CENPR_HUMAN
ID CENPR_HUMAN Reviewed; 177 AA.
AC Q13352; B2R7D8; Q13353; Q5RJ42; Q5RJ44; Q5RJ45; Q7KYX2; Q96CD5; Q9UKB6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Centromere protein R;
DE Short=CENP-R;
DE AltName: Full=Beta-3-endonexin;
DE AltName: Full=Integrin beta-3-binding protein;
DE AltName: Full=Nuclear receptor-interacting factor 3;
GN Name=ITGB3BP; Synonyms=CENPR, NRIF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP INTERACTION WITH ITGB3.
RC TISSUE=B-cell;
RX PubMed=7593198; DOI=10.1083/jcb.131.3.807;
RA Shattil S.J., O'Toole T.E., Eigenthaler M.J., Thon V., Williams M.J.,
RA Babior B.M., Ginsberg M.H.;
RT "Beta 3-endonexin, a novel polypeptide that interacts specifically with the
RT cytoplasmic tail of the integrin beta 3 subunit.";
RL J. Cell Biol. 131:807-816(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COACTIVATOR FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH RXRA AND THRA, AND MUTAGENESIS OF LEU-9 AND
RP 172-LEU--LEU-176.
RC TISSUE=Cervix carcinoma;
RX PubMed=10490654; DOI=10.1128/mcb.19.10.7191;
RA Li D., Desai-Yajnik V., Lo E., Schapira M., Abagyan R., Samuels H.H.;
RT "NRIF3 is a novel coactivator mediating functional specificity of nuclear
RT hormone receptors.";
RL Mol. Cell. Biol. 19:7191-7202(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Bone marrow, and Placenta;
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 [6]
RP ALTERNATIVE SPLICING (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF 63-LYS--LYS-65.
RX PubMed=11864709; DOI=10.1016/s0049-3848(01)00405-4;
RA Fujimoto T.-T., Katsutani S., Shimomura T., Fujimura K.;
RT "Novel alternatively spliced form of beta(3)-endonexin.";
RL Thromb. Res. 105:63-70(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9182673; DOI=10.1083/jcb.137.6.1433;
RA Kashiwagi H., Schwartz M.A., Eigenthaler M., Davis K.A., Ginsberg M.H.,
RA Shattil S.J.;
RT "Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin,
RT a selective binding partner of the beta3 integrin cytoplasmic tail.";
RL J. Cell Biol. 137:1433-1443(1997).
RN [8]
RP INTERACTION WITH CCNA2.
RX PubMed=10673397; DOI=10.1006/bbrc.1999.2007;
RA Ohtoshi A., Maeda T., Higashi H., Ashizawa S., Yamada M., Hatakeyama M.;
RT "Beta3-endonexin as a novel inhibitor of cyclin A-associated kinase.";
RL Biochem. Biophys. Res. Commun. 267:947-952(2000).
RN [9]
RP FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, HOMODIMERIZATION,
RP PHOSPHORYLATION AT SER-28, AND MUTAGENESIS OF SER-28; LEU-89 AND LEU-96.
RX PubMed=11713274; DOI=10.1128/mcb.21.24.8371-8384.2001;
RA Li D., Wang F., Samuels H.H.;
RT "Domain structure of the NRIF3 family of coregulators suggests potential
RT dual roles in transcriptional regulation.";
RL Mol. Cell. Biol. 21:8371-8384(2001).
RN [10]
RP FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, INTERACTION WITH NFKB1,
RP AND MUTAGENESIS OF 63-LYS--LYS-66.
RX PubMed=12244126; DOI=10.1242/jcs.00081;
RA Besta F., Massberg S., Brand K., Mueller E., Page S., Gruener S.,
RA Lorenz M., Sadoul K., Kolanus W., Lengyel E., Gawaz M.;
RT "Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent
RT expression of urokinase-type plasminogen activator receptor.";
RL J. Cell Sci. 115:3879-3888(2002).
RN [11]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF SER-28.
