dbPTM

NOC2L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NOC2L_HUMAN
UniProt AC	Q9Y3T9
Protein Name	Nucleolar complex protein 2 homolog
Gene Name	NOC2L
Organism	Homo sapiens (Human).
Sequence Length	749
Subcellular Localization	Nucleus, nucleoplasm. Nucleus, nucleolus. 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 de
Protein 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..
Protein Sequence	MAAAGSRKRRLAELTVDEFLASGFDSESESESENSPQAETREAREAARSPDKPGGSPSASRRKGRASEHKDQLSRLKDRDPEFYKFLQENDQSLLNFSDSDSSEEEEGPFHSLPDVLEEASEEEDGAEEGEDGDRVPRGLKGKKNSVPVTVAMVERWKQAAKQRLTPKLFHEVVQAFRAAVATTRGDQESAEANKFQVTDSAAFNALVTFCIRDLIGCLQKLLFGKVAKDSSRMLQPSSSPLWGKLRVDIKAYLGSAIQLVSCLSETTVLAAVLRHISVLVPCFLTFPKQCRMLLKRMVIVWSTGEESLRVLAFLVLSRVCRHKKDTFLGPVLKQMYITYVRNCKFTSPGALPFISFMQWTLTELLALEPGVAYQHAFLYIRQLAIHLRNAMTTRKKETYQSVYNWQYVHCLFLWCRVLSTAGPSEALQPLVYPLAQVIIGCIKLIPTARFYPLRMHCIRALTLLSGSSGAFIPVLPFILEMFQQVDFNRKPGRMSSKPINFSVILKLSNVNLQEKAYRDGLVEQLYDLTLEYLHSQAHCIGFPELVLPVVLQLKSFLRECKVANYCRQVQQLLGKVQENSAYICSRRQRVSFGVSEQQAVEAWEKLTREEGTPLTLYYSHWRKLRDREIQLEISGKERLEDLNFPEIKRRKMADRKDEDRKQFKDLFDLNSSEEDDTEGFSERGILRPLSTRHGVEDDEEDEEEGEEDSSNSEDGDPDAEAGLAPGELQQLAQGPEDELEDLQLSEDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	KRRLAELTVDEFLAS HHHHHHCCHHHHHHC	19.88	25137130
22	Phosphorylation	TVDEFLASGFDSESE CHHHHHHCCCCCCCC	41.98	21082442
26	Phosphorylation	FLASGFDSESESESE HHHCCCCCCCCCCCC	40.54	21955146
28	Phosphorylation	ASGFDSESESESENS HCCCCCCCCCCCCCC	50.83	21955146
30	Phosphorylation	GFDSESESESENSPQ CCCCCCCCCCCCCCH	56.56	21955146
32	Phosphorylation	DSESESESENSPQAE CCCCCCCCCCCCHHH	51.89	28102081
35	Phosphorylation	SESESENSPQAETRE CCCCCCCCCHHHHHH	17.84	16565220
40	Phosphorylation	ENSPQAETREAREAA CCCCHHHHHHHHHHH	36.50	20068231
49	Phosphorylation	EAREAARSPDKPGGS HHHHHHHCCCCCCCC	32.49	29255136
49	O-linked_Glycosylation	EAREAARSPDKPGGS HHHHHHHCCCCCCCC	32.49	28510447
52	2-Hydroxyisobutyrylation	EAARSPDKPGGSPSA HHHHCCCCCCCCCCH	49.28	-
56	Phosphorylation	SPDKPGGSPSASRRK CCCCCCCCCCHHHHC	22.92	29255136
58	Phosphorylation	DKPGGSPSASRRKGR CCCCCCCCHHHHCCC	40.34	29255136
60	Phosphorylation	PGGSPSASRRKGRAS CCCCCCHHHHCCCHH	36.63	29255136
67	Phosphorylation	SRRKGRASEHKDQLS HHHCCCHHHCHHHHH	38.58	29496963
70	2-Hydroxyisobutyrylation	KGRASEHKDQLSRLK CCCHHHCHHHHHHHH	43.02	-
70	Ubiquitination	KGRASEHKDQLSRLK CCCHHHCHHHHHHHH	43.02	29967540
77	Ubiquitination	KDQLSRLKDRDPEFY HHHHHHHHHCCHHHH	50.00	27667366
93	Phosphorylation	FLQENDQSLLNFSDS HHHHCCHHHHCCCCC	37.37	20068231
98	Phosphorylation	DQSLLNFSDSDSSEE CHHHHCCCCCCCCCC	34.82	20068231
100	Phosphorylation	SLLNFSDSDSSEEEE HHHCCCCCCCCCCCC	37.89	20068231
102	Phosphorylation	LNFSDSDSSEEEEGP HCCCCCCCCCCCCCC	43.53	20068231
103	Phosphorylation	NFSDSDSSEEEEGPF CCCCCCCCCCCCCCC	54.76	20068231
112	Phosphorylation	EEEGPFHSLPDVLEE CCCCCCCCHHHHHHH	41.81	20068231
