RED_HUMAN
ID RED_HUMAN Reviewed; 557 AA.
AC Q13123; Q6IPD8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein Red {ECO:0000303|PubMed:10216252};
DE AltName: Full=Cytokine IK {ECO:0000303|PubMed:7970704};
DE AltName: Full=IK factor {ECO:0000303|PubMed:7970704};
DE AltName: Full=Protein RER;
GN Name=IK; Synonyms=RED {ECO:0000303|PubMed:10216252}, RER;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Leukemia;
RX PubMed=10216252; DOI=10.1016/s0378-1119(99)00066-9;
RA Assier E., Bouzinba-Segard H., Stolzenberg M.-C., Stephens R., Bardos J.,
RA Freemont P., Charron D., Trowsdale J., Rich T.;
RT "Isolation, sequencing and expression of RED, a novel human gene encoding
RT an acidic-basic dipeptide repeat.";
RL Gene 230:145-154(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [MRNA] OF 316-477.
RC TISSUE=Leukemia;
RX PubMed=7970704;
RA Krief P., Augery-Bourget Y., Plaisance S., Merck M.F., Assier E.,
RA Tanchou V., Billard M., Boucheix C., Jasmin C., Azzarone B.;
RT "A new cytokine (IK) down-regulating HLA class II: monoclonal antibodies,
RT cloning and chromosome localization.";
RL Oncogene 9:3449-3456(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP 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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, 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 [9]
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 [10]
RP FUNCTION, INTERACTION WITH MAD1L1, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=22351768; DOI=10.1074/jbc.m111.299131;
RA Yeh P.C., Yeh C.C., Chen Y.C., Juang Y.L.;
RT "RED, a spindle pole-associated protein, is required for kinetochore
RT localization of MAD1, mitotic progression, and activation of the spindle
RT assembly checkpoint.";
RL J. Biol. Chem. 287:11704-11716(2012).
RN [11]
RP SUBUNIT, AND INTERACTION WITH SMU1.
RX PubMed=22365833; DOI=10.1016/j.molcel.2011.12.034;
RA Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S., Weimann M.,
RA Will C.L., Pena V., Luehrmann R., Stelzl U.;
RT "Dynamic protein-protein interaction wiring of the human spliceosome.";
RL Mol. Cell 45:567-580(2012).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DHX15.
RX PubMed=24252166; DOI=10.1186/2050-7771-1-11;
RA Hu L., Yang F., Liu X., Xu D., Dai W.;
RT "Nuclear protein IK undergoes dynamic subcellular translocation and forms
RT unique nuclear bodies during the cell cycle.";
RL Biomark. Res. 1:11-11(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-417 AND SER-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-544, 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 [16]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SMU1, INTERACTION
RP (MICROBIAL INFECTION) WITH INFLUENZA A VIRUS RNA POLYMERASE SUBUNITS PB1
RP AND PB2, AND SUBCELLULAR LOCATION.
RX PubMed=24945353; DOI=10.1371/journal.ppat.1004164;
RA Fournier G., Chiang C., Munier S., Tomoiu A., Demeret C., Vidalain P.O.,
RA Jacob Y., Naffakh N.;
RT "Recruitment of RED-SMU1 complex by Influenza A Virus RNA polymerase to
RT control Viral mRNA splicing.";
RL PLoS Pathog. 10:E1004164-E1004164(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151; LYS-310; LYS-331; LYS-386;
RP LYS-388; LYS-404; LYS-408; LYS-496; LYS-501; LYS-509; LYS-541; LYS-543;
RP LYS-544 AND LYS-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome (PubMed:28781166). Auxiliary spliceosomal protein that
CC regulates selection of alternative splice sites in a small set of
CC target pre-mRNA species (Probable). Required for normal mitotic cell
CC cycle progression (PubMed:22351768, PubMed:24252166). Recruits MAD1L1
CC and MAD2L1 to kinetochores, and is required to trigger the spindle
CC assembly checkpoint (PubMed:22351768). Required for normal accumulation
CC of SMU1 (PubMed:24945353). {ECO:0000269|PubMed:22351768,
CC ECO:0000269|PubMed:24252166, ECO:0000269|PubMed:24945353,
CC ECO:0000269|PubMed:28781166, ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Required, together with SMU1, for
CC normal splicing of influenza A virus NS1 pre-mRNA, which is required
CC for the production of the exportin NS2 and for the production of
CC influenza A virus particles. Not required for the production of VSV
CC virus particles. {ECO:0000269|PubMed:24945353}.
CC -!- SUBUNIT: (Microbial infection) Identified in a complex with SMU1 and
CC influenza A virus RNA polymerase subunits PB1 and PB2. Directly
CC interacts with SMU1 and with influenza A virus RNA polymerase subunits
CC PB1 and PB2. {ECO:0000269|PubMed:22365833}.
CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:22365833,
CC PubMed:28781166). Interacts with SMU1 (PubMed:22365833,
CC PubMed:24945353). Interacts with MAD1L1 (PubMed:22351768). May interact
CC with DHX15 (PubMed:24252166). {ECO:0000269|PubMed:22351768,
CC ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166,
CC ECO:0000305|PubMed:22365833, ECO:0000305|PubMed:24252166}.
