dbPTM

KAT6A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAT6A_HUMAN
UniProt AC	Q92794
Protein Name	Histone acetyltransferase KAT6A
Gene Name	KAT6A
Organism	Homo sapiens (Human).
Sequence Length	2004
Subcellular Localization	Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus, PML body. Recruited into PML body after DNA damage.
Protein Description	Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML..
Protein Sequence	MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKSIERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKESCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGPGRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPSPDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEKDMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	KKQKQRPSEERICNA HHHCCCCCHHHHHHH	55.04	20068231
37	Phosphorylation	ERICNAVSSSHGLDR HHHHHHHHHCCCCCH	24.58	20068231
38	Phosphorylation	RICNAVSSSHGLDRK HHHHHHHHCCCCCHH	21.54	20068231
39	Phosphorylation	ICNAVSSSHGLDRKT HHHHHHHCCCCCHHH	17.67	20068231
94	Acetylation	NHGKLDNKQNVDWNK CCCCCCCCCCCCHHH	42.80	25953088
116	Phosphorylation	GLAESGGSTLKSIER HHHHCCCHHHHHHHH	33.81	-
117	Phosphorylation	LAESGGSTLKSIERF HHHCCCHHHHHHHHH	41.29	-
120	Phosphorylation	SGGSTLKSIERFLKG CCCHHHHHHHHHHCC	32.56	26437602
132	Phosphorylation	LKGQKDVSALFGGSA HCCCCCHHHHHCCCH	29.41	-
138	Phosphorylation	VSALFGGSAASGFHQ HHHHHCCCHHCCHHH	22.50	-
141	Phosphorylation	LFGGSAASGFHQQLR HHCCCHHCCHHHHHH	41.53	-
172	Acetylation	PLYRLNTKATNVDGK CEEEECCCCCCCCCC	52.74	25953088
216	Acetylation	CSFCLGTKEQNREKK CCCCCCCHHHCCCCC	56.35	26051181
245	Phosphorylation	HPSCLKFSPELTVRV CHHHHCCCCHHHHHE	18.84	21815630
332	Phosphorylation	AQIKRRYTNPIGRPK HHHHHHHCCCCCCCC	32.48	24719451
344	Acetylation	RPKNRLKKQNTVSKG CCCHHCCCCCCCCCC	54.06	25953088
347	Phosphorylation	NRLKKQNTVSKGPFS HHCCCCCCCCCCCCC	24.54	-
350	Acetylation	KKQNTVSKGPFSKVR CCCCCCCCCCCCCCC	67.29	19608861
355	Acetylation	VSKGPFSKVRTGPGR CCCCCCCCCCCCCCC	35.79	19608861
369	Phosphorylation	RGRKRKITLSSQSAS CCCCEEEEECCCCCC	24.50	23431171
371	Phosphorylation	RKRKITLSSQSASSS CCEEEEECCCCCCCC	20.06	22210691
374	Phosphorylation	KITLSSQSASSSSEE EEEECCCCCCCCCCC	31.87	22210691
376	Phosphorylation	TLSSQSASSSSEEGY EECCCCCCCCCCCCC	35.68	30576142
377	Phosphorylation	LSSQSASSSSEEGYL ECCCCCCCCCCCCCH	37.28	28985074
378	Phosphorylation	SSQSASSSSEEGYLE CCCCCCCCCCCCCHH	38.99	30576142
379	Phosphorylation	SQSASSSSEEGYLER CCCCCCCCCCCCHHE	41.43	-
383	Phosphorylation	SSSSEEGYLERIDGL CCCCCCCCHHEECCC	14.52	-
399	Phosphorylation	FCRDSNVSLKFNKKT CCCCCCCEEEECCCC	30.05	22210691
401	Acetylation	RDSNVSLKFNKKTKG CCCCCEEEECCCCCC	39.11	25953088
407	Acetylation	LKFNKKTKGLIDGLT EEECCCCCCCCCHHH	61.68	23236377
415	Acetylation	GLIDGLTKFFTPSPD CCCCHHHHCCCCCCC	43.45	19608861
