ID KAT6B_MOUSE Reviewed; 1872 AA.
AC Q8BRB7; E9QK86; Q7TNW5; Q8BG35; Q8C441; Q9JKX5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 168.
DE RecName: Full=Histone acetyltransferase KAT6B;
DE EC=2.3.1.48 {ECO:0000269|PubMed:10821753};
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4;
DE Short=MYST-4;
DE AltName: Full=Protein querkopf;
GN Name=Kat6b; Synonyms=Myst4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, ENZYME ACTIVITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Brain;
RX PubMed=10821753; DOI=10.1242/dev.127.12.2537;
RA Thomas T., Voss A.K., Chowdhury K., Gruss P.;
RT "Querkopf, a MYST family histone acetyltransferase, is required for normal
RT cerebral cortex development.";
RL Development 127:2537-2548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-933 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, Heart, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 696-1872.
RC STRAIN=C57BL/6J;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=22077973; DOI=10.1016/j.ajhg.2011.10.008;
RA Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B.,
RA Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E.,
RA Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S.,
RA Smith J., Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.;
RT "Whole-exome-sequencing identifies mutations in histone acetyltransferase
RT gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo
RT syndrome.";
RL Am. J. Hum. Genet. 89:675-681(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-856 AND LYS-860, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in both
CC positive and negative regulation of transcription. Required for RUNX2-
CC dependent transcriptional activation. Component of the MOZ/MORF complex
CC which has a histone H3 acetyltransferase activity (By similarity).
CC Involved in cerebral cortex development. {ECO:0000250,
CC ECO:0000269|PubMed:10821753}.
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; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:10821753};
CC -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5,
CC KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts
CC with RUNX1 and RUNX2. {ECO:0000250|UniProtKB:Q8WYB5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BRB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRB7-2; Sequence=VSP_014592;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10821753}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the ventricular zone of the
CC developing cerebral cortex. {ECO:0000269|PubMed:10821753}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional activation while
CC the C-terminus is involved in transcriptional repression.
CC {ECO:0000250}.
CC -!- PTM: Autoacetylation at Lys-633 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- DISRUPTION PHENOTYPE: Mice have a low body weight, craniofacial
CC abnormalities, and defects in cortex development. Mice carrying a gene
CC trap insertion in the gene, produces approximately 5% of the normal
CC amount of mRNA. The hypomorphic mutant displays a number of defects
CC that mirror SBBYSS syndrome, although the phenotype is milder. Mice are
CC of normal size at birth but fail to thrive and have brain developmental
CC defects as well as craniofacial defects. Observed abnormalities include
CC short and narrow palpebral fissures, low set ears, and malocclusion.
CC Similar to individuals with SBBYSS, mice carrying the gene trap
CC insertion have long, slender feet and disproportionally long first
CC digits. {ECO:0000269|PubMed:10821753, ECO:0000269|PubMed:22077973}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33305.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC34930.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC38771.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF222800; AAF26744.1; -; mRNA.
DR EMBL; AK045188; BAC32253.2; -; mRNA.
DR EMBL; AK048336; BAC33305.1; ALT_SEQ; mRNA.
DR EMBL; AK052307; BAC34930.1; ALT_SEQ; mRNA.
DR EMBL; AK083123; BAC38771.1; ALT_SEQ; mRNA.
DR EMBL; AC115122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC148978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY294423; AAQ01512.1; -; Genomic_DNA.
DR CCDS; CCDS59615.1; -. [Q8BRB7-2]
DR RefSeq; NP_059507.2; NM_017479.3. [Q8BRB7-2]
DR RefSeq; XP_006519331.1; XM_006519268.3.
DR RefSeq; XP_017171572.1; XM_017316083.1.
DR AlphaFoldDB; Q8BRB7; -.
DR SMR; Q8BRB7; -.
DR BioGRID; 207589; 5.
DR ComplexPortal; CPX-803; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-804; MORF3 histone acetyltransferase complex.
