ID KAT2B_HUMAN Reviewed; 832 AA. AC Q92831; Q6NSK1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 27-MAR-2024, entry version 233. DE RecName: Full=Histone acetyltransferase KAT2B; DE EC=2.3.1.48 {ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:8945521}; DE AltName: Full=Histone acetyltransferase PCAF {ECO:0000303|PubMed:12486002}; DE Short=Histone acetylase PCAF {ECO:0000303|PubMed:12486002}; DE AltName: Full=Lysine acetyltransferase 2B {ECO:0000303|PubMed:27796307}; DE AltName: Full=P300/CBP-associated factor {ECO:0000303|PubMed:12486002}; DE Short=P/CAF {ECO:0000303|PubMed:12486002}; DE AltName: Full=Spermidine acetyltransferase KAT2B; DE EC=2.3.1.57 {ECO:0000269|PubMed:27389534}; GN Name=KAT2B {ECO:0000303|PubMed:27796307, ECO:0000312|HGNC:HGNC:8638}; GN Synonyms=PCAF {ECO:0000303|PubMed:12486002}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC50890.2}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND RP INTERACTION WITH EP300 AND CREBBP. RC TISSUE=Liver; RX PubMed=8684459; DOI=10.1038/382319a0; RA Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.; RT "A p300/CBP-associated factor that competes with the adenoviral oncoprotein RT E1A."; RL Nature 382:319-324(1996). RN [2] {ECO:0000305} RP SEQUENCE REVISION. RC TISSUE=Liver; RA Nakatani Y.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8945521; DOI=10.1016/s0092-8674(00)82001-2; RA Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.; RT "The transcriptional coactivators p300 and CBP are histone RT acetyltransferases."; RL Cell 87:953-959(1996). RN [5] RP INTERACTION WITH NCOA3. RX PubMed=9346901; DOI=10.1074/jbc.272.44.27629; RA Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.; RT "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, RT exhibits distinct properties from steroid receptor coactivator-1."; RL J. Biol. Chem. 272:27629-27634(1997). RN [6] RP INTERACTION WITH NCOA1. RX PubMed=9296499; DOI=10.1038/38304; RA Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., Mizzen C.A., RA McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.; RT "Steroid receptor coactivator-1 is a histone acetyltransferase."; RL Nature 389:194-198(1997). RN [7] RP INTERACTION WITH KLF1, AND FUNCTION. RX PubMed=9707565; DOI=10.1073/pnas.95.17.9855; RA Zhang W., Bieker J.J.; RT "Acetylation and modulation of erythroid Krueppel-like factor (EKLF) RT activity by interaction with histone acetyltransferases."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998). RN [8] RP INTERACTION WITH E2F1, AND FUNCTION. RX PubMed=10675335; DOI=10.1093/emboj/19.4.662; RA Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A., Kouzarides T.; RT "Regulation of E2F1 activity by acetylation."; RL EMBO J. 19:662-671(2000). RN [9] RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION). RX PubMed=10766811; DOI=10.1074/jbc.275.16.11852; RA Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y., RA Giam C.-Z.; RT "p300 and p300/cAMP-responsive element-binding protein associated factor RT interact with human T-cell lymphotropic virus type-1 Tax in a multi-histone RT acetyltransferase/activator-enhancer complex."; RL J. Biol. Chem. 275:11852-11857(2000). RN [10] RP INTERACTION WITH MECOM. RX PubMed=11568182; DOI=10.1074/jbc.m106733200; RA Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.; RT "Interaction of EVI1 with cAMP-responsive element-binding protein-binding RT protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible RT acetylation of EVI1 and in co-localization in nuclear speckles."; RL J. Biol. Chem. 276:44936-44943(2001). RN [11] RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION). RX PubMed=12486002; DOI=10.1093/emboj/cdf669; RA Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T., Nakatani Y., RA Emiliani S., Benkirane M., Kiernan R.E.; RT "Differential acetylation of Tat coordinates its interaction with the co- RT activators cyclin T1 and PCAF."; RL EMBO J. 21:6811-6819(2002). RN [12] RP FUNCTION, AND INTERACTION WITH NPAS2; BMAL1 AND CLOCK. RX PubMed=14645221; DOI=10.1074/jbc.m311973200; RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., RA Chakravarti D., FitzGerald G.A., McNamara