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Histone acetyltransferase KAT2B (EC 2.3.1.48) (Histone acetyltransferase PCAF) (Histone acetylase PCAF) (Lysine acetyltransferase 2B) (P300/CBP-associated factor) (P/CAF)

 KAT2B_HUMAN             Reviewed;         832 AA.
Q92831; Q6NSK1;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 3.
12-SEP-2018, entry version 200.
RecName: Full=Histone acetyltransferase KAT2B;
EC=2.3.1.48 {ECO:0000269|PubMed:8945521};
AltName: Full=Histone acetyltransferase PCAF {ECO:0000303|PubMed:12486002};
Short=Histone acetylase PCAF {ECO:0000303|PubMed:12486002};
AltName: Full=Lysine acetyltransferase 2B {ECO:0000303|PubMed:27796307};
AltName: Full=P300/CBP-associated factor {ECO:0000303|PubMed:12486002};
Short=P/CAF {ECO:0000303|PubMed:12486002};
Name=KAT2B {ECO:0000303|PubMed:27796307, ECO:0000312|HGNC:HGNC:8638};
Synonyms=PCAF {ECO:0000303|PubMed:12486002};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC50890.2};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
INTERACTION WITH EP300 AND CREBBP.
TISSUE=Liver;
PubMed=8684459; DOI=10.1038/382319a0;
Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
"A p300/CBP-associated factor that competes with the adenoviral
oncoprotein E1A.";
Nature 382:319-324(1996).
[2] {ECO:0000305}
SEQUENCE REVISION.
TISSUE=Liver;
Nakatani Y.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ENZYME ACTIVITY.
PubMed=8945521; DOI=10.1016/S0092-8674(00)82001-2;
Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.;
"The transcriptional coactivators p300 and CBP are histone
acetyltransferases.";
Cell 87:953-959(1996).
[5]
INTERACTION WITH NCOA3.
PubMed=9346901; DOI=10.1074/jbc.272.44.27629;
Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.;
"TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule,
exhibits distinct properties from steroid receptor coactivator-1.";
J. Biol. Chem. 272:27629-27634(1997).
[6]
INTERACTION WITH NCOA1.
PubMed=9296499; DOI=10.1038/38304;
Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J.,
Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Steroid receptor coactivator-1 is a histone acetyltransferase.";
Nature 389:194-198(1997).
[7]
INTERACTION WITH KLF1, AND FUNCTION.
PubMed=9707565; DOI=10.1073/pnas.95.17.9855;
Zhang W., Bieker J.J.;
"Acetylation and modulation of erythroid Krueppel-like factor (EKLF)
activity by interaction with histone acetyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998).
[8]
INTERACTION WITH E2F1, AND FUNCTION.
PubMed=10675335; DOI=10.1093/emboj/19.4.662;
Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A.,
Kouzarides T.;
"Regulation of E2F1 activity by acetylation.";
EMBO J. 19:662-671(2000).
[9]
INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
PubMed=10766811; DOI=10.1074/jbc.275.16.11852;
Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y.,
Giam C.-Z.;
"p300 and p300/cAMP-responsive element-binding protein associated
factor interact with human T-cell lymphotropic virus type-1 Tax in a
multi-histone acetyltransferase/activator-enhancer complex.";
J. Biol. Chem. 275:11852-11857(2000).
[10]
INTERACTION WITH MECOM.
PubMed=11568182; DOI=10.1074/jbc.M106733200;
Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
"Interaction of EVI1 with cAMP-responsive element-binding protein-
binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
in reversible acetylation of EVI1 and in co-localization in nuclear
speckles.";
J. Biol. Chem. 276:44936-44943(2001).
[11]
INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
PubMed=12486002; DOI=10.1093/emboj/cdf669;
Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T.,
Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E.;
"Differential acetylation of Tat coordinates its interaction with the
co-activators cyclin T1 and PCAF.";
EMBO J. 21:6811-6819(2002).
