dbPTM

KAT7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAT7_HUMAN
UniProt AC	O95251
Protein Name	Histone acetyltransferase KAT7
Gene Name	KAT7
Organism	Homo sapiens (Human).
Sequence Length	611
Subcellular Localization	Nucleus, nucleoplasm . Cytoplasm, cytosol . Nucleus . Associates with replication origins specifically during the G1 phase of the cell cycle (PubMed:18832067).
Protein Description	Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Involved in H3K14 (histone H3 lysine 14) acetylation and cell proliferation (By similarity). Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Acts as a coactivator of the licensing factor CDT1. [PubMed: 18832067 Specifically represses AR-mediated transcription.]
Protein Sequence	MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASEDLEKLRLQGQITEGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKTMDPSCLKWTPPKGT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RRKRNAGSSSDGTED CCCCCCCCCCCCCCC	25.02	30278072
11	Phosphorylation	RKRNAGSSSDGTEDS CCCCCCCCCCCCCCC	31.37	30278072
11 (in isoform 4)	Phosphorylation	-	31.37	24719451
12	Phosphorylation	KRNAGSSSDGTEDSD CCCCCCCCCCCCCCC	41.58	23663014
15	Phosphorylation	AGSSSDGTEDSDFST CCCCCCCCCCCCCCC	41.43	23927012
18	Phosphorylation	SSDGTEDSDFSTDLE CCCCCCCCCCCCCCC	34.03	23927012
18 (in isoform 4)	Phosphorylation	-	34.03	24719451
21	Phosphorylation	GTEDSDFSTDLEHTD CCCCCCCCCCCCCCC	26.46	25849741
22	Phosphorylation	TEDSDFSTDLEHTDS CCCCCCCCCCCCCCC	44.59	23663014
27	Phosphorylation	FSTDLEHTDSSESDG CCCCCCCCCCCCCCC	28.35	23927012
29	Phosphorylation	TDLEHTDSSESDGTS CCCCCCCCCCCCCCC	36.84	21406692
30	Phosphorylation	DLEHTDSSESDGTSR CCCCCCCCCCCCCCH	43.88	21406692
32	Phosphorylation	EHTDSSESDGTSRRS CCCCCCCCCCCCHHH	43.20	21406692
35	Phosphorylation	DSSESDGTSRRSARV CCCCCCCCCHHHHEE	24.85	21406692
36	Phosphorylation	SSESDGTSRRSARVT CCCCCCCCHHHHEEE	31.09	21406692
39	Phosphorylation	SDGTSRRSARVTRSS CCCCCHHHHEEEHHH	21.22	23828894
39 (in isoform 3)	Phosphorylation	-	21.22	27251275
39 (in isoform 5)	Phosphorylation	-	21.22	27251275
43 (in isoform 3)	Phosphorylation	-	21.20	27251275
43 (in isoform 5)	Phosphorylation	-	21.20	27251275
45	Phosphorylation	RSARVTRSSARLSQS HHHEEEHHHHHHHCC	20.98	21955146
46	Phosphorylation	SARVTRSSARLSQSS HHEEEHHHHHHHCCC	17.70	25072903
50	Phosphorylation	TRSSARLSQSSQDSS EHHHHHHHCCCCCCC	23.59	29255136
50 (in isoform 3)	Phosphorylation	-	23.59	27251275
50 (in isoform 4)	Phosphorylation	-	23.59	24719451
