NAA16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NAA16_HUMAN
• UniProt AC: Q6N069
• Protein Name: N-alpha-acetyltransferase 16, NatA auxiliary subunit
• Gene Name: NAA16
• Organism: Homo sapiens (Human).
• Sequence Length: 864
• Protein Description: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity..
• Protein Sequence: MPNVLLPPKESNLFKRILKCYEQKQYKNGLKFCKMILSNPKFAEHGETLAMKGLTLNCLGKKEEAYEFVRKGLRNDVKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKLDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPTQRASWIGYAIAYHLLKDYDMALKLLEEFRQTQQVPPNKIDYEYSELILYQNQVMREADLLQESLEHIEMYEKQICDKLLVEEIKGEILLKLGRLKEASEVFKNLIDRNAENWCYYEGLEKALQISTLEERLQIYEEISKQHPKAITPRRLPLTLVPGERFRELMDKFLRVNFSKGCPPLFTTLKSLYYNTEKVSIIQELVTNYEASLKTCDFFSPYENGEKEPPTTLLWVQYFLAQHFDKLGQYSLALDYINAAIASTPTLIELFYMKAKIYKHIGNLKEAAKWMDEAQSLDTADRFINSKCAKYMLRANMIKEAEEMCSKFTREGTSAMENLNEMQCMWFQTECISAYQRLGRYGDALKKCHEVERHFFEITDDQFDFHTYCMRKMTLRAYVDLLRLEDILRRHAFYFKAARSAIEIYLKLYDNPLTNESKQQEINSENLSAKELKKMLSKQRRAQKKAKLEEERKHAERERQQKNQKKKRDEEEEEASGLKEELIPEKLERVENPLEEAVKFLIPLKNLVADNIDTHLLAFEIYFRKGKFLLMLQSVKRAFAINSNNPWLHECLIRFSKSVSNHSNLPDIVSKVLSQEMQKIFVKKDLESFNEDFLKRNATSLQHLLSGAKMMYFLDKSRQEKAIAIATRLDETIKDKDVKTLIKVSEALLDGSFGNCSSQYEEYRMACHNLLPFTSAFLPAVNEVDNPNVALNHTANYDVLANEI

