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RED_MOUSE
ID   RED_MOUSE               Reviewed;         557 AA.
AC   Q9Z1M8; Q8R0P0; Q95H93;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 141.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Erythroleukemia;
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, Eye, and Salivary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC       spliceosome. Auxiliary spliceosomal protein that regulates selection of
CC       alternative splice sites in a small set of target pre-mRNA species.
CC       Required for normal mitotic cell cycle progression. Recruits MAD1L1 and
CC       MAD2L1 to kinetochores, and is required to trigger the spindle assembly
CC       checkpoint. Required for normal accumulation of SMU1.
CC       {ECO:0000250|UniProtKB:Q13123}.
CC   -!- SUBUNIT: Component of the spliceosome B complex. Interacts with SMU1.
CC       Interacts with MAD1L1. May interact with DHX15.
CC       {ECO:0000250|UniProtKB:Q13123}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13123}. Nucleus,
CC       nucleoplasm {ECO:0000250|UniProtKB:Q13123}. Chromosome
CC       {ECO:0000250|UniProtKB:Q13123}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:Q13123}. 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       Colocalizes with MAD1L1 at mitotic spindle poles during metaphase and
CC       anaphase. {ECO:0000250|UniProtKB:Q13123}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
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DR   EMBL; AJ006130; CAA06880.1; -; mRNA.
DR   EMBL; BC014739; AAH14739.1; -; mRNA.
DR   EMBL; BC026569; AAH26569.1; -; mRNA.
DR   EMBL; BC029671; AAH29671.1; -; mRNA.
DR   EMBL; BC029694; AAH29694.1; -; mRNA.
DR   EMBL; BC033356; AAH33356.1; -; mRNA.
DR   CCDS; CCDS57119.1; -.
DR   RefSeq; NP_036009.1; NM_011879.2.
DR   AlphaFoldDB; Q9Z1M8; -.
DR   SMR; Q9Z1M8; -.
DR   BioGRID; 204851; 22.
DR   STRING; 10090.ENSMUSP00000007042; -.
DR   iPTMnet; Q9Z1M8; -.
DR   PhosphoSitePlus; Q9Z1M8; -.
DR   EPD; Q9Z1M8; -.
DR   MaxQB; Q9Z1M8; -.
DR   PaxDb; Q9Z1M8; -.
DR   PRIDE; Q9Z1M8; -.
DR   ProteomicsDB; 254911; -.
DR   Antibodypedia; 7468; 133 antibodies from 28 providers.
DR   DNASU; 24010; -.
DR   Ensembl; ENSMUST00000007042; ENSMUSP00000007042; ENSMUSG00000024474.
DR   GeneID; 24010; -.
DR   KEGG; mmu:24010; -.
DR   UCSC; uc033hgh.1; mouse.
DR   CTD; 3550; -.
DR   MGI; MGI:1345142; Ik.
DR   VEuPathDB; HostDB:ENSMUSG00000024474; -.
DR   eggNOG; KOG2498; Eukaryota.
DR   GeneTree; ENSGT00940000153727; -.
DR   HOGENOM; CLU_026814_2_0_1; -.
DR   InParanoid; Q9Z1M8; -.
DR   OMA; EPEYKSA; -.
DR   OrthoDB; 500537at2759; -.
DR   PhylomeDB; Q9Z1M8; -.
DR   TreeFam; TF321907; -.
DR   BioGRID-ORCS; 24010; 24 hits in 72 CRISPR screens.
DR   ChiTaRS; Ik; mouse.
DR   PRO; PR:Q9Z1M8; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q9Z1M8; protein.
DR   Bgee; ENSMUSG00000024474; Expressed in optic fissure and 260 other tissues.
DR   ExpressionAtlas; Q9Z1M8; baseline and differential.
DR   Genevisible; Q9Z1M8; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
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   Acetylation; Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Spliceosome; Ubl conjugation.
FT   CHAIN           1..557
FT                   /note="Protein Red"
FT                   /id="PRO_0000097236"
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..90
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..402
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:0000250|UniProtKB:Q13123"
FT   MOD_RES         137
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         287
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   MOD_RES         460
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         485
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   MOD_RES         536
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        310
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        331
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        386
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        388
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        404
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        408
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        496
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        501
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        509
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        541
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        543
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CROSSLNK        553
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13123"
FT   CONFLICT        91
FT                   /note="R -> G (in Ref. 1; CAA06880)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   557 AA;  65616 MW;  15FD9334FC974C13 CRC64;
     MPERDSEPFS NPLAPDGHDV DDPHSFHQSK LTNEDFRKLL MTPRAAPTSA PPSKSRHHEM
     PREYNEDEDP AARRRKKKSY YAKLRQQEIE RERELAEKYR DRAKERRDGV NKDYEETELI
     STTANYRAVG PTAEADKSAA EKRRQLIQES KFLGGDMEHT HLVKGLDFAL LQKVRAEIAS
     KEKEEEELME KPQKETKKDE DPENKIEFKT RLGRNVYRML FKSKSYERNE LFLPGRMAYV
     VDLDDEYADT DIPTTLIRSK ADCPTMEAQT TLTTNDIVIS KLTQILSYLR QGTRNKKLKK
     KDKGKLEEKK PPEADMNIFE DIGDYVPSTT KTPRDKERER YRERERDRER DRDRERDRER
     DRERERERDR EREREEEKKR HSYFEKPKVD DEPMDVDKGP GSAKELIKSI NEKFAGSAGW
     EGTESLKKPE DKKQLGDFFG MSNSYAECYP ATMDDMAVDS DEEVDYSKMD QGNKKGPLGR
     WDFDTQEEYS EYMNNKEALP KAAFQYGIKM SEGRKTRRFK ETNDKAELDR QWKKISAIIE
     KRKRMEADGV EVKRPKY
 
 
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