NOP16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NOP16_HUMAN
• UniProt AC: Q9Y3C1
• Protein Name: Nucleolar protein 16
• Gene Name: NOP16
• Organism: Homo sapiens (Human).
• Sequence Length: 178
• Subcellular Localization: Nucleus, nucleolus .
• Protein Sequence: MPKAKGKTRRQKFGYSVNRKRLNRNARRKAAPRIECSHIRHAWDHAKSVRQNLAEMGLAVDPNRAVPLRKRKVKAMEVDIEERPKELVRKPYVLNDLEAEASLPEKKGNTLSRDLIDYVRYMVENHGEDYKAMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPKAKGKTRRQKFGY CCCCCCCCCHHHHCC	39.49	21406692
12	Ubiquitination	KGKTRRQKFGYSVNR CCCCCHHHHCCCCCH	38.66	-
15	Phosphorylation	TRRQKFGYSVNRKRL CCHHHHCCCCCHHHH	16.75	28152594
16	Phosphorylation	RRQKFGYSVNRKRLN CHHHHCCCCCHHHHC	17.19	25159151
47	2-Hydroxyisobutyrylation	RHAWDHAKSVRQNLA HHHHHHHHHHHHHHH	46.17	-
47	Acetylation	RHAWDHAKSVRQNLA HHHHHHHHHHHHHHH	46.17	26822725
47	Ubiquitination	RHAWDHAKSVRQNLA HHHHHHHHHHHHHHH	46.17	-
48	Phosphorylation	HAWDHAKSVRQNLAE HHHHHHHHHHHHHHH	24.26	26434776
74	Sumoylation	PLRKRKVKAMEVDIE CCCCCCCCEEECCHH	45.08	28112733
76	Sulfoxidation	RKRKVKAMEVDIEER CCCCCCEEECCHHHC	4.23	21406390
77	Acetylation	KRKVKAMEVDIEERP CCCCCEEECCHHHCC	41.73	19608861
90	Ubiquitination	RPKELVRKPYVLNDL CCHHHHCCCCCCCCH	32.97	19608861
90	Acetylation	RPKELVRKPYVLNDL CCHHHHCCCCCCCCH	32.97	19608861
92	Phosphorylation	KELVRKPYVLNDLEA HHHHCCCCCCCCHHH	22.17	28152594
102	Phosphorylation	NDLEAEASLPEKKGN CCHHHHHCCCCCCCC	35.64	28450419
106	Ubiquitination	AEASLPEKKGNTLSR HHHCCCCCCCCCCCH	65.13	-
106	Acetylation	AEASLPEKKGNTLSR HHHCCCCCCCCCCCH	65.13	26051181
106	2-Hydroxyisobutyrylation	AEASLPEKKGNTLSR HHHCCCCCCCCCCCH	65.13	-
112	Phosphorylation	EKKGNTLSRDLIDYV CCCCCCCCHHHHHHH	23.01	29214152
130	Phosphorylation	VENHGEDYKAMARDE HHHCCHHHHHHHHHC	9.06	-
131	Acetylation	ENHGEDYKAMARDEK HHCCHHHHHHHHHCC	43.96	26051181
134 (in isoform 2)	Ubiquitination	-	22.19	-
135	Ubiquitination	EDYKAMARDEKNYYQ HHHHHHHHHCCCCCC	39.27	-
138	2-Hydroxyisobutyrylation	KAMARDEKNYYQDTP HHHHHHCCCCCCCCH	55.31	-
138	Acetylation	KAMARDEKNYYQDTP HHHHHHCCCCCCCCH	55.31	26051181
140	Phosphorylation	MARDEKNYYQDTPKQ HHHHCCCCCCCCHHH	17.36	27174698
141	Phosphorylation	ARDEKNYYQDTPKQI HHHCCCCCCCCHHHH	14.87	27174698
144	Phosphorylation	EKNYYQDTPKQIRSK CCCCCCCCHHHHHHH	19.50	25159151
146	Malonylation	NYYQDTPKQIRSKIN CCCCCCHHHHHHHHH	61.52	26320211
146	Acetylation	NYYQDTPKQIRSKIN CCCCCCHHHHHHHHH	61.52	26051181
146	Ubiquitination	NYYQDTPKQIRSKIN CCCCCCHHHHHHHHH	61.52	-
169	Phosphorylation	EWQDFLDSLQKRKME HHHHHHHHHHHHHHC	34.54	22199227
216 (in isoform 3)	Phosphorylation	-		28674419

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

Oops, there are no upstream regulatory protein records of NOP16_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NOP16_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NOP16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
HERC5_HUMAN	HERC5	physical	28514442
NP1L1_HUMAN	NAP1L1	physical	28514442

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-16 AND THR-144, AND MASSSPECTROMETRY.
PubMed: 18669648