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   27-MAR-2024, entry version 176.
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=7; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   EMDB; EMD-3766; -.
DR   SMR; Q13123; -.
DR   BioGRID; 109766; 229.
DR   CORUM; Q13123; -.
DR   IntAct; Q13123; 78.
DR   MINT; Q13123; -.
DR   STRING; 9606.ENSP00000396301; -.
DR   BindingDB; Q13123; -.
DR   ChEMBL; CHEMBL2321616; -.
DR   GlyGen; Q13123; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q13123; -.
DR   MetOSite; Q13123; -.
DR   PhosphoSitePlus; Q13123; -.
DR   SwissPalm; Q13123; -.
DR   BioMuta; IK; -.
DR   DMDM; 296452987; -.
DR   EPD; Q13123; -.
DR   jPOST; Q13123; -.
DR   MassIVE; Q13123; -.
DR   MaxQB; Q13123; -.
DR   PaxDb; 9606-ENSP00000396301; -.
DR   PeptideAtlas; Q13123; -.
DR   ProteomicsDB; 59173; -.
DR   Pumba; Q13123; -.
DR   Antibodypedia; 7468; 148 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   AGR; HGNC:5958; -.
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; YGPVQPS; -.
DR   OrthoDB; 228226at2759; -.
DR   PhylomeDB; Q13123; -.
DR   TreeFam; TF321907; -.
DR   PathwayCommons; Q13123; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q13123; -.
DR   BioGRID-ORCS; 3550; 633 hits in 1161 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 211 other cell types or tissues.
DR   ExpressionAtlas; Q13123; baseline and differential.
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:SF5; PROTEIN RED; 1.
DR   PANTHER; PTHR12765; RED PROTEIN IK FACTOR CYTOKINE IK; 1.
DR   Pfam; PF07807; RED_C; 1.
DR   Pfam; PF07808; RED_N; 1.
DR   Genevisible; Q13123; HS.
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
//