CCAR2_MOUSE
ID CCAR2_MOUSE Reviewed; 922 AA.
AC Q8VDP4; Q6PIB1; Q8BWR5; Q8C0F0; Q8R3G6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell cycle and apoptosis regulator protein 2;
DE AltName: Full=Cell division cycle and apoptosis regulator protein 2;
GN Name=Ccar2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 226-248, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-680, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-677 AND SER-680, AND
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 [6]
RP FUNCTION AS SUV39H1 INHIBITOR, AND INTERACTION WITH SUV39H1.
RX PubMed=19218236; DOI=10.1074/jbc.m900956200;
RA Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.;
RT "Inhibition of SUV39H1 methyltransferase activity by DBC1.";
RL J. Biol. Chem. 284:10361-10366(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-674; SER-677;
RP SER-680; TYR-684 AND SER-686, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP FUNCTION, AND INTERACTION WITH HDAC3; HDAC1 AND MEF2D.
RX PubMed=21030595; DOI=10.1074/jbc.m110.153270;
RA Chini C.C., Escande C., Nin V., Chini E.N.;
RT "HDAC3 is negatively regulated by the nuclear protein DBC1.";
RL J. Biol. Chem. 285:40830-40837(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH NR1D1.
RX PubMed=23398316; DOI=10.1042/bj20121085;
RA Chini C.C., Escande C., Nin V., Chini E.N.;
RT "DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of
RT the nuclear receptor Rev-erbalpha.";
RL Biochem. J. 451:453-461(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24415752; DOI=10.1074/jbc.m113.512913;
RA Nin V., Chini C.C., Escande C., Capellini V., Chini E.N.;
RT "Deleted in breast cancer 1 (DBC1) protein regulates hepatic
RT gluconeogenesis.";
RL J. Biol. Chem. 289:5518-5527(2014).
RN [11]
RP FUNCTION, INTERACTION WITH TP53, AND DISRUPTION PHENOTYPE.
RX PubMed=25732823; DOI=10.1016/j.celrep.2015.01.066;
RA Qin B., Minter-Dykhouse K., Yu J., Zhang J., Liu T., Zhang H., Lee S.,
RA Kim J., Wang L., Lou Z.;
RT "DBC1 functions as a tumor suppressor by regulating p53 stability.";
RL Cell Rep. 10:1324-1334(2015).
CC -!- FUNCTION: Core component of the DBIRD complex, a multiprotein complex
CC that acts at the interface between core mRNP particles and RNA
CC polymerase II (RNAPII) and integrates transcript elongation with the
CC regulation of alternative splicing: the DBIRD complex affects local
CC transcript elongation rates and alternative splicing of a large set of
CC exons embedded in (A + T)-rich DNA regions (By similarity). Inhibits
CC SIRT1 deacetylase activity leading to increasing levels of p53/TP53
CC acetylation and p53-mediated apoptosis (By similarity). Inhibits
CC SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand-
CC dependent transcriptional activation by nuclear hormone receptors (By
CC similarity). Plays a critical role in maintaining genomic stability and
CC cellular integrity following UV-induced genotoxic stress (By
CC similarity). Regulates the circadian expression of the core clock
CC components NR1D1 and ARNTL/BMAL1 (PubMed:23398316). Enhances the
CC transcriptional repressor activity of NR1D1 through stabilization of
CC NR1D1 protein levels by preventing its ubiquitination and subsequent
CC degradation (PubMed:23398316). Represses the ligand-dependent
CC transcriptional activation function of ESR2 (By similarity). Acts as a
CC regulator of PCK1 expression and gluconeogenesis by a mechanism that
CC involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752).
CC Negatively regulates the deacetylase activity of HDAC3 and can alter
CC its subcellular localization (PubMed:21030595). Positively regulates
CC the beta-catenin pathway (canonical Wnt signaling pathway) and is
CC required for MCC-mediated repression of the beta-catenin pathway (By
CC similarity). Represses ligand-dependent transcriptional activation
CC function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with
CC NR1H3 (By similarity). Plays an important role in tumor suppression
CC through p53/TP53 regulation; stabilizes p53/TP53 by affecting its
CC interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the
CC transcriptional activator activity of BRCA1 (By similarity). Inhibits
CC SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity
CC of CHEK2 in vitro (By similarity). {ECO:0000250|UniProtKB:Q8N163,
CC ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:21030595,
CC ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752,
CC ECO:0000269|PubMed:25732823}.