50 (in isoform 5)	Phosphorylation	-	23.59	27251275
52	Phosphorylation	SSARLSQSSQDSSPV HHHHHHCCCCCCCCC	26.96	29255136
52 (in isoform 3)	Phosphorylation	-	26.96	27251275
52 (in isoform 5)	Phosphorylation	-	26.96	27251275
53	Phosphorylation	SARLSQSSQDSSPVR HHHHHCCCCCCCCCC	30.30	29255136
53 (in isoform 3)	Phosphorylation	-	30.30	27251275
53 (in isoform 4)	Phosphorylation	-	30.30	24719451
53 (in isoform 5)	Phosphorylation	-	30.30	27251275
55	Ubiquitination	RLSQSSQDSSPVRNL HHHCCCCCCCCCCCH	53.70	21890473
56	Phosphorylation	LSQSSQDSSPVRNLQ HHCCCCCCCCCCCHH	28.98	29255136
57	Phosphorylation	SQSSQDSSPVRNLQS HCCCCCCCCCCCHHH	35.39	29255136
57 (in isoform 4)	Phosphorylation	-	35.39	24719451
58 (in isoform 3)	Phosphorylation	-	32.79	27251275
58 (in isoform 5)	Phosphorylation	-	32.79	27251275
64	Phosphorylation	SPVRNLQSFGTEEPA CCCCCHHHCCCCCCC	28.89	25159151
67	Phosphorylation	RNLQSFGTEEPAYST CCHHHCCCCCCCCCC	34.85	23927012
72	Phosphorylation	FGTEEPAYSTRRVTR CCCCCCCCCCCCCCC	22.69	23927012
73	Phosphorylation	GTEEPAYSTRRVTRS CCCCCCCCCCCCCCC	19.97	23927012
74	Phosphorylation	TEEPAYSTRRVTRSQ CCCCCCCCCCCCCCC	15.15	23927012
77 (in isoform 3)	Phosphorylation	-	4.74	25056879
78	Phosphorylation	AYSTRRVTRSQQQPT CCCCCCCCCCCCCCC	23.85	22964224
80	Phosphorylation	STRRVTRSQQQPTPV CCCCCCCCCCCCCCC	23.99	28176443
82	Ubiquitination	RRVTRSQQQPTPVTP CCCCCCCCCCCCCCC	53.09	29967540
85	Phosphorylation	TRSQQQPTPVTPKKY CCCCCCCCCCCCCCC	26.50	25159151
85 (in isoform 4)	Phosphorylation	-	26.50	24719451
88	Phosphorylation	QQQPTPVTPKKYPLR CCCCCCCCCCCCCCC	30.51	19664994
88 (in isoform 4)	Phosphorylation	-	30.51	24719451
90	Acetylation	QPTPVTPKKYPLRQT CCCCCCCCCCCCCCC	56.42	26051181
90	Ubiquitination	QPTPVTPKKYPLRQT CCCCCCCCCCCCCCC	56.42	29967540
92	Phosphorylation	TPVTPKKYPLRQTRS CCCCCCCCCCCCCCC	17.39	24732914
97	Phosphorylation	KKYPLRQTRSSGSET CCCCCCCCCCCCCCC	26.53	21955146
99	Phosphorylation	YPLRQTRSSGSETEQ CCCCCCCCCCCCCEE	42.30	23927012
99 (in isoform 2)	Phosphorylation	-	42.30	29743597
99 (in isoform 4)	Phosphorylation	-	42.30	24719451
100	Phosphorylation	PLRQTRSSGSETEQV CCCCCCCCCCCCEEE	42.94	25159151
100 (in isoform 2)	Phosphorylation	-	42.94	29743597
100 (in isoform 4)	Phosphorylation	-	42.94	24719451
102	Phosphorylation	RQTRSSGSETEQVVD CCCCCCCCCCEEEEE	43.20	29255136
102 (in isoform 2)	Phosphorylation	-	43.20	29743597
102 (in isoform 4)	Phosphorylation	-	43.20	24719451
104	Phosphorylation	TRSSGSETEQVVDFS CCCCCCCCEEEEECC	33.15	23927012