P.; RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular RT clock."; RL J. Biol. Chem. 279:7091-7097(2004). RN [13] RP INTERACTION WITH NFE4. RX PubMed=15273251; DOI=10.1074/jbc.m405129200; RA Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.; RT "Site-specific acetylation of the fetal globin activator NF-E4 prevents its RT ubiquitination and regulates its interaction with the histone deacetylase, RT HDAC1."; RL J. Biol. Chem. 279:41477-41486(2004). RN [14] RP INTERACTION WITH TACC1; TACC2 AND TACC3. RX PubMed=14767476; DOI=10.1038/sj.onc.1207424; RA Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.; RT "The transforming acidic coiled coil proteins interact with nuclear histone RT acetyltransferases."; RL Oncogene 23:2559-2563(2004). RN [15] RP INTERACTION WITH NR2C2. RX PubMed=16887930; DOI=10.1074/mcp.m600180-mcp200; RA Huq M.D., Gupta P., Tsai N.P., Wei L.N.; RT "Modulation of testicular receptor 4 activity by mitogen-activated protein RT kinase-mediated phosphorylation."; RL Mol. Cell. Proteomics 5:2072-2082(2006). RN [16] RP INTERACTION WITH DDX17. RX PubMed=17226766; DOI=10.1002/jcb.21250; RA Shin S., Janknecht R.; RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the RT coactivators p300 and P/CAF."; RL J. Cell. Biochem. 101:1252-1265(2007). RN [17] RP INTERACTION WITH CEBPB. RX PubMed=17301242; DOI=10.1073/pnas.0607378104; RA Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.; RT "Glucocorticoid-stimulated preadipocyte differentiation is mediated through RT acetylation of C/EBPbeta by GCN5."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007). RN [18] RP IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX. RX PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024; RA Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., RA Tempst P., Glass C.K., Rosenfeld M.G.; RT "A histone H2A deubiquitinase complex coordinating histone acetylation and RT H1 dissociation in transcriptional regulation."; RL Mol. Cell 27:609-621(2007). RN [19] RP INTERACTION WITH BCAS3. RX PubMed=17505058; DOI=10.1210/me.2006-0514; RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.; RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 RT (PELP1)."; RL Mol. Endocrinol. 21:1847-1860(2007). RN [20] RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=20940255; DOI=10.1242/jcs.068924; RA Pickard A., Wong P.P., McCance D.J.; RT "Acetylation of Rb by PCAF is required for nuclear localization and RT keratinocyte differentiation."; RL J. Cell Sci. 123:3718-3726(2010). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=21131905; DOI=10.1038/emboj.2010.318; RA Jin Q., Yu L.R., Wang L., Zhang Z., Kasper L.H., Lee J.E., Wang C., RA Brindle P.K., Dent S.Y., Ge K.; RT "Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated RT H3K18/27ac in nuclear receptor transactivation."; RL EMBO J. 30:249-262(2011). RN [22] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23001180; DOI=10.1073/pnas.1202639109; RA Xia P., Wang Z., Liu X., Wu B., Wang J., Ward T., Zhang L., Ding X., RA Gibbons G., Shi Y., Yao X.; RT "EB1 acetylation by P300/CBP-associated factor (PCAF) ensures accurate RT kinetochore-microtubule interactions in mitosis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:16564-16569(2012). RN [23] RP FUNCTION. RX PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002; RA Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.; RT "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and RT tumor growth."; RL Mol. Cell 51:506-518(2013). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=27389534; DOI=10.1080/14756366.2016.1205045; RA Burgio G., Corona D.F., Nicotra C.M., Carruba G., Taibi G.; RT "P/CAF-mediated spermidine acetylation regulates histone acetyltransferase RT activity."; RL J. Enzym. Inhib. Med. Chem. 31:75-82(2016). RN [26] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK4. RX PubMed=27796307; DOI=10.1038/ncomms13227; RA Fournier M., Orpinell M., Grauffel C., Scheer E., Garnier J.M., Ye T., RA Chavant V., Joint M., Esashi F., Dejaegere A., Goenczy P., Tora L.; RT "KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in RT preventing centrosome amplification."; RL Nat. Commun. 