[12]
FUNCTION, AND INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
PubMed=14645221; DOI=10.1074/jbc.M311973200;
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
Chakravarti D., FitzGerald G.A., McNamara P.;
"Histone acetyltransferase-dependent chromatin remodeling and the
vascular clock.";
J. Biol. Chem. 279:7091-7097(2004).
[13]
INTERACTION WITH NFE4.
PubMed=15273251; DOI=10.1074/jbc.M405129200;
Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.;
"Site-specific acetylation of the fetal globin activator NF-E4
prevents its ubiquitination and regulates its interaction with the
histone deacetylase, HDAC1.";
J. Biol. Chem. 279:41477-41486(2004).
[14]
INTERACTION WITH TACC1; TACC2 AND TACC3.
PubMed=14767476; DOI=10.1038/sj.onc.1207424;
Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
"The transforming acidic coiled coil proteins interact with nuclear
histone acetyltransferases.";
Oncogene 23:2559-2563(2004).
[15]
INTERACTION WITH NR2C2.
PubMed=16887930; DOI=10.1074/mcp.M600180-MCP200;
Huq M.D., Gupta P., Tsai N.P., Wei L.N.;
"Modulation of testicular receptor 4 activity by mitogen-activated
protein kinase-mediated phosphorylation.";
Mol. Cell. Proteomics 5:2072-2082(2006).
[16]
INTERACTION WITH DDX17.
PubMed=17226766; DOI=10.1002/jcb.21250;
Shin S., Janknecht R.;
"Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
coactivators p300 and P/CAF.";
J. Cell. Biochem. 101:1252-1265(2007).
[17]
INTERACTION WITH CEBPB.
PubMed=17301242; DOI=10.1073/pnas.0607378104;
Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
"Glucocorticoid-stimulated preadipocyte differentiation is mediated
through acetylation of C/EBPbeta by GCN5.";
Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
[18]
IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024;
Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H.,
Tempst P., Glass C.K., Rosenfeld M.G.;
"A histone H2A deubiquitinase complex coordinating histone acetylation
and H1 dissociation in transcriptional regulation.";
Mol. Cell 27:609-621(2007).
[19]
INTERACTION WITH BCAS3.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[20]
FUNCTION.
PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002;
Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.;
"Acetylation stabilizes ATP-citrate lyase to promote lipid
biosynthesis and tumor growth.";
Mol. Cell 51:506-518(2013).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK4.
PubMed=27796307; DOI=10.1038/ncomms13227;
Fournier M., Orpinell M., Grauffel C., Scheer E., Garnier J.M., Ye T.,
Chavant V., Joint M., Esashi F., Dejaegere A., Goenczy P., Tora L.;
"KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in
preventing centrosome amplification.";
Nat. Commun. 7:13227-13227(2016).
[22]
FUNCTION, AND INTERACTION WITH TBX5.
PubMed=29174768; DOI=10.1016/j.yjmcc.2017.11.013;
Ghosh T.K., Aparicio-Sanchez J.J., Buxton S., Ketley A., Mohamed T.,
Rutland C.S., Loughna S., Brook J.D.;
"Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb
development.";
J. Mol. Cell. Cardiol. 114:185-198(2017).
[23]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 493-658 IN COMPLEX WITH
COENZYME A, AND ACTIVE SITE.
PubMed=10393169; DOI=10.1093/emboj/18.13.3521;
Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L.,
Marmorstein R.;
"Crystal structure of the histone acetyltransferase domain of the
human PCAF transcriptional regulator bound to coenzyme A.";
EMBO J. 18:3521-3532(1999).
[24]
STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760;
TYR-802 AND TYR-809.
TISSUE=Liver;
PubMed=10365964; DOI=10.1038/20974;
Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.;
"Structure and ligand of a histone acetyltransferase bromodomain.";
Nature 399:491-496(1999).
[25]
STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
PubMed=11931765; DOI=10.1016/S1097-2765(02)00483-5;
Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M.,
Verdin E., Zhou M.-M.;
"Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF
bromodomain.";
Mol. Cell 9:575-586(2002).