CC -!- SUBUNIT: Component of the DBIRD complex (By similarity). Interacts with
CC ZNF326/ZIRD; the interaction is direct (By similarity). Interacts (via
CC N-terminus) with SIRT1, which inhibits the deacetylation of substrates
CC (PubMed:21030595). Interacts (via N-terminus) with SUV39H1; this
CC interaction abolishes the interaction with SIRT1 (PubMed:19218236).
CC Component of a nuclear receptor-mediated transcription complex composed
CC of at least ZNF335, CCAR2 and EMSY; the complex stimulates the
CC transcription of nuclear receptor target genes such as SOX9 and HOXA1
CC (By similarity). Within the complex interacts with EMSY and interacts
CC with ZNF335 (via C-terminus) (By similarity). Components of this
CC complex may associate with components of a histone methylation complex
CC to form a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY,
CC MKI67, RBBP5, ASH2L and WDR5 (By similarity). Within this complex,
CC interacts with ASH2L (By similarity). Interacts with NR1D1
CC (PubMed:23398316). Interacts (via N-terminus) with ESR1 and ESR2 (By
CC similarity). Interacts (via N-terminus) with HDAC3 (via C-terminus)
CC (PubMed:21030595). Interacts with HDAC1 and MED2F (PubMed:21030595).
CC Interacts with MCC (By similarity). Interacts (via N-terminus) with
CC NR1H2 and NR1H3 in a ligand-independent manner (By similarity).
CC Interacts with CSNK2A1 (By similarity). Interacts (via N-terminus) with
CC p53/TP53 (PubMed:25732823). Interacts (via N-terminus) with BRCA1 (via
CC the BRCT domains) (By similarity). Interacts (via N-terminus) with
CC CHEK2 (via protein kinase domain) (By similarity). Interacts with PSEM3
CC (By similarity). Interacts (via N-terminus) with PSIA3 and SENP1 (By
CC similarity). The sumoylated form shows a preferential interaction with
CC SIRT1 as compared to its unmodified form (By similarity).
CC {ECO:0000250|UniProtKB:Q8N163, ECO:0000269|PubMed:19218236,
CC ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:23398316,
CC ECO:0000269|PubMed:25732823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N163}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8N163}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q8N163}. Note=Recruited to chromatin, post-UV
CC irradiation. Sequestered to the cytoplasm in the presence of MCC.
CC Translocated to the cytoplasm during UV-induced apoptosis.
CC {ECO:0000250|UniProtKB:Q8N163}.
CC -!- PTM: Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory
CC binding to SIRT1 and increases its deacetylase activity.
CC {ECO:0000250|UniProtKB:Q8N163}.
CC -!- PTM: Genotoxic stress induces its sumoylation and sumoylation promotes
CC the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated
CC deacetylation of p53/TP53. Sumoylation leads to transcriptional
CC activation of p53/TP53 by sequestering SIRT1 from p53/TP53.
CC Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8N163}.
CC -!- DISRUPTION PHENOTYPE: Mice mimic a fasted state and therefore, display
CC an increased production of glucose. Display elevated levels of PCK1 and
CC are glucose-intolerant in both a normal and a high-fat diet
CC (PubMed:24415752). Mice develop more tumors including lymphomas, liver
CC tumors, lung tumors (PubMed:25732823). {ECO:0000269|PubMed:24415752,
CC ECO:0000269|PubMed:25732823}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27420.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34139.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK031472; BAC27420.1; ALT_INIT; mRNA.
DR EMBL; AK050238; BAC34139.2; ALT_INIT; mRNA.
DR EMBL; BC021475; AAH21475.2; -; mRNA.
DR EMBL; BC025471; AAH25471.1; -; mRNA.
DR EMBL; BC038346; AAH38346.1; -; mRNA.
DR CCDS; CCDS49534.1; -.
DR RefSeq; NP_666167.3; NM_146055.3.
DR RefSeq; XP_006518959.1; XM_006518896.3.
DR AlphaFoldDB; Q8VDP4; -.
DR SMR; Q8VDP4; -.
DR BioGRID; 230123; 21.
DR IntAct; Q8VDP4; 10.
DR MINT; Q8VDP4; -.
DR STRING; 10090.ENSMUSP00000036924; -.
DR iPTMnet; Q8VDP4; -.
DR PhosphoSitePlus; Q8VDP4; -.
DR EPD; Q8VDP4; -.
DR jPOST; Q8VDP4; -.
DR MaxQB; Q8VDP4; -.
DR PaxDb; Q8VDP4; -.
DR PeptideAtlas; Q8VDP4; -.
DR PRIDE; Q8VDP4; -.
DR ProteomicsDB; 265360; -.
