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Q9Y3T9

- NOC2L_HUMAN

UniProt

Q9Y3T9 - NOC2L_HUMAN

Protein

Nucleolar complex protein 2 homolog

Gene

NOC2L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. Acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent apoptosis. Associates together with TP63 isoform TA*-gamma to the p21/CDKN1A promoter.3 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone binding Source: UniProtKB
    3. nucleosome binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. repressing transcription factor binding Source: UniProtKB
    7. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular response to UV Source: UniProtKB
    3. chromatin assembly Source: UniProtKB
    4. negative regulation of B cell apoptotic process Source: UniProtKB
    5. negative regulation of histone acetylation Source: UniProtKB
    6. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. nucleolus to nucleoplasm transport Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolar complex protein 2 homolog
    Short name:
    Protein NOC2 homolog
    Alternative name(s):
    NOC2-like protein
    Novel INHAT repressor
    Gene namesi
    Name:NOC2L
    Synonyms:NIR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24517. NOC2L.

    Subcellular locationi

    Nucleusnucleoplasm. Nucleusnucleolus
    Note: Translocates from the nucleoli to the nucleoplasm in presence of several stressors like ultraviolet irradiation and actinomycin-D. Predominantly detected in the nucleoli in non-mitotic cells. Predominantly detected in nucleoplasma in cells undergoing mitosis.

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671261.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 749749Nucleolar complex protein 2 homologPRO_0000121048Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphoserine4 Publications
    Modified residuei56 – 561Phosphoserine1 Publication
    Modified residuei672 – 6721Phosphoserine4 Publications
    Modified residuei673 – 6731Phosphoserine2 Publications
    Modified residuei678 – 6781Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y3T9.
    PaxDbiQ9Y3T9.
    PRIDEiQ9Y3T9.

    2D gel databases

    SWISS-2DPAGEQ9Y3T9.

    PTM databases

    PhosphoSiteiQ9Y3T9.

    Expressioni

    Inductioni

    Up-regulated by IL4 and CD40L in B-cells.1 Publication

    Gene expression databases

    BgeeiQ9Y3T9.
    CleanExiHS_NOC2L.
    GenevestigatoriQ9Y3T9.

    Organism-specific databases

    HPAiHPA044258.

    Interactioni

    Subunit structurei

    Interacts with p53/TP53. Interacts (via the N- and C-terminus domains) with AURKB (via the middle kinase domain). Interacts with TP63 isoform TA*-gamma (via activation domain). Interacts with histone H3 (via N-terminus and non-acetylated form preferentially). Associates with core histones and nucleosomes.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN7O152652EBI-751547,EBI-708350
    TP53P046378EBI-751547,EBI-366083

    Protein-protein interaction databases

    BioGridi117586. 23 interactions.
    IntActiQ9Y3T9. 11 interactions.
    MINTiMINT-1461800.
    STRINGi9606.ENSP00000317992.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y3T9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi104 – 1074Poly-Glu
    Compositional biasi641 – 749109Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the NOC2 family.Curated

    Phylogenomic databases

    eggNOGiCOG5604.
    HOGENOMiHOG000007977.
    HOVERGENiHBG029261.
    InParanoidiQ9Y3T9.
    KOiK14833.
    OMAiFILEIFQ.
    OrthoDBiEOG7JMGD1.
    PhylomeDBiQ9Y3T9.
    TreeFamiTF314829.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR005343. Noc2.
    [Graphical view]
    PANTHERiPTHR12687. PTHR12687. 1 hit.
    PfamiPF03715. Noc2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9Y3T9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAGSRKRR LAELTVDEFL ASGFDSESES ESENSPQAET REAREAARSP    50
    DKPGGSPSAS RRKGRASEHK DQLSRLKDRD PEFYKFLQEN DQSLLNFSDS 100
    DSSEEEEGPF HSLPDVLEEA SEEEDGAEEG EDGDRVPRGL KGKKNSVPVT 150
    VAMVERWKQA AKQRLTPKLF HEVVQAFRAA VATTRGDQES AEANKFQVTD 200
    SAAFNALVTF CIRDLIGCLQ KLLFGKVAKD SSRMLQPSSS PLWGKLRVDI 250
    KAYLGSAIQL VSCLSETTVL AAVLRHISVL VPCFLTFPKQ CRMLLKRMVI 300
    VWSTGEESLR VLAFLVLSRV CRHKKDTFLG PVLKQMYITY VRNCKFTSPG 350
    ALPFISFMQW TLTELLALEP GVAYQHAFLY IRQLAIHLRN AMTTRKKETY 400
    QSVYNWQYVH CLFLWCRVLS TAGPSEALQP LVYPLAQVII GCIKLIPTAR 450
    FYPLRMHCIR ALTLLSGSSG AFIPVLPFIL EMFQQVDFNR KPGRMSSKPI 500
    NFSVILKLSN VNLQEKAYRD GLVEQLYDLT LEYLHSQAHC IGFPELVLPV 550
    VLQLKSFLRE CKVANYCRQV QQLLGKVQEN SAYICSRRQR VSFGVSEQQA 600
    VEAWEKLTRE EGTPLTLYYS HWRKLRDREI QLEISGKERL EDLNFPEIKR 650
    RKMADRKDED RKQFKDLFDL NSSEEDDTEG FSERGILRPL STRHGVEDDE 700
    EDEEEGEEDS SNSEDGDPDA EAGLAPGELQ QLAQGPEDEL EDLQLSEDD 749
    Length:749
    Mass (Da):84,919
    Last modified:January 11, 2011 - v4
    Checksum:iB178FE65E711CFDB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781R → Q in CAB43240. (PubMed:11230166)Curated
    Sequence conflicti345 – 3451K → E in CAB43240. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti271 – 2711A → V.
    Corresponds to variant rs3828049 [ dbSNP | Ensembl ].
    VAR_028145
    Natural varianti300 – 3001I → V.2 Publications
    Corresponds to variant rs3748597 [ dbSNP | Ensembl ].
    VAR_028146
    Natural varianti556 – 5561S → L.
    Corresponds to variant rs35471880 [ dbSNP | Ensembl ].
    VAR_050289

