CIR1_MOUSE
ID CIR1_MOUSE Reviewed; 450 AA.
AC Q9DA19; Q3V2N9; Q4KL44; Q52KL9; Q5FW66;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Corepressor interacting with RBPJ 1;
DE AltName: Full=CBF1-interacting corepressor;
GN Name=Cir1; Synonyms=Cir;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-304 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Heart, Mammary tumor, and Thyroid;
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 FUNCTION, INTERACTION WITH RP9; SNW1; SFRS1; SFRS2 AND U2AF1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15652350; DOI=10.1016/j.yexcr.2004.10.012;
RA Maita H., Kitaura H., Ariga H., Iguchi-Ariga S.M.M.;
RT "CIR, a corepressor of CBF1, binds to PAP-1 and effects alternative
RT splicing.";
RL Exp. Cell Res. 303:375-387(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and 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 INTERACTION WITH NKAPL.
RX PubMed=25875095; DOI=10.1371/journal.pone.0124293;
RA Okuda H., Kiuchi H., Takao T., Miyagawa Y., Tsujimura A., Nonomura N.,
RA Miyata H., Okabe M., Ikawa M., Kawakami Y., Goshima N., Wada M., Tanaka H.;
RT "A novel transcriptional factor Nkapl is a germ cell-specific suppressor of
RT Notch signaling and is indispensable for spermatogenesis.";
RL PLoS ONE 10:E0124293-E0124293(2015).
CC -!- FUNCTION: Regulates transcription and acts as corepressor for RBPJ.
CC Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required
CC for RBPJ-mediated repression of transcription (By similarity). May
CC modulate splice site selection during alternative splicing of pre-
CC mRNAs. {ECO:0000250, ECO:0000269|PubMed:15652350}.
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 (PubMed:25875095).
CC {ECO:0000250|UniProtKB:Q86X95, ECO:0000269|PubMed:15652350,
CC ECO:0000269|PubMed:25875095}.
CC -!- INTERACTION:
CC Q9DA19; P97762: rp9; NbExp=6; IntAct=EBI-309693, EBI-626715;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15652350}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DA19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DA19-3; Sequence=VSP_020093;
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94283.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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; AK006260; BAB24488.1; -; mRNA.
DR EMBL; AK131674; BAE20758.1; -; mRNA.
DR EMBL; BC089602; AAH89602.1; -; mRNA.
DR EMBL; BC094283; AAH94283.1; ALT_SEQ; mRNA.
DR EMBL; BC099444; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS16127.1; -. [Q9DA19-1]
DR RefSeq; NP_080130.2; NM_025854.3. [Q9DA19-1]
DR AlphaFoldDB; Q9DA19; -.
DR SMR; Q9DA19; -.
DR BioGRID; 211822; 4.
DR IntAct; Q9DA19; 3.
DR MINT; Q9DA19; -.
DR STRING; 10090.ENSMUSP00000049834; -.
DR iPTMnet; Q9DA19; -.
DR PhosphoSitePlus; Q9DA19; -.
DR EPD; Q9DA19; -.
DR jPOST; Q9DA19; -.
DR MaxQB; Q9DA19; -.
DR PaxDb; Q9DA19; -.
DR PeptideAtlas; Q9DA19; -.
DR PRIDE; Q9DA19; -.
DR ProteomicsDB; 279082; -. [Q9DA19-1]
DR ProteomicsDB; 279083; -. [Q9DA19-3]
DR Antibodypedia; 19463; 142 antibodies from 24 providers.
DR DNASU; 66935; -.
DR Ensembl; ENSMUST00000058615; ENSMUSP00000049834; ENSMUSG00000041777. [Q9DA19-1]
DR GeneID; 66935; -.
DR KEGG; mmu:66935; -.
DR UCSC; uc008kck.2; mouse. [Q9DA19-1]
DR CTD; 9541; -.
DR MGI; MGI:1914185; Cir1.
DR VEuPathDB; HostDB:ENSMUSG00000041777; -.
DR eggNOG; KOG3794; Eukaryota.
DR GeneTree; ENSGT00730000111135; -.
DR HOGENOM; CLU_035642_2_0_1; -.
DR InParanoid; Q9DA19; -.
DR OMA; HKKKHES; -.
DR OrthoDB; 1604301at2759; -.
DR PhylomeDB; Q9DA19; -.
DR TreeFam; TF317567; -.
DR BioGRID-ORCS; 66935; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Cir1; mouse.
DR PRO; PR:Q9DA19; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DA19; protein.
DR Bgee; ENSMUSG00000041777; Expressed in bone marrow and 71 other tissues.
DR Genevisible; Q9DA19; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
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 Alternative splicing; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..450
FT /note="Corepressor interacting with RBPJ 1"
FT /id="PRO_0000247985"
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:0000269|PubMed:15652350"
FT REGION 218..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 235..247
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 307..314
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 228..261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..450
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:21183079"
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 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86X95"
FT VAR_SEQ 107..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020093"
FT CONFLICT 9
FT /note="M -> T (in Ref. 2; AAH89602)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..272
FT /note="Missing (in Ref. 2; AAH94283)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> T (in Ref. 2; BAB24488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 51838 MW; 242A44EE6E89C374 CRC64;
MGKSFANFMC KKDFHPASKS NIKKVWMAEQ KISYDKKKQE ELMQQYLKEQ ESYDNRLLMG
DERVKNGLNF MYEAPPGVKK ENKEKEETEG ETEYKFEWQK GAPREKYAKD DMNIRDQPFG
IQVRNVRCIK CHKWGHVNTD RECPLFGLSG INASSVPTDG SGPSMHPSEL IAEMRNSGFA
LKRNVLGRNL TANDPSQDYV ASDCEEDPEV EFLKSLTTKQ KQKLLRKLDR LEKKKKKKKS
DKKKKKLQKS KNKHKKRKNK SPSSSSSSSS SSSSSSSSSS SSSSSSETSD SSSESDNKEK
KREKEKRKKK KKTKCSESKS SDCKEDKPKN MLYEELSSSH SDRGKAQEKL RFPKQESSGE
NSMWVHSASD RTSRSHRHSP EKKGSDRNRG IRSRSRSRAE SSRRSRSRSP YRQKHREVRS
RPHRSPSEEQ KGRKGTRSHG EGDHRREHVR