[26]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831.
PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
Gingras A.C., Arrowsmith C.H., Knapp S.;
"Histone recognition and large-scale structural analysis of the human
bromodomain family.";
Cell 149:214-231(2012).
[27]
VARIANT GLY-130.
PubMed=28493397; DOI=10.1002/humu.23246;
UK10K;
Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
FitzPatrick D.R.;
"A recurrent de novo mutation in ACTG1 causes isolated ocular
coloboma.";
Hum. Mutat. 38:942-946(2017).
-!- FUNCTION: 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 (PubMed:29174768). Acts as a
negative regulator of centrosome amplification by mediating
acetylation of PLK4 (PubMed:27796307).
{ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:14645221,
ECO:0000269|PubMed:23932781, ECO:0000269|PubMed:27796307,
ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:8684459,
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}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:8945521}.
-!- SUBUNIT: Interacts with SIRT1. Interacts (unsumoylated form) with
NR2C1; the interaction promotes transactivation activity (By
similarity). Interacts with EP300, CREBBP and DDX17. Interacts
with NCOA1 and NCOA3. Component of a large chromatin remodeling
complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and
KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and
unsumoylated form); the interaction promotes the transactivation
activity of NR2C2. Interacts with KLF1; the interaction does not
acetylate KLF1 and there is no enhancement of its
transactivational activity. Interacts with NFE4. Interacts with
MECOM. Interacts with E2F1; the interaction acetylates E2F1
augmenting its DNA-binding and transcriptional activity. Interacts
with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with BCAS3. Interacts
with CEBPB (PubMed:17301242). Interacts with NR4A3 (By
similarity). Interacts with NFATC2 (By similarity). Interacts with
TBX5 (PubMed:29174768). Interacts with PLK4 (PubMed:27796307).
{ECO:0000250|UniProtKB:Q9JHD1, ECO:0000269|PubMed:10675335,
ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11931765,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:14767476,
ECO:0000269|PubMed:15273251, ECO:0000269|PubMed:16887930,
ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:17707232,
ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768,
ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:9296499,
ECO:0000269|PubMed:9346901, ECO:0000269|PubMed:9707565}.
-!- SUBUNIT: (Microbial infection) Interacts with and acetylates HIV-1
Tat. {ECO:0000269|PubMed:12486002}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax.
{ECO:0000269|PubMed:10766811}.
-!- INTERACTION:
P03255:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-2603114;
P03255-2:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-6859460;
O60566:BUB1B; NbExp=14; IntAct=EBI-477430, EBI-1001438;
P28033:Cebpb (xeno); NbExp=2; IntAct=EBI-477430, EBI-1029979;
Q92793:CREBBP; NbExp=4; IntAct=EBI-477430, EBI-81215;
P03129:E7 (xeno); NbExp=3; IntAct=EBI-477430, EBI-866453;
Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-477430, EBI-744366;
Q09472:EP300; NbExp=2; IntAct=EBI-477430, EBI-447295;
Q16665:HIF1A; NbExp=2; IntAct=EBI-477430, EBI-447269;
P02299:His3:CG33854 (xeno); NbExp=2; IntAct=EBI-477430, EBI-522090;
P84040:His4:CG33909 (xeno); NbExp=2; IntAct=EBI-477430, EBI-185028;
Q9Y5W3:KLF2; NbExp=2; IntAct=EBI-477430, EBI-9846663;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-477430, EBI-1802965;
Q8IXJ6:SIRT2; NbExp=4; IntAct=EBI-477430, EBI-477232;
Q16594:TAF9; NbExp=3; IntAct=EBI-477430, EBI-712521;
O88898-2:Tp63 (xeno); NbExp=3; IntAct=EBI-477430, EBI-2338228;
Q15672:TWIST1; NbExp=2; IntAct=EBI-477430, EBI-1797287;
P22415:USF1; NbExp=5; IntAct=EBI-477430, EBI-1054489;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29174768}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:29174768}. 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.
