MBB1A_HUMAN
ID MBB1A_HUMAN Reviewed; 1328 AA.
AC Q9BQG0; Q86VM3; Q9BW49; Q9P0V5; Q9UF99;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Myb-binding protein 1A;
GN Name=MYBBP1A; Synonyms=P160;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10644447; DOI=10.1006/geno.1999.6035;
RA Keough R., Woollatt E., Crawford J., Sutherland G.R., Plummer S., Casey G.,
RA Gonda T.J.;
RT "Molecular cloning and chromosomal mapping of the human homologue of MYB
RT binding protein (P160) 1A (MYBBP1A) to 17p13.3.";
RL Genomics 62:483-489(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-1328 (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1328 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-775, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION IN THE B-WICH COMPLEX.
RX PubMed=16603771; DOI=10.1074/jbc.m600233200;
RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear
RT proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-1163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775 AND SER-1290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775; SER-1159;
RP SER-1163; SER-1186; THR-1190; THR-1196; SER-1207; SER-1248; SER-1267;
RP SER-1303; SER-1308 AND SER-1314, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775 AND SER-1267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-158, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775; SER-1163;
RP SER-1267; SER-1290; SER-1308; SER-1310 AND SER-1314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775; SER-1163; SER-1232;
RP SER-1267; THR-1269 AND SER-1290, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-1159; SER-1163;
RP SER-1186; THR-1239; SER-1241; SER-1248; SER-1267; SER-1290; SER-1308;
RP SER-1310 AND SER-1314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP FUNCTION.
RX PubMed=29065309; DOI=10.1016/j.devcel.2017.09.022;
RA Liu Y., Mattila J., Ventelae S., Yadav L., Zhang W., Lamichane N.,
RA Sundstroem J., Kauko O., Grenman R., Varjosalo M., Westermarck J.,
RA Hietakangas V.;
RT "PWP1 Mediates Nutrient-Dependent Growth Control through Nucleolar
RT Regulation of Ribosomal Gene Expression.";
RL Dev. Cell 43:240-252(2017).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1148, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May activate or repress transcription via interactions with
CC sequence specific DNA-binding proteins (By similarity). Repression may
CC be mediated at least in part by histone deacetylase activity (HDAC
CC activity) (By similarity). Acts as a corepressor and in concert with
CC CRY1, represses the transcription of the core circadian clock component
CC PER2 (By similarity). Preferentially binds to dimethylated histone H3
CC 'Lys-9' (H3K9me2) on the PER2 promoter (By similarity). Has a role in
CC rRNA biogenesis together with PWP1 (PubMed:29065309).
CC {ECO:0000250|UniProtKB:Q7TPV4, ECO:0000269|PubMed:29065309}.
CC -!- SUBUNIT: Binds to and represses JUN and MYB via the leucine zipper
CC regions present in these proteins. Also binds to and represses
CC PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated
CC by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to
CC KPNA2. Interacts with CLOCK and CRY1 (By similarity). Component of the
CC B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1,
CC DEK, MYO1C, ERCC6, MYBBP1A and DDX21. {ECO:0000250|UniProtKB:Q7TPV4,
CC ECO:0000269|PubMed:16603771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12429849}. Nucleus
CC {ECO:0000269|PubMed:12429849}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12429849}. Note=Shuttles between the nucleus and
CC cytoplasm. Nuclear import may be mediated by KPNA2, while export
CC appears to depend partially on XPO1/CRM1 (By similarity). Predominantly
CC nucleolar. {ECO:0000250|UniProtKB:Q7TPV4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQG0-2; Sequence=VSP_014786;
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q7TPV4}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing donor and acceptor
CC splice sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MYBBP1A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66530.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYBBP1AID41467ch17p13.html";
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DR EMBL; AF147709; AAF33021.1; -; mRNA.
DR EMBL; BC000641; AAH00641.2; -; mRNA.
DR EMBL; BC050546; AAH50546.1; -; mRNA.
DR EMBL; AL136595; CAB66530.1; ALT_INIT; mRNA.
DR EMBL; AL133098; CAB61409.1; -; mRNA.
DR CCDS; CCDS11046.1; -. [Q9BQG0-1]
DR CCDS; CCDS42238.1; -. [Q9BQG0-2]
DR PIR; T42680; T42680.
DR RefSeq; NP_001099008.1; NM_001105538.1. [Q9BQG0-2]
DR RefSeq; NP_055335.2; NM_014520.3. [Q9BQG0-1]
DR AlphaFoldDB; Q9BQG0; -.
DR BioGRID; 115770; 388.
DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex.
DR CORUM; Q9BQG0; -.
DR IntAct; Q9BQG0; 100.
DR MINT; Q9BQG0; -.
DR STRING; 9606.ENSP00000370968; -.
DR GlyGen; Q9BQG0; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q9BQG0; -.
DR MetOSite; Q9BQG0; -.