111	Phosphorylation	TEQVVDFSDRETKNT CEEEEECCHHCCCCC	31.15	23401153
111	Ubiquitination	TEQVVDFSDRETKNT CEEEEECCHHCCCCC	31.15	24816145
111 (in isoform 4)	Phosphorylation	-	31.15	24719451
113	Ubiquitination	QVVDFSDRETKNTAD EEEECCHHCCCCCCC	52.89	33845483
115	Phosphorylation	VDFSDRETKNTADHD EECCHHCCCCCCCCC	30.41	21955146
118	Phosphorylation	SDRETKNTADHDESP CHHCCCCCCCCCCCC	34.71	30278072
124	Phosphorylation	NTADHDESPPRTPTG CCCCCCCCCCCCCCC	46.38	29255136
128	Phosphorylation	HDESPPRTPTGNAPS CCCCCCCCCCCCCCC	30.86	23927012
130	Phosphorylation	ESPPRTPTGNAPSSE CCCCCCCCCCCCCCH	42.32	30278072
135	Phosphorylation	TPTGNAPSSESDIDI CCCCCCCCCHHCCCC	44.31	30278072
136	Phosphorylation	PTGNAPSSESDIDIS CCCCCCCCHHCCCCC	39.81	30278072
136 (in isoform 2)	Phosphorylation	-	39.81	25056879
138	Phosphorylation	GNAPSSESDIDISSP CCCCCCHHCCCCCCC	41.64	23927012
141	Ubiquitination	PSSESDIDISSPNVS CCCHHCCCCCCCCCC	39.44	24816145
143	Phosphorylation	SESDIDISSPNVSHD CHHCCCCCCCCCCCC	35.67	23927012
143	Ubiquitination	SESDIDISSPNVSHD CHHCCCCCCCCCCCC	35.67	33845483
144	Phosphorylation	ESDIDISSPNVSHDE HHCCCCCCCCCCCCH	22.34	23927012
148	Phosphorylation	DISSPNVSHDESIAK CCCCCCCCCCHHHHH	31.68	23927012
152	Phosphorylation	PNVSHDESIAKDMSL CCCCCCHHHHHCCCC	33.62	23927012
154	Ubiquitination	VSHDESIAKDMSLKD CCCCHHHHHCCCCCC	15.86	29967540
155	Acetylation	SHDESIAKDMSLKDS CCCHHHHHCCCCCCC	52.90	26822725
158	Phosphorylation	ESIAKDMSLKDSGSD HHHHHCCCCCCCCCC	42.26	23927012
158 (in isoform 4)	Phosphorylation	-	42.26	24719451
160	Acetylation	IAKDMSLKDSGSDLS HHHCCCCCCCCCCCC	42.41	23749302
160	Ubiquitination	IAKDMSLKDSGSDLS HHHCCCCCCCCCCCC	42.41	25015289
162	Phosphorylation	KDMSLKDSGSDLSHR HCCCCCCCCCCCCCC	38.31	23401153
162 (in isoform 4)	Phosphorylation	-	38.31	24719451
164	Phosphorylation	MSLKDSGSDLSHRPK CCCCCCCCCCCCCCH	39.05	30266825
167	Phosphorylation	KDSGSDLSHRPKRRR CCCCCCCCCCCHHHC	23.57	23927012
169	Ubiquitination	SGSDLSHRPKRRRFH CCCCCCCCCHHHCCH	34.75	21890473
169	Ubiquitination	SGSDLSHRPKRRRFH CCCCCCCCCHHHCCH	34.75	21890473
170	Ubiquitination	GSDLSHRPKRRRFHE CCCCCCCCHHHCCHH	29.13	24816145
171	Acetylation	SDLSHRPKRRRFHES CCCCCCCHHHCCHHH	59.50	23749302
171	Ubiquitination	SDLSHRPKRRRFHES CCCCCCCHHHCCHHH	59.50	25015289
172	Ubiquitination	DLSHRPKRRRFHESY CCCCCCHHHCCHHHH	37.38	33845483
178	Phosphorylation	KRRRFHESYNFNMKC HHHCCHHHHCCCCCC	19.46	25159151
179	Phosphorylation	RRRFHESYNFNMKCP HHCCHHHHCCCCCCC	22.31	20068231
184	Sumoylation	ESYNFNMKCPTPGCN HHHCCCCCCCCCCCC	37.86	-
184	Sumoylation	ESYNFNMKCPTPGCN HHHCCCCCCCCCCCC	37.86	-
