BCOR_MOUSE
ID BCOR_MOUSE Reviewed; 1759 AA.
AC Q8CGN4; B1AXK3; B1AXK4; B1AXK5; B1AXK6; Q6PDK5; Q6ZPM3; Q8BKF5; Q8CGN1;
AC Q8CGN2; Q8CGN3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=BCL-6 corepressor;
DE Short=BCoR;
GN Name=Bcor; Synonyms=Kiaa1575;
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 1; 2; 3 AND 4), FUNCTION, INTERACTION
RP WITH MLLT3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=12776190; DOI=10.1038/sj.onc.1206361;
RA Srinivasan R.S., de Erkenez A.C., Hemenway C.S.;
RT "The mixed lineage leukemia fusion partner AF9 binds specific isoforms of
RT the BCL-6 corepressor.";
RL Oncogene 22:3395-3406(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-945.
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [6]
RP INTERACTION WITH CPNE4.
RX PubMed=12522145; DOI=10.1074/jbc.m212632200;
RA Tomsig J.L., Snyder S.L., Creutz C.E.;
RT "Identification of targets for calcium signaling through the copine family
RT of proteins. Characterization of a coiled-coil copine-binding motif.";
RL J. Biol. Chem. 278:10048-10054(2003).
RN [7]
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1128; SER-1131; SER-1143 AND
RP SER-1348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Transcriptional corepressor. May specifically inhibit gene
CC expression when recruited to promoter regions by sequence-specific DNA-
CC binding proteins such as BCL6 and MLLT3. This repression may be
CC mediated at least in part by histone deacetylase activities which can
CC associate with this corepressor. Involved in the repression of TFAP2A;
CC impairs binding of BCL6 and KDM2B to TFAP2A promoter regions. Via
CC repression of TFAP2A acts as a negative regulator of osteo-dentiogenic
CC capacity in adult stem cells; the function implies inhibition of
CC methylation on histone H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2) (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12776190}.
CC -!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
CC Isoform 1 may interact with MLLT3/AF9 (PubMed:12776190). Interacts with
CC BCL6; the interaction is direct. Forms ternary complexes with BCL6 and
CC SMRT/NCOR2 on selected target genes promoters; potently repress
CC expression. Can interact with HDAC1, HDAC3 and HDAC5. Interacts with
CC PCGF1; the interaction is direct. Interacts with KDM2B. Component of an
CC approximately 800 kDa repressive BCOR complex at least composed of
CC BCOR, RYBP, PCGF1, RING1, RNF2/RING2, KDM2B and SKP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6W2J9, ECO:0000269|PubMed:12522145,
CC ECO:0000269|PubMed:12776190}.
CC -!- INTERACTION:
CC Q8CGN4; P41183: Bcl6; NbExp=2; IntAct=EBI-1216174, EBI-6253762;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12776190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q8CGN4-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q8CGN4-2; Sequence=VSP_012558;
CC Name=3; Synonyms=C;
CC IsoId=Q8CGN4-3; Sequence=VSP_012559;
CC Name=4; Synonyms=D;
CC IsoId=Q8CGN4-4; Sequence=VSP_012558, VSP_012559;
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, lung, skeletal muscle,
CC spleen and testis. {ECO:0000269|PubMed:12776190}.
CC -!- SIMILARITY: Belongs to the BCOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98208.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY161170; AAN85318.1; -; mRNA.
DR EMBL; AY161171; AAN85319.1; -; mRNA.
DR EMBL; AY161172; AAN85320.1; -; mRNA.
DR EMBL; AY161173; AAN85321.1; -; mRNA.
DR EMBL; AK129398; BAC98208.1; ALT_INIT; mRNA.
DR EMBL; AL808012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058656; AAH58656.1; -; mRNA.
DR EMBL; AK053309; BAC35338.1; -; mRNA.
DR CCDS; CCDS30021.1; -. [Q8CGN4-3]
DR CCDS; CCDS30022.1; -. [Q8CGN4-4]
DR CCDS; CCDS40872.1; -. [Q8CGN4-2]
DR CCDS; CCDS40873.1; -. [Q8CGN4-1]
DR RefSeq; NP_001161793.1; NM_001168321.1. [Q8CGN4-4]
DR RefSeq; NP_083786.2; NM_029510.3. [Q8CGN4-1]
DR RefSeq; NP_778209.2; NM_175044.3. [Q8CGN4-2]
DR RefSeq; NP_778210.2; NM_175045.3. [Q8CGN4-3]
DR RefSeq; NP_778211.2; NM_175046.3. [Q8CGN4-4]
DR RefSeq; XP_017174110.1; XM_017318621.1. [Q8CGN4-1]
DR RefSeq; XP_017174111.1; XM_017318622.1. [Q8CGN4-1]
DR RefSeq; XP_017174112.1; XM_017318623.1. [Q8CGN4-1]
DR RefSeq; XP_017174113.1; XM_017318624.1. [Q8CGN4-1]
DR AlphaFoldDB; Q8CGN4; -.