DR ComplexPortal; CPX-805; MORF2 histone acetyltransferase complex.
DR IntAct; Q8BRB7; 1.
DR MINT; Q8BRB7; -.
DR STRING; 10090.ENSMUSP00000138377; -.
DR GlyGen; Q8BRB7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8BRB7; -.
DR PhosphoSitePlus; Q8BRB7; -.
DR MaxQB; Q8BRB7; -.
DR PaxDb; 10090-ENSMUSP00000138421; -.
DR ProteomicsDB; 269177; -. [Q8BRB7-1]
DR ProteomicsDB; 269178; -. [Q8BRB7-2]
DR Antibodypedia; 1807; 103 antibodies from 22 providers.
DR DNASU; 54169; -.
DR Ensembl; ENSMUST00000069648.14; ENSMUSP00000066693.8; ENSMUSG00000021767.20. [Q8BRB7-1]
DR Ensembl; ENSMUST00000182405.9; ENSMUSP00000138377.2; ENSMUSG00000021767.20. [Q8BRB7-2]
DR Ensembl; ENSMUST00000182855.8; ENSMUSP00000138511.2; ENSMUSG00000021767.20. [Q8BRB7-2]
DR Ensembl; ENSMUST00000182964.3; ENSMUSP00000138421.2; ENSMUSG00000021767.20. [Q8BRB7-1]
DR GeneID; 54169; -.
DR KEGG; mmu:54169; -.
DR UCSC; uc007slg.2; mouse. [Q8BRB7-2]
DR UCSC; uc007slk.1; mouse. [Q8BRB7-1]
DR AGR; MGI:1858746; -.
DR CTD; 23522; -.
DR MGI; MGI:1858746; Kat6b.
DR VEuPathDB; HostDB:ENSMUSG00000021767; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000157372; -.
DR HOGENOM; CLU_001232_1_1_1; -.
DR InParanoid; Q8BRB7; -.
DR OrthoDB; 118560at2759; -.
DR PhylomeDB; Q8BRB7; -.
DR TreeFam; TF106483; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 54169; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Kat6b; mouse.
DR PRO; PR:Q8BRB7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BRB7; Protein.
DR Bgee; ENSMUSG00000021767; Expressed in animal zygote and 78 other cell types or tissues.
DR ExpressionAtlas; Q8BRB7; baseline and differential.
DR Genevisible; Q8BRB7; MM.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0050793; P:regulation of developmental process; NAS:ComplexPortal.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:1903706; P:regulation of hemopoiesis; NAS:ComplexPortal.
DR CDD; cd15689; PHD1_MORF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF73; HISTONE ACETYLTRANSFERASE KAT6B; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS52014; SAMD1_WH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Alternative splicing;
KW Chromatin regulator; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1872
FT /note="Histone acetyltransferase KAT6B"
FT /id="PRO_0000051577"
FT DOMAIN 1..77
FT /note="SAMD1-like winged helix (WH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01358"
FT DOMAIN 104..177
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 533..807
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 214..273
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 270..321
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 566..591
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 70..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..535
FT /note="Negatively regulates HAT activity"
FT /evidence="ECO:0000250"
FT REGION 536..826
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 570..826
FT /note="Interaction with BRPF1"
FT /evidence="ECO:0000250"
FT REGION 846..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1872