7:13227-13227(2016). RN [27] RP FUNCTION. RX PubMed=26867678; DOI=10.1038/ncomms10734; RA Chen S., Blank M.F., Iyer A., Huang B., Wang L., Grummt I., Voit R.; RT "SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA RT processing."; RL Nat. Commun. 7:10734-10734(2016). RN [28] RP FUNCTION, AND INTERACTION WITH TBX5. RX PubMed=29174768; DOI=10.1016/j.yjmcc.2017.11.013; RA Ghosh T.K., Aparicio-Sanchez J.J., Buxton S., Ketley A., Mohamed T., RA Rutland C.S., Loughna S., Brook J.D.; RT "Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb RT development."; RL J. Mol. Cell. Cardiol. 114:185-198(2017). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 493-658 IN COMPLEX WITH COENZYME RP A, AND ACTIVE SITE. RX PubMed=10393169; DOI=10.1093/emboj/18.13.3521; RA Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L., RA Marmorstein R.; RT "Crystal structure of the histone acetyltransferase domain of the human RT PCAF transcriptional regulator bound to coenzyme A."; RL EMBO J. 18:3521-3532(1999). RN [30] RP STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760; TYR-802 RP AND TYR-809. RC TISSUE=Liver; RX PubMed=10365964; DOI=10.1038/20974; RA Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.; RT "Structure and ligand of a histone acetyltransferase bromodomain."; RL Nature 399:491-496(1999). RN [31] RP STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT. RX PubMed=11931765; DOI=10.1016/s1097-2765(02)00483-5; RA Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M., Verdin E., RA Zhou M.-M.; RT "Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF RT bromodomain."; RL Mol. Cell 9:575-586(2002). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). RN [33] RP VARIANT GLY-130. RX PubMed=28493397; DOI=10.1002/humu.23246; RG UK10K; RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D., RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M., RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G., RA FitzPatrick D.R.; RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma."; RL Hum. Mutat. 38:942-946(2017). CC -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to promote CC transcriptional activation (PubMed:8945521). Has significant histone CC acetyltransferase activity with core histones (H3 and H4), and also CC with nucleosome core particles (PubMed:8945521). Has a a strong CC preference for acetylation of H3 at 'Lys-9' (H3K9ac) (PubMed:21131905). CC Also acetylates non-histone proteins, such as ACLY, MAPRE1/EB1, PLK4, CC RRP9/U3-55K and TBX5 (PubMed:9707565, PubMed:10675335, PubMed:23001180, CC PubMed:27796307, PubMed:23932781, PubMed:26867678, PubMed:29174768). CC Inhibits cell-cycle progression and counteracts the mitogenic activity CC of the adenoviral oncoprotein E1A (PubMed:8684459). Acts as a circadian CC transcriptional coactivator which enhances the activity of the CC circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 CC heterodimers (PubMed:14645221). Involved in heart and limb development CC by mediating acetylation of TBX5, acetylation regulating CC nucleocytoplasmic shuttling of TBX5 (PubMed:29174768). Acts as a CC negative regulator of centrosome amplification by mediating acetylation CC of PLK4 (PubMed:27796307). Acetylates RRP9/U3-55K, a core subunit of CC the U3 snoRNP complex, impairing pre-rRNA processing (PubMed:26867678). CC Acetylates MAPRE1/EB1, promoting dynamic kinetochore-microtubule CC interactions in early mitosis (PubMed:23001180). Also acetylates CC spermidine (PubMed:27389534). {ECO:0000269|PubMed:10675335, CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21131905, CC ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:23932781, CC ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:27389534, CC ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768, CC ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:8945521, CC ECO:0000269|PubMed:9707565}. CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, it is CC recruited by the viral protein Tat. Regulates Tat's transactivating CC activity and may help inducing chromatin remodeling of proviral genes. CC {ECO:0000269|PubMed:12486002}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:8945521}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:21131905}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000269|PubMed:23001180, ECO:0000269|PubMed:27389534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000269|PubMed:23001180, ECO:0000305|PubMed:27389534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(8)-acetylspermidine; CC Xref=Rhea:RHEA:28270, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58535; EC=2.3.1.57; CC Evidence={ECO:0000269|PubMed:27389534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28271; CC Evidence={ECO:0000305|PubMed:27389534}; CC -!