dbPTM

KAT2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAT2B_MOUSE
UniProt AC	Q9JHD1
Protein Name	Histone acetyltransferase KAT2B
Gene Name	Kat2b {ECO:0000312\|MGI:MGI:1343094}
Organism	Mus musculus (Mouse).
Sequence Length	813
Subcellular Localization	Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Mainly localizes to the nucleus. Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation.
Protein Description	Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY, PLK4 and TBX5. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5. Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4..
Protein Sequence	MAEAGGAGSPALPPAPPHGSPRTLATAAGSSASCGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRGDLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMDRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKERQTTIELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTIMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSPLGIQTVISPPVTGTALFSSNSTSHEQINGGRTSPGCRGSSGLEANPGEKRKMNNSHAPEEAKRSRVMGDIPVELINEVMSTITDPAGMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPQIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPKDPEQLYSTLKNILQQVKNHPNAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLRNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASILEKFFFSKIKEAGLIDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	AEAGGAGSPALPPAP CCCCCCCCCCCCCCC	13.38	26643407
20	Phosphorylation	PPAPPHGSPRTLATA CCCCCCCCCCCCHHH	14.26	30352176
99	Phosphorylation	GWKNPNPSPTPPRGD CCCCCCCCCCCCCCC	48.31	26643407
101	Phosphorylation	KNPNPSPTPPRGDLQ CCCCCCCCCCCCCHH	50.71	26643407
113	Phosphorylation	DLQQIIVSLTESCRS CHHHHHHHHHHHHHH	21.11	23984901
710	Phosphorylation	PKDPEQLYSTLKNIL CCCHHHHHHHHHHHH	10.17	-
711	Phosphorylation	KDPEQLYSTLKNILQ CCHHHHHHHHHHHHH	35.54	18266315
712	Phosphorylation	DPEQLYSTLKNILQQ CHHHHHHHHHHHHHH	28.35	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	Mdm2	P23804	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KAT2B_MOUSE !!

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 KAT2B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOTC1_MOUSE	Notch1	physical	10747963
NOTCH_DROME	N	physical	10747963
EP300_MOUSE	Ep300	physical	20211142
SMAD1_MOUSE	Smad1	physical	14500836
KAT2B_MOUSE	Kat2b	physical	14500836
MYOD1_MOUSE	Myod1	physical	9659901
HNF1B_MOUSE	Hnf1b	physical	15647252
RPA1_MOUSE	Polr1a	physical	23667505

Drug and Disease Associations

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

Regulatory Network of KAT2B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	17242355 [Abstract]