CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023795
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleolar complex protein 2 homolog 
Protein Synonyms/Alias
 Protein NOC2 homolog; NOC2-like protein; Novel INHAT repressor 
Gene Name
 NOC2L 
Gene Synonyms/Alias
 NIR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
144PRGLKGKKNSVPVTVubiquitination[1]
168AKQRLTPKLFHEVVQubiquitination[2]
226LQKLLFGKVAKDSSRubiquitination[1, 3]
245SSSPLWGKLRVDIKAubiquitination[1, 3]
289PCFLTFPKQCRMLLKubiquitination[4]
498KPGRMSSKPINFSVIubiquitination[3]
516SNVNLQEKAYRDGLVubiquitination[1, 2, 3, 4, 5, 6]
576QVQQLLGKVQENSAYubiquitination[3, 4]
606QAVEAWEKLTREEGTubiquitination[1, 2, 3, 4, 5, 6]
637IQLEISGKERLEDLNubiquitination[1, 2, 3, 5, 6]
649DLNFPEIKRRKMADRubiquitination[1, 3, 4, 5, 6, 7]
665DEDRKQFKDLFDLNSubiquitination[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 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. 
Sequence Annotation
 MOD_RES 49 49 Phosphoserine.
 MOD_RES 56 56 Phosphoserine.
 MOD_RES 672 672 Phosphoserine.
 MOD_RES 673 673 Phosphoserine.
 MOD_RES 678 678 Phosphothreonine.  
Keyword
 Apoptosis; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 749 AA 
Protein Sequence
MAAAGSRKRR LAELTVDEFL ASGFDSESES ESENSPQAET REAREAARSP DKPGGSPSAS 60
RRKGRASEHK DQLSRLKDRD PEFYKFLQEN DQSLLNFSDS DSSEEEEGPF HSLPDVLEEA 120
SEEEDGAEEG EDGDRVPRGL KGKKNSVPVT VAMVERWKQA AKQRLTPKLF HEVVQAFRAA 180
VATTRGDQES AEANKFQVTD SAAFNALVTF CIRDLIGCLQ KLLFGKVAKD SSRMLQPSSS 240
PLWGKLRVDI KAYLGSAIQL VSCLSETTVL AAVLRHISVL VPCFLTFPKQ CRMLLKRMVI 300
VWSTGEESLR VLAFLVLSRV CRHKKDTFLG PVLKQMYITY VRNCKFTSPG ALPFISFMQW 360
TLTELLALEP GVAYQHAFLY IRQLAIHLRN AMTTRKKETY QSVYNWQYVH CLFLWCRVLS 420
TAGPSEALQP LVYPLAQVII GCIKLIPTAR FYPLRMHCIR ALTLLSGSSG AFIPVLPFIL 480
EMFQQVDFNR KPGRMSSKPI NFSVILKLSN VNLQEKAYRD GLVEQLYDLT LEYLHSQAHC 540
IGFPELVLPV VLQLKSFLRE CKVANYCRQV QQLLGKVQEN SAYICSRRQR VSFGVSEQQA 600
VEAWEKLTRE EGTPLTLYYS HWRKLRDREI QLEISGKERL EDLNFPEIKR RKMADRKDED 660
RKQFKDLFDL NSSEEDDTEG FSERGILRPL STRHGVEDDE EDEEEGEEDS SNSEDGDPDA 720
EAGLAPGELQ QLAQGPEDEL EDLQLSEDD 749 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0031491; F:nucleosome binding; IDA:UniProtKB.
 GO:0070491; F:repressing transcription factor binding; IDA:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0034644; P:cellular response to UV; IDA:UniProtKB.
 GO:0002903; P:negative regulation of B cell apoptotic process; IMP:UniProtKB.
 GO:0035067; P:negative regulation of histone acetylation; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0032066; P:nucleolus to nucleoplasm transport; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR016024; ARM-type_fold.
 IPR005343; Noc2. 
Pfam
 PF03715; Noc2 
SMART
  
PROSITE
  
PRINTS