FT /note="Interaction with RUNX1 and RUNX2"
FT /evidence="ECO:0000250"
FT REGION 1388..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..909
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 709
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 674..678
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 683..689
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 713
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 633
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 856
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 862
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT VAR_SEQ 374..482
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:10821753"
FT /id="VSP_014592"
FT CONFLICT 1033
FT /note="E -> Q (in Ref. 1; AAF26744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="V -> I (in Ref. 1; AAF26744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1872 AA; 208526 MW; 2807D9D473EE22C7 CRC64;
MVKLANPLYT EWILEAVQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK PTKGSKGPPC NDLRNVDWNK LLKRAIEGLE
EPNGSSLKNI EKYLRSQSDL TGTTNHPAFQ QRLRLGAKRA VNNGRLLKEG PQYRVNSGSS
DGKGAPQYPS AFPSSLPPVS LLPHEKDQPR ADPIPICSFC LGTKESNREK KPEELLSCAD
CGSSGHPSCL KFCPELTANV KALRWQCIEC KTCSACRVQG KNADNMLFCD SCDRGFHMEC
CDPPLSRMPK GMWICQVCRP KKKGRKLLHE KAAQIKRRYA KPIGRPKNKL KQRLLSVTSD
EGSMSAFTGR GSPGRGQKTK VSTTPSSGHA ASGKHSSSRL AVTDPTRPGA TTKTTTSSTY
ISASTLKVNK KTKGLIDGLT KFFTPSPDGR RSRGEIIDFS KHYRPRKKVS QKQSCTSHVL
ATDTDIKISI KQESADVSLV GNKELVTEED LDVFKQAQEL SWEKIECESG VEDCGRYPSV
IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG WFHPPANEIY
RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN DEKGCHLVGY
FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK PLSDLGRLSY
LAYWKSVILE YLYRHHERHI SIKAISRATG MCPHDIATTL QHLHMIDRRD GRFVIIRREK
LILGHMEKLK NCSRPNELDP ESLRWTPMLI SNAVVSEEER EAEKEAERLM EQASCWEKEE
QEILSSRVSS RQSSAKVQSK NKYLHSPERR PVAGERGQLL ELSKESSEEE EEEEEEDDEE
EEEEEEEESI QTSPPRLTKP QSVSIKRKRP FVVKKKRGRK RRRINSSVTT ETISETTEVL
NEPFDNSDEE RPMPQLEPTC EIPVEEGGRK PVLRKAFPHQ PGKKRQTEEE EGEDNHFFKT
AALCRKDVDD DAEHLKEGSK DNPEPLKCRQ VWPKGAKRGL SKWKQSKERK TGFKLNLYTP
PETPMEPEDQ VTIEEQKELS EDKGSPVGME REVTETVDAL LPQEGSRREE TGIPVSPHKS
PGGKVDEEDL IRGEEEGEEE GEEEGEREEQ EEEEEVTTEK DLDGAKSKEN PEPEISMEKE
DPVHLGDHEE DEDEEEEPSH NEDHDADDED DGHMEAANME RGDLPRETFK DALEGQEAFL
DLSIQPSHSN PEVLMNCGVD LTMSCNSEPK ELAGDTGTAP ESDAEPPEEQ TQKQDQKNSD
GVDAELEEGG PAAVEIDSET AQAVQSLTQE NREHDDTFPD CAETQEACRS LQNYTHTDQS
PQIATTLDEC QQSDHSSPVS SVHSHPGQSV RSVNSPSVPA LENSYAQISP DQTAITVPPL
QNMETSPMMD VPSVSDHSQQ VVDSGFSDLG SIESTTENYE NPSSYDSTMG GSICGNGSSQ
NSCSYSSLTS SNLTQNSCAV TQQMSNISGS CSMLQQTSIS SPPTCSVKSP QGCVVERPPS
SSQQLAQCSM AANFTPPMQL ADIPETSNAN IGLYERMGQS DFGAGHYPQP SATFSLAKLQ
QLTNTLIDHS LPYSHSAAVT SYANSASLST PLSNTGLVQL SQSPHSVPGG PQAQATMTPP
PNLTPPPMNL PPPLLQRNMA ASNIGISHSQ RLQTQIASKG HVSMRTKAAS LSPAAATHQS
QIYGRSQTVA MQGPARTLTM QRGMNMSVNL MPAPAYNVNS VNMNMNTLNA MNGYSMSQPM
MNSGYHSNHG YMNQTPQYPM QMQMGMMGSQ PYAQQPMQTP PHANMMYTAP GHHGYMNTGM
SKQSLNGSYM RR
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