121	Phosphorylation	PDVLEEASEEEDGAE HHHHHHHHCCCCCCC	49.15	20068231
144	Ubiquitination	PRGLKGKKNSVPVTV CCCCCCCCCCCCCHH	64.22	27667366
146	Phosphorylation	GLKGKKNSVPVTVAM CCCCCCCCCCCHHHH	36.36	20860994
150	Phosphorylation	KKNSVPVTVAMVERW CCCCCCCHHHHHHHH	9.11	20860994
158	Ubiquitination	VAMVERWKQAAKQRL HHHHHHHHHHHHHCC	35.96	27667366
162	Ubiquitination	ERWKQAAKQRLTPKL HHHHHHHHHCCCHHH	38.68	23000965
168	Ubiquitination	AKQRLTPKLFHEVVQ HHHCCCHHHHHHHHH	59.56	23000965
168	Acetylation	AKQRLTPKLFHEVVQ HHHCCCHHHHHHHHH	59.56	25953088
221	Ubiquitination	DLIGCLQKLLFGKVA HHHHHHHHHHHCHHH	33.92	22817900
226	Ubiquitination	LQKLLFGKVAKDSSR HHHHHHCHHHCCCCC	31.52	21906983
226	2-Hydroxyisobutyrylation	LQKLLFGKVAKDSSR HHHHHHCHHHCCCCC	31.52	-
226	Acetylation	LQKLLFGKVAKDSSR HHHHHHCHHHCCCCC	31.52	25953088
229	Ubiquitination	LLFGKVAKDSSRMLQ HHHCHHHCCCCCCCC	62.22	22817900
238	Phosphorylation	SSRMLQPSSSPLWGK CCCCCCCCCCCCCCC	30.41	25159151
239	Phosphorylation	SRMLQPSSSPLWGKL CCCCCCCCCCCCCCH	42.53	20068231
240	Phosphorylation	RMLQPSSSPLWGKLR CCCCCCCCCCCCCHH	28.49	25159151
245	Acetylation	SSSPLWGKLRVDIKA CCCCCCCCHHHHHHH	22.87	26051181
245	Ubiquitination	SSSPLWGKLRVDIKA CCCCCCCCHHHHHHH	22.87	21906983
289	Acetylation	PCFLTFPKQCRMLLK HHHHCCHHHHHHHHH	58.81	26051181
289	Ubiquitination	PCFLTFPKQCRMLLK HHHHCCHHHHHHHHH	58.81	21963094
318	Phosphorylation	VLAFLVLSRVCRHKK HHHHHHHHHHHHCCC	18.39	24719451
325	2-Hydroxyisobutyrylation	SRVCRHKKDTFLGPV HHHHHCCCCCCHHHH	56.74	-
393	Phosphorylation	IHLRNAMTTRKKETY HHHHHHCHHCCHHHH	22.49	-
495	Sulfoxidation	FNRKPGRMSSKPINF CCCCCCCCCCCCCCC	7.04	28183972
496	Phosphorylation	NRKPGRMSSKPINFS CCCCCCCCCCCCCCH	33.57	28555341
497	Phosphorylation	RKPGRMSSKPINFSV CCCCCCCCCCCCCHH	32.86	28555341
498	Acetylation	KPGRMSSKPINFSVI CCCCCCCCCCCCHHE	42.48	26051181
498	Ubiquitination	KPGRMSSKPINFSVI CCCCCCCCCCCCHHE	42.48	21906983
516	2-Hydroxyisobutyrylation	SNVNLQEKAYRDGLV CCCCCCHHHHHCCHH	37.44	-
516	Ubiquitination	SNVNLQEKAYRDGLV CCCCCCHHHHHCCHH	37.44	21906983
516	Acetylation	SNVNLQEKAYRDGLV CCCCCCHHHHHCCHH	37.44	26051181
533	Phosphorylation	LYDLTLEYLHSQAHC HHHHHHHHHHHCCHH	16.90	-
556	Phosphorylation	PVVLQLKSFLRECKV HHHHHHHHHHHHHHH	37.80	24719451
562	Ubiquitination	KSFLRECKVANYCRQ HHHHHHHHHHHHHHH	39.36	33845483
576	Acetylation	QVQQLLGKVQENSAY HHHHHHHHHHCCCCE	40.49	26051181
576	Ubiquitination	QVQQLLGKVQENSAY HHHHHHHHHHCCCCE	40.49	21906983
581	Phosphorylation	LGKVQENSAYICSRR HHHHHCCCCEECCCC	23.00	28152594
583	Phosphorylation	KVQENSAYICSRRQR HHHCCCCEECCCCHH	11.41	28152594
586	Phosphorylation	ENSAYICSRRQRVSF CCCCEECCCCHHEEC	22.42	28152594
606	Acetylation	QAVEAWEKLTREEGT HHHHHHHHHHHHCCC	44.44	26051181
606	Ubiquitination	QAVEAWEKLTREEGT HHHHHHHHHHHHCCC	44.44	21906983
613	Phosphorylation	KLTREEGTPLTLYYS HHHHHCCCCCEEEEE	20.57	27050516
