dbPTM

KAT5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAT5_HUMAN
UniProt AC	Q92993
Protein Name	Histone acetyltransferase KAT5
Gene Name	KAT5
Organism	Homo sapiens (Human).
Sequence Length	513
Subcellular Localization	Nucleus . Nucleus, nucleolus. Cytoplasm, perinuclear region. Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies.
Protein Description	Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. [PubMed: 17360565 Acetylates RAN at 'Lys-134']
Protein Sequence	MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6 (in isoform 4)	Phosphorylation	-	46.07	25159151
6 (in isoform 3)	Phosphorylation	-	46.07	25159151
33	Phosphorylation	WPLAEILSVKDISGR CCHHHEEEEEECCCC	32.55	24719451
35	Ubiquitination	LAEILSVKDISGRKL HHHEEEEEECCCCEE	46.07	2190698
35 (in isoform 1)	Ubiquitination	-	46.07	21906983
35 (in isoform 3)	Phosphorylation	-	46.07	21815630
35 (in isoform 4)	Phosphorylation	-	46.07	21815630
44	Phosphorylation	ISGRKLFYVHYIDFN CCCCEEEEEEEEECC	9.21	-
52	Acetylation	VHYIDFNKRLDEWVT EEEEECCHHHHHHHH	55.09	19608861
68 (in isoform 3)	Ubiquitination	-	4.95	21906983
68 (in isoform 2)	Ubiquitination	-	4.95	21906983
76	Acetylation	QFPKKEAKTPTKNGL CCCHHHCCCCCCCCC	57.01	22470428
77	Phosphorylation	FPKKEAKTPTKNGLP CCHHHCCCCCCCCCC	43.15	26074081
79	Phosphorylation	KKEAKTPTKNGLPGS HHHCCCCCCCCCCCC	42.23	26074081
80	Acetylation	KEAKTPTKNGLPGSR HHCCCCCCCCCCCCC	50.66	22470428
85	Acetylation	PTKNGLPGSRPGSPE CCCCCCCCCCCCCCC	41.13	19608861
86 (in isoform 2)	Phosphorylation	-	33.10	25159151
86	Phosphorylation	TKNGLPGSRPGSPER CCCCCCCCCCCCCCC	33.10	23401153
90	Phosphorylation	LPGSRPGSPEREVPA CCCCCCCCCCCCCCC	26.69	23401153
90 (in isoform 2)	Phosphorylation	-	26.69	28731282
98	Phosphorylation	PEREVPASAQASGKT CCCCCCCCCCCCCCC	18.16	30624053
102	Phosphorylation	VPASAQASGKTLPIP CCCCCCCCCCCCCEE	28.83	23312004
103 (in isoform 2)	Phosphorylation	-	29.95	25849741
104	Acetylation	ASAQASGKTLPIPVQ CCCCCCCCCCCEEEE	44.38	26051181
106 (in isoform 2)	Phosphorylation	-	4.05	25159151
119 (in isoform 4)	Phosphorylation	-	37.25	25159151
120	Acetylation	TLRFNLPKEREAIPG EEEECCCCCCCCCCC	72.99	104995799
123 (in isoform 4)	Phosphorylation	-	52.63	28731282
136 (in isoform 4)	Phosphorylation	-	33.67	25849741
139 (in isoform 4)	Phosphorylation	-	4.40	25159151
148	Acetylation	QPNHRSTKRKVEVVS CCCCCCCCCCEEEEC	52.01	104995815
150	Acetylation	NHRSTKRKVEVVSPA CCCCCCCCEEEECCC	44.28	22470428
155	Phosphorylation	KRKVEVVSPATPVPS CCCEEEECCCCCCCC	17.62	30266825
158	Phosphorylation	VEVVSPATPVPSETA EEEECCCCCCCCCCC	28.36	30266825
162	Phosphorylation	SPATPVPSETAPASV CCCCCCCCCCCCCCC	48.06	19690332
164	Phosphorylation	ATPVPSETAPASVFP CCCCCCCCCCCCCCC	42.13	25850435
168	Phosphorylation	PSETAPASVFPQNGA CCCCCCCCCCCCCCH	24.19	27251275
187	Acetylation	VAAQPGRKRKSNCLG HHCCCCCCCCCCCCC	70.82	22470428
189	Acetylation	AQPGRKRKSNCLGTD CCCCCCCCCCCCCCC	49.40	20100829
190	Phosphorylation	QPGRKRKSNCLGTDE CCCCCCCCCCCCCCC	36.49	30266825
195	Phosphorylation	RKSNCLGTDEDSQDS CCCCCCCCCCCCCCC	24.22	30266825
