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 07-JAN-2015, entry version 111. DE RecName: Full=Protein Red; DE AltName: Full=Cytokine IK; DE AltName: Full=IK factor; DE AltName: Full=Protein RER; GN Name=IK; Synonyms=RED, 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]. 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). CC -!- FUNCTION: May bind to chromatin. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-713456, EBI-713456; CC O14965:AURKA; NbExp=3; IntAct=EBI-713456, EBI-448680; 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=2; 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. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DEVELOPMENTAL STAGE: Expressed at similar levels in fetal and CC adult tissues. 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 UniGene; Hs.421245; -. DR ProteinModelPortal; Q13123; -. DR BioGrid; 109766; 71. DR IntAct; Q13123; 32. DR MINT; MINT-1371308; -. DR STRING; 9606.ENSP00000396301; -. DR BindingDB; Q13123; -. DR ChEMBL; CHEMBL2321616; -. DR PhosphoSite; Q13123; -. DR DMDM; 296452987; -. DR MaxQB; Q13123; -. DR PaxDb; Q13123; -. DR PeptideAtlas; Q13123; -. DR PRIDE; Q13123; -. DR Ensembl; ENST00000417647; ENSP00000396301; ENSG00000113141. DR Ensembl; ENST00000610522; ENSP00000481369; ENSG00000113141. DR GeneID; 3550; -. DR KEGG; hsa:3550; -. DR UCSC; uc003lgq.3; human. DR CTD; 3550; -. DR GeneCards; GC05P140028; -. DR HGNC; HGNC:5958; IK. DR HPA; HPA019754; -. DR MIM; 600549; gene. DR neXtProt; NX_Q13123; -. DR PharmGKB; PA29774; -. DR eggNOG; NOG85622; -. DR GeneTree; ENSGT00630000089902; -. DR HOGENOM; HOG000007717; -. DR HOVERGEN; HBG017223; -. DR InParanoid; Q13123; -. DR KO; K13109; -. DR OMA; IDIDKGP; -. DR OrthoDB; EOG7RNK0J; -. DR PhylomeDB; Q13123; -. DR TreeFam; TF321907; -. DR ChiTaRS; IK; human. DR GeneWiki; IK_(gene); -. DR GenomeRNAi; 3550; -. DR NextBio; 13860; -. DR PMAP-CutDB; Q13123; -. DR PRO; PR:Q13123; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; Q13123; -. DR CleanEx; HS_IK; -. DR ExpressionAtlas; Q13123; baseline and differential. DR Genevestigator; Q13123; -. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR InterPro; IPR012492; RED_C. DR InterPro; IPR012916; RED_N. DR Pfam; PF07807; RED_C; 1. DR Pfam; PF07808; RED_N; 1. DR ProDom; PD311621; RED_C; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Nucleus; Phosphoprotein; KW Reference proteome; Repeat. 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 184 187 Poly-Glu. FT MOD_RES 98 98 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 137 137 N6-acetyllysine. {ECO:0000250}. FT MOD_RES 460 460 Phosphoserine. FT {ECO:0000269|PubMed:18669648}. FT MOD_RES 485 485 Phosphothreonine. FT {ECO:0000269|PubMed:17525332}. 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}. 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 //