RX PubMed=15082778; DOI=10.1128/mcb.24.9.3838-3848.2004;
RA Li D., Das S., Yamada T., Samuels H.H.;
RT "The NRIF3 family of transcriptional coregulators induces rapid and
RT profound apoptosis in breast cancer cells.";
RL Mol. Cell. Biol. 24:3838-3848(2004).
RN [12]
RP FUNCTION, INDUCTION, AND INTERACTION WITH MTA1.
RX PubMed=15254226; DOI=10.1128/mcb.24.15.6581-6591.2004;
RA Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R.;
RT "Metastasis-associated protein 1 interacts with NRIF3, an estrogen-
RT inducible nuclear receptor coregulator.";
RL Mol. Cell. Biol. 24:6581-6591(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP CENPH; CENPI; CENPK; CENPN; CENPO; CENPP; CENPQ AND CENPU, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16622420; DOI=10.1038/ncb1396;
RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA Desai A., Fukagawa T.;
RT "The CENP-H-I complex is required for the efficient incorporation of newly
RT synthesized CENP-A into centromeres.";
RL Nat. Cell Biol. 8:446-457(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD
RP COMPLEX WITH CENPI; CENPK; CENPL; CENPO; CENPP; CENPQ AND CENPS.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-71, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-71, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-22, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription coregulator that can have both coactivator and
CC corepressor functions. Isoform 1, but not other isoforms, is involved
CC in the coactivation of nuclear receptors for retinoid X (RXRs) and
CC thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it
CC does not coactivate nuclear receptors for retinoic acid, vitamin D,
CC progesterone receptor, nor glucocorticoid. Acts as a coactivator for
CC estrogen receptor alpha. Acts as a transcriptional corepressor via its
CC interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering
CC with the transactivation domain of NFKB1. Induces apoptosis in breast
CC cancer cells, but not in other cancer cells, via a caspase-2 mediated
CC pathway that involves mitochondrial membrane permeabilization but does
CC not require other caspases. May also act as an inhibitor of cyclin A-
CC associated kinase. Also acts a component of the CENPA-CAD (nucleosome
CC distal) complex, a complex recruited to centromeres which is involved
CC in assembly of kinetochore proteins, mitotic progression and chromosome
CC segregation. May be involved in incorporation of newly synthesized
CC CENPA into centromeres via its interaction with the CENPA-NAC complex.
CC {ECO:0000269|PubMed:11713274, ECO:0000269|PubMed:12244126,
CC ECO:0000269|PubMed:15082778, ECO:0000269|PubMed:15254226,
CC ECO:0000269|PubMed:16622420}.
CC -!- SUBUNIT: Homodimer; mediated by the coiled coil domain. Isoform 3, but
CC not other isoforms, interacts with the cytoplasmic tail of integrin
CC ITGB3. The relevance of the interaction with ITGB3 is however
CC uncertain, since isoform 3 is mainly nuclear. Interacts with CCNA2 and
CC MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of the CENPA-
CC CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ,
CC CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC
CC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT
CC and CENPU. Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQ82, ECO:0000269|PubMed:10490654,
CC ECO:0000269|PubMed:10673397, ECO:0000269|PubMed:12244126,
CC ECO:0000269|PubMed:15254226, ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:7593198}.