DR PhosphoSitePlus; Q9BQG0; -.
DR SwissPalm; Q9BQG0; -.
DR BioMuta; MYBBP1A; -.
DR DMDM; 71153825; -.
DR SWISS-2DPAGE; Q9BQG0; -.
DR CPTAC; CPTAC-980; -.
DR EPD; Q9BQG0; -.
DR jPOST; Q9BQG0; -.
DR MassIVE; Q9BQG0; -.
DR MaxQB; Q9BQG0; -.
DR PaxDb; Q9BQG0; -.
DR PeptideAtlas; Q9BQG0; -.
DR PRIDE; Q9BQG0; -.
DR ProteomicsDB; 78674; -. [Q9BQG0-1]
DR ProteomicsDB; 78675; -. [Q9BQG0-2]
DR Antibodypedia; 23280; 271 antibodies from 31 providers.
DR DNASU; 10514; -.
DR Ensembl; ENST00000254718.9; ENSP00000254718.4; ENSG00000132382.15. [Q9BQG0-1]
DR Ensembl; ENST00000381556.6; ENSP00000370968.2; ENSG00000132382.15. [Q9BQG0-2]
DR GeneID; 10514; -.
DR KEGG; hsa:10514; -.
DR MANE-Select; ENST00000254718.9; ENSP00000254718.4; NM_014520.4; NP_055335.2.
DR UCSC; uc002fxz.5; human. [Q9BQG0-1]
DR CTD; 10514; -.
DR DisGeNET; 10514; -.
DR GeneCards; MYBBP1A; -.
DR HGNC; HGNC:7546; MYBBP1A.
DR HPA; ENSG00000132382; Low tissue specificity.
DR MIM; 604885; gene.
DR neXtProt; NX_Q9BQG0; -.
DR OpenTargets; ENSG00000132382; -.
DR PharmGKB; PA31346; -.
DR VEuPathDB; HostDB:ENSG00000132382; -.
DR eggNOG; KOG1926; Eukaryota.
DR GeneTree; ENSGT00390000017457; -.
DR HOGENOM; CLU_005997_1_0_1; -.
DR InParanoid; Q9BQG0; -.
DR OMA; PWVEVMV; -.
DR OrthoDB; 86051at2759; -.
DR PhylomeDB; Q9BQG0; -.
DR TreeFam; TF317401; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q9BQG0; -.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR SignaLink; Q9BQG0; -.
DR SIGNOR; Q9BQG0; -.
DR BioGRID-ORCS; 10514; 626 hits in 1084 CRISPR screens.
DR ChiTaRS; MYBBP1A; human.
DR GeneWiki; MYBBP1A; -.
DR GenomeRNAi; 10514; -.
DR Pharos; Q9BQG0; Tbio.
DR PRO; PR:Q9BQG0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BQG0; protein.
DR Bgee; ENSG00000132382; Expressed in sural nerve and 140 other tissues.
DR ExpressionAtlas; Q9BQG0; baseline and differential.
DR Genevisible; Q9BQG0; HS.
DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:2000210; P:positive regulation of anoikis; IMP:CACAO.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007015; DNA_pol_V/MYBBP1A.
DR PANTHER; PTHR13213; PTHR13213; 1.
DR Pfam; PF04931; DNA_pol_phi; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Biological rhythms;
KW Citrullination; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribosome biogenesis; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1328
FT /note="Myb-binding protein 1A"
FT /id="PRO_0000096255"
FT REGION 1..582
FT /note="Interaction with MYB"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1328
FT /note="Required for nuclear and nucleolar localization"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT REGION 1306..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..258
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT MOTIF 263..281
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT COMPBIAS 698..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1179
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1190
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1196
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1239
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1307
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q7TPV4"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 1148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1322..1328
FT /note="VRKAGKP -> TLRFTISSSKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_014786"
FT VARIANT 8
FT /note="Q -> E (in dbSNP:rs3809849)"
FT /id="VAR_023064"
FT VARIANT 680
FT /note="H -> Y (in dbSNP:rs899440)"
FT /id="VAR_051156"
FT VARIANT 958
FT /note="H -> P (in dbSNP:rs879797)"
FT /id="VAR_051157"
FT VARIANT 1208
FT /note="M -> L (in dbSNP:rs9905742)"
FT /id="VAR_051158"
FT CONFLICT 307
FT /note="R -> H (in Ref. 1; AAF33021)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="R -> H (in Ref. 1; AAF33021)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="L -> F (in Ref. 1; AAF33021)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="H -> R (in Ref. 2; AAH50546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1328 AA; 148855 MW; 0B053465D5B3511F CRC64;
MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY
LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD
LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA
LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS
DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP
ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL
EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD
SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL
FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP
WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL
LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA
QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE
DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE
LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP
ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL
HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP
TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI
TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ
QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK
TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT
GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ
VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA
QVRKAGKP
