ID RED_HUMAN Reviewed; 557 AA. AC Q13123; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 13-OCT-2009, entry version 65. DE RecName: Full=Protein Red; DE AltName: Full=Protein RER; DE AltName: Full=IK factor; DE AltName: Full=Cytokine IK; 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 MEDLINE=99234094; 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 [MRNA] OF 316-477. RC TISSUE=Leukemia; RX MEDLINE=95060801; 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485, AND MASS RP SPECTROMETRY. 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS RP SPECTROMETRY. 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 [5] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-98; LYS-386 AND RP LYS-408, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: Not known. May bind to chromatin. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DEVELOPMENTAL STAGE: Expressed at similar levels in fetal and CC adult tissues. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the RED family. CC -!- CAUTION: Was originally (PubMed:7970704) thought to be the IK CC factor, a cytokine involved in the negative regulatory pathway of CC constitutive MHC class II antigens expression. 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; S74221; AAB32531.1; -; mRNA. DR IPI; IPI00011875; -. DR PIR; I58408; I58408. DR UniGene; Hs.421245; -. DR IntAct; Q13123; 6. DR STRING; Q13123; -. DR PhosphoSite; Q13123; -. DR PeptideAtlas; Q13123; -. DR PRIDE; Q13123; -. DR Ensembl; ENST00000261812; ENSP00000261812; ENSG00000113141; Homo sapiens. DR Ensembl; ENST00000417647; ENSP00000396301; ENSG00000113141; Homo sapiens. DR GeneID; 3550; -. DR GeneCards; GC05P139993; -. DR H-InvDB; HIX0005237; -. DR HGNC; HGNC:5958; IK. DR HPA; HPA019754; -. DR MIM; 600549; gene. DR PharmGKB; PA25354; -. DR HOGENOM; Q13123; -. DR HOVERGEN; Q13123; -. DR PMAP-CutDB; Q13123; -. DR ArrayExpress; Q13123; -. DR Bgee; Q13123; -. DR CleanEx; HS_IK; -. DR Genevestigator; Q13123; -. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005625; C:soluble fraction; TAS:ProtInc. 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. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Nucleus; Phosphoprotein; 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 83 83 N6-acetyllysine. FT MOD_RES 98 98 N6-acetyllysine. FT MOD_RES 386 386 N6-acetyllysine. FT MOD_RES 408 408 N6-acetyllysine. FT MOD_RES 460 460 Phosphoserine. FT MOD_RES 485 485 Phosphothreonine. SQ SEQUENCE 557 AA; 65630 MW; 09091E1FD4E4E5FD CRC64; MPERDSEPFS NPLAPDGHDV DDPHSFHQSK LTNEDFRKLL MTPRAAPTSA PPSKSRHHEM PREYNEDEDP AARRRKKKSY YAKLRQQEIE RERELAEKYR DRAKERRDGV NKDYEETELI STTANYRAVG PTAEADKSAA EKRRQLIQES KFLGGDMEHT HLVKGLDFAL LQKVRLEIAS KDKEEEELME 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 //