199	Phosphorylation	CLGTDEDSQDSSDGI CCCCCCCCCCCCCCC	33.56	23401153
202	Phosphorylation	TDEDSQDSSDGIPSA CCCCCCCCCCCCCCC	23.77	30266825
203	Phosphorylation	DEDSQDSSDGIPSAP CCCCCCCCCCCCCCC	48.42	30266825
208	Phosphorylation	DSSDGIPSAPRMTGS CCCCCCCCCCCCCCC	49.32	30266825
227	Phosphorylation	RSHDDIVTRMKNIEC CCHHHHHHHHHCEEE	25.94	-
230	Acetylation	DDIVTRMKNIECIEL HHHHHHHHCEEEEEC	52.03	-
230	Ubiquitination	DDIVTRMKNIECIEL HHHHHHHHCEEEEEC	52.03	-
249	Acetylation	LKPWYFSPYPQELTT CCCCCCCCCCHHHCH	34.62	16001085
263	Acetylation	TLPVLYLCEFCLKYG HHHHHHHHHHHHHHC	2.08	16001085
263 (in isoform 3)	Ubiquitination	-	2.08	-
268	Acetylation	YLCEFCLKYGRSLKC HHHHHHHHHCCHHHH	47.00	16001085
274	Ubiquitination	LKYGRSLKCLQRHLT HHHCCHHHHHHHHHH	33.86	-
281	Phosphorylation	KCLQRHLTKCDLRHP HHHHHHHHHCCCCCC	24.41	-
282	Ubiquitination	CLQRHLTKCDLRHPP HHHHHHHHCCCCCCC	31.92	16001085
282	Acetylation	CLQRHLTKCDLRHPP HHHHHHHHCCCCCCC	31.92	16001085
294	Phosphorylation	HPPGNEIYRKGTISF CCCCCCEEECCEEEE	10.49	-
296	Ubiquitination	PGNEIYRKGTISFFE CCCCEEECCEEEEEE	43.35	-
301	Acetylation	YRKGTISFFEIDGRK EECCEEEEEEECCCC	5.87	16001085
307 (in isoform 3)	Ubiquitination	-	35.31	-
310	Ubiquitination	EIDGRKNKSYSQNLC EECCCCCCCHHHHHH	54.53	-
315	Acetylation	KNKSYSQNLCLLAKC CCCCHHHHHHHHHHH	27.12	16001085
315 (in isoform 3)	Ubiquitination	-	27.12	-
327	Acetylation	AKCFLDHKTLYYDTD HHHHHCCCCEECCCC	39.63	22470428
343 (in isoform 3)	Ubiquitination	-	22.68	-
383	Acetylation	YQRRGYGKLLIEFSY CCCCCCHHEEEEEEE	31.47	22470428
404	Ubiquitination	GKTGTPEKPLSDLGL CCCCCCCCCHHHHCC	53.08	-
404	Acetylation	GKTGTPEKPLSDLGL CCCCCCCCCHHHHCC	53.08	26051181
430	Sumoylation	LEILMGLKSESGERP HHHHHCCCCCCCCCC	46.58	-
430	Sumoylation	LEILMGLKSESGERP HHHHHCCCCCCCCCC	46.58	17704809
431	Phosphorylation	EILMGLKSESGERPQ HHHHCCCCCCCCCCE	41.88	-
437 (in isoform 3)	Ubiquitination	-	26.14	-
451	Ubiquitination	ISEITSIKKEDVIST HHHHCCCCHHHHHHH	50.29	-
451	Sumoylation	ISEITSIKKEDVIST HHHHCCCCHHHHHHH	50.29	17704809
451	Sumoylation	ISEITSIKKEDVIST HHHHCCCCHHHHHHH	50.29	-
472	Phosphorylation	INYYKGQYILTLSED HHHHCCCEEEEEEHH	13.43	18083107
498	Ubiquitination	RLLRIDSKCLHFTPK HHHHHCCCCCCCCCC	36.75	-
505	Ubiquitination	KCLHFTPKDWSKRGK CCCCCCCCHHHHCCC	69.63	-
531 (in isoform 3)	Ubiquitination	-		-
538 (in isoform 3)	Ubiquitination	-		-

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
44	Y	Phosphorylation	Kinase	ABL	P00519	PSP
86	S	Phosphorylation	Kinase	CDK1	P06493	PSP
86	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
86	S	Phosphorylation	Kinase	GSK3	-	Uniprot
90	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
90	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
106	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
158	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
294	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:11927554

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
86	S	Phosphorylation	12468530
Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase.