DR SMR; Q8CGN4; -.
DR BioGRID; 214722; 10.
DR DIP; DIP-29852N; -.
DR IntAct; Q8CGN4; 7.
DR MINT; Q8CGN4; -.
DR STRING; 10090.ENSMUSP00000111175; -.
DR iPTMnet; Q8CGN4; -.
DR PhosphoSitePlus; Q8CGN4; -.
DR EPD; Q8CGN4; -.
DR jPOST; Q8CGN4; -.
DR MaxQB; Q8CGN4; -.
DR PaxDb; Q8CGN4; -.
DR PeptideAtlas; Q8CGN4; -.
DR PRIDE; Q8CGN4; -.
DR ProteomicsDB; 273445; -. [Q8CGN4-1]
DR ProteomicsDB; 273446; -. [Q8CGN4-2]
DR ProteomicsDB; 273447; -. [Q8CGN4-3]
DR ProteomicsDB; 273448; -. [Q8CGN4-4]
DR Antibodypedia; 24949; 302 antibodies from 34 providers.
DR DNASU; 71458; -.
DR Ensembl; ENSMUST00000043441; ENSMUSP00000048024; ENSMUSG00000040363. [Q8CGN4-4]
DR Ensembl; ENSMUST00000065143; ENSMUSP00000068618; ENSMUSG00000040363. [Q8CGN4-3]
DR Ensembl; ENSMUST00000115512; ENSMUSP00000111174; ENSMUSG00000040363. [Q8CGN4-2]
DR Ensembl; ENSMUST00000115513; ENSMUSP00000111175; ENSMUSG00000040363. [Q8CGN4-1]
DR Ensembl; ENSMUST00000124033; ENSMUSP00000116258; ENSMUSG00000040363. [Q8CGN4-4]
DR GeneID; 71458; -.
DR KEGG; mmu:71458; -.
DR UCSC; uc009sqq.2; mouse. [Q8CGN4-1]
DR UCSC; uc009sqr.2; mouse. [Q8CGN4-3]
DR UCSC; uc009sqs.2; mouse. [Q8CGN4-2]
DR UCSC; uc009sqt.2; mouse. [Q8CGN4-4]
DR CTD; 54880; -.
DR MGI; MGI:1918708; Bcor.
DR VEuPathDB; HostDB:ENSMUSG00000040363; -.
DR eggNOG; ENOG502RZ5N; Eukaryota.
DR GeneTree; ENSGT00940000153737; -.
DR HOGENOM; CLU_003863_0_0_1; -.
DR InParanoid; Q8CGN4; -.
DR OMA; CTEEKHP; -.
DR OrthoDB; 85469at2759; -.
DR PhylomeDB; Q8CGN4; -.
DR TreeFam; TF333317; -.
DR BioGRID-ORCS; 71458; 6 hits in 80 CRISPR screens.
DR ChiTaRS; Bcor; mouse.
DR PRO; PR:Q8CGN4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8CGN4; protein.
DR Bgee; ENSMUSG00000040363; Expressed in ectoplacental cone and 244 other tissues.
DR ExpressionAtlas; Q8CGN4; baseline and differential.
DR Genevisible; Q8CGN4; MM.
DR GO; GO:0140261; C:BCOR complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IPI:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISO:MGI.
DR GO; GO:0000415; P:negative regulation of histone H3-K36 methylation; ISO:MGI.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0070171; P:negative regulation of tooth mineralization; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0042476; P:odontogenesis; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; ISO:MGI.
DR GO; GO:0065001; P:specification of axis polarity; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.10.260.40; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR031628; BCOR.
DR InterPro; IPR032365; PUFD.
DR InterPro; IPR038227; PUFD_som_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF15808; BCOR; 1.
