KAT2B
entrez
8850
canonical
uniprot
Q92831
canonical
ensembl
ENSG00000114166
resolver
ensp
ENSP00000263754
resolver
ensp
ENSP00000792159
resolver
enst
ENST00000263754
resolver
genesymbol
KAT2B
resolver
genesymbol_syn
PCAF
resolver
hgnc
HGNC:8638
resolver
uniprot
Q6NSK1
resolver
uniprot_entry
KAT2B_HUMAN
resolver
uniprot_sec
Q6NSK1
resolver
activity_regulation
ACTIVITY REGULATION: Activated in vitro by very low concentrations of spermidine, but inhibited at spermidine concentrations higher than 4 uM. The activating effect of low spermidine concentrations may be mediated by N(8)-acetylspermidine produced by KAT2B/P/CAF itself acting as a positive feedback loop. {ECO:0000269|PubMed:27389534}.
uniprot
proteins
amino_acid_sequence
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in KAT2B has been found in a patient with isolated coloboma, a defect of the eye characterized by the absence of ocular structures due to abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). Isolated colobomas may be associated with an abnormally small eye (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}.
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
ec_number
2.3.1.57
uniprot
proteins
function
FUNCTION: Functions as a histone acetyltransferase (HAT) to promote transcriptional activation (PubMed:8945521). Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles (PubMed:8945521). Has a a strong preference for acetylation of H3 at 'Lys-9' (H3K9ac) (PubMed:21131905). Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, RRP9/U3-55K and TBX5 (PubMed:10675335, PubMed:23001180, PubMed:23932781, PubMed:26867678, PubMed:27796307, PubMed:29174768, PubMed:9707565). Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A (PubMed:8684459). Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (PubMed:14645221). Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 (PubMed:29174768). Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 (PubMed:27796307). Acetylates RRP9/U3-55K, a core subunit of the U3 snoRNP complex, impairing pre-rRNA processing (PubMed:26867678). Acetylates MAPRE1/EB1, promoting dynamic kinetochore-microtubule interactions in early mitosis (PubMed:23001180). Also acetylates spermidine (PubMed:27389534). {ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:27389534, ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:8945521, ECO:0000269|PubMed:9707565}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. {ECO:0000269|PubMed:12486002}.
uniprot
proteins
mass_dalton
93013
uniprot
proteins
mutagenesis
MUTAGEN 752; /note="V->A: Reduced acetyl-lysine binding."; /evidence="ECO:0000269|PubMed:10365964"; MUTAGEN 760; /note="Y->A: Reduced acetyl-lysine binding."; /evidence="ECO:0000269|PubMed:10365964"; MUTAGEN 802; /note="Y->A: Reduced acetyl-lysine binding."; /evidence="ECO:0000269|PubMed:10365964"; MUTAGEN 809; /note="Y->A: Complete loss of acetyl-lysine binding."; /evidence="ECO:0000269|PubMed:10365964
uniprot
proteins
protein_family
Acetyltransferase family
uniprot
proteins
protein_family
GCN5 subfamily
uniprot
proteins
pubmed
10365964
uniprot
proteins
pubmed
10393169
uniprot
proteins
pubmed
10675335
uniprot
proteins
pubmed
10766811
uniprot
proteins
pubmed
11568182
uniprot
proteins
pubmed
11931765
uniprot
proteins
pubmed
12486002
uniprot
proteins
pubmed
14645221
uniprot
proteins
pubmed
14767476
uniprot
proteins
pubmed
15273251
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16887930
uniprot
proteins
pubmed
17226766
uniprot
proteins
pubmed
17301242
uniprot
proteins
pubmed
17505058
uniprot
proteins
pubmed
17707232
uniprot
proteins
pubmed
20940255
uniprot
proteins
pubmed
21131905
uniprot
proteins
pubmed
22464331
uniprot
proteins
pubmed
23001180
uniprot
proteins
pubmed
23932781
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
26867678
uniprot
proteins
pubmed
27389534
uniprot
proteins
pubmed
27796307
uniprot
proteins
pubmed
28493397
uniprot
proteins
pubmed
29174768
uniprot
proteins
pubmed
37179361
uniprot
proteins
pubmed
8684459
uniprot
proteins
pubmed
8945521
uniprot
proteins
pubmed
9296499
uniprot
proteins
pubmed
9346901
uniprot
proteins
pubmed
9707565
uniprot
proteins
sequence_length
832
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:29174768}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29174768}. Cytoplasm {ECO:0000269|PubMed:20940255}. Note=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. Subcellular location may vary depending upon cell differentiation state. Cytoplasmic at the very stages of keratinocyte differentiation, becomes nuclear at later differentiation stages. Cytoplasmic in basal epithelial cells (undifferentiated cells) and nuclear in parabasal cells (differentiated cells) (PubMed:20940255). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000269|PubMed:20940255, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:29174768}.
uniprot
proteins