86	S	Phosphorylation	12468530
Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase activity.
86	S	Phosphorylation	12468530
Phosphorylation at Ser-90 is a prerequisite for phosphorylation at Ser-86 by GSK3.
90	S	Phosphorylation	12468530
Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase.
90	S	Phosphorylation	12468530
Phosphorylation at Ser-90 is a prerequisite for phosphorylation at Ser-86 by GSK3.
327	K	Acetylation
Autoacetylation at Lys-327 is required for proper function.
430	K	Sumoylation	17704809
Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.
451	K	Sumoylation	17704809
Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.

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 KAT5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ETV6_HUMAN	ETV6	physical	12737628
LRP1_HUMAN	LRP1	physical	12888553
MYC_HUMAN	MYC	physical	12776177
HDAC7_HUMAN	HDAC7	physical	12551922
CREB1_HUMAN	CREB1	physical	10720489
MDM2_HUMAN	MDM2	physical	11927554
ANDR_HUMAN	AR	physical	11994312
PA24A_HUMAN	PLA2G4A	physical	11416127
TRI68_HUMAN	TRIM68	physical	18451177
FACD2_HUMAN	FANCD2	physical	18263878
ZN363_HUMAN	RCHY1	physical	18263878
TRRAP_HUMAN	TRRAP	physical	16387653
ING3_HUMAN	ING3	physical	16387653
FOXP3_HUMAN	FOXP3	physical	17360565
ESR1_HUMAN	ESR1	physical	17418098
KAT5_HUMAN	KAT5	physical	20100829
SIR1_HUMAN	SIRT1	physical	20100829
MDM2_HUMAN	MDM2	physical	19150978
SIR1_HUMAN	SIRT1	physical	19895790
PRKDC_HUMAN	PRKDC	physical	16603769
P53_HUMAN	TP53	physical	16601686
TBX5_HUMAN	TBX5	physical	15591049
SRF_HUMAN	SRF	physical	15591049
MRGBP_HUMAN	MRGBP	physical	18218781
E2F1_HUMAN	E2F1	physical	15121871
ANDR_HUMAN	AR	physical	10364196
NR1D2_HUMAN	NR1D2	physical	17996965
NMI_HUMAN	NMI	physical	17406968
KLF4_HUMAN	KLF4	physical	17827213
H31_HUMAN	HIST1H3A	physical	20351180
TRRAP_HUMAN	TRRAP	physical	20070254
RAD50_HUMAN	RAD50	physical	20070254
NBN_HUMAN	NBN	physical	20070254
MRE11_HUMAN	MRE11A	physical	20070254
EP400_HUMAN	EP400	physical	20070254
TRRAP_HUMAN	TRRAP	physical	20946988
EP400_HUMAN	EP400	physical	20946988
DMAP1_HUMAN	DMAP1	physical	20946988
BRD8_HUMAN	BRD8	physical	20946988
EPC2_HUMAN	EPC2	physical	20946988
VPS72_HUMAN	VPS72	physical	20946988
EPC1_HUMAN	EPC1	physical	20946988
ING3_HUMAN	ING3	physical	20946988
ACTH_HUMAN	ACTG2	physical	20946988
ACTB_HUMAN	ACTB	physical	20946988
ACTG_HUMAN	ACTG1	physical	20946988
LDHA_HUMAN	LDHA	physical	20946988
HDGF_HUMAN	HDGF	physical	20946988
MYC_HUMAN	MYC	physical	20946988
MAX_HUMAN	MAX	physical	20946988
KAT5_HUMAN	KAT5	physical	20946988
SRSF2_HUMAN	SRSF2	physical	21157427
TRRAP_HUMAN	TRRAP	physical	14966270
DMAP1_HUMAN	DMAP1	physical	14966270
EPC1_HUMAN	EPC1	physical	14966270
RUVB1_HUMAN	RUVBL1	physical	14966270
ACL6A_HUMAN	ACTL6A	physical	14966270
MO4L1_HUMAN	MORF4L1	physical	14966270
YETS4_HUMAN	YEATS4	physical	14966270
KAT5_HUMAN	KAT5	physical	14966270
RUVB2_HUMAN	RUVBL2	physical	14966270
BRD8_HUMAN	BRD8	physical	14966270
SRCAP_HUMAN	SRCAP	physical	14966270
ACTS_HUMAN	ACTA1	physical	14966270
ING3_HUMAN	ING3	physical	14966270
EAF6_HUMAN	MEAF6	physical	14966270
DNMT1_HUMAN	DNMT1	physical	21045206