CC -!- INTERACTION:
CC Q13352; X5D778: ANKRD11; NbExp=3; IntAct=EBI-712105, EBI-17183751;
CC Q13352; P53365: ARFIP2; NbExp=4; IntAct=EBI-712105, EBI-638194;
CC Q13352; P46379-2: BAG6; NbExp=3; IntAct=EBI-712105, EBI-10988864;
CC Q13352; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-712105, EBI-725606;
CC Q13352; Q9Y5P4: CERT1; NbExp=4; IntAct=EBI-712105, EBI-739994;
CC Q13352; O14645: DNALI1; NbExp=3; IntAct=EBI-712105, EBI-395638;
CC Q13352; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-712105, EBI-743105;
CC Q13352; P22607: FGFR3; NbExp=3; IntAct=EBI-712105, EBI-348399;
CC Q13352; P01100: FOS; NbExp=3; IntAct=EBI-712105, EBI-852851;
CC Q13352; P50440: GATM; NbExp=3; IntAct=EBI-712105, EBI-2552594;
CC Q13352; P62993: GRB2; NbExp=3; IntAct=EBI-712105, EBI-401755;
CC Q13352; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-712105, EBI-740290;
CC Q13352; P01112: HRAS; NbExp=3; IntAct=EBI-712105, EBI-350145;
CC Q13352; Q00613: HSF1; NbExp=3; IntAct=EBI-712105, EBI-719620;
CC Q13352; O75031: HSF2BP; NbExp=3; IntAct=EBI-712105, EBI-7116203;
CC Q13352; Q6ICG6-3: KIAA0930; NbExp=3; IntAct=EBI-712105, EBI-12401561;
CC Q13352; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-712105, EBI-2125614;
CC Q13352; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-712105, EBI-14069005;
CC Q13352; O14901: KLF11; NbExp=6; IntAct=EBI-712105, EBI-948266;
CC Q13352; Q13449: LSAMP; NbExp=3; IntAct=EBI-712105, EBI-4314821;
CC Q13352; P45984: MAPK9; NbExp=3; IntAct=EBI-712105, EBI-713568;
CC Q13352; O14770-4: MEIS2; NbExp=3; IntAct=EBI-712105, EBI-8025850;
CC Q13352; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-712105, EBI-16439278;
CC Q13352; A6NI15: MSGN1; NbExp=3; IntAct=EBI-712105, EBI-11991020;
CC Q13352; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-712105, EBI-1042642;
CC Q13352; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-712105, EBI-741158;
CC Q13352; Q9BVL2: NUP58; NbExp=6; IntAct=EBI-712105, EBI-2811583;
CC Q13352; Q96AL5: PBX3; NbExp=3; IntAct=EBI-712105, EBI-741171;
CC Q13352; Q8WWB5: PIH1D2; NbExp=7; IntAct=EBI-712105, EBI-10232538;
CC Q13352; Q92569: PIK3R3; NbExp=3; IntAct=EBI-712105, EBI-79893;
CC Q13352; P62491: RAB11A; NbExp=3; IntAct=EBI-712105, EBI-745098;
CC Q13352; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-712105, EBI-12004298;
CC Q13352; P51687: SUOX; NbExp=3; IntAct=EBI-712105, EBI-3921347;
CC Q13352; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-712105, EBI-11059915;
CC Q13352; P14927: UQCRB; NbExp=3; IntAct=EBI-712105, EBI-743128;
CC Q13352; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-712105, EBI-739895;
CC Q13352; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-712105, EBI-14096082;
CC Q13352-5; P53365: ARFIP2; NbExp=3; IntAct=EBI-10175826, EBI-638194;
CC Q13352-5; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-10175826, EBI-2125614;
CC Q13352-5; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-10175826, EBI-10232538;
CC Q13352-5; B2RDC9; NbExp=3; IntAct=EBI-10175826, EBI-10175830;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Chromosome, centromere.
CC Chromosome, centromere, kinetochore.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Isoform 3
CC is predominantly nuclear and weakly cytoplasmic.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q13352-1; Sequence=Displayed;
CC Name=2; Synonyms=Long, EnL, En-L;
CC IsoId=Q13352-2; Sequence=VSP_010834;
CC Name=3; Synonyms=Short, EnS, En-S;
CC IsoId=Q13352-3; Sequence=VSP_010833;
CC Name=4;
CC IsoId=Q13352-4; Sequence=VSP_010832;
CC Name=5;
CC IsoId=Q13352-5; Sequence=VSP_010831;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus,
CC prostate, ovary, small intestine and white blood cells. Highly
CC expressed in testis and colon. Isoform 4 is expressed in platelets,
CC lymphocytes and granulocytes. {ECO:0000269|PubMed:11864709,
CC ECO:0000269|PubMed:7593198}.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:15254226}.