DR Pfam; PF16553; PUFD; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Chromatin regulator;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1759
FT /note="BCL-6 corepressor"
FT /id="PRO_0000066979"
FT REPEAT 1466..1499
FT /note="ANK 1"
FT REPEAT 1500..1529
FT /note="ANK 2"
FT REPEAT 1533..1562
FT /note="ANK 3"
FT REGION 100..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..514
FT /note="Interaction with BCL6"
FT /evidence="ECO:0000250"
FT REGION 540..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1752
FT /note="Necessary and sufficient for interaction with PCGF1"
FT /evidence="ECO:0000250"
FT COMPBIAS 103..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 1128
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT CROSSLNK 873
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT CROSSLNK 1259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT CROSSLNK 1417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6W2J9"
FT VAR_SEQ 1005..1022
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12776190,
FT ECO:0000303|PubMed:14621295"
FT /id="VSP_012558"
FT VAR_SEQ 1171..1204
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12776190,
FT ECO:0000303|PubMed:14621295, ECO:0000303|PubMed:15489334"
FT /id="VSP_012559"
FT CONFLICT 161
FT /note="A -> V (in Ref. 1; AAN85318/AAN85319/AAN85320/
FT AAN85321)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="G -> S (in Ref. 1; AAN85318/AAN85319/AAN85320/
FT AAN85321)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="I -> V (in Ref. 1; AAN85318/AAN85319/AAN85320/
FT AAN85321)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="E -> D (in Ref. 5; BAC35338)"
FT /evidence="ECO:0000305"
FT CONFLICT 1424
FT /note="D -> G (in Ref. 1; AAN85318/AAN85319/AAN85320/
FT AAN85321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1759 AA; 192631 MW; C7FF21CFB3C60D49 CRC64;
MLSATPLYGN VHSWMNSERV RMCGTSEDRK IPVNDGDASK ARLELREETP LSHSVVDTSG
AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SGLCGLGSEK GREATPSSLS GLGFSSERNP
EMQFKPNTPE TVEASAVSGK PPNGFSAIYK TPPGIQKSAV ATAESLGLDR PASDKQSPLN
INGASYLRLP WVNPYMEGAT PAIYPFLDSP NKYSLNMYKA LLPQQSYGLA QPLYSPVCTS
GERFLYLPPP HYVNPHIPSS LASPMRLSTP SASAAIPPLV HCSDKSLPWK MGVNPGNPVD
SHSYPHIQNS KQPRVTSAKA VNSGLPGDTA LLLPPSPRPS ARVHLPTQPA AETYSEFHKH
YPRISTSPSV TLTKPYMTAN SEFSTSRLSN GKYPKALDGG DCAQSMPGHT RKTTVQDRKD
GGSPPLLEKQ TVTKDVTDKP LDLSSKVVDA DASKGDHMKK MAPTVLVHSR AASGLVLSGS
EIPKETLSPP GNGCSIYRSE IISTAPSSWV VPGPSPNEEN NGKSLSLKNK ALDWAIPQQR
SSSCPRMGGT DAVVTNVSGS VSSSGRPASA SPAPNANANA DGTKTSRSSV DTTPSVIQHV
GQPSSTPAKH GGSTSSKGAK ANPEPSFKAS ENGLPPTSIF LSPNEAFRSP AIPYPRSYLP
YAAPEGIALS PLSLHGKGPV YPHPVLLPNG SLFPGHLAPK PGLPYGLHTS RPEFVTYQDA
LGLGMVHPML IPHTPIEITK EEKPERRSRS HERARYEDPT LRSRFSEMLE ASSTKLHPEV
PTDKNLKPNS SWNQGKTGVK SDKLVYVDLL REEADTKTDA GAPKAGLVAE NVGQDTEATK
PSADPVIQQR REFISLREEL GRITDFHESF TFKQASSQPV FSLGKDSGAA GTNKENLGVQ
VATPFLETAL GSEGPAVTFG KTQEDPKPFC VGGAPPNMDV TPAYTKEGTD EAESNDGKVL
KPKPSKLAKR IANSAGYVGD RFKCVTTELY ADSSQLSREQ RALQMEGLQE DSILCLPAAY
CERAMMRFSE LEMKEREGSH PATKDSEVCK FSPADWERLK GNQEKKPKSV TLEEAIADQN
DSERCEYSTG NKHDLFEAPE DKDLPVEKYF LERPPVSEPP SDQGVVDTPH SPTLRLDRKR
KLSGDSTHTE TAVEELAEDP LKAKRRRISK DDWPEREMTN SSSNHLEDPH CNELTNLKVC
IELTGLHPKK QRHLLHLRER WEQQVSAAES KPGRQSRKEV AQAVQPEVTS QGTNITEEKP
GRKKAEAKGN RGWSEESLKS CDNEQGLPVL SGSPPMKSLS STNASGKKQT QPSCTPASRL
PAKQQKIKES QKTDVLCTGE DEDCQAASPL QKYTDNIEKP SGKRLCKTKH LIPQESRRSL
QITGDYYVEN TDTKMTVRRF RKRPEPSSDY DLSPPAKQEP KPFDRLQQLL PATQATQLPR
SNSPQETTQS RPMPPEARRL IVNKNAGETL LQRAARLGYE EVVLYCLENK VCDVNHRDNA
GYCALHEACA RGWLNIVRHL LEYGADVNCS AQDGTRPLHD AVENDHLEIV RLLLSYGADP
TLATYSGRTI MKMTHSELME KFLTDYLNDL QGRSEDDTSG AWEFYGSSVC EPDDESGYDV
LANPPGPEDP DEEEDTYSDL FEFEFAESSL LPCYNIQVSV AQGPRNWLLL SDVLKKLKMS
SRIFRSNFPN LEIVTIAEAE FYRQVSTSLL FSCPKDLEAF NPESKELLDL VEFTNELQTL
LGSSVEWLHP SDTGHENYW
