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Q9Y3T9 (NOC2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar complex protein 2 homolog

Short name=Protein NOC2 homolog
Alternative name(s):
NOC2-like protein
Novel INHAT repressor
Gene names
Name:NOC2L
Synonyms:NIR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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*-gammato the p21/CDKN1A promoter. Ref.1 Ref.11 Ref.14

Subunit structure

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. Ref.1 Ref.11 Ref.14

Subcellular location

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. Ref.5 Ref.11 Ref.14

Induction

Up-regulated by IL4 and CD40L in B-cells. Ref.14

Sequence similarities

Belongs to the NOC2 family.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to UV

Inferred from direct assay Ref.14. Source: UniProtKB

chromatin assembly

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of B cell apoptotic process

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of histone acetylation

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.1. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11Ref.14. Source: UniProtKB

nucleolus to nucleoplasm transport

Inferred from direct assay Ref.11. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay Ref.11. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1Ref.14. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from direct assay Ref.1Ref.11. Source: UniProtKB

histone binding

Inferred from direct assay Ref.1. Source: UniProtKB

nucleosome binding

Inferred from direct assay Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1Ref.11Ref.14. Source: UniProtKB

repressing transcription factor binding

Inferred from direct assay Ref.1. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN7O152652EBI-751547,EBI-708350
TP53P046378EBI-751547,EBI-366083

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Nucleolar complex protein 2 homolog
PRO_0000121048

Regions

Compositional bias104 – 1074Poly-Glu
Compositional bias641 – 749109Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue491Phosphoserine Ref.7 Ref.8 Ref.12 Ref.15
Modified residue561Phosphoserine Ref.15
Modified residue6721Phosphoserine Ref.8 Ref.10 Ref.12 Ref.15
Modified residue6731Phosphoserine Ref.8 Ref.10
Modified residue6781Phosphothreonine Ref.8

Natural variations

Natural variant2711A → V.
Corresponds to variant rs3828049 [ dbSNP | Ensembl ].
VAR_028145
Natural variant3001I → V. Ref.2 Ref.4
Corresponds to variant rs3748597 [ dbSNP | Ensembl ].
VAR_028146
Natural variant5561S → L.
Corresponds to variant rs35471880 [ dbSNP | Ensembl ].
VAR_050289

Experimental info

Sequence conflict1781R → Q in CAB43240. Ref.2
Sequence conflict3451K → E in CAB43240. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y3T9 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: B178FE65E711CFDB

FASTA74984,919
        10         20         30         40         50         60 
MAAAGSRKRR LAELTVDEFL ASGFDSESES ESENSPQAET REAREAARSP DKPGGSPSAS 

        70         80         90        100        110        120 
RRKGRASEHK DQLSRLKDRD PEFYKFLQEN DQSLLNFSDS DSSEEEEGPF HSLPDVLEEA 

       130        140        150        160        170        180 
SEEEDGAEEG EDGDRVPRGL KGKKNSVPVT VAMVERWKQA AKQRLTPKLF HEVVQAFRAA 

       190        200        210        220        230        240 
VATTRGDQES AEANKFQVTD SAAFNALVTF CIRDLIGCLQ KLLFGKVAKD SSRMLQPSSS 

       250        260        270        280        290        300 
PLWGKLRVDI KAYLGSAIQL VSCLSETTVL AAVLRHISVL VPCFLTFPKQ CRMLLKRMVI 

       310        320        330        340        350        360 
VWSTGEESLR VLAFLVLSRV CRHKKDTFLG PVLKQMYITY VRNCKFTSPG ALPFISFMQW 

       370        380        390        400        410        420 
TLTELLALEP GVAYQHAFLY IRQLAIHLRN AMTTRKKETY QSVYNWQYVH CLFLWCRVLS 

       430        440        450        460        470        480 
TAGPSEALQP LVYPLAQVII GCIKLIPTAR FYPLRMHCIR ALTLLSGSSG AFIPVLPFIL 

       490        500        510        520        530        540 
EMFQQVDFNR KPGRMSSKPI NFSVILKLSN VNLQEKAYRD GLVEQLYDLT LEYLHSQAHC 

       550        560        570        580        590        600 
IGFPELVLPV VLQLKSFLRE CKVANYCRQV QQLLGKVQEN SAYICSRRQR VSFGVSEQQA 

       610        620        630        640        650        660 
VEAWEKLTRE EGTPLTLYYS HWRKLRDREI QLEISGKERL EDLNFPEIKR RKMADRKDED 

       670        680        690        700        710        720 
RKQFKDLFDL NSSEEDDTEG FSERGILRPL STRHGVEDDE EDEEEGEEDS SNSEDGDPDA 

       730        740 
EAGLAPGELQ QLAQGPEDEL EDLQLSEDD 

« Hide

References

« Hide 'large scale' references
[1]"NIR is a novel INHAT repressor that modulates the transcriptional activity of p53."
Hublitz P., Kunowska N., Mayer U.P., Muller J.M., Heyne K., Yin N., Fritzsche C., Poli C., Miguet L., Schupp I.W., van Grunsven L.A., Potiers N., van Dorsselaer A., Metzger E., Roemer K., Schule R.
Genes Dev. 19:2912-2924(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN INHIBITION OF HISTONE ACETYLATION, INTERACTION WITH TP53, ASSOCIATION WITH CORE HISTONES AND NUCLEOSOMES.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. 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].
[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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"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-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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL050019 mRNA. Translation: CAB43240.2.
AL645608 Genomic DNA. Translation: CAI15568.1.
BC003555 mRNA. Translation: AAH03555.1.
CCDSCCDS3.1.
RefSeqNP_056473.2. NM_015658.3.
UniGeneHs.405987.

3D structure databases

ProteinModelPortalQ9Y3T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117586. 23 interactions.
IntActQ9Y3T9. 11 interactions.
MINTMINT-1461800.
STRING9606.ENSP00000317992.

PTM databases

PhosphoSiteQ9Y3T9.

Polymorphism databases

DMDM317373580.

2D gel databases

SWISS-2DPAGEQ9Y3T9.

Proteomic databases

MaxQBQ9Y3T9.
PaxDbQ9Y3T9.
PRIDEQ9Y3T9.

Protocols and materials databases

DNASU26155.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327044; ENSP00000317992; ENSG00000188976.
GeneID26155.
KEGGhsa:26155.
UCSCuc001abz.4. human.

Organism-specific databases

CTD26155.
GeneCardsGC01M000879.
H-InvDBHIX0029966.
HIX0030002.
HGNCHGNC:24517. NOC2L.
HPAHPA044258.
MIM610770. gene.
neXtProtNX_Q9Y3T9.
PharmGKBPA142671261.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5604.
HOGENOMHOG000007977.
HOVERGENHBG029261.
InParanoidQ9Y3T9.
KOK14833.
OMAFILEIFQ.
OrthoDBEOG7JMGD1.
PhylomeDBQ9Y3T9.
TreeFamTF314829.

Gene expression databases

BgeeQ9Y3T9.
CleanExHS_NOC2L.
GenevestigatorQ9Y3T9.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR005343. Noc2.
[Graphical view]
PANTHERPTHR12687. PTHR12687. 1 hit.
PfamPF03715. Noc2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSNOC2L. human.
GeneWikiNOC2L.
GenomeRNAi26155.
NextBio48247.
PROQ9Y3T9.
SOURCESearch...

Entry information

Entry nameNOC2L_HUMAN
AccessionPrimary (citable) accession number: Q9Y3T9
Secondary accession number(s): Q5SVA3, Q9BTN6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 126 of the entry and version 4 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

SIMILARITY comments

Index of protein domains and families

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