616	Phosphorylation	REEGTPLTLYYSHWR HHCCCCCEEEEEHHH	17.58	22817900
618	Phosphorylation	EGTPLTLYYSHWRKL CCCCCEEEEEHHHHH	9.55	22817900
620	Phosphorylation	TPLTLYYSHWRKLRD CCCEEEEEHHHHHHC	11.74	22817900
635	Phosphorylation	REIQLEISGKERLED CEEEEEECCHHHHHH	34.14	25159151
637	Ubiquitination	IQLEISGKERLEDLN EEEEECCHHHHHHCC	32.63	21906983
649	Acetylation	DLNFPEIKRRKMADR HCCCHHHHHHHHCCC	44.48	25953088
649	Ubiquitination	DLNFPEIKRRKMADR HCCCHHHHHHHHCCC	44.48	21906983
649	2-Hydroxyisobutyrylation	DLNFPEIKRRKMADR HCCCHHHHHHHHCCC	44.48	-
652	Ubiquitination	FPEIKRRKMADRKDE CHHHHHHHHCCCCHH	42.34	22817900
662	Ubiquitination	DRKDEDRKQFKDLFD CCCHHHHHHHHHHHC	72.85	22817900
665	Ubiquitination	DEDRKQFKDLFDLNS HHHHHHHHHHHCCCC	51.53	21906983
672	Phosphorylation	KDLFDLNSSEEDDTE HHHHCCCCCCCCCCC	46.56	29255136
673	Phosphorylation	DLFDLNSSEEDDTEG HHHCCCCCCCCCCCC	43.88	29255136
678	Phosphorylation	NSSEEDDTEGFSERG CCCCCCCCCCCCCCC	50.78	29255136
682	Phosphorylation	EDDTEGFSERGILRP CCCCCCCCCCCCCCC	36.92	23927012
691	Phosphorylation	RGILRPLSTRHGVED CCCCCCCCCCCCCCC	26.52	18212344
692	Phosphorylation	GILRPLSTRHGVEDD CCCCCCCCCCCCCCC	34.08	26434776
710	Phosphorylation	EEEGEEDSSNSEDGD HHCCCCCCCCCCCCC	34.40	20068231
711	Phosphorylation	EEGEEDSSNSEDGDP HCCCCCCCCCCCCCC	57.61	20068231
713	Phosphorylation	GEEDSSNSEDGDPDA CCCCCCCCCCCCCCH	38.73	20068231
746	Phosphorylation	ELEDLQLSEDD---- HHHHHCCCCCC----	26.47	11230166

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of NOC2L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NOC2L_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NOC2L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRIF1_HUMAN	LRIF1	physical	16189514
AURKB_HUMAN	AURKB	physical	20959462
P53_HUMAN	TP53	physical	20959462
H31T_HUMAN	HIST3H3	physical	16322561
H2A2A_HUMAN	HIST2H2AA3	physical	16322561
P53_HUMAN	TP53	physical	16322561
A4_HUMAN	APP	physical	21832049
MDM2_HUMAN	MDM2	physical	24413661
JAK1_HUMAN	JAK1	physical	24413661
CEBPZ_HUMAN	CEBPZ	physical	26344197
DDX52_HUMAN	DDX52	physical	26344197
DDX54_HUMAN	DDX54	physical	26344197
MK67I_HUMAN	NIFK	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
SDA1_HUMAN	SDAD1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NOC2L_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-673, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-56; SER-672;SER-673 AND THR-678, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-672 AND SER-673,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-56 ANDSER-121, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49 AND SER-672,AND MASS SPECTROMETRY.	16565220 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). 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,AND MASS SPECTROMETRY.	17081983 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY.	16083285 [Abstract]