KAT6A_MOUSE
ID KAT6A_MOUSE Reviewed; 2003 AA.
AC Q8BZ21; Q8BW52; Q8BYH1; Q8C1F3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Histone acetyltransferase KAT6A;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92794};
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3;
DE Short=MYST-3;
DE AltName: Full=Monocytic leukemia zinc finger homolog;
DE AltName: Full=Monocytic leukemia zinc finger protein;
GN Name=Kat6a; Synonyms=Moz, Myst3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1010.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, Spinal cord, and Vagina;
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 INTERACTION WITH RUNX1, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
RA Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
RT "Activation of AML1-mediated transcription by MOZ and inhibition by the
RT MOZ-CBP fusion protein.";
RL EMBO J. 20:7184-7196(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-813 AND LYS-816, 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 that acetylates lysine residues in
CC histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex
CC which has a histone H3 acetyltransferase activity. May act as a
CC transcriptional coactivator for RUNX1 and RUNX2 (By similarity).
CC Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its
CC transcriptional activity via association with PML (By similarity).
CC {ECO:0000250|UniProtKB:Q92794, ECO:0000269|PubMed:11742995}.
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:0000250|UniProtKB:Q92794};
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 (By
CC similarity). Interacts with RUNX2 (By similarity). Interacts with
CC RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts
CC with p53/TP53 (By similarity). Interacts with PML and this interaction
CC positively regulates its acetylation activity towards p53/TP53 (By
CC similarity). {ECO:0000250|UniProtKB:Q92794}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92794}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q92794}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q92794}. Note=Recruited into PML body after DNA
CC damage. {ECO:0000250|UniProtKB:Q92794}.
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: Autoacetylated. Autoacetylation at Lys-603 is required for proper
CC function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction
CC with PML and negatively regulates its acetylation activity towards
CC p53/TP53. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AC115361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK028058; BAC25728.1; -; mRNA.
DR EMBL; AK036885; BAC29621.1; -; mRNA.
DR EMBL; AK039615; BAC30401.1; -; mRNA.
DR EMBL; AK054322; BAC35729.1; -; mRNA.
DR CCDS; CCDS40294.1; -.
DR AlphaFoldDB; Q8BZ21; -.
DR BMRB; Q8BZ21; -.
DR SMR; Q8BZ21; -.
DR ComplexPortal; CPX-800; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-801; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-802; MOZ3 histone acetyltransferase complex.
DR IntAct; Q8BZ21; 1.
DR STRING; 10090.ENSMUSP00000038181; -.
DR BindingDB; Q8BZ21; -.
DR ChEMBL; CHEMBL4523382; -.
DR iPTMnet; Q8BZ21; -.
DR PhosphoSitePlus; Q8BZ21; -.
DR EPD; Q8BZ21; -.
DR jPOST; Q8BZ21; -.
DR MaxQB; Q8BZ21; -.
DR PaxDb; Q8BZ21; -.
DR PRIDE; Q8BZ21; -.
DR ProteomicsDB; 263574; -.
DR MGI; MGI:2442415; Kat6a.
DR eggNOG; KOG2747; Eukaryota.
DR InParanoid; Q8BZ21; -.
DR PhylomeDB; Q8BZ21; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR ChiTaRS; Kat6a; mouse.
DR PRO; PR:Q8BZ21; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BZ21; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR031280; KAT6A.
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:SF26; PTHR10615:SF26; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 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; Chromatin regulator;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2003
FT /note="Histone acetyltransferase KAT6A"
FT /id="PRO_0000051573"
FT DOMAIN 95..171
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 503..777
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 206..265
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 262..313
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 536..561
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..144
FT /note="Required for activation of RUNX1-1"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT REGION 52..166
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 144..663
FT /note="Interaction with PML"
FT /evidence="ECO:0000250"
FT REGION 312..663
FT /note="Interaction with RUNX1-1"
FT /evidence="ECO:0000250"
FT REGION 336..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..777
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 506..809
FT /note="Mediates interaction with BRPF1, required for
FT histone H3 acetyltransferase activity"
FT /evidence="ECO:0000250"
FT REGION 784..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1740
FT /note="Interaction with PML"
FT /evidence="ECO:0000250"
FT REGION 1511..1636
FT /note="Interaction with RUNX1-2"
FT /evidence="ECO:0000250"
FT REGION 1546..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1947
FT /note="Required for activation of RUNX1-2"
FT /evidence="ECO:0000250"
FT COMPBIAS 799..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1029
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1079
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1172
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 679
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 644..648
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 653..659
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 683
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 369
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 603
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 813
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 816
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 901
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5TKR9"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1007
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT CROSSLNK 836
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT CROSSLNK 1336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
SQ SEQUENCE 2003 AA; 224919 MW; 93D0D687A1621B31 CRC64;
MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ LELSVKDGTI
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN KLLKRAFEGL AETGGSTLKS
IERFLKSQKD VSAACGGSAA PGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAASAEGKE
GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS
CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK GPFSKVRTGP
GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK FNKKTKGLID GLTKFFTPSP
DGRKARGEVV DYSEQYRIRK KGNRKSSTSD WPTDNQDGWE SKQENEERLF GSQEIMTERD
MELFRDIQEQ ALQKVGVTGP PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE
FCLKYMKSRT ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL
DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP QYQRKGYGRF
LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE CLYHQNDKQI SIKKLSKLTG
VCPQDITSTL HHLRMLDFRS DQFVIIRREK LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV
SNSVVSEDED EEADEGEKEE PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK
ELASSSRLSK QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ
YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ LKKSPETLKC
RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN SPPILTKPTL KRKKPILHRR
RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEMEEE EEEEEEESEL
FPRGYFHCLS SQDILRCQSS SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL
EPDTSTPMKK KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG
RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP LDSSNSPEAE
PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT EANQNEDHDA DDEDEGHLDS
LKTKEPEEQP AREDDKEEPG IQGSFLAANM QDSRENTKDK DEAEPDSEED QPSHEASVVS
ETMPGSEEDH EEDSNTKEEL IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC
EETLAACQTL QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE
SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI ESTTENYENP
SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT QQMANMGNSC SMLQQNTVQP
AANCNIKSPQ TCVVERPPSN QQPPPPPPPP PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ
QQPPPPQQQP QPPPPQQQPP LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA
GSYSQPSATF SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA
GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV KGHISIRSKS
APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV NLMPTPAYNV NSMNMNTLNA
MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP
SHHSYMNAAG VPKQSLNGPY MRR
