NFRKB_HUMAN
ID NFRKB_HUMAN Reviewed; 1299 AA.
AC Q6P4R8; Q12869; Q15312; Q9H048;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nuclear factor related to kappa-B-binding protein;
DE AltName: Full=DNA-binding protein R kappa-B;
DE AltName: Full=INO80 complex subunit G;
GN Name=NFRKB; Synonyms=INO80G;
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] (ISOFORMS 1 AND 2), DNA-BINDING, AND TISSUE
RP SPECIFICITY.
RX PubMed=1777480;
RA Adams B.S., Leung K.Y., Hanley E.W., Nabel G.J.;
RT "Cloning of R kappa B, a novel DNA-binding protein that recognizes the
RT interleukin-2 receptor alpha chain kappa B site.";
RL New Biol. 3:1063-1073(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Nieters A., Bouwmeester T., Scheidereit C.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-1299 (ISOFORM 3).
RC TISSUE=Fetal brain;
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 IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [6]
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 SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80 COMPLEX,
RP INTERACTION WITH UCHL5, AND FUNCTION.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1237, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-1022 AND SER-1291,
RP AND IDENTIFICATION BY 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 [13]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-298; SER-1022 AND
RP SER-1291, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-1291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-327; LYS-469 AND LYS-488, AND
RP IDENTIFICATION BY MASS 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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 370-495.
RX PubMed=22984442; DOI=10.1371/journal.pone.0043761;
RA Kumar A., Mocklinghoff S., Yumoto F., Jaroszewski L., Farr C.L.,
RA Grzechnik A., Nguyen P., Weichenberger C.X., Chiu H.J., Klock H.E.,
RA Elsliger M.A., Deacon A.M., Godzik A., Lesley S.A., Conklin B.R.,
RA Fletterick R.J., Wilson I.A.;
RT "Structure of a novel winged-helix like domain from human NFRKB protein.";
RL PLoS ONE 7:E43761-E43761(2012).
CC -!- FUNCTION: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.
CC {ECO:0000269|PubMed:18922472}.
CC -!- FUNCTION: Putative regulatory component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Modulates the deubiquitinase
CC activity of UCHL5 in the INO80 complex. {ECO:0000269|PubMed:18922472}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the N-terminus of
CC INO80. Interacts with UCHL5; NFRKB competes with ADRM1 for interaction
CC with UCHL5. {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC Q6P4R8; Q9Y5K5: UCHL5; NbExp=12; IntAct=EBI-2511210, EBI-1051183;
CC Q6P4R8; Q9Y5K5-3: UCHL5; NbExp=3; IntAct=EBI-2511210, EBI-11749875;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P4R8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P4R8-2; Sequence=VSP_017592, VSP_017593;
CC Name=3;
CC IsoId=Q6P4R8-3; Sequence=VSP_017594;
CC -!- TISSUE SPECIFICITY: Expressed in thymus, brain, testes, spleen and
CC liver. {ECO:0000269|PubMed:1777480}.
CC -!- DOMAIN: NFRKB seems to be mostly disordered. The wing-helix like domain
CC doesn't bind DNA.
CC -!- SIMILARITY: Belongs to the NFRKB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17871.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U08191; AAA17871.1; ALT_SEQ; mRNA.
DR EMBL; X80878; CAA56846.1; -; mRNA.
DR EMBL; BC063280; AAH63280.1; -; mRNA.
DR EMBL; AL512730; CAC21663.1; -; mRNA.
DR CCDS; CCDS44770.1; -. [Q6P4R8-1]
DR CCDS; CCDS8483.1; -. [Q6P4R8-2]
DR PIR; S52863; S52863.
DR RefSeq; NP_001137307.1; NM_001143835.1. [Q6P4R8-1]
DR RefSeq; NP_006156.2; NM_006165.3. [Q6P4R8-2]
DR RefSeq; XP_011541153.1; XM_011542851.2. [Q6P4R8-2]
DR RefSeq; XP_011541154.1; XM_011542852.2. [Q6P4R8-2]
DR RefSeq; XP_016873285.1; XM_017017796.1. [Q6P4R8-1]
DR PDB; 3U21; X-ray; 2.18 A; A/B=370-495.
DR PDB; 4UF5; X-ray; 3.70 A; B=40-170.
DR PDB; 4UF6; X-ray; 3.69 A; C/F/I/L=40-101.
DR PDB; 4WLP; X-ray; 3.10 A; B=40-153.
