LAP2B_MOUSE
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 03-AUG-2022, entry version 181.
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, 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 [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; 13.
DR IntAct; Q61029; 4.
DR iPTMnet; Q61029; -.
DR PhosphoSitePlus; Q61029; -.
DR SwissPalm; Q61029; -.
DR EPD; Q61029; -.
DR jPOST; Q61029; -.
DR MaxQB; Q61029; -.
DR PeptideAtlas; Q61029; -.
DR PRIDE; Q61029; -.
DR ProteomicsDB; 264967; -. [Q61029-1]
DR ProteomicsDB; 264968; -. [Q61029-2]
DR ProteomicsDB; 264969; -. [Q61029-3]
DR ProteomicsDB; 264970; -. [Q61029-4]
DR TopDownProteomics; Q61029-1; -. [Q61029-1]
DR Antibodypedia; 2387; 408 antibodies from 37 providers.
DR DNASU; 21917; -.
DR Ensembl; ENSMUST00000072239; ENSMUSP00000072092; ENSMUSG00000019961. [Q61029-1]
DR Ensembl; ENSMUST00000092219; ENSMUSP00000089864; ENSMUSG00000019961. [Q61029-3]
DR Ensembl; ENSMUST00000099355; ENSMUSP00000096956; ENSMUSG00000019961. [Q61029-2]
DR Ensembl; ENSMUST00000105293; ENSMUSP00000100930; ENSMUSG00000019961. [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 CTD; 7112; -.
DR MGI; MGI:106920; Tmpo.
DR VEuPathDB; HostDB:ENSMUSG00000019961; -.
DR GeneTree; ENSGT00940000154098; -.
DR HOGENOM; CLU_032534_1_0_1; -.
DR OMA; METTSIN; -.
DR BioGRID-ORCS; 21917; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmpo; mouse.
DR Proteomes; UP000000589; Chromosome 10.
DR Bgee; ENSMUSG00000019961; Expressed in ectoderm and 276 other tissues.
DR ExpressionAtlas; Q61029; baseline and differential.
DR Genevisible; Q61029; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 transcription, DNA-templated; IDA:MGI.
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; 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; AAC52574/AAC52575/AAC52576/
FT AAC52577)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..424
FT /note="VAV -> GAC (in Ref. 1; AAC52574/AAC52575/AAC52576/
FT 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