DR Antibodypedia; 9629; 315 antibodies from 37 providers.
DR Ensembl; ENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712.
DR GeneID; 219158; -.
DR KEGG; mmu:219158; -.
DR UCSC; uc007unf.1; mouse.
DR CTD; 57805; -.
DR MGI; MGI:2444228; Ccar2.
DR VEuPathDB; HostDB:ENSMUSG00000033712; -.
DR eggNOG; KOG4246; Eukaryota.
DR GeneTree; ENSGT00530000063672; -.
DR HOGENOM; CLU_008030_2_0_1; -.
DR InParanoid; Q8VDP4; -.
DR OMA; VAQNICQ; -.
DR OrthoDB; 614048at2759; -.
DR PhylomeDB; Q8VDP4; -.
DR TreeFam; TF316387; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 219158; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ccar2; mouse.
DR PRO; PR:Q8VDP4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8VDP4; protein.
DR Bgee; ENSMUSG00000033712; Expressed in dorsal pancreas and 232 other tissues.
DR Genevisible; Q8VDP4; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2000003; P:positive regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0090311; P:regulation of protein deacetylation; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR045354; BURAN.
DR InterPro; IPR025224; CCAR1/CCAR2.
DR InterPro; IPR028811; CCAR2.
DR InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR045353; LAIKA.
DR InterPro; IPR025223; S1-like_RNA-bd_dom.
DR PANTHER; PTHR14304; PTHR14304; 1.
DR PANTHER; PTHR14304:SF12; PTHR14304:SF12; 1.
DR Pfam; PF19257; BURAN; 1.
DR Pfam; PF14443; DBC1; 1.
DR Pfam; PF19256; LAIKA; 1.
DR Pfam; PF14444; S1-like; 1.
DR SMART; SM01122; DBC1; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Apoptosis; Biological rhythms; Cell cycle;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW DNA damage; Isopeptide bond; Metalloenzyme inhibitor; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..922
FT /note="Cell cycle and apoptosis regulator protein 2"
FT /id="PRO_0000050814"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..669
FT /note="Interaction with MCC"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT REGION 703..922
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT COILED 573..596
FT /evidence="ECO:0000255"
FT COILED 828..898
FT /evidence="ECO:0000255"
FT COMPBIAS 187..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 112
FT /note="N6-acetyllysine; by KAT8"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 123
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 180
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 215
FT /note="N6-acetyllysine; by KAT8"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT MOD_RES 896
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2 and SUMO3); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8N163"
FT CONFLICT 527..529
FT /note="RPK -> HAS (in Ref. 2; AAH25471)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="H -> L (in Ref. 2; AAH38346)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="G -> R (in Ref. 1; BAC27420)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 103002 MW; 19F43ECEE58F461C CRC64;
MSQFKRQRIN PLPGGRNFSG AASTSLLGPP PGLLTPPVAT DLSQNARHLQ SGEKQRVFTG
IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP
LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR
FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LSPYRVHLTP YTVDSPTCDF
LELQRRYRSL LVPSDFLSVH LSWLSAFPLG QPFSLHHPSR IQVSSEKEAA PDTGAEPSPE
DSDPTYSSKV LLLSSPGLEE FYRCCMLFVD DMAEPRETPE HPLKQLKFLL GRKEEEAVLV
GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSTCT KWWRFAEFQY LQPGPPRQLH
TVVVYLPDVW TIMPTLEEWE ALCQQKATEA APQPHEASGE AEATEQAPDV SEQADTSKQN
TETMEATTQQ DVDTDLPEAP PPPLEPAVMA RPRCVNLSLY GIVEDRRPKE RISFEVVVLA
ELFVEMLQRD FGYRIYKTLL SLPEKVVSPP EPEKEEAAKE DAVKEEEAVK EEAVKVSKDE
VQNEGTAAES DSPLKEDGLL PKRPSSGGEE EEKARGEAAE DLCEMALDPD LLLLRDDGED
EFAGAKLEET EVRSVASNQS EMEYSSLQDM PKELDPSTVL PLDCLLAFVF FDANWCGYLH
RRDLERVLLT LGIRLSAEQA KQLVSRVVAQ NICQYRSLQY SRAEVLDDGL PEDVLFGNLD
LLPPSGKSTK PGAAPTEHKG LVPHNGSLIN VGSLLQRAEQ QDSGRLYLEN KIHTLELKLE
ESHNRFSATE VTNKTLAAEM QELRARLAEA EETARTAERQ KNQLQRQMQD FRRRLTPLHL
EMQRIVEKAD SWVEKEEPTP SN
