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 16-OCT-2019, entry version 153. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL RP 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., RA Bardos J., Freemont P., Charron D., Trowsdale J., Rich T.; RT "Isolation, sequencing and expression of RED, a novel human gene RT encoding 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., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA 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 RT project: 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 RT antibodies, cloning and chromosome localization."; RL Oncogene 9:3449-3456(1994). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485, AND IDENTIFICATION RP BY 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, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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 RP 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 [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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, AND IDENTIFICATION BY RP 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., RA Walther T.C., 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., RA Buerckstuemmer T., 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 RP 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 RT spindle 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., RA Weimann M., Will C.L., Pena V., Luehrmann R., Stelzl U.; RT "Dynamic protein-protein interaction wiring of the human RT 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 RT forms 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 RP SER-536, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-544, AND IDENTIFICATION BY RP MASS 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 RP PB1 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., RA Vidalain P.O., Jacob Y., Naffakh N.; RT "Recruitment of RED-SMU1 complex by Influenza A Virus RNA polymerase RT to 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; RP LYS-386; LYS-388; LYS-404; LYS-408; LYS-496; LYS-501; LYS-509; RP LYS-541; LYS-543; LYS-544 AND LYS-553, 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- RT modification 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 CC cell cycle progression (PubMed:22351768, PubMed:24252166). CC Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to CC trigger the spindle assembly checkpoint (PubMed:22351768). CC Required for normal accumulation of SMU1 (PubMed:24945353). CC {ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:24252166, CC ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166, CC ECO:0000305}. CC -!- FUNCTION: (Microbial infection) Required, together with SMU1, for CC normal splicing of influenza A virus NS1 pre-mRNA, which is CC required for the production of the exportin NS2 and for the CC production of influenza A virus particles. Not required for the CC production of VSV virus particles. {ECO:0000269|PubMed:24945353}. CC -!- SUBUNIT: (Microbial infection) Identified in a complex with SMU1 CC and influenza A virus RNA polymerase subunits PB1 and PB2. CC Directly interacts with SMU1 and with influenza A virus RNA CC polymerase subunits 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 CC interact with DHX15 (PubMed:24252166). CC {ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:24945353, CC ECO:0000269|PubMed:28781166, ECO:0000305|PubMed:22365833, CC 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}. CC Chromosome {ECO:0000269|PubMed:24252166}. Cytoplasm, cytoskeleton, CC spindle pole {ECO:0000269|PubMed:22351768}. Note=Predominantly CC present throughout the nucleoplasm during prometaphase, metaphase CC and anaphase. Is also detected in nuclear foci that are not CC identical with Cajal bodies. Starts to accumulate at chromosomes CC during telophase, and is nearly exclusively associated with CC chromosomes in newly divided cells (PubMed:24252166). Colocalizes CC with MAD1L1 at mitotic spindle poles during metaphase and anaphase CC (PubMed:22351768). {ECO:0000269|PubMed:24252166}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10216252}. CC -!- DEVELOPMENTAL STAGE: Expressed at similar levels in fetal and CC adult 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 CC class 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 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; -. DR PMAP-CutDB; Q13123; -. DR PRO; PR:Q13123; -. DR Proteomes; UP000005640; Chromosome 5. 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; Complete proteome; Cytoplasm; KW Cytoskeleton; Host-virus interaction; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Spliceosome; Ubl conjugation. FT CHAIN 1 557 Protein Red. FT /FTId=PRO_0000097235. FT REPEAT 342 343 1. FT REPEAT 344 345 2. FT REPEAT 346 347 3. FT REPEAT 348 349 4. FT REPEAT 350 351 5. FT REPEAT 352 353 6. FT REPEAT 354 355 7. FT REPEAT 356 357 8. FT REPEAT 358 359 9. FT REPEAT 360 361 10. FT REPEAT 362 363 11. FT REPEAT 364 365 12. FT REPEAT 366 367 13. FT REPEAT 368 369 14. FT REPEAT 370 371 15. FT REPEAT 372 373 16. FT REPEAT 374 375 17. FT REGION 342 375 17 X 2 AA tandem repeats of R-[ED]. FT COMPBIAS 182 187 Poly-Glu. {ECO:0000255}. FT COMPBIAS 334 374 Arg-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00002}. FT MOD_RES 98 98 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 137 137 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9Z1M8}. FT MOD_RES 287 287 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 417 417 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 460 460 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 485 485 Phosphothreonine. FT {ECO:0000244|PubMed:17525332}. FT MOD_RES 536 536 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT CROSSLNK 151 151 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 310 310 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 404 404 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 408 408 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 496 496 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 501 501 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 509 509 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 541 541 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 543 543 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 544 544 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 553 553 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CONFLICT 176 176 A -> L (in Ref. 1; CAA06607). FT {ECO:0000305}. FT CONFLICT 182 182 E -> D (in Ref. 1; CAA06607). FT {ECO:0000305}. FT HELIX 212 220 {ECO:0000244|PDB:6Q8I}. FT STRAND 233 236 {ECO:0000244|PDB:6Q8I}. FT STRAND 238 240 {ECO:0000244|PDB:6Q8I}. FT STRAND 254 256 {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 //