CC -!- INTERACTION:
CC Q13123; O14965: AURKA; NbExp=3; IntAct=EBI-713456, EBI-448680;
CC Q13123; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-713456, EBI-739624;
CC Q13123; P26196: DDX6; NbExp=3; IntAct=EBI-713456, EBI-351257;
CC Q13123; O75190: DNAJB6; NbExp=3; IntAct=EBI-713456, EBI-1053164;
CC Q13123; Q01658: DR1; NbExp=3; IntAct=EBI-713456, EBI-750300;
CC Q13123; Q15029: EFTUD2; NbExp=2; IntAct=EBI-713456, EBI-357897;
CC Q13123; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-713456, EBI-1175354;
CC Q13123; Q70Z53: FRA10AC1; NbExp=2; IntAct=EBI-713456, EBI-710176;
CC Q13123; Q00403: GTF2B; NbExp=3; IntAct=EBI-713456, EBI-389564;
CC Q13123; Q13123: IK; NbExp=2; IntAct=EBI-713456, EBI-713456;
CC Q13123; P02545: LMNA; NbExp=3; IntAct=EBI-713456, EBI-351935;
CC Q13123; O95983-2: MBD3; NbExp=3; IntAct=EBI-713456, EBI-11978579;
CC Q13123; P55081: MFAP1; NbExp=2; IntAct=EBI-713456, EBI-1048159;
CC Q13123; Q96CV9: OPTN; NbExp=3; IntAct=EBI-713456, EBI-748974;
CC Q13123; O94906: PRPF6; NbExp=2; IntAct=EBI-713456, EBI-536755;
CC Q13123; P47897: QARS1; NbExp=3; IntAct=EBI-713456, EBI-347462;
CC Q13123; P98175: RBM10; NbExp=2; IntAct=EBI-713456, EBI-721525;
CC Q13123; O15541: RNF113A; NbExp=2; IntAct=EBI-713456, EBI-2130294;
CC Q13123; Q2TAY7: SMU1; NbExp=6; IntAct=EBI-713456, EBI-298027;
CC Q13123; Q8TAD8: SNIP1; NbExp=2; IntAct=EBI-713456, EBI-749336;
CC Q13123; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-713456, EBI-5235340;
CC Q13123; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-713456, EBI-295232;
CC Q13123; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-713456, EBI-3920997;
CC Q13123; P04618: rev; Xeno; NbExp=3; IntAct=EBI-713456, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24945353,
CC ECO:0000269|PubMed:28781166}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24252166, ECO:0000269|PubMed:24945353}. Chromosome
CC {ECO:0000269|PubMed:24252166}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:22351768}. Note=Predominantly present throughout
CC the nucleoplasm during prometaphase, metaphase and anaphase. Is also
CC detected in nuclear foci that are not identical with Cajal bodies.
CC Starts to accumulate at chromosomes during telophase, and is nearly
CC exclusively associated with chromosomes in newly divided cells
CC (PubMed:24252166). Colocalizes with MAD1L1 at mitotic spindle poles
CC during metaphase and anaphase (PubMed:22351768).
CC {ECO:0000269|PubMed:24252166}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10216252}.
CC -!- DEVELOPMENTAL STAGE: Expressed at similar levels in fetal and adult
CC tissues. {ECO:0000269|PubMed:10216252}.
CC -!- INDUCTION: Up-regulated during mitosis (at protein level).
CC {ECO:0000269|PubMed:22351768}.
CC -!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the IK factor, a cytokine
CC involved in the negative regulatory pathway of constitutive MHC class
CC II antigens expression. {ECO:0000305|PubMed:7970704}.
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DR EMBL; AJ005579; CAA06607.1; -; mRNA.
DR EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071964; AAH71964.1; -; mRNA.
DR EMBL; S74221; AAB32531.1; -; mRNA.
DR CCDS; CCDS47280.1; -.
DR PIR; I58408; I58408.
DR RefSeq; NP_006074.2; NM_006083.3.
DR PDB; 5O9Z; EM; 4.50 A; R=1-557.
DR PDB; 6Q8I; X-ray; 3.17 A; C/D/G/H/K/L/O/P=1-557.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6Q8I; -.
DR AlphaFoldDB; Q13123; -.
DR SMR; Q13123; -.
DR BioGRID; 109766; 200.
DR CORUM; Q13123; -.
DR IntAct; Q13123; 76.
DR MINT; Q13123; -.
DR STRING; 9606.ENSP00000396301; -.
DR BindingDB; Q13123; -.
DR ChEMBL; CHEMBL2321616; -.
DR GlyGen; Q13123; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13123; -.
DR MetOSite; Q13123; -.
DR PhosphoSitePlus; Q13123; -.
DR BioMuta; IK; -.
DR DMDM; 296452987; -.
DR EPD; Q13123; -.
DR jPOST; Q13123; -.
DR MassIVE; Q13123; -.
DR MaxQB; Q13123; -.
