Q9Y3T9 (NOC2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	749 AA.
Sequence status	Complete.
Protein existence	Evidence 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*-gamma to the p21/CDKN1A promoter. Ref.1 Ref.15 Ref.17
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.15 Ref.17
Subcellular location	Nucleus › nucleoplasm. Nucleus › nucleolus. 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.15 Ref.17
Induction	Up-regulated by IL4 and CD40L in B cells. Ref.17
Sequence similarities	Belongs to the NOC2 family.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to UV Inferred from direct assay Ref.17. Source: UniProtKB negative regulation of B cell apoptosis Inferred from mutant phenotype Ref.17. Source: UniProtKB negative regulation of histone acetylation Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.15Ref.17. Source: UniProtKB nucleolus to nucleoplasm transport Inferred from direct assay Ref.15. Source: UniProtKB
Cellular component	chromatin assembly complex Inferred from direct assay Ref.1. Source: UniProtKB nucleolus Inferred from direct assay Ref.15. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.15. Source: UniProtKB
Molecular function	histone binding Inferred from direct assay Ref.1. Source: UniProtKB nucleosome binding Inferred from direct assay Ref.1. 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 749	749	Nucleolar complex protein 2 homolog		PRO_0000121048
Regions
	Compositional bias	104 – 107	4	Poly-Glu
	Compositional bias	641 – 749	109	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	26	1	Phosphoserine Ref.7
	Modified residue	28	1	Phosphoserine Ref.7
	Modified residue	30	1	Phosphoserine Ref.7
	Modified residue	32	1	Phosphoserine Ref.7
	Modified residue	35	1	Phosphoserine Ref.7 Ref.8 Ref.10
	Modified residue	49	1	Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12
	Modified residue	56	1	Phosphoserine Ref.6 Ref.10 Ref.12
	Modified residue	67	1	Phosphoserine Ref.9
	Modified residue	93	1	Phosphoserine Ref.7
	Modified residue	98	1	Phosphoserine Ref.7
	Modified residue	100	1	Phosphoserine Ref.7
	Modified residue	102	1	Phosphoserine Ref.7
	Modified residue	103	1	Phosphoserine Ref.7
	Modified residue	121	1	Phosphoserine Ref.10
	Modified residue	672	1	Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	673	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	678	1	Phosphothreonine Ref.12
	Modified residue	746	1	Phosphoserine Ref.7
Natural variations
	Natural variant	271	1	A → V. Corresponds to variant rs3828049 [ dbSNP | Ensembl ].		VAR_028145
	Natural variant	300	1	I → V. Ref.2 Ref.4 Corresponds to variant rs3748597 [ dbSNP | Ensembl ].		VAR_028146
	Natural variant	556	1	S → L. Corresponds to variant rs35471880 [ dbSNP | Ensembl ].		VAR_050289
Experimental info
	Sequence conflict	178	1	R → Q in CAB43240. Ref.2
	Sequence conflict	345	1	K → E in CAB43240. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y3T9 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: B178FE65E711CFDB	FASTA	749	84,919
	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

References

	« Hide 'large scale' referencesShow '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: 16322561] [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. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [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. , 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: 16710414] [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: 15489334] [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: 12429849] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-28; SER-30; SER-32; SER-35; SER-93; SER-98; SER-100; SER-102; SER-103 AND SER-746, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49 AND SER-672, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-56 AND SER-121, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-672 AND SER-673, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-56; SER-672; SER-673 AND THR-678, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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: 20123734] [Abstract] Cited for: FUNCTION, INTERACTION WITH TP53 AND TP63, SUBCELLULAR LOCATION.
[16]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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: 20959462] [Abstract] Cited for: FUNCTION, INTERACTION WITH AURKB AND TP53, INDUCTION, SUBCELLULAR LOCATION.
+	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.
IPI	IPI00411886.
RefSeq	NP_056473.2. NM_015658.3.
UniGene	Hs.405987.
3D structure databases
ProteinModelPortal	Q9Y3T9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y3T9. 4 interactions.
MINT	MINT-1461800.
STRING	Q9Y3T9.
PTM databases
PhosphoSite	Q9Y3T9.
Polymorphism databases
DMDM	23503106.
2D gel databases
SWISS-2DPAGE	Q9Y3T9.
Proteomic databases
PRIDE	Q9Y3T9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000327044; ENSP00000317992; ENSG00000188976.
GeneID	26155.
KEGG	hsa:26155.
UCSC	uc001abz.2. human.
Organism-specific databases
CTD	26155.
GeneCards	GC01M000879.
H-InvDB	HIX0000009. HIX0029966. HIX0030002.
HGNC	HGNC:24517. NOC2L.
HPA	HPA044258.
MIM	610770. gene.
neXtProt	NX_Q9Y3T9.
PharmGKB	PA142671261.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18718.
GeneTree	ENSGT00390000010057.
HOGENOM	HBG445502.
HOVERGEN	HBG029261.
InParanoid	Q9Y3T9.
OMA	YFPLRFH.
OrthoDB	EOG4G1MG5.
PhylomeDB	Q9Y3T9.
Gene expression databases
ArrayExpress	Q9Y3T9.
Bgee	Q9Y3T9.
CleanEx	HS_NOC2L.
Genevestigator	Q9Y3T9.
GermOnline	ENSG00000188976. Homo sapiens.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR005343. UPF0120. [Graphical view]
KO	K14833.
PANTHER	PTHR12687. UPF0120. 1 hit.
Pfam	PF03715. Noc2. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	48247.
SOURCE	Search...

Entry information

Entry name

NOC2L_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.