION          137..242
FT                   /note="NAKAP95-binding N"
FT   REGION          149..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..370
FT                   /note="Binds lamins B"
FT   REGION          299..373
FT                   /note="NAKAP95-binding C"
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..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
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:0000269|PubMed:10413518,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
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:0000269|PubMed:10413518,
FT                   ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
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         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:10413518"
FT   MOD_RES         179
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:10413518"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         206
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         210
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         311
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         319
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   MOD_RES         388
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   CROSSLNK        400
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P42167"
FT   VAR_SEQ         221..329
FT                   /note="Missing (in isoform Gamma)"
FT                   /evidence="ECO:0000303|PubMed:8743987"
FT                   /id="VSP_010132"
FT   VAR_SEQ         221..292
FT                   /note="Missing (in isoform Delta)"
FT                   /evidence="ECO:0000303|PubMed:8743987"
FT                   /id="VSP_010131"
FT   VAR_SEQ         221..260
FT                   /note="Missing (in isoform Epsilon)"
FT                   /evidence="ECO:0000303|PubMed:8743987"
FT                   /id="VSP_010130"
FT   CONFLICT        72..73
FT                   /note="EP -> DA (in Ref. 1;
FT                   AAC52574/AAC52575/AAC52576/AAC52577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        422..424
FT                   /note="VAV -> GAC (in Ref. 1;
FT                   AAC52574/AAC52575/AAC52576/AAC52577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   452 AA;  50373 MW;  132AF11B458DCFBA CRC64;
     MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK
     GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK PRLEDKDDLD VTELSNEELL
     DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGTESRSSTP LPTVSSSAEN TRQNGSNDSD
     RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ SYSQAGVTET EWTSGSSTGG
     PLQALTREST RGSRRTPRKR VETSQHFRID GAVISESTPI AETIKASSNE SLVANRLTGN
     FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVD RDILKEMFPY EASTPTGISA
     SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYAPLADVK SEKTKKRRSV PMWIKMLLFA
     LVAVFLFLVY QAMETNQGNP FTNFLQDTKI SN
//