CC -!- DOMAIN: The DD1 domain (also called RepD1 domain) mediates the
CC corepressor function and is essential in the triggering of apoptosis.
CC {ECO:0000269|PubMed:15082778}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known
CC to be important for the association with nuclear receptors. Such motif,
CC which is required for an efficient association with nuclear receptors,
CC is however not essential. {ECO:0000269|PubMed:15082778}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is
CC essential for the association with nuclear receptors.
CC {ECO:0000269|PubMed:15082778}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14385.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U37139; AAC50295.1; -; mRNA.
DR EMBL; U37139; AAC50294.1; -; mRNA.
DR EMBL; AF175306; AAF00239.1; -; mRNA.
DR EMBL; AK312944; BAG35785.1; -; mRNA.
DR EMBL; BX004807; CAI15771.1; -; Genomic_DNA.
DR EMBL; AL592218; CAI15771.1; JOINED; Genomic_DNA.
DR EMBL; BX004807; CAI15772.1; -; Genomic_DNA.
DR EMBL; AL592218; CAI15772.1; JOINED; Genomic_DNA.
DR EMBL; AL592218; CAI18958.1; -; Genomic_DNA.
DR EMBL; BX004807; CAI18958.1; JOINED; Genomic_DNA.
DR EMBL; AL592218; CAI18959.1; -; Genomic_DNA.
DR EMBL; BX004807; CAI18959.1; JOINED; Genomic_DNA.
DR EMBL; BC009929; AAH09929.1; -; mRNA.
DR EMBL; BC014385; AAH14385.1; ALT_INIT; mRNA.
DR CCDS; CCDS30736.1; -. [Q13352-1]
DR CCDS; CCDS55603.1; -. [Q13352-5]
DR PIR; A57277; A57277.
DR RefSeq; NP_001193668.1; NM_001206739.1. [Q13352-5]
DR RefSeq; NP_001334077.1; NM_001347148.1.
DR RefSeq; NP_055103.3; NM_014288.4. [Q13352-1]
DR AlphaFoldDB; Q13352; -.
DR SMR; Q13352; -.
DR BioGRID; 116992; 70.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR CORUM; Q13352; -.
DR ELM; Q13352; -.
DR IntAct; Q13352; 94.
DR MINT; Q13352; -.
DR STRING; 9606.ENSP00000360133; -.
DR GlyGen; Q13352; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13352; -.
DR PhosphoSitePlus; Q13352; -.
DR BioMuta; ITGB3BP; -.
DR DMDM; 50400855; -.
DR EPD; Q13352; -.
DR jPOST; Q13352; -.
DR MassIVE; Q13352; -.
DR MaxQB; Q13352; -.
DR PaxDb; Q13352; -.
DR PeptideAtlas; Q13352; -.
DR PRIDE; Q13352; -.
DR ProteomicsDB; 59336; -. [Q13352-1]
DR ProteomicsDB; 59337; -. [Q13352-2]
DR ProteomicsDB; 59338; -. [Q13352-3]
DR ProteomicsDB; 59339; -. [Q13352-4]
DR ProteomicsDB; 59340; -. [Q13352-5]
DR TopDownProteomics; Q13352-1; -. [Q13352-1]
DR Antibodypedia; 33352; 215 antibodies from 30 providers.
DR DNASU; 23421; -.
DR Ensembl; ENST00000271002.15; ENSP00000271002.10; ENSG00000142856.17. [Q13352-1]
DR Ensembl; ENST00000371092.7; ENSP00000360133.3; ENSG00000142856.17. [Q13352-5]
DR Ensembl; ENST00000489099.5; ENSP00000432904.1; ENSG00000142856.17. [Q13352-2]
DR GeneID; 23421; -.
DR KEGG; hsa:23421; -.
DR MANE-Select; ENST00000271002.15; ENSP00000271002.10; NM_014288.5; NP_055103.3.
DR UCSC; uc001dba.3; human. [Q13352-1]
DR CTD; 23421; -.