184	Ubiquitination	ESYNFNMKCPTPGCN HHHCCCCCCCCCCCC	37.86	29967540
187	Phosphorylation	NFNMKCPTPGCNSLG CCCCCCCCCCCCCHH	41.61	25159151
192	Phosphorylation	CPTPGCNSLGHLTGK CCCCCCCCHHHCCCC	39.54	25159151
199	Ubiquitination	SLGHLTGKHERHFSI CHHHCCCCCCCCEEE	36.74	21890473
199	Acetylation	SLGHLTGKHERHFSI CHHHCCCCCCCCEEE	36.74	19608861
199	Ubiquitination	SLGHLTGKHERHFSI CHHHCCCCCCCCEEE	36.74	21890473
200	Ubiquitination	LGHLTGKHERHFSIS HHHCCCCCCCCEEEE	38.37	24816145
202	Ubiquitination	HLTGKHERHFSISGC HCCCCCCCCEEEECC	35.55	33845483
205	Phosphorylation	GKHERHFSISGCPLY CCCCCCEEEECCCCC	15.10	25159151
207	Phosphorylation	HERHFSISGCPLYHN CCCCEEEECCCCCCC	32.90	30576142
207 (in isoform 4)	Phosphorylation	-	32.90	24719451
212	Phosphorylation	SISGCPLYHNLSADE EEECCCCCCCCCHHH	3.62	21712546
213	Ubiquitination	ISGCPLYHNLSADEC EECCCCCCCCCHHHH	36.12	29967540
216	Phosphorylation	CPLYHNLSADECKVR CCCCCCCCHHHHHHH	38.70	25159151
216 (in isoform 4)	Phosphorylation	-	38.70	25056879
221	Acetylation	NLSADECKVRAQSRD CCCHHHHHHHHHHHH	32.48	23749302
221	Ubiquitination	NLSADECKVRAQSRD CCCHHHHHHHHHHHH	32.48	29967540
228	Ubiquitination	KVRAQSRDKQIEERM HHHHHHHHHHHHHHH	53.08	21890473
228	Ubiquitination	KVRAQSRDKQIEERM HHHHHHHHHHHHHHH	53.08	21890473
229	Acetylation	VRAQSRDKQIEERML HHHHHHHHHHHHHHH	52.65	23749302
241	Ubiquitination	RMLSHRQDDNNRHAT HHHHCCCCCCCCCCC	61.64	21890473
243	Ubiquitination	LSHRQDDNNRHATRH HHCCCCCCCCCCCCC	56.58	33845483
250	Ubiquitination	NNRHATRHQAPTERQ CCCCCCCCCCCCHHH	24.65	24816145
252	Ubiquitination	RHATRHQAPTERQLR CCCCCCCCCCHHHHH	13.57	33845483
254	Ubiquitination	ATRHQAPTERQLRYK CCCCCCCCHHHHHHH	46.98	21890473
258	Ubiquitination	QAPTERQLRYKEKVA CCCCHHHHHHHHHHH	8.94	21890473
259	Ubiquitination	APTERQLRYKEKVAE CCCHHHHHHHHHHHH	31.94	23000965
261	Acetylation	TERQLRYKEKVAELR CHHHHHHHHHHHHHH	44.62	11922421
263	Acetylation	RQLRYKEKVAELRKK HHHHHHHHHHHHHHH	42.46	25953088
269	Acetylation	EKVAELRKKRNSGLS HHHHHHHHHHHCCCC	69.57	7677559
270	Acetylation	KVAELRKKRNSGLSK HHHHHHHHHHCCCCH	50.83	7677569
273	Phosphorylation	ELRKKRNSGLSKEQK HHHHHHHCCCCHHHH	45.18	28176443
273	Ubiquitination	ELRKKRNSGLSKEQK HHHHHHHCCCCHHHH	45.18	33845483
277	Acetylation	KRNSGLSKEQKEKYM HHHCCCCHHHHHHHH	70.02	23749302
280	Ubiquitination	SGLSKEQKEKYMEHR CCCCHHHHHHHHHHH	58.21	24816145
282	Ubiquitination	LSKEQKEKYMEHRQT CCHHHHHHHHHHHHH	57.86	33845483
293	Ubiquitination	HRQTYGNTREPLLEN HHHHHCCCCHHHHHH	31.85	29967540
302	Ubiquitination	EPLLENLTSEYDLDL HHHHHHHCCHHCHHH	30.97	33845483
