Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CQ82 (CENPR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein R

Short name=CENP-R
Alternative name(s):
Nuclear receptor-interacting factor 3
Gene names
Name:Itgb3bp
Synonyms:Cenpr, Nrif3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex By similarity.

Subunit structure

Homodimer; mediated by the coiled coil domain. Interacts with CCNA2 and MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU By similarity.

Subcellular location

Nucleus By similarity. Chromosomecentromere By similarity. Chromosomecentromerekinetochore By similarity.

Domain

The DD1 domain (also called RepD1 domain) mediates the corepressor function and is essential in the triggering of apoptosis By similarity.

Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is essential for the association with nuclear receptors By similarity.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CQ82-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9CQ82-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
     78-84: TVKDRDG → MISLKKI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 176176Centromere protein R
PRO_0000057950

Regions

Region20 – 5031DD1
Coiled coil82 – 11231 Potential
Motif63 – 664Nuclear localization signal By similarity
Motif171 – 1755LXXIL motif

Amino acid modifications

Modified residue171Phosphoserine By similarity
Modified residue711Phosphoserine By similarity

Natural variations

Alternative sequence1 – 7777Missing in isoform 2.
VSP_020453
Alternative sequence78 – 847TVKDRDG → MISLKKI in isoform 2.
VSP_020454

Experimental info

Sequence conflict71L → V in BAE38732. Ref.1
Sequence conflict501P → S in BAE38732. Ref.1
Sequence conflict821R → S in BAE38732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B55F0C100CAE5973

FASTA17620,026
        10         20         30         40         50         60 
MPVKRSLKLD DQFEKNSFSP SKIVRKKSIT AYSPTTGTYQ LSPFSSPATP KEQEHRNGPS 

        70         80         90        100        110        120 
NETRKRSNLS SPVRQESTVK DRDGFMVLLS KIEISSEKTM EIMKNLSSIQ ALEGNRQLED 

       130        140        150        160        170 
LIGVSLVPCS LKSEARKTKE LMTKVIKQKL FEKKKSRITP KDHHLDSFEF LKAILN 

« Hide

Isoform 2 [UniParc].

Checksum: 112AA4C302DED413
Show »

FASTA9911,390

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Embryo, Mammary gland, Oviduct and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005779 mRNA. Translation: BAB24235.1.
AK013373 mRNA. Translation: BAB28815.1.
AK015557 mRNA. Translation: BAB29892.1.
AK045037 mRNA. Translation: BAC32192.1.
AK165072 mRNA. Translation: BAE38024.1.
AK166362 mRNA. Translation: BAE38732.1.
BC049557 mRNA. Translation: AAH49557.1.
CCDSCCDS18387.1. [Q9CQ82-1]
RefSeqNP_080624.1. NM_026348.3. [Q9CQ82-1]
UniGeneMm.257094.

3D structure databases

ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CQ82.

Proteomic databases

MaxQBQ9CQ82.
PRIDEQ9CQ82.

Protocols and materials databases

DNASU67733.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000146258; ENSMUSP00000117153; ENSMUSG00000028549. [Q9CQ82-1]
GeneID67733.
KEGGmmu:67733.
UCSCuc008tux.1. mouse. [Q9CQ82-1]

Organism-specific databases

CTD23421.
MGIMGI:1914983. Itgb3bp.

Phylogenomic databases

eggNOGNOG80433.
GeneTreeENSGT00390000004336.
HOGENOMHOG000049271.
HOVERGENHBG080553.
KOK11510.
OMAQMSPFAS.
OrthoDBEOG7SR4P3.
PhylomeDBQ9CQ82.
TreeFamTF336291.

Gene expression databases

ArrayExpressQ9CQ82.
BgeeQ9CQ82.
CleanExMM_ITGB3BP.
GenevestigatorQ9CQ82.

Family and domain databases

InterProIPR009601. CENP-R.
[Graphical view]
PANTHERPTHR15581. PTHR15581. 1 hit.
PfamPF06729. CENP-R. 1 hit.
[Graphical view]
PIRSFPIRSF011860. NRIF3_coact_rcpt. 1 hit.
ProtoNetSearch...

Other

NextBio325407.
PROQ9CQ82.
SOURCESearch...

Entry information

Entry nameCENPR_MOUSE
AccessionPrimary (citable) accession number: Q9CQ82
Secondary accession number(s): Q3TLR0, Q3TNR4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot