CENPR_MOUSE
ID CENPR_MOUSE Reviewed; 176 AA.
AC Q9CQ82; Q3TLR0; Q3TNR4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Centromere protein R;
DE Short=CENP-R;
DE AltName: Full=Nuclear receptor-interacting factor 3;
GN Name=Itgb3bp; Synonyms=Cenpr, Nrif3;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Mammary gland, Oviduct, and 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 1).
RC TISSUE=Testis;
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 INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: Transcription coregulator that can have both coactivator and
CC corepressor functions. Involved in the coactivation of nuclear
CC receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-
CC dependent fashion. In contrast, it does not coactivate nuclear
CC receptors for retinoic acid, vitamin D, progesterone receptor, nor
CC glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts
CC as a transcriptional corepressor via its interaction with the NFKB1 NF-
CC kappa-B subunit, possibly by interfering with the transactivation
CC domain of NFKB1. Induces apoptosis in breast cancer cells, but not in
CC other cancer cells, via a caspase-2 mediated pathway that involves
CC mitochondrial membrane permeabilization but does not require other
CC caspases. May also act as an inhibitor of cyclin A-associated kinase.
CC Also acts a component of the CENPA-CAD (nucleosome distal) complex, a
CC complex recruited to centromeres which is involved in assembly of
CC kinetochore proteins, mitotic progression and chromosome segregation.
CC May be involved in incorporation of newly synthesized CENPA into
CC centromeres via its interaction with the CENPA-NAC complex (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; mediated by the coiled coil domain. Interacts with
CC CCNA2 and MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of
CC the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP,
CC CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-
CC NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN,
CC CENPT and CENPU (By similarity). Interacts with TASOR
CC (PubMed:31112734). {ECO:0000250|UniProtKB:Q13352,
CC ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQ82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQ82-2; Sequence=VSP_020453, VSP_020454;
CC -!- TISSUE SPECIFICITY: Expressed in the spermatogonia and spermatocytes.
CC {ECO:0000269|PubMed:31112734}.
CC -!- DOMAIN: The DD1 domain (also called RepD1 domain) mediates the
CC corepressor function and is essential in the triggering of apoptosis.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is
CC essential for the association with nuclear receptors. {ECO:0000250}.
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DR EMBL; AK005779; BAB24235.1; -; mRNA.
DR EMBL; AK013373; BAB28815.1; -; mRNA.
DR EMBL; AK015557; BAB29892.1; -; mRNA.
DR EMBL; AK045037; BAC32192.1; -; mRNA.
DR EMBL; AK165072; BAE38024.1; -; mRNA.
DR EMBL; AK166362; BAE38732.1; -; mRNA.
DR EMBL; BC049557; AAH49557.1; -; mRNA.
DR CCDS; CCDS18387.1; -. [Q9CQ82-1]
DR RefSeq; NP_080624.1; NM_026348.3. [Q9CQ82-1]
DR AlphaFoldDB; Q9CQ82; -.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR CORUM; Q9CQ82; -.
DR STRING; 10090.ENSMUSP00000117153; -.
DR iPTMnet; Q9CQ82; -.
DR PhosphoSitePlus; Q9CQ82; -.
DR EPD; Q9CQ82; -.
DR jPOST; Q9CQ82; -.
DR MaxQB; Q9CQ82; -.
DR PaxDb; Q9CQ82; -.
DR PeptideAtlas; Q9CQ82; -.
DR PRIDE; Q9CQ82; -.
DR ProteomicsDB; 281190; -. [Q9CQ82-1]
DR ProteomicsDB; 281191; -. [Q9CQ82-2]
DR Antibodypedia; 33352; 215 antibodies from 30 providers.
DR DNASU; 67733; -.
DR Ensembl; ENSMUST00000146258; ENSMUSP00000117153; ENSMUSG00000028549. [Q9CQ82-1]
DR GeneID; 67733; -.
DR KEGG; mmu:67733; -.
DR UCSC; uc008tux.1; mouse. [Q9CQ82-1]
DR CTD; 23421; -.
DR MGI; MGI:1914983; Itgb3bp.
DR VEuPathDB; HostDB:ENSMUSG00000028549; -.
DR eggNOG; ENOG502S4AR; Eukaryota.
DR GeneTree; ENSGT00390000004336; -.
DR HOGENOM; CLU_122442_0_0_1; -.
DR InParanoid; Q9CQ82; -.
DR OMA; TRQMSPF; -.
DR OrthoDB; 1343610at2759; -.
DR PhylomeDB; Q9CQ82; -.
DR TreeFam; TF336291; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 67733; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Itgb3bp; mouse.
DR PRO; PR:Q9CQ82; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CQ82; protein.
DR Bgee; ENSMUSG00000028549; Expressed in testis and 62 other tissues.
DR Genevisible; Q9CQ82; MM.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR009601; CENP-R.
DR PANTHER; PTHR15581; PTHR15581; 1.
DR Pfam; PF06729; CENP-R; 1.
DR PIRSF; PIRSF011860; NRIF3_coact_rcpt; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Apoptosis; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; Isopeptide bond; Kinetochore; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..176
FT /note="Centromere protein R"
FT /id="PRO_0000057950"
FT REGION 20..50
FT /note="DD1"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..112
FT /evidence="ECO:0000255"
FT MOTIF 63..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 171..175
FT /note="LXXIL motif"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020453"
FT VAR_SEQ 78..84
FT /note="TVKDRDG -> MISLKKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020454"
FT CONFLICT 7
FT /note="L -> V (in Ref. 1; BAE38732)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="P -> S (in Ref. 1; BAE38732)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> S (in Ref. 1; BAE38732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20026 MW; B55F0C100CAE5973 CRC64;
MPVKRSLKLD DQFEKNSFSP SKIVRKKSIT AYSPTTGTYQ LSPFSSPATP KEQEHRNGPS
NETRKRSNLS SPVRQESTVK DRDGFMVLLS KIEISSEKTM EIMKNLSSIQ ALEGNRQLED
LIGVSLVPCS LKSEARKTKE LMTKVIKQKL FEKKKSRITP KDHHLDSFEF LKAILN