308	Ubiquitination	LTSEYDLDLFRRAQA HCCHHCHHHHHHHHH	40.64	21890473
308	Ubiquitination	LTSEYDLDLFRRAQA HCCHHCHHHHHHHHH	40.64	21890473
323	Acetylation	RASEDLEKLRLQGQI HHCHHHHHHHHCCCC	46.32	23749302
323	Sumoylation	RASEDLEKLRLQGQI HHCHHHHHHHHCCCC	46.32	28112733
323	Ubiquitination	RASEDLEKLRLQGQI HHCHHHHHHHHCCCC	46.32	29967540
331	Phosphorylation	LRLQGQITEGSNMIK HHHCCCCCCCCCCEE	26.80	21406692
332	Ubiquitination	RLQGQITEGSNMIKT HHCCCCCCCCCCEEE	63.35	33845483
334	Phosphorylation	QGQITEGSNMIKTIA CCCCCCCCCCEEEEE	19.59	21406692
336	Sulfoxidation	QITEGSNMIKTIAFG CCCCCCCCEEEEEEE	3.39	21406390
338	Ubiquitination	TEGSNMIKTIAFGRY CCCCCCEEEEEEECE	24.10	21890473
339	Phosphorylation	EGSNMIKTIAFGRYE CCCCCEEEEEEECEE	13.45	24275569
355	Ubiquitination	DTWYHSPYPEEYARL CCCCCCCCHHHHHHH	26.70	21890473
355	Ubiquitination	DTWYHSPYPEEYARL CCCCCCCCHHHHHHH	26.70	21890473
368	Ubiquitination	RLGRLYMCEFCLKYM HHCHHHHHHHHHHHH	1.98	21890473
368	Ubiquitination	RLGRLYMCEFCLKYM HHCHHHHHHHHHHHH	1.98	21890473
373	Ubiquitination	YMCEFCLKYMKSQTI HHHHHHHHHHHHHHH	44.47	23000965
376	"N6,N6-dimethyllysine"	EFCLKYMKSQTILRR HHHHHHHHHHHHHHH	36.00	-
376	Methylation	EFCLKYMKSQTILRR HHHHHHHHHHHHHHH	36.00	23644510
376	Ubiquitination	EFCLKYMKSQTILRR HHHHHHHHHHHHHHH	36.00	-
382	Ubiquitination	MKSQTILRRHMAKCV HHHHHHHHHHHHHHH	23.70	33845483
385	Ubiquitination	QTILRRHMAKCVWKH HHHHHHHHHHHHHCC	3.46	21890473
385	Ubiquitination	QTILRRHMAKCVWKH HHHHHHHHHHHHHCC	3.46	21890473
398	Ubiquitination	KHPPGDEIYRKGSIS CCCCCCHHCCCCCEE	4.85	21890473
398	Ubiquitination	KHPPGDEIYRKGSIS CCCCCCHHCCCCCEE	4.85	21890473
399	Phosphorylation	HPPGDEIYRKGSISV CCCCCHHCCCCCEEE	12.29	-
403	Phosphorylation	DEIYRKGSISVFEVD CHHCCCCCEEEEEEC	18.09	25849741
403	Ubiquitination	DEIYRKGSISVFEVD CHHCCCCCEEEEEEC	18.09	23000965
405	Phosphorylation	IYRKGSISVFEVDGK HCCCCCEEEEEECCC	23.58	30108239
412	Ubiquitination	SVFEVDGKKNKIYCQ EEEEECCCCCEEEHH	49.02	33845483
414	Ubiquitination	FEVDGKKNKIYCQNL EEECCCCCEEEHHHH	39.17	21890473
414	Ubiquitination	FEVDGKKNKIYCQNL EEECCCCCEEEHHHH	39.17	21890473
418	Ubiquitination	GKKNKIYCQNLCLLA CCCCEEEHHHHHHHH	2.17	29967540
427	Ubiquitination	NLCLLAKLFLDHKTL HHHHHHHHHCCCCCE	4.24	21890473
427	Ubiquitination	NLCLLAKLFLDHKTL HHHHHHHHHCCCCCE	4.24	21890473
432	Acetylation	AKLFLDHKTLYYDVE HHHHCCCCCEECCCH	39.63	21466224
432	Ubiquitination	AKLFLDHKTLYYDVE HHHHCCCCCEECCCH	39.63	23000965
444	Ubiquitination	DVEPFLFYVMTEADN CCHHHEEEEEECCCC	7.46	21890473