- ACTIVITY REGULATION: Activated in vitro by very low concentrations of CC spermidine, but inhibited at spermidine concentrations higher than 4 CC uM. The activating effect of low spermidine concentrations may be CC mediated by N(8)-acetylspermidine produced by KAT2B/P/CAF itself acting CC as a positive feedback loop. {ECO:0000269|PubMed:27389534}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.74 uM for acetyl-CoA {ECO:0000269|PubMed:27389534}; CC KM=2.29 uM for spermidine {ECO:0000269|PubMed:27389534}; CC -!- SUBUNIT: Interacts with SIRT1. Interacts (unsumoylated form) with CC NR2C1; the interaction promotes transactivation activity (By CC similarity). Interacts with EP300, CREBBP and DDX17. Interacts with CC NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at CC least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts CC with NR2C2 (hypophosphorylated and unsumoylated form); the interaction CC promotes the transactivation activity of NR2C2. Interacts with KLF1; CC the interaction does not acetylate KLF1 and there is no enhancement of CC its transactivational activity. Interacts with NFE4. Interacts with CC MECOM. Interacts with E2F1; the interaction acetylates E2F1 augmenting CC its DNA-binding and transcriptional activity. Interacts with NPAS2, CC BMAL1 and CLOCK. Interacts with BCAS3. Interacts with CEBPB CC (PubMed:17301242). Interacts with NR4A3 (By similarity). Interacts with CC NFATC2 (By similarity). Interacts with TBX5 (PubMed:29174768). CC Interacts with PLK4 (PubMed:27796307). Interacts with RB1; this CC interaction leads to RB1 acetylation (By similarity). CC {ECO:0000250|UniProtKB:Q9JHD1, ECO:0000269|PubMed:10675335, CC ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11931765, CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:14767476, CC ECO:0000269|PubMed:15273251, ECO:0000269|PubMed:16887930, CC ECO:0000269|PubMed:17226766, ECO:0000269|PubMed:17301242, CC ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:17707232, CC ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768, CC ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:9296499, CC ECO:0000269|PubMed:9346901, ECO:0000269|PubMed:9707565}. CC -!- SUBUNIT: (Microbial infection) Interacts with and acetylates HIV-1 Tat. CC {ECO:0000269|PubMed:12486002}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax. CC {ECO:0000269|PubMed:10766811}. CC -!- INTERACTION: CC Q92831; O60566: BUB1B; NbExp=14; IntAct=EBI-477430, EBI-1001438; CC Q92831; Q92793: CREBBP; NbExp=4; IntAct=EBI-477430, EBI-81215; CC Q92831; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-477430, EBI-744366; CC Q92831; Q09472: EP300; NbExp=2; IntAct=EBI-477430, EBI-447295; CC Q92831; Q16665: HIF1A; NbExp=2; IntAct=EBI-477430, EBI-447269; CC Q92831; Q9Y5W3: KLF2; NbExp=2; IntAct=EBI-477430, EBI-9846663; CC Q92831; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-477430, EBI-1802965; CC Q92831; Q8IXJ6: SIRT2; NbExp=4; IntAct=EBI-477430, EBI-477232; CC Q92831; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-477430, EBI-5235340; CC Q92831; Q16594: TAF9; NbExp=3; IntAct=EBI-477430, EBI-712521; CC Q92831; Q15672: TWIST1; NbExp=2; IntAct=EBI-477430, EBI-1797287; CC Q92831; P22415: USF1; NbExp=5; IntAct=EBI-477430, EBI-1054489; CC Q92831; P28033: Cebpb; Xeno; NbExp=2; IntAct=EBI-477430, EBI-1029979; CC Q92831; P03129: E7; Xeno; NbExp=3; IntAct=EBI-477430, EBI-866453; CC Q92831; P02299: His3:CG33854; Xeno; NbExp=2; IntAct=EBI-477430, EBI-522090; CC Q92831; P84040: His4:CG33909; Xeno; NbExp=2; IntAct=EBI-477430, EBI-185028; CC