DR PDBsum; 3U21; -.
DR PDBsum; 4UF5; -.
DR PDBsum; 4UF6; -.
DR PDBsum; 4WLP; -.
DR AlphaFoldDB; Q6P4R8; -.
DR SMR; Q6P4R8; -.
DR BioGRID; 110864; 90.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q6P4R8; -.
DR IntAct; Q6P4R8; 58.
DR MINT; Q6P4R8; -.
DR STRING; 9606.ENSP00000436926; -.
DR CarbonylDB; Q6P4R8; -.
DR GlyConnect; 2888; 1 O-Linked glycan (2 sites).
DR GlyGen; Q6P4R8; 30 sites, 2 O-linked glycans (30 sites).
DR iPTMnet; Q6P4R8; -.
DR MetOSite; Q6P4R8; -.
DR PhosphoSitePlus; Q6P4R8; -.
DR BioMuta; NFRKB; -.
DR DMDM; 90101417; -.
DR EPD; Q6P4R8; -.
DR jPOST; Q6P4R8; -.
DR MassIVE; Q6P4R8; -.
DR MaxQB; Q6P4R8; -.
DR PaxDb; Q6P4R8; -.
DR PeptideAtlas; Q6P4R8; -.
DR PRIDE; Q6P4R8; -.
DR ProteomicsDB; 66983; -. [Q6P4R8-1]
DR ProteomicsDB; 66984; -. [Q6P4R8-2]
DR ProteomicsDB; 66985; -. [Q6P4R8-3]
DR Antibodypedia; 1820; 122 antibodies from 25 providers.
DR DNASU; 4798; -.
DR Ensembl; ENST00000446488.7; ENSP00000400476.2; ENSG00000170322.15. [Q6P4R8-1]
DR Ensembl; ENST00000524746.5; ENSP00000433572.1; ENSG00000170322.15. [Q6P4R8-1]
DR Ensembl; ENST00000524794.5; ENSP00000436926.1; ENSG00000170322.15. [Q6P4R8-2]
DR Ensembl; ENST00000682444.1; ENSP00000506850.1; ENSG00000170322.15. [Q6P4R8-1]
DR GeneID; 4798; -.
DR KEGG; hsa:4798; -.
DR MANE-Select; ENST00000682444.1; ENSP00000506850.1; NM_001143835.2; NP_001137307.1.
DR UCSC; uc001qfg.4; human. [Q6P4R8-1]
DR CTD; 4798; -.
DR DisGeNET; 4798; -.
DR GeneCards; NFRKB; -.
DR HGNC; HGNC:7802; NFRKB.
DR HPA; ENSG00000170322; Low tissue specificity.
DR MIM; 164013; gene.
DR neXtProt; NX_Q6P4R8; -.
DR OpenTargets; ENSG00000170322; -.
DR PharmGKB; PA31606; -.
DR VEuPathDB; HostDB:ENSG00000170322; -.
DR eggNOG; KOG1927; Eukaryota.
DR GeneTree; ENSGT00390000016213; -.
DR HOGENOM; CLU_007638_0_0_1; -.
DR InParanoid; Q6P4R8; -.
DR OMA; VKCPPVP; -.
DR OrthoDB; 140291at2759; -.
DR PhylomeDB; Q6P4R8; -.
DR TreeFam; TF324944; -.
DR PathwayCommons; Q6P4R8; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q6P4R8; -.
DR BioGRID-ORCS; 4798; 319 hits in 1093 CRISPR screens.
DR ChiTaRS; NFRKB; human.
DR EvolutionaryTrace; Q6P4R8; -.
DR GeneWiki; NFRKB; -.
DR GenomeRNAi; 4798; -.
DR Pharos; Q6P4R8; Tbio.
DR PRO; PR:Q6P4R8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6P4R8; protein.
DR Bgee; ENSG00000170322; Expressed in buccal mucosa cell and 196 other tissues.
DR ExpressionAtlas; Q6P4R8; baseline and differential.
DR Genevisible; Q6P4R8; HS.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR Gene3D; 1.10.10.2430; -; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR024867; NFRKB.
DR InterPro; IPR025220; NFRKB_winged_dom.
DR InterPro; IPR038106; NFRKB_winged_sf.
DR PANTHER; PTHR13052; PTHR13052; 1.
DR Pfam; PF14465; NFRKB_winged; 1.