448	Ubiquitination	FLFYVMTEADNTGCH HEEEEEECCCCCCEE	35.61	29967540
457	Ubiquitination	DNTGCHLIGYFSKEK CCCCEEEEEEEECCC	1.55	21890473
462	Ubiquitination	HLIGYFSKEKNSFLN EEEEEEECCCCCCCC	63.91	23000965
466	Phosphorylation	YFSKEKNSFLNYNVS EEECCCCCCCCCCEE	42.02	-
470	Phosphorylation	EKNSFLNYNVSCILT CCCCCCCCCEEEEEE	21.06	22817900
476 (in isoform 4)	Phosphorylation	-	3.83	24719451
477	Ubiquitination	YNVSCILTMPQYMRQ CCEEEEEECHHHHHC	13.59	29967540
481	Phosphorylation	CILTMPQYMRQGYGK EEEECHHHHHCCCHH	6.60	22817900
486	Phosphorylation	PQYMRQGYGKMLIDF HHHHHCCCHHHHHHH	12.77	22817900
494	Ubiquitination	GKMLIDFSYLLSKVE HHHHHHHHHHHHHHH	15.89	21890473
494	Ubiquitination	GKMLIDFSYLLSKVE HHHHHHHHHHHHHHH	15.89	21890473
506	Phosphorylation	KVEEKVGSPERPLSD HHHHHHCCCCCCHHH	26.95	21712546
507	Ubiquitination	VEEKVGSPERPLSDL HHHHHCCCCCCHHHH	35.37	21890473
507	Ubiquitination	VEEKVGSPERPLSDL HHHHHCCCCCCHHHH	35.37	21890473
512	Phosphorylation	GSPERPLSDLGLISY CCCCCCHHHHCCEEH	33.21	24732914
512	Ubiquitination	GSPERPLSDLGLISY CCCCCCHHHHCCEEH	33.21	23000965
524	Acetylation	ISYRSYWKEVLLRYL EEHHHHHHHHHHHHH	29.70	26051181
524	Ubiquitination	ISYRSYWKEVLLRYL EEHHHHHHHHHHHHH	29.70	21890473
537	Ubiquitination	YLHNFQGKEISIKEI HHHHCCCCEEEHHHH	40.88	23000965
540	Phosphorylation	NFQGKEISIKEISQE HCCCCEEEHHHHCHH	28.79	-
542	Ubiquitination	QGKEISIKEISQETA CCCEEEHHHHCHHCC	42.05	23000965
545	Phosphorylation	EISIKEISQETAVNP EEEHHHHCHHCCCCH	24.05	-
557	Ubiquitination	VNPVDIVSTLQALQM CCHHHHHHHHHHHHH	24.59	29967540
576 (in isoform 4)	Phosphorylation	-	40.30	24719451
587	Ubiquitination	LIDEWIAKEAKRSNS HHHHHHHHHHHHHCC	49.42	29967540
596	Acetylation	AKRSNSNKTMDPSCL HHHHCCCCCCCHHHH	45.08	30584323
601	Phosphorylation	SNKTMDPSCLKWTPP CCCCCCHHHHCCCCC	28.02	23401153
604	Acetylation	TMDPSCLKWTPPKGT CCCHHHHCCCCCCCC	54.04	26051181
606	Phosphorylation	DPSCLKWTPPKGT-- CHHHHCCCCCCCC--	28.29	20873877
609	Ubiquitination	CLKWTPPKGT----- HHCCCCCCCC-----	76.12	-
611	Phosphorylation	KWTPPKGT------- CCCCCCCC-------	41.38	26074081

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
50	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
53	S	Phosphorylation	Kinase	ATR	Q13535	Uniprot
57	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
85	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
88	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
88	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
50	S	Phosphorylation	18669648
Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation.