{ECO:0000269|PubMed:29174768}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed but most abundant in
heart and skeletal muscle. {ECO:0000269|PubMed:8684459}.
-!- DOMAIN: (Microbial infection) The bromodomain mediates binding to
HIV-1 Tat. {ECO:0000269|PubMed:11931765}.
-!- 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}.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
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EMBL; U57317; AAC50890.2; -; mRNA.
EMBL; BC060823; AAH60823.1; -; mRNA.
EMBL; BC070075; AAH70075.1; -; mRNA.
CCDS; CCDS2634.1; -.
PIR; S71788; S71788.
RefSeq; NP_003875.3; NM_003884.4.
UniGene; Hs.533055; -.
PDB; 1CM0; X-ray; 2.30 A; A/B=493-658.
PDB; 1JM4; NMR; -; B=719-832.
PDB; 1N72; NMR; -; A=719-832.
PDB; 1WUG; NMR; -; A=719-832.
PDB; 1WUM; NMR; -; A=719-832.
PDB; 1ZS5; NMR; -; A=719-832.
PDB; 2RNW; NMR; -; A=719-832.
PDB; 2RNX; NMR; -; A=719-832.
PDB; 3GG3; X-ray; 2.25 A; A/B=715-831.
PDB; 4NSQ; X-ray; 2.31 A; A/B/C/D=493-658.
PDB; 5FDZ; X-ray; 2.40 A; A/B=715-831.
PDB; 5FE0; X-ray; 2.30 A; A/B=715-831.
PDB; 5FE1; X-ray; 2.22 A; A/B=715-831.
PDB; 5FE2; X-ray; 2.25 A; A/B=715-831.
PDB; 5FE3; X-ray; 2.12 A; A/B=715-831.
PDB; 5FE4; X-ray; 2.15 A; A/B=715-831.
PDB; 5FE5; X-ray; 2.12 A; A/B=715-831.
PDB; 5FE6; X-ray; 1.77 A; A/B=715-831.
PDB; 5FE7; X-ray; 2.08 A; A/B=715-831.
PDB; 5FE8; X-ray; 2.10 A; A/B=715-831.
PDB; 5FE9; X-ray; 2.35 A; A/B=715-831.
PDB; 5LVQ; X-ray; 2.05 A; A/B=715-831.
PDB; 5LVR; X-ray; 2.05 A; A/B=715-831.
PDB; 5MKX; X-ray; 1.68 A; A/B=715-831.
PDBsum; 1CM0; -.
PDBsum; 1JM4; -.
PDBsum; 1N72; -.
PDBsum; 1WUG; -.
PDBsum; 1WUM; -.
PDBsum; 1ZS5; -.
PDBsum; 2RNW; -.
PDBsum; 2RNX; -.
PDBsum; 3GG3; -.
PDBsum; 4NSQ; -.
PDBsum; 5FDZ; -.
PDBsum; 5FE0; -.
PDBsum; 5FE1; -.
PDBsum; 5FE2; -.
PDBsum; 5FE3; -.
PDBsum; 5FE4; -.
PDBsum; 5FE5; -.
PDBsum; 5FE6; -.
PDBsum; 5FE7; -.
PDBsum; 5FE8; -.
PDBsum; 5FE9; -.
PDBsum; 5LVQ; -.
PDBsum; 5LVR; -.
PDBsum; 5MKX; -.
ProteinModelPortal; Q92831; -.
SMR; Q92831; -.
BioGrid; 114375; 190.
ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
ComplexPortal; CPX-989; PCAF histone acetylase complex.
CORUM; Q92831; -.
DIP; DIP-29778N; -.
IntAct; Q92831; 40.
MINT; Q92831; -.
STRING; 9606.ENSP00000263754; -.
BindingDB; Q92831; -.
ChEMBL; CHEMBL5500; -.
DrugBank; DB08186; (3E)-4-(1-METHYL-1H-INDOL-3-YL)BUT-3-EN-2-ONE.
DrugBank; DB01992; Coenzyme A.