415	Ubiquitination	GLIDGLTKFFTPSPD CCCCHHHHCCCCCCC	43.45	21890473
418	Phosphorylation	DGLTKFFTPSPDGRK CHHHHCCCCCCCCCC	26.45	30266825
420	Phosphorylation	LTKFFTPSPDGRKAR HHHCCCCCCCCCCCC	32.34	30266825
433	Phosphorylation	ARGEVVDYSEQYRIR CCCEECCHHHHHCCH	11.51	-
434	Phosphorylation	RGEVVDYSEQYRIRK CCEECCHHHHHCCHH	17.48	28555341
437	Phosphorylation	VVDYSEQYRIRKRGN ECCHHHHHCCHHCCC	12.17	-
447	Phosphorylation	RKRGNRKSSTSDWPT HHCCCCCCCCCCCCC	35.29	25159151
448	Phosphorylation	KRGNRKSSTSDWPTD HCCCCCCCCCCCCCC	34.66	23401153
449	Phosphorylation	RGNRKSSTSDWPTDN CCCCCCCCCCCCCCC	37.48	23927012
450	Phosphorylation	GNRKSSTSDWPTDNQ CCCCCCCCCCCCCCC	39.36	23927012
454	Phosphorylation	SSTSDWPTDNQDGWD CCCCCCCCCCCCCCC	43.24	20068231
463	Acetylation	NQDGWDGKQENEERL CCCCCCCCHHHHHHH	52.55	23236377
463	Ubiquitination	NQDGWDGKQENEERL CCCCCCCCHHHHHHH	52.55	-
473	Phosphorylation	NEERLFGSQEIMTEK HHHHHHCCHHHCCHH	19.80	17525332
478	Phosphorylation	FGSQEIMTEKDMELF HCCHHHCCHHHHHHH	45.61	29255136
480	Ubiquitination	SQEIMTEKDMELFRD CHHHCCHHHHHHHHH	53.89	-
495	Acetylation	IQEQALQKVGVTGPP HHHHHHHHHCCCCCC	41.63	25953088
495	Ubiquitination	IQEQALQKVGVTGPP HHHHHHHHHCCCCCC	41.63	-
517	Phosphorylation	SVIEFGKYEIHTWYS CEEEEECEEEEECCC	22.09	23663014
521	Phosphorylation	FGKYEIHTWYSSPYP EECEEEEECCCCCCC	31.59	23663014
523	Phosphorylation	KYEIHTWYSSPYPQE CEEEEECCCCCCCHH	10.63	23663014
524	Phosphorylation	YEIHTWYSSPYPQEY EEEEECCCCCCCHHH	19.19	23663014
525	Phosphorylation	EIHTWYSSPYPQEYS EEEECCCCCCCHHHC	16.86	23663014
527	Phosphorylation	HTWYSSPYPQEYSRL EECCCCCCCHHHCCC	21.35	23663014
531	Phosphorylation	SSPYPQEYSRLPKLY CCCCCHHHCCCCHHH	8.21	23663014
532	Phosphorylation	SPYPQEYSRLPKLYL CCCCHHHCCCCHHHH	26.96	23663014
604	Acetylation	AKLFLDHKTLYYDVE HHHHCCCCCEECCCH	39.63	155401
619	Phosphorylation	PFLFYVLTQNDVKGC HHHEEEECCCCCCCC	18.45	30576142
641	Acetylation	KEKHCQQKYNVSCIM CCCCHHHCCCEEEEE	16.95	25953088
678	Phosphorylation	KREGQAGSPEKPLSD HCCCCCCCCCCCHHH	32.66	30266825
684	Phosphorylation	GSPEKPLSDLGRLSY CCCCCCHHHHHHHHH	39.04	30266825
777	Phosphorylation	DPECLRWTPVIVSNS CHHHHCCCEEEEECC	10.97	27251275
782	Phosphorylation	RWTPVIVSNSVVSEE CCCEEEEECCCCCHH	16.56	30576142
784	Phosphorylation	TPVIVSNSVVSEEEE CEEEEECCCCCHHHH	19.18	30266825
787	Phosphorylation	IVSNSVVSEEEEEEA EEECCCCCHHHHHHH	36.82	30266825
812	Phosphorylation	QERELEISVGKSVSH HHHEEEEEECCCCCC	18.55	30266825
815	Acetylation	ELEISVGKSVSHENK EEEEEECCCCCCCCC	45.59	16916647
822	Acetylation	KSVSHENKEQDSYSV CCCCCCCCCCCCCCC	54.49	23236377
826	Phosphorylation	HENKEQDSYSVESEK CCCCCCCCCCCCCCC	20.99	21815630
827	Phosphorylation	ENKEQDSYSVESEKK CCCCCCCCCCCCCCC	25.65	30576142
828	Phosphorylation	NKEQDSYSVESEKKP CCCCCCCCCCCCCCC	24.30	30576142
831	Phosphorylation	QDSYSVESEKKPEVM CCCCCCCCCCCCCCC	53.19	30576142
833	Acetylation	SYSVESEKKPEVMAP CCCCCCCCCCCCCCC	80.87	26051181
834	Acetylation	YSVESEKKPEVMAPV CCCCCCCCCCCCCCC	42.21	25953088
834	Sumoylation	YSVESEKKPEVMAPV CCCCCCCCCCCCCCC	42.21	28112733
842	Phosphorylation	PEVMAPVSSTRLSKQ CCCCCCCCCCCCCCC	25.57	20068231
843	Phosphorylation	EVMAPVSSTRLSKQV CCCCCCCCCCCCCCC	20.13	20068231
844	Phosphorylation	VMAPVSSTRLSKQVL CCCCCCCCCCCCCCC	28.29	20068231
847	Phosphorylation	PVSSTRLSKQVLPHD CCCCCCCCCCCCCCC	20.11	27282143
848	Acetylation	VSSTRLSKQVLPHDS CCCCCCCCCCCCCCC	49.36	25953088
882	Acetylation	TQERFGDKDSKLLLE HHHHHCCCCHHHHHH	65.37	25953088
891	Phosphorylation	SKLLLEETSSAPQEQ HHHHHHHCCCCCHHH	20.71	25627689
892	Phosphorylation	KLLLEETSSAPQEQY HHHHHHCCCCCHHHH	27.99	25627689
893	Phosphorylation	LLLEETSSAPQEQYG HHHHHCCCCCHHHHC	51.92	25627689
899	Phosphorylation	SSAPQEQYGECGEKS CCCCHHHHCCCCCCC	17.71	-
905	Acetylation	QYGECGEKSEATQEQ HHCCCCCCCHHHHHH	38.59	26051181
909	Phosphorylation	CGEKSEATQEQYTES CCCCCHHHHHHHCCC	28.70	17525332
913	Phosphorylation	SEATQEQYTESEEQL CHHHHHHHCCCHHHH	16.24	30576142
914	Phosphorylation	EATQEQYTESEEQLV HHHHHHHCCCHHHHH	32.50	30576142
916	Phosphorylation	TQEQYTESEEQLVAS HHHHHCCCHHHHHHC	38.34	30576142
932	Acetylation	EQPSQDGKPDLPKRR CCCCCCCCCCCCCCH	43.58	23236377
941	Phosphorylation	DLPKRRLSEGVEPWR CCCCCHHHCCCCCCC	30.41	23401153
954	Phosphorylation	WRGQLKKSPEALKCR CCCCCCCCHHHHHCC	26.78	23401153
973	Phosphorylation	SERLPRRYSEGDRAV CCCCCCCCCHHHHHH	16.62	23312004
974	Phosphorylation	ERLPRRYSEGDRAVL CCCCCCCCHHHHHHH	33.04	25159151
985	Phosphorylation	RAVLRGFSESSEEEE HHHHHCCCCCCCCCC	39.12	27732954
987	Phosphorylation	VLRGFSESSEEEEEP HHHCCCCCCCCCCCC	41.68	27732954
988	Phosphorylation	LRGFSESSEEEEEPE HHCCCCCCCCCCCCC	45.00	20873877
996	Phosphorylation	EEEEEPESPRSSSPP CCCCCCCCCCCCCCC	36.01	20873877
999	Phosphorylation	EEPESPRSSSPPILT CCCCCCCCCCCCCCC	38.25	30266825
1000	Phosphorylation	EPESPRSSSPPILTK CCCCCCCCCCCCCCC	48.41	30266825
1001	Phosphorylation	PESPRSSSPPILTKP CCCCCCCCCCCCCCC	35.62	23401153
1006	Phosphorylation	SSSPPILTKPTLKRK CCCCCCCCCCCCCCC	35.38	30266825
1007	Acetylation	SSPPILTKPTLKRKK CCCCCCCCCCCCCCC	32.34	19608861
1009	Phosphorylation	PPILTKPTLKRKKPF CCCCCCCCCCCCCCC	46.60	23927012
1014	Acetylation	KPTLKRKKPFLHRRR CCCCCCCCCCHHHHH	45.06	23749302
1041	Phosphorylation	VTETISETTEVLDEP CEEECCCHHCCCCCC	22.82	26074081
1042	Phosphorylation	TETISETTEVLDEPF EEECCCHHCCCCCCC	21.75	26074081
1052	Phosphorylation	LDEPFEDSDSERPMP CCCCCCCCCCCCCCC	35.52	29116813
1054	Phosphorylation	EPFEDSDSERPMPRL CCCCCCCCCCCCCCC	39.18	30576142
1064	Phosphorylation	PMPRLEPTFEIDEEE CCCCCCCCEECCHHH	25.23	26074081
1089	Phosphorylation	REYFRRLSSQDVLRC HHHHHHHCHHHHHHC	24.92	23401153
1090	Phosphorylation	EYFRRLSSQDVLRCQ HHHHHHCHHHHHHCC	34.68	30266825
