ID   CIR1_RAT                Reviewed;         451 AA.
AC   Q5U2T8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Corepressor interacting with RBPJ 1;
DE   AltName: Full=CBF1-interacting corepressor;
GN   Name=Cir1; Synonyms=Cir;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May modulate splice site selection during alternative
CC       splicing of pre-mRNAs. Regulates transcription and acts as corepressor
CC       for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC).
CC       Required for RBPJ-mediated repression of transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RP9, SNW1, SFRS1, SFRS2,U2AF1, RBPJ, SAP30,
CC       HDAC2 NKAP and NEK6. Interacts with Epstein-Barr virus RPMS1. Component
CC       of the histone deacetylase complex. Component of the Notch corepressor
CC       complex. Interacts with NKAPL. {ECO:0000250|UniProtKB:Q86X95,
CC       ECO:0000250|UniProtKB:Q9DA19}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Note=Colocalizes with NEK6 in the centrosome. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
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DR   EMBL; BC085869; AAH85869.1; -; mRNA.
DR   RefSeq; NP_001007800.1; NM_001007799.1.
DR   AlphaFoldDB; Q5U2T8; -.
DR   SMR; Q5U2T8; -.
DR   STRING; 10116.ENSRNOP00000060978; -.
DR   iPTMnet; Q5U2T8; -.
DR   PhosphoSitePlus; Q5U2T8; -.
DR   PaxDb; Q5U2T8; -.
DR   PRIDE; Q5U2T8; -.
DR   Ensembl; ENSRNOT00000064662; ENSRNOP00000060978; ENSRNOG00000018719.
DR   GeneID; 362149; -.
DR   KEGG; rno:362149; -.
DR   CTD; 9541; -.
DR   RGD; 1309199; Cir1.
DR   eggNOG; KOG3794; Eukaryota.
DR   GeneTree; ENSGT00730000111135; -.
DR   HOGENOM; CLU_035642_2_0_1; -.
DR   InParanoid; Q5U2T8; -.
DR   OMA; HKKKHES; -.
DR   OrthoDB; 1604301at2759; -.
DR   PRO; PR:Q5U2T8; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000018719; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q5U2T8; RN.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR040014; CIR1.
DR   InterPro; IPR019339; CIR_N_dom.
DR   PANTHER; PTHR13151; PTHR13151; 1.
DR   Pfam; PF10197; Cir_N; 1.
DR   SMART; SM01083; Cir_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Isopeptide bond; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..451
FT                   /note="Corepressor interacting with RBPJ 1"
FT                   /id="PRO_0000247986"
FT   REGION          1..121
FT                   /note="Interaction with RBPJ"
FT                   /evidence="ECO:0000250"
FT   REGION          204..232
FT                   /note="Interaction with RP9"
FT                   /evidence="ECO:0000250"
FT   REGION          213..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           233..247
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           307..315
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        213..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..261
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        79
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86X95"
FT   CROSSLNK        355
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q86X95"
SQ   SEQUENCE   451 AA;  51416 MW;  600B045F9452BD25 CRC64;
     MGKSFANFMC KKDFHPASKS NIKKVWMAEQ KISYDKKKQE ELMQQYLKEQ ESYDNRLLMG
     DERVKNGLNF MYEAPPGVKK ENKEKEETEG ETEYKFEWQK GAPREKYAKD DMNIRDQPFG
     IQVRNVRCIK CHKWGHVNTD RECPLFGLSG INASSVPTDG SGPSMHPSEL IAEMRNSGFA
     LKRNVLGRNL TANDPSQDYV ASDGEEDPEV EFLKSLTTKQ KQKLLRKLDR LEKKKKKKKS
     DKKKKKLQKS KNKHKKHKKS SSSSSSSSSS SSSSSSSSSS SSSSSTSSSE TDSSSESDNK
     EKKEKEKRKK RKKTKCSGNK SGDCKEYKSK NMLYEELSSS HSDRGKAQEK LRLLKQESSG
     ENSTWVHSGS DRKSRSHQHS PERKGSDRNG GSRSRSRAEG SRRSRSRSPC GQKHREREAR
     SRPHQSPSEE QKGRKGTRSH GDSEHRRERA R