dbPTM

KAT8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAT8_HUMAN
UniProt AC	Q9H7Z6
Protein Name	Histone acetyltransferase KAT8
Gene Name	KAT8
Organism	Homo sapiens (Human).
Sequence Length	458
Subcellular Localization	Nucleus . Chromosome.
Protein Description	Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'..
Protein Sequence	MAAQGAAAAVAAGTSGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAQGAAAA ------CCHHHHHHH	14.43	22814378
14	Phosphorylation	AAAVAAGTSGVAGEG HHHHHHCCCCCCCCC	19.99	28348404
15	Phosphorylation	AAVAAGTSGVAGEGE HHHHHCCCCCCCCCC	30.28	28348404
34	Phosphorylation	ENAAAEGTAPSPGRV CCCCCCCCCCCCCCC	27.22	29255136
37	Phosphorylation	AAEGTAPSPGRVSPP CCCCCCCCCCCCCCC	37.21	29255136
42	Phosphorylation	APSPGRVSPPTPARG CCCCCCCCCCCCCCC	24.65	30266825
45	Phosphorylation	PGRVSPPTPARGEPE CCCCCCCCCCCCCCE	32.72	30266825
54	Phosphorylation	ARGEPEVTVEIGETY CCCCCEEEEEECCEE	15.68	26074081
90	Phosphorylation	QEGREEFYVHYVGFN CCCCEEEEEEEEECC	6.92	-
106 (in isoform 2)	Ubiquitination	-	34.06	-
106	Ubiquitination	RLDEWVDKNRLALTK CHHHHHHHHHHHCCH	34.06	-
106	Acetylation	RLDEWVDKNRLALTK CHHHHHHHHHHHCCH	34.06	25953088
113	Acetylation	KNRLALTKTVKDAVQ HHHHHCCHHHHHHHH	52.77	19608861
113 (in isoform 2)	Ubiquitination	-	52.77	-
113	Ubiquitination	KNRLALTKTVKDAVQ HHHHHCCHHHHHHHH	52.77	29967540
114	Phosphorylation	NRLALTKTVKDAVQK HHHHCCHHHHHHHHH	27.79	19413330
116	Acetylation	LALTKTVKDAVQKNS HHCCHHHHHHHHHCH	45.24	23749302
125 (in isoform 2)	Ubiquitination	-	51.84	-
125	Ubiquitination	AVQKNSEKYLSELAE HHHHCHHHHHHHHHH	51.84	29967540
126	Phosphorylation	VQKNSEKYLSELAEQ HHHCHHHHHHHHHHC	16.06	23532336
143	Acetylation	RKITRNQKRKHDEIN HHCCHHHHHCHHHHH	67.95	22918831
145	Acetylation	ITRNQKRKHDEINHV CCHHHHHCHHHHHHH	63.54	22918831
154	Acetylation	DEINHVQKTYAEMDP HHHHHHHHHHHHCCC	42.27	22918831
154	Ubiquitination	DEINHVQKTYAEMDP HHHHHHHHHHHHCCC	42.27	29967540
155	Phosphorylation	EINHVQKTYAEMDPT HHHHHHHHHHHCCCC	15.75	28796482
156	Phosphorylation	INHVQKTYAEMDPTT HHHHHHHHHHCCCCH	13.96	28796482
168	Acetylation	PTTAALEKEHEAITK CCHHHHHHHHHHHHC	66.28	23749302
168	Ubiquitination	PTTAALEKEHEAITK CCHHHHHHHHHHHHC	66.28	29967540
174	Phosphorylation	EKEHEAITKVKYVDK HHHHHHHHCCEEEEE	36.51	-
175	Ubiquitination	KEHEAITKVKYVDKI HHHHHHHCCEEEEEE	30.53	29967540
175	Acetylation	KEHEAITKVKYVDKI HHHHHHHCCEEEEEE	30.53	22918831
177	Acetylation	HEAITKVKYVDKIHI HHHHHCCEEEEEEEE	40.90	22918831
238	Acetylation	QWRQPPGKEIYRKSN EECCCCCCEEEECCC	46.87	19608861
241	Phosphorylation	QPPGKEIYRKSNISV CCCCCEEEECCCEEE	17.06	-
243	Ubiquitination	PGKEIYRKSNISVYE CCCEEEECCCEEEEE	30.77	29967540
254	Ubiquitination	SVYEVDGKDHKIYCQ EEEEECCCCCEEHHH	52.80	29967540
257	Ubiquitination	EVDGKDHKIYCQNLC EECCCCCEEHHHHHH	45.57	29967540
274	Acetylation	AKLFLDHKTLYFDVE HHHHCCCCCEEECCC	39.63	21217699
344	Phosphorylation	YELSKLESTVGSPEK EEHHHHHHCCCCCCC	38.54	29255136
345	Phosphorylation	ELSKLESTVGSPEKP EHHHHHHCCCCCCCC	21.36	29255136
348	Phosphorylation	KLESTVGSPEKPLSD HHHHCCCCCCCCHHH	26.08	21217699
351	Acetylation	STVGSPEKPLSDLGK HCCCCCCCCHHHHCC	55.43	23954790
351	Ubiquitination	STVGSPEKPLSDLGK HCCCCCCCCHHHHCC	55.43	29967540
354	Phosphorylation	GSPEKPLSDLGKLSY CCCCCCHHHHCCHHH	39.04	29255136
386	Phosphorylation	TLSIKDLSQMTSITQ CCCHHHHHHCCCCCH	28.21	24043423
389	Phosphorylation	IKDLSQMTSITQNDI HHHHHHCCCCCHHHH	14.89	24043423
390	Phosphorylation	KDLSQMTSITQNDII HHHHHCCCCCHHHHH	20.49	24043423
392	Phosphorylation	LSQMTSITQNDIIST HHHCCCCCHHHHHHH	22.53	24043423
398	Phosphorylation	ITQNDIISTLQSLNM CCHHHHHHHHHHHCC	24.33	24043423
399	Phosphorylation	TQNDIISTLQSLNMV CHHHHHHHHHHHCCH	20.57	28674151
402	Phosphorylation	DIISTLQSLNMVKYW HHHHHHHHHCCHHHC	25.48	28674151
410	Ubiquitination	LNMVKYWKGQHVICV HCCHHHCCCCEEEEE	45.67	29967540
410	Acetylation	LNMVKYWKGQHVICV HCCHHHCCCCEEEEE	45.67	22918831
427	Ubiquitination	KLVEEHLKSAQYKKP HHHHHHHHHCCCCCC	45.73	29967540
427 (in isoform 2)	Ubiquitination	-	45.73	-
433	Ubiquitination	LKSAQYKKPPITVDS HHHCCCCCCCCEEEE	51.60	29967540
444	Ubiquitination	TVDSVCLKWAPPKHK EEEEEEECCCCCCCC	35.86	29967540
449	Acetylation	CLKWAPPKHKQVKLS EECCCCCCCCCCCCC	63.48	22918831
454	Acetylation	PPKHKQVKLSKK--- CCCCCCCCCCCC---	44.54	22918831
456	Phosphorylation	KHKQVKLSKK----- CCCCCCCCCC-----	32.45	17192257
457	Acetylation	HKQVKLSKK------ CCCCCCCCC------	73.30	22918831