1104	Phosphorylation	QSSSKRKSKDEEEDE CCCCCCCCCCHHHHC	49.74	23927012
1113	Phosphorylation	DEEEDEESDDADDTP CHHHHCCCCCCCCCC	38.45	23927012
1119	Phosphorylation	ESDDADDTPILKPVS CCCCCCCCCCCCHHH	16.87	23403867
1126	Phosphorylation	TPILKPVSLLRKRDV CCCCCHHHHHCCCCC	30.16	23403867
1136	Phosphorylation	RKRDVKNSPLEPDTS CCCCCCCCCCCCCCC	25.74	30266825
1142	Phosphorylation	NSPLEPDTSTPLKKK CCCCCCCCCCCCCCC	45.26	30266825
1143	Phosphorylation	SPLEPDTSTPLKKKK CCCCCCCCCCCCCCC	35.09	30266825
1144	Phosphorylation	PLEPDTSTPLKKKKG CCCCCCCCCCCCCCC	34.43	23401153
1147	Acetylation	PDTSTPLKKKKGWPK CCCCCCCCCCCCCCC	64.84	26051181
1147	Methylation	PDTSTPLKKKKGWPK CCCCCCCCCCCCCCC	64.84	115973607
1148	Acetylation	DTSTPLKKKKGWPKG CCCCCCCCCCCCCCC	68.36	26051181
1148	Methylation	DTSTPLKKKKGWPKG CCCCCCCCCCCCCCC	68.36	115973615
1174	Acetylation	PGRKPGFKLSREIMP CCCCCCCCCCCEECC	52.01	25953088
1174	Methylation	PGRKPGFKLSREIMP CCCCCCCCCCCEECC	52.01	115973623
1330	"N6,N6-dimethyllysine"	HLESTKKKELEEQPT CCHHHCHHHHHCCCC	69.92	-
1330	Methylation	HLESTKKKELEEQPT CCHHHCHHHHHCCCC	69.92	23644510
1342	Sumoylation	QPTREDVKEEPGVQE CCCHHHHHHCCCCCH	69.55	28112733
1350	Phosphorylation	EEPGVQESFLDANMQ HCCCCCHHHHHHHHH	17.64	28555341
1369	Phosphorylation	KIKDKEETELDSEEE HHCCHHHHCCCCCCC	42.83	22210691
1373	Phosphorylation	KEETELDSEEEQPSH HHHHCCCCCCCCCCC	60.58	25849741
1379	Phosphorylation	DSEEEQPSHDTSVVS CCCCCCCCCCHHHHH	33.42	22210691
1382	Phosphorylation	EEQPSHDTSVVSEQM CCCCCCCHHHHHHHH	20.28	24043423
1383	Phosphorylation	EQPSHDTSVVSEQMA CCCCCCHHHHHHHHC	26.95	24043423
1386	Phosphorylation	SHDTSVVSEQMAGSE CCCHHHHHHHHCCCC	21.69	22210691
1392	Phosphorylation	VSEQMAGSEDDHEED HHHHHCCCCCCCCCC	28.45	25849741
1400	Phosphorylation	EDDHEEDSHTKEELI CCCCCCCCCCHHHHH	36.01	24043423
1402	Phosphorylation	DHEEDSHTKEELIEL CCCCCCCCHHHHHHH	44.07	24043423
1436	Phosphorylation	QSLTQEESSEHEGAY HHHCHHHHCCCCCHH	40.03	26074081
1437	Phosphorylation	SLTQEESSEHEGAYQ HHCHHHHCCCCCHHH	46.37	26074081
1732	Phosphorylation	STGNISIYERIPGDF CCCCCEEEECCCCCC	7.74	-
1772	O-linked_Glycosylation	DPHAMPYSHSPAVTS CCCCCCCCCCCCCHH	16.18	29351928
1774	O-linked_Glycosylation	HAMPYSHSPAVTSYA CCCCCCCCCCCHHCC	14.49	29351928
1778	O-linked_Glycosylation	YSHSPAVTSYATSVS CCCCCCCHHCCEEEE	20.37	29351928
1779	O-linked_Glycosylation	SHSPAVTSYATSVSL CCCCCCHHCCEEEEC	13.23	29351928
1856	Phosphorylation	MPVKGHISIRSKSAP CCCCCEEEEEECCCC	13.28	24719451
1859	Phosphorylation	KGHISIRSKSAPLPS CCEEEEEECCCCCCC	29.32	28857561
1861	Phosphorylation	HISIRSKSAPLPSAA EEEEEECCCCCCCHH	36.04	23401153
1866	Phosphorylation	SKSAPLPSAAAHQQQ ECCCCCCCHHHHHHH	37.92	27732954
1875	Phosphorylation	AAHQQQLYGRSPSAV HHHHHHHHCCCHHHH	13.22	23312004
1877	Methylation	HQQQLYGRSPSAVAM HHHHHHCCCHHHHHH	31.66	115484279