DrugBank; DB08291; N-(3-AMINOPROPYL)-2-NITROBENZENAMINE.
GuidetoPHARMACOLOGY; 2737; -.
CarbonylDB; Q92831; -.
iPTMnet; Q92831; -.
PhosphoSitePlus; Q92831; -.
BioMuta; KAT2B; -.
DMDM; 83287776; -.
REPRODUCTION-2DPAGE; Q92831; -.
EPD; Q92831; -.
MaxQB; Q92831; -.
PaxDb; Q92831; -.
PeptideAtlas; Q92831; -.
PRIDE; Q92831; -.
ProteomicsDB; 75508; -.
Ensembl; ENST00000263754; ENSP00000263754; ENSG00000114166.
GeneID; 8850; -.
KEGG; hsa:8850; -.
UCSC; uc003cbq.4; human.
CTD; 8850; -.
DisGeNET; 8850; -.
EuPathDB; HostDB:ENSG00000114166.7; -.
GeneCards; KAT2B; -.
HGNC; HGNC:8638; KAT2B.
HPA; CAB004526; -.
HPA; HPA055839; -.
MIM; 602303; gene.
neXtProt; NX_Q92831; -.
OpenTargets; ENSG00000114166; -.
PharmGKB; PA162392705; -.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00920000149009; -.
HOGENOM; HOG000007151; -.
InParanoid; Q92831; -.
KO; K06062; -.
OMA; QVIRFPM; -.
OrthoDB; EOG091G03ZO; -.
PhylomeDB; Q92831; -.
TreeFam; TF105399; -.
BRENDA; 2.3.1.48; 2681.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5578768; Physiological factors.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SIGNOR; Q92831; -.
ChiTaRS; KAT2B; human.
EvolutionaryTrace; Q92831; -.
GeneWiki; PCAF; -.
GenomeRNAi; 8850; -.
PRO; PR:Q92831; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114166; Expressed in 230 organ(s), highest expression level in corpus callosum.
CleanEx; HS_KAT2B; -.
Genevisible; Q92831; HS.
GO; GO:0031672; C:A band; IEA:Ensembl.
GO; GO:0042641; C:actomyosin; IEA:Ensembl.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0031674; C:I band; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000125; C:PCAF complex; NAS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISS:UniProtKB.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
GO; GO:0043970; P:histone H3-K9 acetylation; IEA:Ensembl.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0060173; P:limb development; ISS:UniProtKB.
GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0046600; P:negative regulation of centriole replication; IDA:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:BHF-UCL.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; TAS:Reactome.
GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:BHF-UCL.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR037800; GCN5.
InterPro; IPR016376; GCN5/PCAF.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR009464; PCAF_N.
PANTHER; PTHR22880:SF124; PTHR22880:SF124; 1.
Pfam; PF00583; Acetyltransf_1; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF06466; PCAF_N; 1.
PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Activator; Acyltransferase; Biological rhythms;
Bromodomain; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Host-virus interaction; Nucleus; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Transferase.
CHAIN 1 832 Histone acetyltransferase KAT2B.
/FTId=PRO_0000211208.
DOMAIN 503 651 N-acetyltransferase.
{ECO:0000250|UniProtKB:Q92830,
ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 740 810 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035, ECO:0000305}.
REGION 574 576 Acetyl-CoA binding.
{ECO:0000269|PubMed:10393169}.
REGION 581 587 Acetyl-CoA binding.
{ECO:0000269|PubMed:10393169}.
REGION 612 615 Acetyl-CoA binding.
{ECO:0000269|PubMed:10393169}.
ACT_SITE 570 570 Proton donor/acceptor.
{ECO:0000303|PubMed:10393169}.
VARIANT 130 130 V -> G (found in a patient with isolated
coloboma; unknown pathological
significance).
{ECO:0000269|PubMed:28493397}.
/FTId=VAR_079852.
VARIANT 386 386 N -> S (in dbSNP:rs17006625).