50	S	Phosphorylation	18669648
Phosphorylation at Ser-50 and Ser-53 by ATR in response to ultraviolet-induced DNA, promotes localization to DNA damage sites.
50	S	ubiquitylation	18669648
Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation.
53	S	Phosphorylation	26572825
Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation.
53	S	Phosphorylation	26572825
Phosphorylation at Ser-50 and Ser-53 by ATR in response to ultraviolet-induced DNA, promotes localization to DNA damage sites.
53	S	ubiquitylation	26572825
Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation.
57	S	Phosphorylation	18669648
Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1.
85	T	Phosphorylation	18669648
Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1.
88	T	Phosphorylation	16964243
Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1.
338	K	ubiquitylation	23319590
Ubiquitinated at Lys-338, leading to proteasomal degradation.
432	K	Acetylation	-
Autoacetylation at Lys-432 is required 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 KAT7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP70_HUMAN	CEP70	physical	16189514
HOOK2_HUMAN	HOOK2	physical	16189514
NINL_HUMAN	NINL	physical	16189514
BACD1_HUMAN	KCTD13	physical	16189514
ZBT8A_HUMAN	ZBTB8A	physical	16189514
ANDR_HUMAN	AR	physical	10930412
ORC1_HUMAN	ORC1	physical	10438470
ING5_HUMAN	ING5	physical	16387653
JADE1_HUMAN	JADE1	physical	16387653
JADE2_HUMAN	JADE2	physical	16387653
JADE3_HUMAN	JADE3	physical	16387653
ING4_HUMAN	ING4	physical	16387653
EAF6_HUMAN	MEAF6	physical	16387653
P53_HUMAN	TP53	physical	17954561
CDT1_HUMAN	CDT1	physical	18832067
JUN_HUMAN	JUN	physical	16880509
GEMI_HUMAN	GMNN	physical	16428461
CDC6_HUMAN	CDC6	physical	16428461
ORC2_HUMAN	ORC2	physical	16428461
MCM2_HUMAN	MCM2	physical	16428461
CD11B_HUMAN	CDK11B	physical	15963510
H31_HUMAN	HIST1H3A	physical	15963510
H2A2C_HUMAN	HIST2H2AC	physical	15963510
CDT1_HUMAN	CDT1	physical	20980834
JADE1_HUMAN	JADE1	physical	22144582
HAP1_HUMAN	HAP1	physical	15383276
LRIF1_HUMAN	LRIF1	physical	15383276
A4_HUMAN	APP	physical	21832049
JADE1_HUMAN	JADE1	physical	24739512
JADE3_HUMAN	JADE3	physical	28514442
BRPF3_HUMAN	BRPF3	physical	28514442
BRD1_HUMAN	BRD1	physical	28514442
ING5_HUMAN	ING5	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 KAT7_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-199, AND MASS SPECTROMETRY.	19608861 [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-57; THR-85; THR-88 ANDSER-102, AND MASS SPECTROMETRY.	19690332 [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 SER-52; SER-53; SER-56;SER-57; THR-85; THR-88 AND SER-102, AND MASS SPECTROMETRY.	19413330 [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 SER-50; SER-53; SER-57;THR-85; THR-88; SER-99; SER-102 AND THR-104, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Role for Plk1 phosphorylation of Hbo1 in regulation of replicationlicensing."; Wu Z.Q., Liu X.; Proc. Natl. Acad. Sci. U.S.A. 105:1919-1924(2008). Cited for: PHOSPHORYLATION AT SER-57 BY PLK1, AND PHOSPHORYLATION AT THR-85 ANDTHR-88 BY CDK1.	18250300 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, AND MASSSPECTROMETRY.	19007248 [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-50; SER-52; SER-53;SER-56 AND SER-57, AND MASS 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-99; SER-100; SER-102;SER-124 AND THR-128, AND MASS SPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, AND MASSSPECTROMETRY.	16964243 [Abstract]

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