1889	Dimethylation	VAMQAGPRALAVQRG HHHHCCHHHHHHHCC	41.12	-
1889	Methylation	VAMQAGPRALAVQRG HHHHCCHHHHHHHCC	41.12	30762639
2003	Methylation	SLNGPYMRR------ HCCCCCCCC------	35.00	115484263
2004	Methylation	LNGPYMRR------- CCCCCCCC-------	34.07	115484271

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
369	T	Phosphorylation	Kinase	AKT1	P31749	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
369	T	Acetylation	23431171
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.
369	T	Phosphorylation	23431171
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.
604	K	Acetylation
Autoacetylation at Lys-604 is required for proper function (By similarity).

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 KAT6A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRPF1_HUMAN	BRPF1	physical	19001415
HSP74_HUMAN	HSPA4	physical	19001415
P53_HUMAN	TP53	physical	19001415
EP300_HUMAN	EP300	physical	19001415
ING5_HUMAN	ING5	physical	18794358
EAF6_HUMAN	MEAF6	physical	18794358
BRPF1_HUMAN	BRPF1	physical	18794358
H31_HUMAN	HIST1H3A	physical	11742995
RUNX1_HUMAN	RUNX1	physical	11742995
CBP_HUMAN	CREBBP	physical	15657427
ESR1_HUMAN	ESR1	physical	17697320
KMT2A_HUMAN	KMT2A	physical	20581860
WDR5_HUMAN	WDR5	physical	20581860
H3C_HUMAN	H3F3C	physical	17925393
H4_HUMAN	HIST1H4I	physical	17925393
H31T_HUMAN	HIST3H3	physical	23063713
H31T_HUMAN	HIST3H3	physical	22713874
PML_HUMAN	PML	physical	23431171
P53_HUMAN	TP53	physical	23431171
SYMPK_HUMAN	SYMPK	physical	23994619
KMT2A_HUMAN	KMT2A	physical	23994619
H31T_HUMAN	HIST3H3	physical	23431171
PHF14_HUMAN	PHF14	physical	26496610
TNR6B_HUMAN	TNRC6B	physical	26496610
PLPL8_HUMAN	PNPLA8	physical	26496610
RSF1_HUMAN	RSF1	physical	26496610
ING5_HUMAN	ING5	physical	26496610
H31_HUMAN	HIST1H3A	physical	27775714

Drug and Disease Associations

Kegg Disease
OMIM Disease
	Note=Chromosomal aberrations involving KAT6A may be a cause of acute myeloid leukemias. Translocation t(8
	16)(p11
	p13) with CREBBP
	translocation t(8
	22)(p11
	q13) with EP300. KAT6A-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription. Inversion inv(8)(p11
	q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation.
616268
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KAT6A_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-350; LYS-355; LYS-604 ANDLYS-1007, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-815, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-418; SER-420 ANDSER-1113, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941, AND MASSSPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND THR-909, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449, AND MASSSPECTROMETRY.	19413330 [Abstract]

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