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 11-DEC-2019, entry version 154. 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:0000244|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 Self; NbExp=2; IntAct=EBI-713456, EBI-713456; CC O14965:AURKA; NbExp=3; IntAct=EBI-713456, EBI-448680; CC Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-713456, EBI-739624; CC Q15029:EFTUD2; NbExp=2; IntAct=EBI-713456, EBI-357897; CC Q70Z53:FRA10AC1; NbExp=2; IntAct=EBI-713456, EBI-710176; CC P55081:MFAP1; NbExp=2; IntAct=EBI-713456, EBI-1048159; CC O94906:PRPF6; NbExp=2; IntAct=EBI-713456, EBI-536755; CC P98175:RBM10; NbExp=2; IntAct=EBI-713456, EBI-721525; CC P04618:rev (xeno); NbExp=3; IntAct=EBI-713456, EBI-6164309; CC O15541:RNF113A; NbExp=2; IntAct=EBI-713456, EBI-2130294; CC Q2TAY7:SMU1; NbExp=7; IntAct=EBI-713456, EBI-298027; CC Q8TAD8:SNIP1; NbExp=2; IntAct=EBI-713456, EBI-749336; CC Q9HCS7:XAB2; NbExp=2; IntAct=EBI-713456, EBI-295232; CC Q96NB3:ZNF830; NbExp=2; IntAct=EBI-713456, EBI-3920997; 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 SMR; Q13123; -. DR BioGrid; 109766; 97. DR CORUM; Q13123; -. DR IntAct; Q13123; 64. DR MINT; Q13123; -. DR STRING; 9606.ENSP00000396301; -. DR BindingDB; Q13123; -. DR ChEMBL; CHEMBL2321616; -. DR iPTMnet; 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 Ensembl; ENST00000417647; ENSP00000396301; ENSG00000113141. DR GeneID; 3550; -. DR KEGG; hsa:3550; -. DR UCSC; uc003lgq.4; human. DR CTD; 3550; -. DR DisGeNET; 3550; -. DR EuPathDB; HostDB:ENSG00000113141.15; -. DR GeneCards; IK; -. DR HGNC; HGNC:5958; IK. DR HPA; HPA048798; -. DR MIM; 600549; gene. DR neXtProt; NX_Q13123; -. DR OpenTargets; ENSG00000113141; -. DR PharmGKB; PA29774; -. DR eggNOG; KOG2498; Eukaryota. DR eggNOG; ENOG410YR3Z; LUCA. DR GeneTree; ENSGT00940000153727; -. DR HOGENOM; HOG000007717; -. DR InParanoid; Q13123; -. DR KO; K13109; -. DR OMA; LEEMNDA; -. DR OrthoDB; 500537at2759; -. DR PhylomeDB; Q13123; -. DR TreeFam; TF321907; -. 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 236 organ(s), highest expression level in testis. 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; 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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. 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 342..375 FT /note="17 X 2 AA tandem repeats of R-[ED]" FT COMPBIAS 182..187 FT /note="Poly-Glu" FT /evidence="ECO:0000255" FT COMPBIAS 334..374 FT /note="Arg-rich" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00002" FT MOD_RES 98 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|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:0000244|PubMed:23186163" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648" FT MOD_RES 485 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:17525332" FT MOD_RES 536 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT CROSSLNK 151 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 310 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 331 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 386 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 388 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 404 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 408 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 496 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 501 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 509 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 541 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 543 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 544 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733" FT CROSSLNK 553 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|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:0000244|PDB:6Q8I" FT STRAND 233..236 FT /evidence="ECO:0000244|PDB:6Q8I" FT STRAND 238..240 FT /evidence="ECO:0000244|PDB:6Q8I" FT STRAND 254..256 FT /evidence="ECO:0000244|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 //