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL050019 mRNA. Translation: CAB43240.2.
    AL645608 Genomic DNA. Translation: CAI15568.1.
    BC003555 mRNA. Translation: AAH03555.1.
    CCDSiCCDS3.1.
    RefSeqiNP_056473.2. NM_015658.3.
    UniGeneiHs.405987.

    Genome annotation databases

    EnsembliENST00000327044; ENSP00000317992; ENSG00000188976.
    GeneIDi26155.
    KEGGihsa:26155.
    UCSCiuc001abz.4. human.

    Polymorphism databases

    DMDMi317373580.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL050019 mRNA. Translation: CAB43240.2 .
    AL645608 Genomic DNA. Translation: CAI15568.1 .
    BC003555 mRNA. Translation: AAH03555.1 .
    CCDSi CCDS3.1.
    RefSeqi NP_056473.2. NM_015658.3.
    UniGenei Hs.405987.

    3D structure databases

    ProteinModelPortali Q9Y3T9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117586. 23 interactions.
    IntActi Q9Y3T9. 11 interactions.
    MINTi MINT-1461800.
    STRINGi 9606.ENSP00000317992.

    PTM databases

    PhosphoSitei Q9Y3T9.

    Polymorphism databases

    DMDMi 317373580.

    2D gel databases

    SWISS-2DPAGE Q9Y3T9.

    Proteomic databases

    MaxQBi Q9Y3T9.
    PaxDbi Q9Y3T9.
    PRIDEi Q9Y3T9.

    Protocols and materials databases

    DNASUi 26155.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327044 ; ENSP00000317992 ; ENSG00000188976 .
    GeneIDi 26155.
    KEGGi hsa:26155.
    UCSCi uc001abz.4. human.

    Organism-specific databases

    CTDi 26155.
    GeneCardsi GC01M000879.
    H-InvDB HIX0029966.
    HIX0030002.
    HGNCi HGNC:24517. NOC2L.
    HPAi HPA044258.
    MIMi 610770. gene.
    neXtProti NX_Q9Y3T9.
    PharmGKBi PA142671261.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5604.
    HOGENOMi HOG000007977.
    HOVERGENi HBG029261.
    InParanoidi Q9Y3T9.
    KOi K14833.
    OMAi FILEIFQ.
    OrthoDBi EOG7JMGD1.
    PhylomeDBi Q9Y3T9.
    TreeFami TF314829.

    Miscellaneous databases

    ChiTaRSi NOC2L. human.
    GeneWikii NOC2L.
    GenomeRNAii 26155.
    NextBioi 48247.
    PROi Q9Y3T9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y3T9.
    CleanExi HS_NOC2L.
    Genevestigatori Q9Y3T9.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR005343. Noc2.
    [Graphical view ]
    PANTHERi PTHR12687. PTHR12687. 1 hit.
    Pfami PF03715. Noc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN INHIBITION OF HISTONE ACETYLATION, INTERACTION WITH TP53, ASSOCIATION WITH CORE HISTONES AND NUCLEOSOMES.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-300.
      Tissue: Brain.
    3. "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].
    4. "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], VARIANT VAL-300.
      Tissue: Placenta.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-672; SER-673 AND THR-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "NIR, an inhibitor of histone acetyltransferases, regulates transcription factor TAp63 and is controlled by the cell cycle."
      Heyne K., Willnecker V., Schneider J., Conrad M., Raulf N., Schule R., Roemer K.
      Nucleic Acids Res. 38:3159-3171(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53 AND TP63, SUBCELLULAR LOCATION.
    12. "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-49 AND SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its DNA-binding domain and subsequent functional suppression."
      Wu L., Ma C.A., Zhao Y., Jain A.
      J. Biol. Chem. 286:2236-2244(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AURKB AND TP53, INDUCTION, SUBCELLULAR LOCATION.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-56 AND SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNOC2L_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3T9
    Secondary accession number(s): Q5SVA3, Q9BTN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 127 of the entry and version 4 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
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3