KAT5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KAT5_MOUSE
• UniProt AC: Q8CHK4
• Protein Name: Histone acetyltransferase KAT5
• Gene Name: Kat5
• Organism: Mus musculus (Mouse).
• 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.
• 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. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. Acetylates RAN at 'Lys-134'..
• Protein Sequence: MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGSARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW

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
6 (in isoform 3)	Phosphorylation	-	46.07	29514104
52	Acetylation	VHYIDFNKRLDEWVT EEEEECCHHHHHHHH	55.09	22826441
77	Phosphorylation	FPKKEAKTPTKNGLP CCHHHCCCCCCCCCC	43.15	20415495
79	Phosphorylation	KKEAKTPTKNGLPGS HHHCCCCCCCCCCCC	42.23	20415495
86	Phosphorylation	TKNGLPGSRPGSPER CCCCCCCCCCCCCCC	33.10	21082442
86 (in isoform 2)	Phosphorylation	-	33.10	25266776
90	Phosphorylation	LPGSRPGSPEREVPA CCCCCCCCCCCCCCC	26.69	21082442
90 (in isoform 2)	Phosphorylation	-	26.69	25266776
103 (in isoform 2)	Phosphorylation	-	29.95	29514104
104	Acetylation	ASAQASGKTLPIPVQ CCCCCCCCCCCEEEE	44.38	23806337
106 (in isoform 2)	Phosphorylation	-	4.05	29514104
155	Phosphorylation	KRKVEVVSPATPVPS CCCEEEECCCCCCCC	17.62	22942356
158	Phosphorylation	VEVVSPATPVPSETA EEEECCCCCCCCCCC	28.36	29514104
190	Phosphorylation	QPGRKRKSNCLGTDE CCCCCCCCCCCCCCC	36.49	21183079
195	Phosphorylation	RKSNCLGTDEDSQDS CCCCCCCCCCCCCCC	24.22	26643407
199	Phosphorylation	CLGTDEDSQDSSDGI CCCCCCCCCCCCCCC	33.56	21082442
202	Phosphorylation	TDEDSQDSSDGIPSA CCCCCCCCCCCCCCC	23.77	21082442
203	Phosphorylation	DEDSQDSSDGIPSAP CCCCCCCCCCCCCCC	48.42	26643407
208	Phosphorylation	DSSDGIPSAPRMTGS CCCCCCCCCCCCCCC	49.32	30635358
213	Phosphorylation	IPSAPRMTGSLVSDR CCCCCCCCCCCCCCC	25.54	22807455
327	Acetylation	AKCFLDHKTLYYDTD HHHHHCCCCEECCCC	39.63	-
416	Phosphorylation	LGLLSYRSYWSQTIL HCCCCHHHHHHHHHH	23.79	25168779
417	Phosphorylation	GLLSYRSYWSQTILE CCCCHHHHHHHHHHH	10.48	25168779
419	Phosphorylation	LSYRSYWSQTILEIL CCHHHHHHHHHHHHH	14.82	25168779
421	Phosphorylation	YRSYWSQTILEILMG HHHHHHHHHHHHHHC	23.24	25168779

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
90	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Mdm2	P23804	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
86	S	Phosphorylation	Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase (By similarity).	22539723
86	S	Phosphorylation	Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase activity.	22539723
86	S	Phosphorylation	Phosphorylation at Ser-90 is a prerequisite for phosphorylation at Ser-86 by GSK3 (By similarity).	22539723
90	S	Phosphorylation	Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase (By similarity).	22539723
90	S	Phosphorylation	Phosphorylation at Ser-90 is a prerequisite for phosphorylation at Ser-86 by GSK3 (By similarity).	22539723
327	K	Acetylation	Autoacetylation at Lys-327 is required for proper function.	-
430	K	Sumoylation	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	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.

Oops, there are no SNP-PTM records of KAT5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PITX2_MOUSE	Pitx2	physical	12464179
ETV6_MOUSE	Etv6	physical	17980166
PA24A_MOUSE	Pla2g4a	physical	15985650
SIR1_MOUSE	Sirt1	physical	22586264
FOXP3_MOUSE	Foxp3	physical	22579476
ATX1_MOUSE	Atxn1	physical	17110330
STK38_MOUSE	Stk38	physical	24302573
RUVB1_MOUSE	Ruvbl1	physical	24302573
RUVB2_MOUSE	Ruvbl2	physical	24302573
ACTS_MOUSE	Acta1	physical	24302573
SUN2_MOUSE	Sun2	physical	24302573
HDAC6_MOUSE	Hdac6	physical	24302573
KAT5_MOUSE	Kat5	physical	24302573
ACTB_MOUSE	Actb	physical	24302573
EPC1_MOUSE	Epc1	physical	24302573
BRD8_MOUSE	Brd8	physical	24302573
YETS4_MOUSE	Yeats4	physical	24302573
EPC2_MOUSE	Epc2	physical	24302573
H2B2B_MOUSE	Hist2h2bb	physical	24302573
ING3_MOUSE	Ing3	physical	24302573
EP400_MOUSE	Ep400	physical	24302573
DMAP1_MOUSE	Dmap1	physical	24302573
HSP7C_MOUSE	Hspa8	physical	24302573
LIMA1_MOUSE	Lima1	physical	24302573
VPS72_MOUSE	Vps72	physical	24302573
ACL6A_MOUSE	Actl6a	physical	24302573
ACTG_MOUSE	Actg1	physical	24302573
H2AV_MOUSE	H2afv	physical	24302573
EAF6_MOUSE	Meaf6	physical	24302573
MBTD1_MOUSE	Mbtd1	physical	24302573
RS18_MOUSE	Rps18	physical	24302573
TBB5_MOUSE	Tubb5	physical	24302573
TBA1A_MOUSE	Tuba1a	physical	24302573
TIF1B_MOUSE	Trim28	physical	24302573
MO4L2_MOUSE	Morf4l2	physical	24302573
MRGBP_MOUSE	Mrgbp	physical	24302573
RAGP1_MOUSE	Rangap1	physical	24302573
SETX_MOUSE	Setx	physical	24302573
SFPQ_MOUSE	Sfpq	physical	24302573
RAB5C_MOUSE	Rab5c	physical	24302573
LRRF2_MOUSE	Lrrfip2	physical	24302573
NONO_MOUSE	Nono	physical	24302573
TPR_MOUSE	Tpr	physical	24302573
HNRPF_MOUSE	Hnrnpf	physical	24302573
SPTB2_MOUSE	Sptbn1	physical	24302573
FLNA_MOUSE	Flna	physical	24302573
FLII_MOUSE	Flii	physical	24302573
HDX_MOUSE	Hdx	physical	24302573
MO4L1_MOUSE	Morf4l1	physical	24302573
TBRG1_MOUSE	Tbrg1	physical	24621507

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.