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Corepressor interacting with RBPJ 1 (CBF1-interacting corepressor) (Recepin)

 CIR1_HUMAN              Reviewed;         450 AA.
Q86X95; A6NFI6; A8K8M4; O95367; Q12804; Q4G1B9; Q6PJI4; Q8IWI2;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-APR-2018, entry version 127.
RecName: Full=Corepressor interacting with RBPJ 1;
AltName: Full=CBF1-interacting corepressor;
AltName: Full=Recepin;
Name=CIR1; Synonyms=CIR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RBPJ; SAP30 AND HDAC2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9874765; DOI=10.1073/pnas.96.1.23;
Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.;
"CIR, a corepressor linking the DNA binding factor CBF1 to the histone
deacetylase complex.";
Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Chai K.X., Li L., Chao J., Chao L.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, Lymph, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH SNW1.
PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
"A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
J. Virol. 74:1939-1947(2000).
[7]
INTERACTION WITH EPSTEIN-BARR VIRUS RPMS1, AND SUBCELLULAR LOCATION.
PubMed=11222720; DOI=10.1128/JVI.75.6.2946-2956.2001;
Zhang J., Chen H., Weinmaster G., Hayward S.D.;
"Epstein-Barr virus BamHi-a rightward transcript-encoded RPMS protein
interacts with the CBF1-associated corepressor CIR to negatively
regulate the activity of EBNA2 and NotchIC.";
J. Virol. 75:2946-2956(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, AND INTERACTION WITH NKAP.
PubMed=19409814; DOI=10.1016/j.immuni.2009.02.011;
Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S.;
"NKAP is a transcriptional repressor of notch signaling and is
required for T cell development.";
Immunity 30:696-707(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-340, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: May modulate splice site selection during alternative
splicing of pre-mRNAs (By similarity). Regulates transcription and
acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone
deacetylase complex (HDAC). Required for RBPJ-mediated repression
of transcription. {ECO:0000250, ECO:0000269|PubMed:19409814,
ECO:0000269|PubMed:9874765}.
-!- SUBUNIT: Interacts with RP9, SNW1, SFRS1, SFRS2,U2AF1, RBPJ,
SAP30, HDAC2 NKAP and NEK6. Interacts with Epstein-Barr virus
RPMS1. Component of the histone deacetylase complex. Component of
the Notch corepressor complex. Interacts with NKAPL (By
similarity). {ECO:0000250|UniProtKB:Q9DA19,
ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11222720,
ECO:0000269|PubMed:19409814, ECO:0000269|PubMed:20873783,
ECO:0000269|PubMed:9874765}.
-!- INTERACTION:
Q8TAP6:CEP76; NbExp=3; IntAct=EBI-627102, EBI-742887;
Q07955:SRSF1; NbExp=3; IntAct=EBI-627102, EBI-398920;
Q01130:SRSF2; NbExp=4; IntAct=EBI-627102, EBI-627047;
Q01081:U2AF1; NbExp=4; IntAct=EBI-627102, EBI-632461;
-!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Colocalizes with
NEK6 in the centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q86X95-1; Sequence=Displayed;
Name=2;
IsoId=Q86X95-2; Sequence=VSP_020091, VSP_020092;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta,
liver, skeletal muscle and pancreas. {ECO:0000269|PubMed:9874765}.
-!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.
-!- SEQUENCE CAUTION:
Sequence=AAA17853.1; Type=Frameshift; Positions=135, 151, 177, 203, 261, 299, 391, 410; Evidence={ECO:0000305};
Sequence=AAH21175.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH38987.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF098297; AAD05243.1; -; mRNA.
EMBL; U03644; AAA17853.1; ALT_FRAME; mRNA.
EMBL; AK292389; BAF85078.1; -; mRNA.
EMBL; AC018470; AAY24216.1; -; Genomic_DNA.
EMBL; BC015040; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC021175; AAH21175.1; ALT_SEQ; mRNA.
EMBL; BC038987; AAH38987.1; ALT_SEQ; mRNA.
EMBL; BC046098; AAH46098.1; -; mRNA.
CCDS; CCDS2256.1; -. [Q86X95-1]
PIR; G01227; G01227.
RefSeq; NP_004873.3; NM_004882.3. [Q86X95-1]
UniGene; Hs.632531; -.
ProteinModelPortal; Q86X95; -.
BioGrid; 114916; 23.
IntAct; Q86X95; 17.
