ID   KAT6A_RAT               Reviewed;        1998 AA.
AC   Q5TKR9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   24-JAN-2024, entry version 147.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-1998.
RC   STRAIN=Wistar;
RA   Ohta K., Osada S., Nishikawa J., Nishihara T.;
RT   "Cloning and characterization of a cDNA encoding histone acetyltransferase
RT   MOZ (monocytic leukemia zinc finger protein) from rat.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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}.
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. Interacts
CC       with RUNX1; phosphorylation of RUNX1 enhances the interaction.
CC       Interacts with RUNX2. Interacts with p53/TP53. Interacts with PML and
CC       this interaction positively regulates its acetylation activity towards
CC       p53/TP53. {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-602 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; AABR03100194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB195309; BAD72833.1; -; mRNA.
DR   RefSeq; NP_001094040.1; NM_001100570.2.
DR   AlphaFoldDB; Q5TKR9; -.
DR   BMRB; Q5TKR9; -.
DR   SMR; Q5TKR9; -.
DR   STRING; 10116.ENSRNOP00000037279; -.
DR   CarbonylDB; Q5TKR9; -.
DR   iPTMnet; Q5TKR9; -.
DR   PhosphoSitePlus; Q5TKR9; -.
DR   PaxDb; 10116-ENSRNOP00000037279; -.
DR   Ensembl; ENSRNOT00000078743.2; ENSRNOP00000071789.2; ENSRNOG00000025174.6.
DR   Ensembl; ENSRNOT00055012752; ENSRNOP00055010169; ENSRNOG00055007618.
DR   Ensembl; ENSRNOT00060048150; ENSRNOP00060040071; ENSRNOG00060027715.
DR   Ensembl; ENSRNOT00065013860; ENSRNOP00065010308; ENSRNOG00065008705.
DR   GeneID; 306571; -.
DR   KEGG; rno:306571; -.
DR   UCSC; RGD:1304892; rat.
DR   AGR; RGD:1304892; -.
DR   CTD; 7994; -.
DR   RGD; 1304892; Kat6a.
DR   eggNOG; KOG2747; Eukaryota.
DR   GeneTree; ENSGT00940000156962; -.
DR   InParanoid; Q5TKR9; -.
DR   OMA; ECIIEPI; -.
DR   OrthoDB; 118560at2759; -.
DR   PhylomeDB; Q5TKR9; -.
DR   TreeFam; TF106483; -.
DR   Reactome; R-RNO-3214847; HATs acetylate histones.
DR   Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
DR   PRO; PR:Q5TKR9; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISO:RGD.
DR   GO; GO:0036408; F:histone H3K14 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0043992; F:histone H3K9 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0043997; F:histone H4K12 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0046972; F:histone H4K16 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0043995; F:histone H4K5 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0043996; F:histone H4K8 acetyltransferase activity; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISO:RGD.
DR   GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR   GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR   GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
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:0010628; P:positive regulation of gene expression; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR   CDD; cd04301; NAT_SF; 1.
DR   CDD; cd15618; PHD1_MOZ_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:SF26; HISTONE ACETYLTRANSFERASE KAT6A; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF00628; PHD; 2.
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; 2.
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; 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..1998
FT                   /note="Histone acetyltransferase KAT6A"
FT                   /id="PRO_0000051574"
FT   DOMAIN          1..77
FT                   /note="SAMD1-like winged helix (WH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01358"
FT   DOMAIN          95..171
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   DOMAIN          502..776
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         199..258
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         255..306
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         535..560
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          72..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..662
FT                   /note="Interaction with PML"
FT                   /evidence="ECO:0000250"
FT   REGION          312..662
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          440..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..776
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          505..808
FT                   /note="Mediates interaction with BRPF1, required for
FT                   histone H3 acetyltransferase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          783..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1195..1436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1450..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1510..1735
FT                   /note="Interaction with PML"
FT                   /evidence="ECO:0000250"
FT   REGION          1510..1635
FT                   /note="Interaction with RUNX1-2"
FT                   /evidence="ECO:0000250"
FT   REGION          1630..1702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1907..1942
FT                   /note="Required for activation of RUNX1-2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        798..842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..903
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1028
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1171
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1201..1228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1313
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1395..1413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1471..1567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1637..1695
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        678
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         643..647
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   BINDING         652..658
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   BINDING         682
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:0000250|UniProtKB:Q8BZ21"
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         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         602
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         785
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZ21"
FT   MOD_RES         815
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZ21"
FT   MOD_RES         900
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         940
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         953
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1006
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1088
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1089
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        835
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
SQ   SEQUENCE   1998 AA;  223331 MW;  37092EED5475855D CRC64;
     MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI
     LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN KLLKRAFEGL AESGGSTLKS
     IERFLKSQKD VSAACGGTAA SGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAANAEGKE
     GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS
     CLKFSPELTV RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
     PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK GPFSKVRTGP
     GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK FNKKTKGLID GLTKFFTPSP
     DGRKARGEAV DYSELRIRKK GNRKSSTSHW PTDNQDGWES KQESEERLFG SQEIMTERDM
     ELFRDIQEQA LQKVGVTGPP DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF
     CLKYMKSRTI LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD
     HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ YQRKGYGRFL
     IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC LYHQNDKQIS IKKLSKLTGV
     CPQDITSTLH HLRMLDFRSD QFVIIRREKL IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS
     NSVVSEEEDE EADDGEKEEP QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE
     LASSSRLSKQ ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY
     GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL KKSPETLKCR
     LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS PPVLTKPTLK RKKPILHRRR
     RVRKRKHHNS SVVTETISET TEVLDEPFED SDSERPMPRL EPTFEIEEEE EEEDENELFP
     RGYFHCLSSQ DILRCQASSK RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE
     PDTSTPMKKK KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR
     KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL DSSNSPDADP
     KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE ANQNEDHDAD DEDDGHLDSL
     KTKEPEGQPA REDGTEEPGT QESFLDASIQ DSRENAKDKD ETEADSEEEQ PSHEASVGSE
     TMPGSEEDHE EDSNTKEELI ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE
     ETLAACQTLQ SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES
     GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE STTENYENPS
     SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ QMASMGNSCS MLQQNSVQPA
     TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP
     QQQPQPPPPP QQQPPLSQCS MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ
     PSATFSLAKL QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA
     QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS IRSKSAPLPS
     ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT PAYNVNSMNM NTLNAMNSYR
     MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY
     MNAAGVPKQS LNGPYMRR
//