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
24	Methylation	ILKCYEQKQYKNGLK HHHHHHHHHHHCHHH	43.59	-
34	Ubiquitination	KNGLKFCKMILSNPK HCHHHHHHHHHHCHH	31.91	-
51	Sulfoxidation	EHGETLAMKGLTLNC HCCHHHHHCCCEEHH	3.88	21406390
52	Ubiquitination	HGETLAMKGLTLNCL CCHHHHHCCCEEHHC	45.20	-
52	Malonylation	HGETLAMKGLTLNCL CCHHHHHCCCEEHHC	45.20	26320211
52	Acetylation	HGETLAMKGLTLNCL CCHHHHHCCCEEHHC	45.20	25953088
55	Phosphorylation	TLAMKGLTLNCLGKK HHHHCCCEEHHCCCH	25.29	28857561
61	Acetylation	LTLNCLGKKEEAYEF CEEHHCCCHHHHHHH	44.02	25953088
61	Ubiquitination	LTLNCLGKKEEAYEF CEEHHCCCHHHHHHH	44.02	-
62	Acetylation	TLNCLGKKEEAYEFV EEHHCCCHHHHHHHH	60.01	26051181
62	Ubiquitination	TLNCLGKKEEAYEFV EEHHCCCHHHHHHHH	60.01	-
66	Phosphorylation	LGKKEEAYEFVRKGL CCCHHHHHHHHHHHH	17.12	-
79	Phosphorylation	GLRNDVKSHVCWHVY HHHHHHHHHHHHHHH	22.47	29083192
86	Phosphorylation	SHVCWHVYGLLQRSD HHHHHHHHHHHHCCC	6.81	27155012
94	Ubiquitination	GLLQRSDKKYDEAIK HHHHCCCHHHHHHHH	55.25	-
95	Ubiquitination	LLQRSDKKYDEAIKC HHHCCCHHHHHHHHH	64.03	-
96	Phosphorylation	LQRSDKKYDEAIKCY HHCCCHHHHHHHHHH	25.42	28796482
101	Ubiquitination	KKYDEAIKCYRNALK HHHHHHHHHHHHHHH	32.06	-
101	Acetylation	KKYDEAIKCYRNALK HHHHHHHHHHHHHHH	32.06	25953088
108	Ubiquitination	KCYRNALKLDKDNLQ HHHHHHHHCCHHHHH	52.83	-
111	Ubiquitination	RNALKLDKDNLQILR HHHHHCCHHHHHHHH	59.98	-
127	Sulfoxidation	LSLLQIQMRDLEGYR HHHHHHHHHCCCCHH	3.73	21406390
177	Phosphorylation	LLEEFRQTQQVPPNK HHHHHHHHCCCCCCC	19.40	23403867
187	Phosphorylation	VPPNKIDYEYSELIL CCCCCCCCCHHHHHH	21.90	27174698
189	Phosphorylation	PNKIDYEYSELILYQ CCCCCCCHHHHHHHH	10.96	27174698
190	Phosphorylation	NKIDYEYSELILYQN CCCCCCHHHHHHHHH	17.62	27174698
195	Phosphorylation	EYSELILYQNQVMRE CHHHHHHHHHHHHHH	9.83	27174698
209	Phosphorylation	EADLLQESLEHIEMY HHHHHHHHHHHHHHH	26.54	27174698
216	Phosphorylation	SLEHIEMYEKQICDK HHHHHHHHHHHHHHH	13.74	27174698
241	Ubiquitination	LLKLGRLKEASEVFK HHHHCCHHHHHHHHH	50.28	-
248	Ubiquitination	KEASEVFKNLIDRNA HHHHHHHHHHHHCCC	56.89	-
266	Ubiquitination	CYYEGLEKALQISTL CHHHHHHHHHHHCCH	60.48	-
285	Ubiquitination	QIYEEISKQHPKAIT HHHHHHHHHCCCCCC	59.28	-
292	Phosphorylation	KQHPKAITPRRLPLT HHCCCCCCCCCCCCC	18.66	24719451
320	Ubiquitination	FLRVNFSKGCPPLFT HHHHCCCCCCCCHHH	61.47	-
425	Ubiquitination	YKHIGNLKEAAKWMD HHHHCCHHHHHHHHH	49.67	-
447	Ubiquitination	ADRFINSKCAKYMLR HHHHHHHHHHHHHHH	33.45	-
466	O-linked_Glycosylation	KEAEEMCSKFTREGT HHHHHHHHHHHHCCC	29.50	30379171
466	Phosphorylation	KEAEEMCSKFTREGT HHHHHHHHHHHHCCC	29.50	22210691
467	Acetylation	EAEEMCSKFTREGTS HHHHHHHHHHHCCCH	45.91	25953088
467	Ubiquitination	EAEEMCSKFTREGTS HHHHHHHHHHHCCCH	45.91	-
493	Phosphorylation	WFQTECISAYQRLGR HHHHHHHHHHHHHHH	32.36	22210691
495	Phosphorylation	QTECISAYQRLGRYG HHHHHHHHHHHHHHH	6.33	22210691
578 (in isoform 1)	Ubiquitination	-	50.23	21906983
578	Ubiquitination	NPLTNESKQQEINSE CCCCCHHHHHHHCCC	50.23	2190698
584	Phosphorylation	SKQQEINSENLSAKE HHHHHHCCCCCCHHH	33.26	28122231
588	Phosphorylation	EINSENLSAKELKKM HHCCCCCCHHHHHHH	49.21	28122231
636	Phosphorylation	DEEEEEASGLKEELI HHHHHHHHCCHHHHC	48.19	19664994
718	Phosphorylation	CLIRFSKSVSNHSNL HHHHHHHHHCCCCCH	29.58	22985185
720	Phosphorylation	IRFSKSVSNHSNLPD HHHHHHHCCCCCHHH	35.60	22985185
723	Phosphorylation	SKSVSNHSNLPDIVS HHHHCCCCCHHHHHH	44.29	22985185
730	Phosphorylation	SNLPDIVSKVLSQEM CCHHHHHHHHHCHHH	19.85	22985185
744	Ubiquitination	MQKIFVKKDLESFNE HHHHHHHHCHHHCCH	63.34	-
755	Ubiquitination	SFNEDFLKRNATSLQ HCCHHHHHCCHHHHH	43.53	-
759	Phosphorylation	DFLKRNATSLQHLLS HHHHCCHHHHHHHHH	33.25	30622161
760	Phosphorylation	FLKRNATSLQHLLSG HHHCCHHHHHHHHHH	24.50	30622161
766	Phosphorylation	TSLQHLLSGAKMMYF HHHHHHHHHHHHHHH	42.96	30622161
772	Phosphorylation	LSGAKMMYFLDKSRQ HHHHHHHHHHCHHHH	9.48	-
787	Phosphorylation	EKAIAIATRLDETIK HHHHHHHHHCCHHCC	26.17	27174698
792	Phosphorylation	IATRLDETIKDKDVK HHHHCCHHCCCCCHH	32.75	27174698

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

Oops, there are no upstream regulatory protein records of NAA16_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NAA16_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 NAA16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TCEA1_HUMAN	TCEA1	physical	22939629
PLCB3_HUMAN	PLCB3	physical	22939629

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.