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Q13352 (CENPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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):
Beta-3-endonexin
Integrin beta-3-binding protein
Nuclear receptor-interacting factor 3
Gene names
Name:ITGB3BP
Synonyms:CENPR, NRIF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1, but not other isoforms, is 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. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subunit structure

Homodimer; mediated by the coiled coil domain. Isoform 3, but not other isoforms, interacts with the cytoplasmic tail of integrin ITGB3. The relevance of the interaction with ITGB3 is however uncertain, since isoform 3 is mainly nuclear. 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. Ref.1 Ref.2 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Isoform 1: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Chromosomecentromere. Chromosomecentromerekinetochore Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13.

Isoform 2: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13.

Isoform 3: Nucleus Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Cytoplasm Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13. Note: Isoform 3 is predominantly nuclear and weakly cytoplasmic. Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13

Isoform 4: Cytoplasm Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13.

Tissue specificity

Widely expressed. Expressed in spleen, thymus, prostate, ovary, small intestine and white blood cells. Highly expressed in testis and colon. Isoform 4 is expressed in platelets, lymphocytes and granulocytes. Ref.1 Ref.6

Induction

By estrogen. Ref.12

Domain

The DD1 domain (also called RepD1 domain) mediates the corepressor function and is essential in the triggering of apoptosis. Ref.11

Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known to be important for the association with nuclear receptors. Such motif, which is required for an efficient association with nuclear receptors, is however not essential. Ref.11

Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is essential for the association with nuclear receptors. Ref.11

Sequence caution

The sequence AAH14385.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionActivator
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCENP-A containing nucleosome assembly at centromere

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleosome assembly

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement Ref.2Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

membrane

Traceable author statement Ref.1. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein C-terminus binding

Traceable author statement Ref.2. Source: ProtInc

signal transducer activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13352-1)

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: Q13352-2)

Also known as: Long; EnL; En-L;

The sequence of this isoform differs from the canonical sequence as follows:
     162-177: ASRHLDSYEFLKAILN → GQPQMSQPL
Isoform 3 (identifier: Q13352-3)

Also known as: Short; EnS; En-S;

The sequence of this isoform differs from the canonical sequence as follows:
     112-177: Missing.
Isoform 4 (identifier: Q13352-4)

The sequence of this isoform differs from the canonical sequence as follows:
     63-177: Missing.
Isoform 5 (identifier: Q13352-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MP → MPFAPVAQARVQWHDFRSLQHLLPAFKRFSCLSLGSSWDYS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 177177Centromere protein R
PRO_0000057949

Regions

Region20 – 5031DD1
Coiled coil83 – 11331 Potential
Motif9 – 135LXXLL motif
Motif63 – 664Nuclear localization signal
Motif172 – 1765LXXIL motif

Amino acid modifications

Modified residue171Phosphoserine Ref.15 Ref.16
Modified residue281Phosphoserine Probable
Modified residue711Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 22MP → MPFAPVAQARVQWHDFRSLQ HLLPAFKRFSCLSLGSSWDY S in isoform 5.
VSP_010831
Alternative sequence63 – 177115Missing in isoform 4.
VSP_010832
Alternative sequence112 – 17766Missing in isoform 3.
VSP_010833
Alternative sequence162 – 17716ASRHL…KAILN → GQPQMSQPL in isoform 2.
VSP_010834
Natural variant301I → V.
Corresponds to variant rs1058057 [ dbSNP | Ensembl ].
VAR_048691

Experimental info

Mutagenesis91L → A: Decreased interaction with nuclear receptors. Ref.2
Mutagenesis281S → A: Loss of repressor function. Ref.9 Ref.11
Mutagenesis63 – 664Missing: Abolishes localization to nucleus. Ref.10
Mutagenesis63 – 653KRK → AAA: Abolishes localization to nucleus. Ref.6
Mutagenesis891L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-96. Ref.9
Mutagenesis961L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-89. Ref.9
Mutagenesis172 – 1765LKAIL → AKAAA: Abolishes interaction with nuclear receptors. Ref.2

Sequences

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

Last modified July 19, 2004. Version 2.
Checksum: C0A6FD5A56E98D43

FASTA17720,194
        10         20         30         40         50         60 
MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS EEQKHRNGLS 

        70         80         90        100        110        120 
NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI MEIMQNLSSI QALEGSRELE 

       130        140        150        160        170 
NLIGISCASH FLKREMQKTK ELMTKVNKQK LFEKSTGLPH KASRHLDSYE FLKAILN 

« Hide

Isoform 2 (Long) (EnL) (En-L) [UniParc].

Checksum: 227EE95365D0AB5C
Show »

FASTA17019,302
Isoform 3 (Short) (EnS) (En-S) [UniParc].

Checksum: 790E4D07D5CC09AF
Show »

FASTA11112,624
Isoform 4 [UniParc].

Checksum: DB8074B62E359160
Show »

FASTA626,902
Isoform 5 [UniParc].

