dbPTM

NAA11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NAA11_HUMAN
UniProt AC	Q9BSU3
Protein Name	N-alpha-acetyltransferase 11
Gene Name	NAA11
Organism	Homo sapiens (Human).
Sequence Length	229
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Displays alpha (N-terminal) acetyltransferase activity. Proposed alternative catalytic subunit of the N-terminal acetyltransferase A (NatA) complex..
Protein Sequence	MNIRNAQPDDLMNMQHCNLLCLPENYQMKYYLYHGLSWPQLSYIAEDEDGKIVGYVLAKMEEEPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRPALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLSQMADELRRQMDLKKGGYVVLGSRENQETQGSTLSDSEEACQQKNPATEESGSDSKEPKESVESTNVQDSSESSDSTS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
73	Phosphorylation	DVPHGHITSLAVKRS CCCCCCHHHHHHHHH	16.41	-
74	Phosphorylation	VPHGHITSLAVKRSH CCCCCHHHHHHHHHH	17.46	-
78	Ubiquitination	HITSLAVKRSHRRLG CHHHHHHHHHHHHHH	42.44	21890473
89	Ubiquitination	RRLGLAQKLMDQASR HHHHHHHHHHHHHHH	39.92	23000965
105	Ubiquitination	MIENFNAKYVSLHVR HHHHHCCEEEEEEEE	47.49	21906983
106	Phosphorylation	IENFNAKYVSLHVRK HHHHCCEEEEEEEEC	7.89	28152594
108	Phosphorylation	NFNAKYVSLHVRKSN HHCCEEEEEEEECCC	15.07	28857561
136	Acetylation	QISEVEPKYYADGED EEEECCCCEECCCHH	37.07	25038526
137	Phosphorylation	ISEVEPKYYADGEDA EEECCCCEECCCHHH	18.01	21406692
138	Phosphorylation	SEVEPKYYADGEDAY EECCCCEECCCHHHH	12.35	21406692
145	Phosphorylation	YADGEDAYAMKRDLS ECCCHHHHHHHHHHH	21.39	21406692
148	Acetylation	GEDAYAMKRDLSQMA CHHHHHHHHHHHHHH	34.29	24430813
148	Ubiquitination	GEDAYAMKRDLSQMA CHHHHHHHHHHHHHH	34.29	21906983
152	Phosphorylation	YAMKRDLSQMADELR HHHHHHHHHHHHHHH	23.38	30622161
180	Phosphorylation	GSRENQETQGSTLSD CCCCCCCCCCCCCCC	28.59	23663014
183	Phosphorylation	ENQETQGSTLSDSEE CCCCCCCCCCCCHHH	19.16	23663014
184	Phosphorylation	NQETQGSTLSDSEEA CCCCCCCCCCCHHHH	36.79	23663014
186	Phosphorylation	ETQGSTLSDSEEACQ CCCCCCCCCHHHHHH	38.90	22617229
188	Phosphorylation	QGSTLSDSEEACQQK CCCCCCCHHHHHHHH	33.68	23663014

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 NAA11_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NAA11_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 NAA11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NAA11_HUMAN !!

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 NAA11_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-136, AND MASS SPECTROMETRY.	19608861 [Abstract]