/FTId=VAR_034372.
MUTAGEN 752 752 V->A: Reduced acetyl-lysine binding.
{ECO:0000269|PubMed:10365964}.
MUTAGEN 760 760 Y->A: Reduced acetyl-lysine binding.
{ECO:0000269|PubMed:10365964}.
MUTAGEN 802 802 Y->A: Reduced acetyl-lysine binding.
{ECO:0000269|PubMed:10365964}.
MUTAGEN 809 809 Y->A: Complete loss of acetyl-lysine
binding. {ECO:0000269|PubMed:10365964}.
CONFLICT 804 805 PP -> AA (in Ref. 1; AAC50890).
{ECO:0000305}.
STRAND 494 499 {ECO:0000244|PDB:1CM0}.
STRAND 503 505 {ECO:0000244|PDB:1CM0}.
HELIX 509 525 {ECO:0000244|PDB:1CM0}.
HELIX 531 538 {ECO:0000244|PDB:1CM0}.
STRAND 543 550 {ECO:0000244|PDB:1CM0}.
STRAND 553 563 {ECO:0000244|PDB:1CM0}.
TURN 564 567 {ECO:0000244|PDB:1CM0}.
STRAND 568 576 {ECO:0000244|PDB:1CM0}.
HELIX 578 580 {ECO:0000244|PDB:1CM0}.
STRAND 582 584 {ECO:0000244|PDB:1CM0}.
HELIX 585 599 {ECO:0000244|PDB:1CM0}.
STRAND 604 609 {ECO:0000244|PDB:1CM0}.
TURN 611 613 {ECO:0000244|PDB:1CM0}.
HELIX 614 618 {ECO:0000244|PDB:1CM0}.
TURN 619 621 {ECO:0000244|PDB:1CM0}.
STRAND 623 625 {ECO:0000244|PDB:1CM0}.
HELIX 630 633 {ECO:0000244|PDB:1CM0}.
STRAND 644 649 {ECO:0000244|PDB:1CM0}.
HELIX 727 741 {ECO:0000244|PDB:5MKX}.
STRAND 742 744 {ECO:0000244|PDB:1WUM}.
HELIX 746 748 {ECO:0000244|PDB:5MKX}.
TURN 754 756 {ECO:0000244|PDB:5MKX}.
STRAND 757 759 {ECO:0000244|PDB:1ZS5}.
HELIX 760 763 {ECO:0000244|PDB:5MKX}.
STRAND 764 766 {ECO:0000244|PDB:1JM4}.
HELIX 770 778 {ECO:0000244|PDB:5MKX}.
HELIX 785 802 {ECO:0000244|PDB:5MKX}.
STRAND 805 807 {ECO:0000244|PDB:1WUG}.
HELIX 808 827 {ECO:0000244|PDB:5MKX}.
STRAND 828 830 {ECO:0000244|PDB:1N72}.
SEQUENCE 832 AA; 93013 MW; 72F516E8BC00CC0C CRC64;
MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG ACGPATAVAA
AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC KAEESCKCNG WKNPNPSPTP
PRADLQQIIV SLTESCRSCS HALAAHVSHL ENVSEEEMNR LLGIVLDVEY LFTCVHKEED
ADTKQVYFYL FKLLRKSILQ RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE
RQTIVELAKM FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR
YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL SMLEEEVYSQ
NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS SSLEQPNAGS SSPACKASSG
LEANPGEKRK MTDSHVLEEA KKPRVMGDIP MELINEVMST ITDPAAMLGP ETNFLSAHSA
RDEAARLEER RGVIEFHVVG NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD
PKHKTLALIK DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH
DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL NPRIPYTEFS
VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI ESIPGIRETG WKPSGKEKSK
EPRDPDQLYS TLKSILQQVK SHQSAWPFME PVKRTEAPGY YEVIRFPMDL KTMSERLKNR
YYVSKKLFMA DLQRVFTNCK EYNPPESEYY KCANILEKFF FSKIKEAGLI DK


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