DR PROSITE; PS51916; DEUBAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1299
FT /note="Nuclear factor related to kappa-B-binding protein"
FT /id="PRO_0000227807"
FT DOMAIN 39..156
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 163..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..495
FT /note="Winged-helix like domain"
FT REGION 669..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
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 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1291
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 ECO:0007744|PubMed:24275569"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MHVFVQSTCGEETM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1777480, ECO:0000303|Ref.2"
FT /id="VSP_017592"
FT VAR_SEQ 213
FT /note="E -> EATLDLQEQFSFE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1777480, ECO:0000303|Ref.2"
FT /id="VSP_017593"
FT VAR_SEQ 687
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017594"
FT CONFLICT 1178
FT /note="G -> E (in Ref. 3; AAH63280)"
FT /evidence="ECO:0000305"
FT CONFLICT 1213
FT /note="N -> D (in Ref. 3; AAH63280)"
FT /evidence="ECO:0000305"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:4WLP"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:4WLP"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4WLP"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 118..151
FT /evidence="ECO:0007829|PDB:4WLP"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:3U21"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 395..406
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:3U21"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:3U21"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:3U21"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:3U21"
SQ SEQUENCE 1299 AA; 139001 MW; 087B212E283C3820 CRC64;
MDSLDHMLTD PLELGPCGDG HGTRIMEDCL LGGTRVSLPE DLLEDPEIFF DVVSLSTWQE
VLSDSQREHL QQFLPQFPED SAEQQNELIL ALFSGENFRF GNPLHIAQKL FRDGHFNPEV
VKYRQLCFKS QYKRYLNSQQ QYFHRLLKQI LASRSDLLEM ARRSGPALPF RQKRPSPSRT
PEEREWRTQQ RYLKVLREVK EECGDTALSS DEEDLSSWLP SSPARSPSPA VPLRVVPTLS
TTDMKTADKV ELGDSDLKIM LKKHHEKRKH QPDHPDLLTG DLTLNDIMTR VNAGRKGSLA
ALYDLAVLKK KVKEKEEKKK KKIKTIKSEA EDLAEPLSST EGVAPLSQAP SPLAIPAIKE
EPLEDLKPCL GINEISSSFF SLLLEILLLE SQASLPMLEE RVLDWQSSPA SSLNSWFSAA
PNWAELVLPA LQYLAGESRA VPSSFSPFVE FKEKTQQWKL LGQSQDNEKE LAALFQLWLE
TKDQAFCKQE NEDSSDATTP VPRVRTDYVV RPSTGEEKRV FQEQERYRYS QPHKAFTFRM
HGFESVVGPV KGVFDKETSL NKAREHSLLR SDRPAYVTIL SLVRDAAARL PNGEGTRAEI
CELLKDSQFL APDVTSTQVN TVVSGALDRL HYEKDPCVKY DIGRKLWIYL HRDRSEEEFE
RIHQAQAAAA KARKALQQKP KPPSKVKSSS KESSIKVLSS GPSEQSQMSL SDSSMPPTPV
TPVTPTTPAL PAIPISPPPV SAVNKSGPST VSEPAKSSSG VLLVSSPTMP HLGTMLSPAS
SQTAPSSQAA ARVVSHSGSA GLSQVRVVAQ PSLPAVPQQS GGPAQTLPQM PAGPQIRVPA
TATQTKVVPQ TVMATVPVKA QTTAATVQRP GPGQTGLTVT SLPATASPVS KPATSSPGTS
APSASTAAVI QNVTGQNIIK QVAITGQLGV KPQTGNSIPL TATNFRIQGK DVLRLPPSSI
TTDAKGQTVL RITPDMMATL AKSQVTTVKL TQDLFGTGGN TTGKGISATL HVTSNPVHAA
DSPAKASSAS APSSTPTGTT VVKVTPDLKP TEASSSAFRL MPALGVSVAD QKGKSTVASS
EAKPAATIRI VQGLGVMPPK AGQTITVATH AKQGASVASG SGTVHTSAVS LPSMNAAVSK
TVAVASGAAS TPISISTGAP TVRQVPVSTT VVSTSQAGKL PTRITVPLSV ISQPMKGKSV
VTAPIIKGNL GANLSGLGRN IILTTMPAGT KLIAGNKPVS FLTAQQLQQL QQQGQATQVR
IQTVPASHLQ QGTASGSSKA VSTVVVTTAP SPKQAPEQQ