Q92831; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-477430, EBI-25475856; CC Q92831; P59595: N; Xeno; NbExp=2; IntAct=EBI-477430, EBI-7602718; CC Q92831; O88898-2: Tp63; Xeno; NbExp=3; IntAct=EBI-477430, EBI-2338228; CC Q92831; P03255; Xeno; NbExp=3; IntAct=EBI-477430, EBI-2603114; CC Q92831; P03255-2; Xeno; NbExp=3; IntAct=EBI-477430, EBI-6859460; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20940255, CC ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:29174768}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:29174768}. Cytoplasm {ECO:0000269|PubMed:20940255}. CC Note=Mainly localizes to the nucleus. Also localizes to centrosomes in CC late G1 and around the G1/S transition, coinciding with the onset of CC centriole formation. Subcellular location may vary depending upon cell CC differentiation state. Cytoplasmic at the very stages of keratinocyte CC differentiation, becomes nuclear at later differentiation stages. CC Cytoplasmic in basal epithelial cells (undifferentiated cells) and CC nuclear in parabasal cells (differentiated cells) (PubMed:20940255). CC Localizes to sites of DNA damage (PubMed:25593309). CC {ECO:0000269|PubMed:20940255, ECO:0000269|PubMed:25593309, CC ECO:0000269|PubMed:29174768}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed but most abundant in heart CC and skeletal muscle. Also expressed in the skin, in keratinocytes (at CC protein level) (PubMed:20940255). {ECO:0000269|PubMed:20940255, CC ECO:0000269|PubMed:8684459}. CC -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte differentiation CC (at protein level). {ECO:0000269|PubMed:20940255}. CC -!- DOMAIN: (Microbial infection) The bromodomain mediates binding to HIV-1 CC Tat. {ECO:0000269|PubMed:11931765}. CC -!- DISEASE: Note=Defects in KAT2B has been found in a patient with CC isolated coloboma, a defect of the eye characterized by the absence of CC ocular structures due to abnormal morphogenesis of the optic cup and CC stalk, and the fusion of the fetal fissure (optic fissure). Isolated CC colobomas may be associated with an abnormally small eye CC (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U57317; AAC50890.2; -; mRNA. DR EMBL; BC060823; AAH60823.1; -; mRNA. DR EMBL; BC070075; AAH70075.1; -; mRNA. DR CCDS; CCDS2634.1; -. DR PIR; S71788; S71788. DR RefSeq; NP_003875.3; NM_003884.4. DR PDB; 1CM0; X-ray; 2.30 A; A/B=493-658. DR PDB; 1JM4; NMR; -; B=719-832. DR PDB; 1N72; NMR; -; A=719-832. DR PDB; 1WUG; NMR; -; A=719-832. DR PDB; 1WUM; NMR; -; A=719-832. DR PDB; 1ZS5; NMR; -; A=719-832. DR PDB; 2RNW; NMR; -; A=719-832. DR PDB; 2RNX; NMR; -; A=719-832. DR PDB; 3GG3; X-ray; 2.25 A; A/B=715-831. DR PDB; 4NSQ; X-ray; 2.31 A; A/B/C/D=493-658. DR PDB; 5FDZ; X-ray; 2.40 A; A/B=715-831. DR PDB; 5FE0; X-ray; 2.30 A; A/B=715-831. DR PDB; 5FE1; X-ray; 2.22 A; A/B=715-831. DR PDB; 5FE2; X-ray; 2.25 A; A/B=715-831. DR PDB; 5FE3; X-ray; 2.12 A; A/B=715-831. DR PDB; 5FE4; X-ray; 2.15 A; A/B=715-831. DR PDB; 5FE5; X-ray; 2.12 A; A/B=715-831. DR PDB; 5FE6; X-ray; 1.77 A; A/B=715-831. DR PDB; 5FE7; X-ray; 2.08 A; A/B=715-831. DR PDB; 5FE8; X-ray; 2.10 A; A/B=715-831. DR PDB; 5FE9; X-ray; 2.35 A; A/B=715-831. DR PDB; 5LVQ; X-ray; 2.05 A; A/B=715-831. DR PDB; 5LVR; X-ray; 2.05 A; A/B=715-831. DR PDB; 5MKX; X-ray; 1.68 A; A/B=715-831. DR PDB; 6J3O; X-ray; 2.11 A; A/B=715-831. DR PDBsum; 1CM0; -. DR PDBsum; 1JM4; -. DR PDBsum; 1N72; -. DR PDBsum; 1WUG; -. DR PDBsum; 1WUM; -. DR PDBsum; 1ZS5; -. DR PDBsum; 2RNW; -. DR PDBsum; 2RNX; -. DR PDBsum; 3GG3; -. DR PDBsum; 4NSQ; -. DR PDBsum; 5FDZ; -. DR PDBsum; 5FE0; -. DR PDBsum; 5FE1; -. DR PDBsum; 5FE2; -. DR PDBsum; 5FE3; -. DR PDBsum; 5FE4; -. DR PDBsum; 5FE5; -. DR PDBsum; 5FE6; -. DR PDBsum; 5FE7; -. DR PDBsum; 5FE8; -. DR PDBsum; 5FE9; -. DR PDBsum; 5LVQ; -. DR PDBsum; 5LVR; -. DR PDBsum; 5MKX; -. DR PDBsum; 6J3O; -. DR AlphaFoldDB; Q92831; -. DR BMRB; Q92831; -. DR SMR; Q92831; -. DR BioGRID; 114375; 244. DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex. DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant. DR ComplexPortal; CPX-989; PCAF histone acetylase complex. DR CORUM; Q92831; -. DR DIP; DIP-29778N; -. DR IntAct; Q92831; 64. DR MINT; Q92831; -. DR STRING; 