NAA50_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NAA50_HUMAN
• UniProt AC: Q9GZZ1
• Protein Name: N-alpha-acetyltransferase 50 {ECO:0000305}
• Gene Name: NAA50 {ECO:0000312|HGNC:HGNC:29533}
• Organism: Homo sapiens (Human).
• Sequence Length: 169
• Subcellular Localization: Cytoplasm . Nucleus . Localizes to the cytoplasm in interphase cells (PubMed:17502424).
• Protein Description: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine. [PubMed: 19744929]
• Protein Sequence: MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN

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
2	Ubiquitination	------MKGSRIELG ------CCCCCEECC	66.64	-
4	Phosphorylation	----MKGSRIELGDV ----CCCCCEECCCC	25.27	25056879
12	Phosphorylation	RIELGDVTPHNIKQL CEECCCCCHHCHHHH	24.46	25159151
17	Ubiquitination	DVTPHNIKQLKRLNQ CCCHHCHHHHHHHCC	55.70	21890473
17 (in isoform 2)	Ubiquitination	-	55.70	21890473
17 (in isoform 1)	Ubiquitination	-	55.70	21890473
17	Acetylation	DVTPHNIKQLKRLNQ CCCHHCHHHHHHHCC	55.70	25953088
17	Malonylation	DVTPHNIKQLKRLNQ CCCHHCHHHHHHHCC	55.70	26320211
20	Ubiquitination	PHNIKQLKRLNQVIF HHCHHHHHHHCCEEE	52.96	-
20 (in isoform 2)	Ubiquitination	-	52.96	-
30	Phosphorylation	NQVIFPVSYNDKFYK CCEEEEECCCCHHHH	20.61	20068231
31	Phosphorylation	QVIFPVSYNDKFYKD CEEEEECCCCHHHHH	27.84	20068231
34 (in isoform 1)	Ubiquitination	-	47.13	21890473
34	Acetylation	FPVSYNDKFYKDVLE EEECCCCHHHHHHHH	47.13	19608861
34 (in isoform 2)	Ubiquitination	-	47.13	21890473
34 (in isoform 2)	Acetylation	-	47.13	19608861
34	Ubiquitination	FPVSYNDKFYKDVLE EEECCCCHHHHHHHH	47.13	19608861
36 (in isoform 2)	Phosphorylation	-	16.42	-
37	Ubiquitination	SYNDKFYKDVLEVGE CCCCHHHHHHHHHHH	44.48	19608861
37 (in isoform 1)	Ubiquitination	-	44.48	21890473
37	Acetylation	SYNDKFYKDVLEVGE CCCCHHHHHHHHHHH	44.48	19608861
38 (in isoform 2)	Ubiquitination	-	38.56	21890473
47	Ubiquitination	LEVGELAKLAYFNDI HHHHHHHHHHHCCCC	46.40	-
47 (in isoform 2)	Ubiquitination	-	46.40	21890473
50	Phosphorylation	GELAKLAYFNDIAVG HHHHHHHHCCCCCEE	17.22	28152594
64 (in isoform 2)	Ubiquitination	-	19.17	21890473
70	2-Hydroxyisobutyrylation	VDHSQNQKRLYIMTL CCCCCCCEEEEEEEH	52.50	-
73	Phosphorylation	SQNQKRLYIMTLGCL CCCCEEEEEEEHHHH	7.84	-
78 (in isoform 2)	Ubiquitination	-	8.67	21890473
91	Ubiquitination	RRLGIGTKMLNHVLN HHCCCCHHHHHHHHH	35.86	20639865
91	Acetylation	RRLGIGTKMLNHVLN HHCCCCHHHHHHHHH	35.86	25953088
110	Phosphorylation	DGTFDNIYLHVQISN CCCCCCEEEEEEECC	9.30	22817900
126	Acetylation	SAIDFYRKFGFEIIE HHHHHHHHHCCEEEE	38.16	25953088
126	Ubiquitination	SAIDFYRKFGFEIIE HHHHHHHHHCCEEEE	38.16	21890473
135	Acetylation	GFEIIETKKNYYKRI CCEEEEECCCHHHHC	26.65	25953088
135	Ubiquitination	GFEIIETKKNYYKRI CCEEEEECCCHHHHC	26.65	2190698
135 (in isoform 1)	Ubiquitination	-	26.65	21890473
136	Ubiquitination	FEIIETKKNYYKRIE CEEEEECCCHHHHCC	58.56	-
139	Phosphorylation	IETKKNYYKRIEPAD EEECCCHHHHCCHHH	11.81	-
140	Acetylation	ETKKNYYKRIEPADA EECCCHHHHCCHHHC	36.22	19744929
140	Ubiquitination	ETKKNYYKRIEPADA EECCCHHHHCCHHHC	36.22	19744929
152 (in isoform 1)	Ubiquitination	-	61.15	21890473
152	Acetylation	ADAHVLQKNLKVPSG HHCHHHHHCCCCCCC	61.15	19608861
152	Ubiquitination	ADAHVLQKNLKVPSG HHCHHHHHCCCCCCC	61.15	21890473
155	Ubiquitination	HVLQKNLKVPSGQNA HHHHHCCCCCCCCCC	62.59	-
166 (in isoform 1)	Ubiquitination	-	58.66	21890473
166	Ubiquitination	GQNADVQKTDN---- CCCCCCCCCCC----	58.66	-
167	Phosphorylation	QNADVQKTDN----- CCCCCCCCCC-----	24.55	-

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

Oops, there are no upstream regulatory protein records of NAA50_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NAA50_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 NAA50_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NAA15_HUMAN	NAA15	physical	16507339
NAA10_HUMAN	NAA10	physical	16507339
DNJC7_HUMAN	DNAJC7	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
HNRDL_HUMAN	HNRNPDL	physical	26344197
NDRG1_HUMAN	NDRG1	physical	26344197
TIM8B_HUMAN	TIMM8B	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.

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-34 AND LYS-37, AND MASSSPECTROMETRY.
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 THR-12, AND MASSSPECTROMETRY.
PubMed: 18669648

"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND MASSSPECTROMETRY.
PubMed: 15592455