UBP7_HUMAN	USP7	physical	21045206
HDAC1_HUMAN	HDAC1	physical	21045206
PCNA_HUMAN	PCNA	physical	21045206
UHRF1_HUMAN	UHRF1	physical	21045206
TRRAP_HUMAN	TRRAP	physical	10966108
H2AJ_CHICK	HIST1H2A9	physical	10966108
H2B1_CHICK	HIST1H2B7	physical	10966108
H33_CHICK	H3F3C	physical	10966108
H4_CHICK	HIST1H47	physical	10966108
ACTB_HUMAN	ACTB	physical	10966108
ACL6A_HUMAN	ACTL6A	physical	10966108
MDM2_HUMAN	MDM2	physical	18264029
MYB_HUMAN	MYB	physical	22110127
EP300_HUMAN	EP300	physical	16001085
TRI29_HUMAN	TRIM29	physical	21463657
RIR1_HUMAN	RRM1	physical	20159953
RIR2_HUMAN	RRM2	physical	20159953
H31T_HUMAN	HIST3H3	physical	19783983
PDCD5_HUMAN	PDCD5	physical	19308289
UL27_HCMVM	UL27	physical	21320693
MYOD1_HUMAN	MYOD1	physical	21936881
RUVB1_HUMAN	RUVBL1	physical	15829968
BCL3_HUMAN	BCL3	physical	15829968
P73_HUMAN	TP73	physical	18499675
MDM2_HUMAN	MDM2	physical	18499675
CEBPA_HUMAN	CEBPA	physical	18239623
KPCE_HUMAN	PRKCE	physical	17851107
MTUS2_HUMAN	MTUS2	physical	17704809
SENP6_HUMAN	SENP6	physical	17704809
KAT5_HUMAN	KAT5	physical	17704809
SUMO1_HUMAN	SUMO1	physical	17704809
P53_HUMAN	TP53	physical	17704809
UBC9_HUMAN	UBE2I	physical	17704809
EP400_HUMAN	EP400	physical	17704809
RUVB2_HUMAN	RUVBL2	physical	17704809
NOTC1_HUMAN	NOTCH1	physical	17636029
SUH_HUMAN	RBPJ	physical	17636029
PLAL2_HUMAN	PLAGL2	physical	17551969
APBB1_HUMAN	APBB1	physical	17368826
P53_HUMAN	TP53	physical	17189186
KAT5_HUMAN	KAT5	physical	17189186
HINT1_HUMAN	HINT1	physical	16835243
RB_HUMAN	RB1	physical	16501607
ATM_HUMAN	ATM	physical	16141325
APBB1_HUMAN	APBB1	physical	16223726
A4_HUMAN	APP	physical	16223726
1433G_HUMAN	YWHAG	physical	16223726
APBB1_HUMAN	APBB1	physical	15331662
A4_HUMAN	APP	physical	15331662
A4_HUMAN	APP	physical	15044485
APBB1_HUMAN	APBB1	physical	15044485
UBF1_HUMAN	UBTF	physical	15016909
ZN363_HUMAN	RCHY1	physical	14701804
A4_HUMAN	APP	physical	14699153
APLP1_HUMAN	APLP1	physical	14699153
APLP2_HUMAN	APLP2	physical	14699153
APBB1_HUMAN	APBB1	physical	14699153
ANDR_HUMAN	AR	physical	11591700
ESR1_HUMAN	ESR1	physical	11591700
ESR2_HUMAN	ESR2	physical	11591700
GCR_HUMAN	NR3C1	physical	11591700
ACK1_HUMAN	TNK2	physical	22586264
SIR1_HUMAN	SIRT1	physical	22586264
ANGL4_HUMAN	ANGPTL4	physical	22573825
ORF73_HHV8P	HHV8GK18_gp81	physical	22379092
TF65_HUMAN	RELA	physical	22249179
TDIF2_HUMAN	DNTTIP2	physical	21668587
UBF1_HUMAN	UBTF	physical	21668587
H32_HUMAN	HIST2H3C	physical	21668587
GA45G_HUMAN	GADD45G	physical	15383276
LRIF1_HUMAN	LRIF1	physical	15383276
HAP1_HUMAN	HAP1	physical	15383276
M3K1_HUMAN	MAP3K1	physical	16469706
A4_HUMAN	APP	physical	21832049
RL30_HUMAN	RPL30	physical	22939629
VHL_HUMAN	VHL	physical	22071692
UBP7_HUMAN	USP7	physical	23775119
ZBT8A_HUMAN	ZBTB8A	physical	21988832
ZBT7B_HUMAN	ZBTB7B	physical	23609452
IKZF3_HUMAN	IKZF3	physical	25416956
NINL_HUMAN	NINL	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
ZN513_HUMAN	ZNF513	physical	25416956
PIHD3_HUMAN	PIH1D3	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
ZBT8A_HUMAN	ZBTB8A	physical	25416956
FOXP3_HUMAN	FOXP3	physical	19996091
BRCA1_HUMAN	BRCA1	physical	25184681