9606.ENSP00000263754; -. DR BindingDB; Q92831; -. DR ChEMBL; CHEMBL5500; -. DR DrugBank; DB08186; (3E)-4-(1-METHYL-1H-INDOL-3-YL)BUT-3-EN-2-ONE. DR DrugBank; DB01992; Coenzyme A. DR DrugBank; DB08291; N-(3-AMINOPROPYL)-2-NITROBENZENAMINE. DR GuidetoPHARMACOLOGY; 2737; -. DR CarbonylDB; Q92831; -. DR iPTMnet; Q92831; -. DR PhosphoSitePlus; Q92831; -. DR BioMuta; KAT2B; -. DR DMDM; 83287776; -. DR REPRODUCTION-2DPAGE; Q92831; -. DR EPD; Q92831; -. DR jPOST; Q92831; -. DR MassIVE; Q92831; -. DR MaxQB; Q92831; -. DR PaxDb; 9606-ENSP00000263754; -. DR PeptideAtlas; Q92831; -. DR ProteomicsDB; 75508; -. DR Antibodypedia; 3865; 528 antibodies from 39 providers. DR DNASU; 8850; -. DR Ensembl; ENST00000263754.5; ENSP00000263754.4; ENSG00000114166.8. DR GeneID; 8850; -. DR KEGG; hsa:8850; -. DR MANE-Select; ENST00000263754.5; ENSP00000263754.4; NM_003884.5; NP_003875.3. DR UCSC; uc003cbq.4; human. DR AGR; HGNC:8638; -. DR CTD; 8850; -. DR DisGeNET; 8850; -. DR GeneCards; KAT2B; -. DR HGNC; HGNC:8638; KAT2B. DR HPA; ENSG00000114166; Low tissue specificity. DR MIM; 602303; gene. DR neXtProt; NX_Q92831; -. DR OpenTargets; ENSG00000114166; -. DR PharmGKB; PA162392705; -. DR VEuPathDB; HostDB:ENSG00000114166; -. DR eggNOG; KOG1472; Eukaryota. DR GeneTree; ENSGT00940000154995; -. DR HOGENOM; CLU_015901_0_0_1; -. DR InParanoid; Q92831; -. DR OMA; DFAIGYF; -. DR OrthoDB; 1760108at2759; -. DR PhylomeDB; Q92831; -. DR TreeFam; TF105399; -. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; Q92831; -. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression. DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-350054; Notch-HLH transcription pathway. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-5578768; Physiological factors. DR Reactome; R-HSA-5689901; Metalloprotease DUBs. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling. DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9617629; Regulation of FOXO transcriptional activity by acetylation. DR Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR SignaLink; Q92831; -. DR SIGNOR; Q92831; -. DR BioGRID-ORCS; 8850; 13 hits in 1186 CRISPR screens. DR ChiTaRS; KAT2B; human. DR EvolutionaryTrace; Q92831; -. DR GeneWiki; PCAF; -. DR GenomeRNAi; 8850; -. DR Pharos; Q92831; Tchem. DR PRO; PR:Q92831; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q92831; Protein. DR Bgee; ENSG00000114166; Expressed in lateral globus pallidus and 207 other cell types or tissues. DR GO; GO:0031672; C:A band; IEA:Ensembl. DR GO; GO:0042641; C:actomyosin; IEA:Ensembl. DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031674; C:I band; IEA:Ensembl. DR GO; GO:0000776; C:kinetochore; IEA:Ensembl. DR GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0000124; C:SAGA complex; NAS:UniProtKB. DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0010484; F:histone H3 acetyltransferase activity; IBA:GO_Central. DR GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0060173; P:limb development; ISS:UniProtKB. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0046600; P:negative regulation of centriole replication; IDA:UniProtKB. DR GO; GO:2000233; P:negative regulation of rRNA processing; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:BHF-UCL. DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:UniProt. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; IEA:Ensembl. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; ISS:ComplexPortal. DR GO; GO:0051302; P:regulation of cell division; ISS:ComplexPortal. DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:ComplexPortal. DR GO; GO:0045995; P:regulation of embryonic development; ISS:ComplexPortal. DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:BHF-UCL. DR GO; GO:0043484; P:regulation of RNA splicing; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:ComplexPortal. DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISS:ComplexPortal. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; TAS:Reactome. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR CDD; cd05509; Bromo_gcn5_like; 1. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR IDEAL; IID00390; -. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR037800; GCN5. DR InterPro; IPR016376; GCN5/PCAF. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR009464; PCAF_N. DR PANTHER; PTHR45750; GH11602P; 1. DR PANTHER; PTHR45750:SF2; HISTONE ACETYLTRANSFERASE KAT2B; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF06466; PCAF_N; 1. DR PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51186; GNAT; 1. DR Genevisible; Q92831; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Acyltransferase; Biological rhythms; Bromodomain; KW Cell cycle; Cytoplasm; Cytoskeleton; Disease variant; KW Host-virus interaction; Nucleus; Reference proteome; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1..832 FT /note="Histone acetyltransferase KAT2B" FT /id="PRO_0000211208" FT DOMAIN 503..651 FT /note="N-acetyltransferase" FT /evidence="ECO:0000250|UniProtKB:Q92830, FT ECO:0000255|PROSITE-ProRule:PRU00532" FT DOMAIN 740..810 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035, FT ECO:0000305" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 395..436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 706..725 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 26..40 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 395..418 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 711..725 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 570 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000303|PubMed:10393169" FT BINDING 574..576 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:10393169" FT BINDING 581..587 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:10393169" FT BINDING 612..615 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000269|PubMed:10393169" FT VARIANT 130 FT /note="V -> G (found in a patient with isolated coloboma; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:28493397" FT /id="VAR_079852" FT VARIANT 386 FT /note="N -> S (in dbSNP:rs17006625)" FT /id="VAR_034372" FT MUTAGEN 752 FT /note="V->A: Reduced acetyl-lysine binding." FT /evidence="ECO:0000269|PubMed:10365964" FT MUTAGEN 760 FT /note="Y->A: Reduced acetyl-lysine binding." FT /evidence="ECO:0000269|PubMed:10365964" FT MUTAGEN 802 FT /note="Y->A: Reduced acetyl-lysine binding." FT /evidence="ECO:0000269|PubMed:10365964" FT MUTAGEN 809 FT /note="Y->A: Complete loss of acetyl-lysine binding." FT /evidence="ECO:0000269|PubMed:10365964" FT CONFLICT 804..805 FT /note="PP -> AA (in Ref. 1; AAC50890)" FT /evidence="ECO:0000305" FT STRAND 494..499 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 509..525 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 531..538 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 543..550 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 553..563 FT /evidence="ECO:0007829|PDB:1CM0" FT TURN 564..567 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 568..576 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 578..580 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 582..584 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 585..599 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 604..609 FT /evidence="ECO:0007829|PDB:1CM0" FT TURN 611..613 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 614..618 FT /evidence="ECO:0007829|PDB:1CM0" FT TURN 619..621 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 623..625 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 630..633 FT /evidence="ECO:0007829|PDB:1CM0" FT STRAND 644..649 FT /evidence="ECO:0007829|PDB:1CM0" FT HELIX 727..741 FT /evidence="ECO:0007829|PDB:5MKX" FT STRAND 742..744 FT /evidence="ECO:0007829|PDB:1WUM" FT HELIX 746..748 FT /evidence="ECO:0007829|PDB:5MKX" FT TURN 754..756 FT /evidence="ECO:0007829|PDB:5MKX" FT STRAND 757..759 FT /evidence="ECO:0007829|PDB:1ZS5" FT HELIX 760..763 FT /evidence="ECO:0007829|PDB:5MKX" FT STRAND 764..766 FT /evidence="ECO:0007829|PDB:1JM4" FT HELIX 770..778 FT /evidence="ECO:0007829|PDB:5MKX" FT HELIX 785..802 FT /evidence="ECO:0007829|PDB:5MKX" FT STRAND 805..807 FT /evidence="ECO:0007829|PDB:1WUG" FT HELIX 808..827 FT /evidence="ECO:0007829|PDB:5MKX" FT STRAND 828..830 FT /evidence="ECO:0007829|PDB:1N72" SQ 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 //