MINT; Q86X95; -.
STRING; 9606.ENSP00000339723; -.
iPTMnet; Q86X95; -.
PhosphoSitePlus; Q86X95; -.
BioMuta; CIR1; -.
DMDM; 74727790; -.
EPD; Q86X95; -.
MaxQB; Q86X95; -.
PaxDb; Q86X95; -.
PeptideAtlas; Q86X95; -.
PRIDE; Q86X95; -.
Ensembl; ENST00000342016; ENSP00000339723; ENSG00000138433. [Q86X95-1]
GeneID; 9541; -.
KEGG; hsa:9541; -.
UCSC; uc002uim.4; human. [Q86X95-1]
CTD; 9541; -.
DisGeNET; 9541; -.
EuPathDB; HostDB:ENSG00000138433.15; -.
GeneCards; CIR1; -.
H-InvDB; HIX0023923; -.
HGNC; HGNC:24217; CIR1.
HPA; HPA015784; -.
MIM; 605228; gene.
neXtProt; NX_Q86X95; -.
OpenTargets; ENSG00000138433; -.
PharmGKB; PA165696415; -.
eggNOG; KOG3794; Eukaryota.
eggNOG; ENOG410ZVMR; LUCA.
GeneTree; ENSGT00730000111135; -.
InParanoid; Q86X95; -.
KO; K06066; -.
OMA; CSMYSIS; -.
OrthoDB; EOG091G0QUH; -.
PhylomeDB; Q86X95; -.
TreeFam; TF317567; -.
SignaLink; Q86X95; -.
SIGNOR; Q86X95; -.
ChiTaRS; CIR1; human.
GeneWiki; CIR_(gene); -.
GenomeRNAi; 9541; -.
PRO; PR:Q86X95; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138433; -.
ExpressionAtlas; Q86X95; baseline and differential.
Genevisible; Q86X95; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; TAS:BHF-UCL.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019339; CIR_N_dom.
Pfam; PF10197; Cir_N; 1.
SMART; SM01083; Cir_N; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 450 Corepressor interacting with RBPJ 1.
/FTId=PRO_0000247984.
REGION 1 121 Interaction with RBPJ.
{ECO:0000269|PubMed:9874765}.
REGION 204 232 Interaction with RP9. {ECO:0000250}.
MOTIF 235 245 Nuclear localization signal.
{ECO:0000255}.
MOTIF 291 298 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 214 368 Lys/Ser-rich.
COMPBIAS 369 450 Arg/Ser-rich (RS domain).
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 79 79 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 340 340 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 162 202 GPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVAS
-> DAVLQIEGFWAIDAPLGANSGDEKQWVCTETKCTGEKL
DRK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020091.
VAR_SEQ 203 450 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020092.
CONFLICT 48 48 K -> R (in Ref. 1; AAD05243).
{ECO:0000305}.
CONFLICT 113 113 N -> S (in Ref. 1; AAD05243).
{ECO:0000305}.
CONFLICT 172 172 A -> G (in Ref. 2; AAA17853).
{ECO:0000305}.
CONFLICT 325 325 S -> T (in Ref. 1; AAD05243 and 2;
AAA17853). {ECO:0000305}.
SEQUENCE 450 AA; 52313 MW; 5D0C1CBD9C87569D CRC64;
MGKSFANFMC KKDFHPASKS NIKKVWMAEQ KISYDKKKQE ELMQQYLKEQ ESYDNRLLMG
DERVKNGLNF MYEAPPGAKK ENKEKEETEG ETEYKFEWQK GAPREKYAKD DMNIRDQPFG
IQVRNVRCIK CHKWGHVNTD RECPLFGLSG INASSVPTDG SGPSMHPSEL IAEMRNSGFA
LKRNVLGRNL TANDPSQEYV ASEGEEDPEV EFLKSLTTKQ KQKLLRKLDR LEKKKKKKDR
KKKKFQKSRS KHKKHKSSSS SSSSSSSSSS TETSESSSES ESNNKEKKIQ RKKRKKNKCS
GHNNSDSEEK DKSKKRKLHE ELSSSHHNRE KAKEKPRFLK HESSREDSKW SHSDSDKKSR
THKHSPEKRG SERKEGSSRS HGREERSRRS RSRSPGSYKQ RETRKRAQRN PGEEQSRRND
SRSHGTDLYR GEKMYREHPG GTHTKVTQRE


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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