P53_HUMAN	TP53	physical	23677994
UHRF1_HUMAN	UHRF1	physical	23677994
KAT5_HUMAN	KAT5	physical	21157427
EP400_HUMAN	EP400	physical	26186194
EAF6_HUMAN	MEAF6	physical	26186194
EPC1_HUMAN	EPC1	physical	26186194
EPC2_HUMAN	EPC2	physical	26186194
DMAP1_HUMAN	DMAP1	physical	26186194
VPS72_HUMAN	VPS72	physical	26186194
TRRAP_HUMAN	TRRAP	physical	26186194
ING3_HUMAN	ING3	physical	26186194
RIR1_HUMAN	RRM1	physical	26186194
UCKL1_HUMAN	UCKL1	physical	26186194
MRGBP_HUMAN	MRGBP	physical	26186194
BRD8_HUMAN	BRD8	physical	26186194
MBTD1_HUMAN	MBTD1	physical	26186194
LRC42_HUMAN	LRRC42	physical	26186194
YETS4_HUMAN	YEATS4	physical	26186194
KAT5_HUMAN	KAT5	physical	25301942
HDAC3_HUMAN	HDAC3	physical	25301942
TBRG1_MOUSE	Tbrg1	physical	24621507
ATF3_HUMAN	ATF3	physical	25865756
TRRAP_HUMAN	TRRAP	physical	27153538
EP400_HUMAN	EP400	physical	27153538
BRD8_HUMAN	BRD8	physical	27153538
EPC1_HUMAN	EPC1	physical	27153538
EPC2_HUMAN	EPC2	physical	27153538
MBTD1_HUMAN	MBTD1	physical	27153538
DMAP1_HUMAN	DMAP1	physical	27153538
ING3_HUMAN	ING3	physical	27153538
RUVB1_HUMAN	RUVBL1	physical	27153538
RUVB2_HUMAN	RUVBL2	physical	27153538
VPS72_HUMAN	VPS72	physical	27153538
ACL6A_HUMAN	ACTL6A	physical	27153538
ACTB_HUMAN	ACTB	physical	27153538
YETS4_HUMAN	YEATS4	physical	27153538
EAF6_HUMAN	MEAF6	physical	27153538
MO4L1_HUMAN	MORF4L1	physical	27153538
MO4L2_HUMAN	MORF4L2	physical	27153538
H2B1B_HUMAN	HIST1H2BB	physical	27153538
H2AZ_HUMAN	H2AFZ	physical	27153538
UHRF2_HUMAN	UHRF2	physical	27743347
YETS4_HUMAN	YEATS4	physical	28514442
EPC2_HUMAN	EPC2	physical	28514442
EPC1_HUMAN	EPC1	physical	28514442
EP400_HUMAN	EP400	physical	28514442
MBTD1_HUMAN	MBTD1	physical	28514442
ING3_HUMAN	ING3	physical	28514442
VPS72_HUMAN	VPS72	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
BRD8_HUMAN	BRD8	physical	28514442
LRC42_HUMAN	LRRC42	physical	28514442
UCKL1_HUMAN	UCKL1	physical	28514442
DMAP1_HUMAN	DMAP1	physical	28514442
RIR1_HUMAN	RRM1	physical	28514442

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 KAT5_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-52, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-86 AND SER-90, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Tip60 acetyltransferase activity is controlled by phosphorylation."; Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D.,Khochbin S.; J. Biol. Chem. 278:4713-4718(2003). Cited for: PHOSPHORYLATION AT SER-86 AND SER-90, AND MUTAGENESIS OF SER-86;SER-90; LEU-254; LEU-257 AND GLY-380.	12468530 [Abstract]
Sumoylation
Reference	PubMed
"Functional characterization of TIP60 sumoylation in UV-irradiated DNAdamage response."; Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z.,Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M.,Liang S., Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.; Oncogene 27:931-941(2008). Cited for: SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 ANDLYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,AND IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.	17704809 [Abstract]

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