DR PaxDb; Q13123; -.
DR PeptideAtlas; Q13123; -.
DR PRIDE; Q13123; -.
DR ProteomicsDB; 59173; -.
DR Antibodypedia; 7468; 133 antibodies from 28 providers.
DR DNASU; 3550; -.
DR Ensembl; ENST00000417647.7; ENSP00000396301.2; ENSG00000113141.19.
DR GeneID; 3550; -.
DR KEGG; hsa:3550; -.
DR MANE-Select; ENST00000417647.7; ENSP00000396301.2; NM_006083.4; NP_006074.2.
DR UCSC; uc003lgq.4; human.
DR CTD; 3550; -.
DR DisGeNET; 3550; -.
DR GeneCards; IK; -.
DR HGNC; HGNC:5958; IK.
DR HPA; ENSG00000113141; Low tissue specificity.
DR MIM; 600549; gene.
DR neXtProt; NX_Q13123; -.
DR OpenTargets; ENSG00000113141; -.
DR PharmGKB; PA29774; -.
DR VEuPathDB; HostDB:ENSG00000113141; -.
DR eggNOG; KOG2498; Eukaryota.
DR GeneTree; ENSGT00940000153727; -.
DR HOGENOM; CLU_026814_2_0_1; -.
DR InParanoid; Q13123; -.
DR OMA; EPEYKSA; -.
DR OrthoDB; 500537at2759; -.
DR PhylomeDB; Q13123; -.
DR TreeFam; TF321907; -.
DR PathwayCommons; Q13123; -.
DR SignaLink; Q13123; -.
DR BioGRID-ORCS; 3550; 616 hits in 1084 CRISPR screens.
DR ChiTaRS; IK; human.
DR GeneWiki; IK_(gene); -.
DR GenomeRNAi; 3550; -.
DR Pharos; Q13123; Tbio.
DR PRO; PR:Q13123; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13123; protein.
DR Bgee; ENSG00000113141; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q13123; baseline and differential.
DR Genevisible; Q13123; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR InterPro; IPR039896; Red-like.
DR InterPro; IPR012492; RED_C.
DR InterPro; IPR012916; RED_N.
DR PANTHER; PTHR12765; PTHR12765; 1.
DR Pfam; PF07807; RED_C; 1.
DR Pfam; PF07808; RED_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Cytoplasm; Cytoskeleton;
KW Host-virus interaction; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..557
FT /note="Protein Red"
FT /id="PRO_0000097235"
FT REPEAT 342..343
FT /note="1"
FT REPEAT 344..345
FT /note="2"
FT REPEAT 346..347
FT /note="3"
FT REPEAT 348..349
FT /note="4"
FT REPEAT 350..351
FT /note="5"
FT REPEAT 352..353
FT /note="6"
FT REPEAT 354..355
FT /note="7"
FT REPEAT 356..357
FT /note="8"
FT REPEAT 358..359
FT /note="9"
FT REPEAT 360..361
FT /note="10"
FT REPEAT 362..363
FT /note="11"
FT REPEAT 364..365
FT /note="12"
FT REPEAT 366..367
FT /note="13"
FT REPEAT 368..369
FT /note="14"
FT REPEAT 370..371
FT /note="15"
FT REPEAT 372..373
FT /note="16"
FT REPEAT 374..375
FT /note="17"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..375
FT /note="17 X 2 AA tandem repeats of R-[ED]"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1M8"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 501
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 176
FT /note="A -> L (in Ref. 1; CAA06607)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="E -> D (in Ref. 1; CAA06607)"
FT /evidence="ECO:0000305"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:6Q8I"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6Q8I"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6Q8I"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6Q8I"
SQ SEQUENCE 557 AA; 65602 MW; BE7B332985D5F4CA CRC64;
MPERDSEPFS NPLAPDGHDV DDPHSFHQSK LTNEDFRKLL MTPRAAPTSA PPSKSRHHEM
PREYNEDEDP AARRRKKKSY YAKLRQQEIE RERELAEKYR DRAKERRDGV NKDYEETELI
STTANYRAVG PTAEADKSAA EKRRQLIQES KFLGGDMEHT HLVKGLDFAL LQKVRAEIAS
KEKEEEELME KPQKETKKDE DPENKIEFKT RLGRNVYRML FKSKAYERNE LFLPGRMAYV
VDLDDEYADT DIPTTLIRSK ADCPTMEAQT TLTTNDIVIS KLTQILSYLR QGTRNKKLKK
KDKGKLEEKK PPEADMNIFE DIGDYVPSTT KTPRDKERER YRERERDRER DRDRDRERER
ERDRERERER DREREEEKKR HSYFEKPKVD DEPMDVDKGP GSTKELIKSI NEKFAGSAGW
EGTESLKKPE DKKQLGDFFG MSNSYAECYP ATMDDMAVDS DEEVDYSKMD QGNKKGPLGR
WDFDTQEEYS EYMNNKEALP KAAFQYGIKM SEGRKTRRFK ETNDKAELDR QWKKISAIIE
KRKKMEADGV EVKRPKY
