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Protein

Nucleolar complex protein 2 homolog

Gene

NOC2L

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

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

  • chromatin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cellular response to UV Source: UniProtKB
  • chromatin assembly Source: UniProtKB
  • negative regulation of B cell apoptotic process Source: UniProtKB
  • negative regulation of histone acetylation Source: UniProtKB
  • negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • nucleolus to nucleoplasm transport Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: 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

  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671261.

Polymorphism and mutation databases

BioMutaiNOC2L.
DMDMi317373580.

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 – 491Phosphoserine5 Publications
Modified residuei56 – 561Phosphoserine1 Publication
Modified residuei93 – 931Phosphoserine1 Publication
Modified residuei672 – 6721Phosphoserine4 Publications
Modified residuei673 – 6731Phosphoserine2 Publications
Modified residuei678 – 6781Phosphothreonine1 Publication
Modified residuei746 – 7461Phosphoserine1 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.
GenevisibleiQ9Y3T9. HS.

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. 37 interactions.
IntActiQ9Y3T9. 13 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.
GeneTreeiENSGT00390000010057.
HOGENOMiHOG000007977.
HOVERGENiHBG029261.
InParanoidiQ9Y3T9.
KOiK14833.
OMAiVLAFRCA.
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

        10         20         30         40         50
MAAAGSRKRR LAELTVDEFL ASGFDSESES ESENSPQAET REAREAARSP
60 70 80 90 100
DKPGGSPSAS RRKGRASEHK DQLSRLKDRD PEFYKFLQEN DQSLLNFSDS
110 120 130 140 150
DSSEEEEGPF HSLPDVLEEA SEEEDGAEEG EDGDRVPRGL KGKKNSVPVT
160 170 180 190 200
VAMVERWKQA AKQRLTPKLF HEVVQAFRAA VATTRGDQES AEANKFQVTD
210 220 230 240 250
SAAFNALVTF CIRDLIGCLQ KLLFGKVAKD SSRMLQPSSS PLWGKLRVDI
260 270 280 290 300
KAYLGSAIQL VSCLSETTVL AAVLRHISVL VPCFLTFPKQ CRMLLKRMVI
310 320 330 340 350
VWSTGEESLR VLAFLVLSRV CRHKKDTFLG PVLKQMYITY VRNCKFTSPG
360 370 380 390 400
ALPFISFMQW TLTELLALEP GVAYQHAFLY IRQLAIHLRN AMTTRKKETY
410 420 430 440 450
QSVYNWQYVH CLFLWCRVLS TAGPSEALQP LVYPLAQVII GCIKLIPTAR
460 470 480 490 500
FYPLRMHCIR ALTLLSGSSG AFIPVLPFIL EMFQQVDFNR KPGRMSSKPI
510 520 530 540 550
NFSVILKLSN VNLQEKAYRD GLVEQLYDLT LEYLHSQAHC IGFPELVLPV
560 570 580 590 600
VLQLKSFLRE CKVANYCRQV QQLLGKVQEN SAYICSRRQR VSFGVSEQQA
610 620 630 640 650
VEAWEKLTRE EGTPLTLYYS HWRKLRDREI QLEISGKERL EDLNFPEIKR
660 670 680 690 700
RKMADRKDED RKQFKDLFDL NSSEEDDTEG FSERGILRPL STRHGVEDDE
710 720 730 740
EDEEEGEEDS SNSEDGDPDA EAGLAPGELQ QLAQGPEDEL EDLQLSEDD
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9Y3T9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117586. 37 interactions.
IntActiQ9Y3T9. 13 interactions.
MINTiMINT-1461800.
STRINGi9606.ENSP00000317992.

PTM databases

PhosphoSiteiQ9Y3T9.

Polymorphism and mutation databases

BioMutaiNOC2L.
DMDMi317373580.

2D gel databases

SWISS-2DPAGEQ9Y3T9.

Proteomic databases

MaxQBiQ9Y3T9.
PaxDbiQ9Y3T9.
PRIDEiQ9Y3T9.

Protocols and materials databases

DNASUi26155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26155.
GeneCardsiGC01M000879.
H-InvDBHIX0029966.
HIX0030002.
HGNCiHGNC:24517. NOC2L.
HPAiHPA044258.
MIMi610770. gene.
neXtProtiNX_Q9Y3T9.
PharmGKBiPA142671261.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5604.
GeneTreeiENSGT00390000010057.
HOGENOMiHOG000007977.
HOVERGENiHBG029261.
InParanoidiQ9Y3T9.
KOiK14833.
OMAiVLAFRCA.
OrthoDBiEOG7JMGD1.
PhylomeDBiQ9Y3T9.
TreeFamiTF314829.

Miscellaneous databases

ChiTaRSiNOC2L. human.
GeneWikiiNOC2L.
GenomeRNAii26155.
NextBioi48247.
PROiQ9Y3T9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3T9.
CleanExiHS_NOC2L.
GenevisibleiQ9Y3T9. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, 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].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-746, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 134 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.