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
392	T	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
274	K	Acetylation
Autoacetylation at Lys-274 is required for binding histone H4 with high affinity and for proper function.

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 KAT8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	17189187
P53_HUMAN	TP53	physical	19854137
BAZ2A_HUMAN	BAZ2A	physical	19578370
MSL1_HUMAN	MSL1	physical	16227571
MSL2_HUMAN	MSL2	physical	16227571
MS3L1_HUMAN	MSL3	physical	16227571
HCFC1_HUMAN	HCFC1	physical	16227571
KANL1_HUMAN	KANSL1	physical	16227571
H31_HUMAN	HIST1H3A	physical	16227571
KMT2A_HUMAN	KMT2A	physical	15960975
RBBP5_HUMAN	RBBP5	physical	15960975
WDR5_HUMAN	WDR5	physical	15960975
RING2_HUMAN	RNF2	physical	15960975
KAT8_HUMAN	KAT8	physical	15960975
ATM_HUMAN	ATM	physical	15923642
TPR_HUMAN	TPR	physical	20479123
PRKDC_HUMAN	PRKDC	physical	20479123
MSL1_HUMAN	MSL1	physical	20479123
HCFC1_HUMAN	HCFC1	physical	20479123
OGT1_HUMAN	OGT	physical	20479123
CCAR2_HUMAN	CCAR2	physical	20479123
PHF20_HUMAN	PHF20	physical	20479123
P20L1_HUMAN	PHF20L1	physical	20479123
MS3L1_HUMAN	MSL3	physical	20479123
MSL2_HUMAN	MSL2	physical	20479123
MCRS1_HUMAN	MCRS1	physical	20479123
WDR5_HUMAN	WDR5	physical	20479123
1433E_HUMAN	YWHAE	physical	19766566
1433Z_HUMAN	YWHAZ	physical	19766566
H31_HUMAN	HIST1H3A	physical	19766566
BRD4_HUMAN	BRD4	physical	19766566
ELOA1_HUMAN	TCEB3	physical	19766566
KAT8_HUMAN	KAT8	physical	21502975
MSL1_HUMAN	MSL1	physical	21217699
KANL1_HUMAN	KANSL1	physical	21217699
ACK1_HUMAN	TNK2	physical	22586264
SIR1_HUMAN	SIRT1	physical	22586264
PP1B_HUMAN	PPP1CB	physical	22939629
PAF1_HUMAN	PAF1	physical	24837678
ROA1_HUMAN	HNRNPA1	physical	26344197
TP53B_HUMAN	TP53BP1	physical	24953651

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 KAT8_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-37; SER-42 AND THR-114, AND MASS SPECTROMETRY.	19413330 [Abstract]
"MYST protein acetyltransferase activity requires active site lysineautoacetylation."; Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,Marmorstein R.; EMBO J. 31:58-70(2012). Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 177-458, ACTIVE SITE, ANDACETYLATION AT LYS-274.	22020126 [Abstract]
"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-113 AND LYS-238, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-37; SER-42 AND THR-114, AND MASS SPECTROMETRY.	19413330 [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-348 AND SER-456, ANDMASS SPECTROMETRY.	18691976 [Abstract]

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