Checksum: 1D131D450750DCF4
Show »

FASTA21624,729

References

« Hide 'large scale' references
[1]"Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit."
Shattil S.J., O'Toole T.E., Eigenthaler M.J., Thon V., Williams M.J., Babior B.M., Ginsberg M.H.
J. Cell Biol. 131:807-816(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, INTERACTION WITH ITGB3.
Tissue: B-cell.
[2]"NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors."
Li D., Desai-Yajnik V., Lo E., Schapira M., Abagyan R., Samuels H.H.
Mol. Cell. Biol. 19:7191-7202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COACTIVATOR FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RXRA AND THRA, MUTAGENESIS OF LEU-9 AND 172-LEU--LEU-176.
Tissue: Cervix carcinoma.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 5).
Tissue: Bone marrow and Placenta.
[6]"Novel alternatively spliced form of beta(3)-endonexin."
Fujimoto T.-T., Katsutani S., Shimomura T., Fujimura K.
Thromb. Res. 105:63-70(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 63-LYS--LYS-65.
[7]"Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tail."
Kashiwagi H., Schwartz M.A., Eigenthaler M., Davis K.A., Ginsberg M.H., Shattil S.J.
J. Cell Biol. 137:1433-1443(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Beta3-endonexin as a novel inhibitor of cyclin A-associated kinase."
Ohtoshi A., Maeda T., Higashi H., Ashizawa S., Yamada M., Hatakeyama M.
Biochem. Biophys. Res. Commun. 267:947-952(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCNA2.
[9]"Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation."
Li D., Wang F., Samuels H.H.
Mol. Cell. Biol. 21:8371-8384(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, HOMODIMERIZATION, PHOSPHORYLATION, MUTAGENESIS OF SER-28; LEU-89 AND LEU-96.
[10]"Role of beta(3)-endonexin in the regulation of NF-kappaB-dependent expression of urokinase-type plasminogen activator receptor."
Besta F., Massberg S., Brand K., Mueller E., Page S., Gruener S., Lorenz M., Sadoul K., Kolanus W., Lengyel E., Gawaz M.
J. Cell Sci. 115:3879-3888(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A COREPRESSOR, SUBCELLULAR LOCATION, INTERACTION WITH NFKB1, MUTAGENESIS OF 63-LYS--LYS-66.
[11]"The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells."
Li D., Das S., Yamada T., Samuels H.H.
Mol. Cell. Biol. 24:3838-3848(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF SER-28.
[12]"Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator."
Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R.
Mol. Cell. Biol. 24:6581-6591(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, INTERACTION WITH MTA1.
[13]"The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres."
Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, Desai A., Fukagawa T.
Nat. Cell Biol. 8:446-457(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPK; CENPN; CENPO; CENPP; CENPQ AND CENPU, FUNCTION, SUBCELLULAR LOCATION.
[14]"The human CENP-A centromeric nucleosome-associated complex."
Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, Cleveland D.W.
Nat. Cell Biol. 8:458-469(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CENPA-CAD COMPLEX WITH CENPI; CENPK; CENPL; CENPO; CENPP; CENPQ AND CENPS.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37139 mRNA. Translation: AAC50295.1.
U37139 mRNA. Translation: AAC50294.1.
AF175306 mRNA. Translation: AAF00239.1.
AK312944 mRNA. Translation: BAG35785.1.
BX004807, AL592218 Genomic DNA. Translation: CAI15771.1.
BX004807, AL592218 Genomic DNA. Translation: CAI15772.1.
AL592218, BX004807 Genomic DNA. Translation: CAI18958.1.
AL592218, BX004807 Genomic DNA. Translation: CAI18959.1.
BC009929 mRNA. Translation: AAH09929.1.
BC014385 mRNA. Translation: AAH14385.1. Different initiation.
PIRA57277.
RefSeqNP_001193668.1. NM_001206739.1.
NP_055103.3. NM_014288.4.
UniGeneHs.166539.

3D structure databases

ProteinModelPortalQ13352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116992. 23 interactions.
IntActQ13352. 31 interactions.
MINTMINT-1378371.

PTM databases

PhosphoSiteQ13352.

Polymorphism databases

DMDM50400855.

Proteomic databases

PaxDbQ13352.
PRIDEQ13352.

Protocols and materials databases

DNASU23421.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271002; ENSP00000271002; ENSG00000142856. [Q13352-1]
ENST00000283568; ENSP00000283568; ENSG00000142856. [Q13352-2]
ENST00000371092; ENSP00000360133; ENSG00000142856. [Q13352-5]
ENST00000489099; ENSP00000432904; ENSG00000142856. [Q13352-2]
GeneID23421.
KEGGhsa:23421.
UCSCuc001dba.2. human. [Q13352-1]
uc001dbb.2. human. [Q13352-5]
uc009wak.1. human. [Q13352-2]

Organism-specific databases

CTD23421.
GeneCardsGC01M063906.
H-InvDBHIX0019635.
HGNCHGNC:6157. ITGB3BP.
HPAHPA028463.
MIM605494. gene.
neXtProtNX_Q13352.
PharmGKBPA29956.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80433.
HOVERGENHBG080553.
KOK11510.
OMAQMSPFAS.
OrthoDBEOG7SR4P3.
PhylomeDBQ13352.
TreeFamTF336291.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ13352.
BgeeQ13352.
GenevestigatorQ13352.

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

ChiTaRSITGB3BP. human.
GeneWikiITGB3BP.
GenomeRNAi23421.
NextBio45639.
PROQ13352.
SOURCESearch...

Entry information

Entry nameCENPR_HUMAN
AccessionPrimary (citable) accession number: Q13352
Secondary accession number(s): B2R7D8 expand/collapse secondary AC list , Q13353, Q5RJ42, Q5RJ44, Q5RJ45, Q7KYX2, Q96CD5, Q9UKB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM