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Q13352

- CENPR_HUMAN

UniProt

Q13352 - CENPR_HUMAN

Protein

Centromere protein R

Gene

ITGB3BP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.5 Publications

    GO - Molecular functioni

    1. protein C-terminus binding Source: ProtInc
    2. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. cell adhesion Source: ProtInc
    3. CENP-A containing nucleosome assembly Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: UniProtKB-KW
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. nucleosome assembly Source: Reactome
    8. positive regulation of apoptotic process Source: Reactome
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. signal transduction Source: ProtInc
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Apoptosis, Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_13643. NRIF signals cell death from the nucleus.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ITGB3BP
    Synonyms:CENPR, NRIF3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6157. ITGB3BP.

    Subcellular locationi

    Isoform 3 : Nucleus. Cytoplasm
    Note: Isoform 3 is predominantly nuclear and weakly cytoplasmic.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. cytosol Source: Reactome
    4. membrane Source: ProtInc
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91L → A: Decreased interaction with nuclear receptors. 1 Publication
    Mutagenesisi28 – 281S → A: Loss of repressor function. 2 Publications
    Mutagenesisi63 – 664Missing: Abolishes localization to nucleus.
    Mutagenesisi63 – 653KRK → AAA: Abolishes localization to nucleus.
    Mutagenesisi89 – 891L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-96. 1 Publication
    Mutagenesisi96 – 961L → R: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-89. 1 Publication
    Mutagenesisi172 – 1765LKAIL → AKAAA: Abolishes interaction with nuclear receptors.

    Organism-specific databases

    PharmGKBiPA29956.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 177177Centromere protein RPRO_0000057949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine3 Publications
    Modified residuei28 – 281Phosphoserine1 Publication
    Modified residuei71 – 711Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13352.
    PaxDbiQ13352.
    PRIDEiQ13352.

    PTM databases

    PhosphoSiteiQ13352.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Inductioni

    By estrogen.1 Publication

    Gene expression databases

    ArrayExpressiQ13352.
    BgeeiQ13352.
    GenevestigatoriQ13352.

    Organism-specific databases

    HPAiHPA028463.

    Interactioni

    Subunit structurei

    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.7 Publications

    Protein-protein interaction databases

    BioGridi116992. 23 interactions.
    IntActiQ13352. 31 interactions.
    MINTiMINT-1378371.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 5031DD1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili83 – 11331Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 135LXXLL motif
    Motifi63 – 664Nuclear localization signal
    Motifi172 – 1765LXXIL motif

    Domaini

    The DD1 domain (also called RepD1 domain) mediates the corepressor function and is essential in the triggering of apoptosis.1 Publication
    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.1 Publication
    Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is essential for the association with nuclear receptors.1 Publication

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG80433.
    HOVERGENiHBG080553.
    KOiK11510.
    OMAiQMSPFAS.
    OrthoDBiEOG7SR4P3.
    PhylomeDBiQ13352.
    TreeFamiTF336291.

    Family and domain databases

    InterProiIPR009601. CENP-R.
    [Graphical view]
    PANTHERiPTHR15581. PTHR15581. 1 hit.
    PfamiPF06729. CENP-R. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011860. NRIF3_coact_rcpt. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13352-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPVKRSLKLD GLLEENSFDP SKITRKKSVI TYSPTTGTCQ MSLFASPTSS    50
    EEQKHRNGLS NEKRKKLNHP SLTESKESTT KDNDEFMMLL SKVEKLSEEI 100
    MEIMQNLSSI QALEGSRELE NLIGISCASH FLKREMQKTK ELMTKVNKQK 150
    LFEKSTGLPH KASRHLDSYE FLKAILN 177
    Length:177
    Mass (Da):20,194
    Last modified:July 19, 2004 - v2
    Checksum:iC0A6FD5A56E98D43
    GO
    Isoform 2 (identifier: Q13352-2) [UniParc]FASTAAdd to Basket

    Also known as: Long, EnL, En-L

    The sequence of this isoform differs from the canonical sequence as follows:
         162-177: ASRHLDSYEFLKAILN → GQPQMSQPL

    Show »
    Length:170
    Mass (Da):19,302
    Checksum:i227EE95365D0AB5C
    GO
    Isoform 3 (identifier: Q13352-3) [UniParc]FASTAAdd to Basket

    Also known as: Short, EnS, En-S

    The sequence of this isoform differs from the canonical sequence as follows:
         112-177: Missing.

    Show »
    Length:111
    Mass (Da):12,624
    Checksum:i790E4D07D5CC09AF
    GO
    Isoform 4 (identifier: Q13352-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         63-177: Missing.

    Show »
    Length:62
    Mass (Da):6,902
    Checksum:iDB8074B62E359160
    GO
    Isoform 5 (identifier: Q13352-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2: MP → MPFAPVAQARVQWHDFRSLQHLLPAFKRFSCLSLGSSWDYS

    Note: No experimental confirmation available.

    Show »
    Length:216
    Mass (Da):24,729
    Checksum:i1D131D450750DCF4
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301I → V.
    Corresponds to variant rs1058057 [ dbSNP | Ensembl ].
    VAR_048691

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 22MP → MPFAPVAQARVQWHDFRSLQ HLLPAFKRFSCLSLGSSWDY S in isoform 5. 1 PublicationVSP_010831
    Alternative sequencei63 – 177115Missing in isoform 4. CuratedVSP_010832Add
    BLAST
    Alternative sequencei112 – 17766Missing in isoform 3. 1 PublicationVSP_010833Add
    BLAST
    Alternative sequencei162 – 17716ASRHL…KAILN → GQPQMSQPL in isoform 2. 1 PublicationVSP_010834Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS30736.1. [Q13352-1]
    CCDS55603.1. [Q13352-5]
    PIRiA57277.
    RefSeqiNP_001193668.1. NM_001206739.1. [Q13352-5]
    NP_055103.3. NM_014288.4. [Q13352-1]
    UniGeneiHs.166539.

    Genome annotation databases

    EnsembliENST00000271002; ENSP00000271002; ENSG00000142856. [Q13352-1]
    ENST00000371092; ENSP00000360133; ENSG00000142856. [Q13352-5]
    ENST00000489099; ENSP00000432904; ENSG00000142856. [Q13352-2]
    GeneIDi23421.
    KEGGihsa:23421.
    UCSCiuc001dba.2. human. [Q13352-1]
    uc001dbb.2. human. [Q13352-5]
    uc009wak.1. human. [Q13352-2]

    Polymorphism databases

    DMDMi50400855.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS30736.1. [Q13352-1 ]
    CCDS55603.1. [Q13352-5 ]
    PIRi A57277.
    RefSeqi NP_001193668.1. NM_001206739.1. [Q13352-5 ]
    NP_055103.3. NM_014288.4. [Q13352-1 ]
    UniGenei Hs.166539.

    3D structure databases

    ProteinModelPortali Q13352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116992. 23 interactions.
    IntActi Q13352. 31 interactions.
    MINTi MINT-1378371.

    PTM databases

    PhosphoSitei Q13352.

    Polymorphism databases

    DMDMi 50400855.

    Proteomic databases

    MaxQBi Q13352.
    PaxDbi Q13352.
    PRIDEi Q13352.

    Protocols and materials databases

    DNASUi 23421.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271002 ; ENSP00000271002 ; ENSG00000142856 . [Q13352-1 ]
    ENST00000371092 ; ENSP00000360133 ; ENSG00000142856 . [Q13352-5 ]
    ENST00000489099 ; ENSP00000432904 ; ENSG00000142856 . [Q13352-2 ]
    GeneIDi 23421.
    KEGGi hsa:23421.
    UCSCi uc001dba.2. human. [Q13352-1 ]
    uc001dbb.2. human. [Q13352-5 ]
    uc009wak.1. human. [Q13352-2 ]

    Organism-specific databases

    CTDi 23421.
    GeneCardsi GC01M063906.
    H-InvDB HIX0019635.
    HGNCi HGNC:6157. ITGB3BP.
    HPAi HPA028463.
    MIMi 605494. gene.
    neXtProti NX_Q13352.
    PharmGKBi PA29956.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80433.
    HOVERGENi HBG080553.
    KOi K11510.
    OMAi QMSPFAS.
    OrthoDBi EOG7SR4P3.
    PhylomeDBi Q13352.
    TreeFami TF336291.

    Enzyme and pathway databases

    Reactomei REACT_13643. NRIF signals cell death from the nucleus.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi ITGB3BP. human.
    GeneWikii ITGB3BP.
    GenomeRNAii 23421.
    NextBioi 45639.
    PROi Q13352.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13352.
    Bgeei Q13352.
    Genevestigatori Q13352.

    Family and domain databases

    InterProi IPR009601. CENP-R.
    [Graphical view ]
    PANTHERi PTHR15581. PTHR15581. 1 hit.
    Pfami PF06729. CENP-R. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011860. NRIF3_coact_rcpt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CENPA-CAD COMPLEX WITH CENPI; CENPK; CENPL; CENPO; CENPP; CENPQ AND CENPS.
    15. 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.

    Entry informationi

    Entry nameiCENPR_HUMAN
    AccessioniPrimary (citable) accession number: Q13352
    Secondary accession number(s): B2R7D8
    , Q13353, Q5RJ42, Q5RJ44, Q5RJ45, Q7KYX2, Q96CD5, Q9UKB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

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