DR DisGeNET; 23421; -.
DR GeneCards; ITGB3BP; -.
DR HGNC; HGNC:6157; ITGB3BP.
DR HPA; ENSG00000142856; Low tissue specificity.
DR MIM; 605494; gene.
DR neXtProt; NX_Q13352; -.
DR OpenTargets; ENSG00000142856; -.
DR PharmGKB; PA29956; -.
DR VEuPathDB; HostDB:ENSG00000142856; -.
DR eggNOG; ENOG502S4AR; Eukaryota.
DR GeneTree; ENSGT00390000004336; -.
DR HOGENOM; CLU_122442_0_0_1; -.
DR InParanoid; Q13352; -.
DR OMA; TRQMSPF; -.
DR OrthoDB; 1343610at2759; -.
DR PhylomeDB; Q13352; -.
DR TreeFam; TF336291; -.
DR PathwayCommons; Q13352; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q13352; -.
DR SIGNOR; Q13352; -.
DR BioGRID-ORCS; 23421; 14 hits in 1042 CRISPR screens.
DR ChiTaRS; ITGB3BP; human.
DR GeneWiki; ITGB3BP; -.
DR GenomeRNAi; 23421; -.
DR Pharos; Q13352; Tbio.
DR PRO; PR:Q13352; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13352; protein.
DR Bgee; ENSG00000142856; Expressed in oocyte and 189 other tissues.
DR Genevisible; Q13352; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
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 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Cytoplasm; Isopeptide bond;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..177
FT /note="Centromere protein R"
FT /id="PRO_0000057949"
FT REGION 20..50
FT /note="DD1"
FT REGION 41..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 83..113
FT /evidence="ECO:0000255"
FT MOTIF 9..13
FT /note="LXXLL motif"
FT MOTIF 63..66
FT /note="Nuclear localization signal"
FT MOTIF 172..176
FT /note="LXXIL motif"
FT COMPBIAS 55..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11713274"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..2
FT /note="MP -> MPFAPVAQARVQWHDFRSLQHLLPAFKRFSCLSLGSSWDYS (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010831"
FT VAR_SEQ 63..177
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010832"
FT VAR_SEQ 112..177
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7593198"
FT /id="VSP_010833"
FT VAR_SEQ 162..177
FT /note="ASRHLDSYEFLKAILN -> GQPQMSQPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7593198"
FT /id="VSP_010834"
FT VARIANT 30
FT /note="I -> V (in dbSNP:rs1058057)"
FT /id="VAR_048691"
FT MUTAGEN 9
FT /note="L->A: Decreased interaction with nuclear receptors."
FT /evidence="ECO:0000269|PubMed:10490654"
FT MUTAGEN 28
FT /note="S->A: Loss of repressor function."
FT /evidence="ECO:0000269|PubMed:11713274,
FT ECO:0000269|PubMed:15082778"
FT MUTAGEN 63..66
FT /note="Missing: Abolishes localization to nucleus."
FT /evidence="ECO:0000269|PubMed:12244126"
FT MUTAGEN 63..65
FT /note="KRK->AAA: Abolishes localization to nucleus."
FT /evidence="ECO:0000269|PubMed:11864709"
FT MUTAGEN 89
FT /note="L->R: Abolishes dimerization, but not interactions
FT with nuclear receptors; when associated with R-96."
FT /evidence="ECO:0000269|PubMed:11713274"
FT MUTAGEN 96
FT /note="L->R: Abolishes dimerization, but not interactions
FT with nuclear receptors; when associated with R-89."
FT /evidence="ECO:0000269|PubMed:11713274"
FT MUTAGEN 172..176
FT /note="LKAIL->AKAAA: Abolishes interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:10490654"
SQ SEQUENCE 177 AA; 20194 MW; C0A6FD5A56E98D43 CRC64;
MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS
NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI MEIMQNLSSI QALEGSRELE
NLIGISCASH FLKREMQKTK ELMTKVNKQK LFEKSTGLPH KASRHLDSYE FLKAILN
