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Q5TKR9

- KAT6A_RAT

UniProt

Q5TKR9 - KAT6A_RAT

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Protein
Histone acetyltransferase KAT6A
Gene
Kat6a, Moz, Myst3
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2 By similarity. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML By similarity.

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei602 – 6021 By similarity
Active sitei644 – 6441Nucleophile By similarity
Binding sitei682 – 6821Acetyl-CoA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri199 – 25860PHD-type 1
Add
BLAST
Zinc fingeri255 – 30652PHD-type 2
Add
BLAST
Zinc fingeri536 – 55823C2HC-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. acetyltransferase activity Source: UniProtKB
  3. histone acetyltransferase activity Source: UniProtKB
  4. transcription factor binding Source: UniProtKB
  5. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular senescence Source: UniProtKB
  2. histone H3 acetylation Source: UniProtKB
  3. histone acetylation Source: UniProtKB
  4. myeloid cell differentiation Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. nucleosome assembly Source: InterPro
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. protein acetylation Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198384. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6A (EC:2.3.1.48)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
Short name:
MYST-3
Monocytic leukemia zinc finger homolog
Monocytic leukemia zinc finger protein
Gene namesi
Name:Kat6a
Synonyms:Moz, Myst3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1304892. Kat6a.

Subcellular locationi

Nucleus By similarity. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. NucleusPML body By similarity
Note: Recruited into PML body after DNA damage By similarity.

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. PML body Source: UniProtKB
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleosome Source: InterPro
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19981998Histone acetyltransferase KAT6A
PRO_0000051574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721N6-acetyllysine By similarity
Modified residuei350 – 3501N6-acetyllysine By similarity
Modified residuei355 – 3551N6-acetyllysine By similarity
Modified residuei369 – 3691Phosphothreonine; by PKB/AKT1 By similarity
Modified residuei471 – 4711Phosphoserine By similarity
Modified residuei602 – 6021N6-acetyllysine; by autocatalysis By similarity
Modified residuei815 – 8151N6-acetyllysine By similarity
Modified residuei900 – 9001Phosphotyrosine1 Publication
Modified residuei1006 – 10061N6-acetyllysine By similarity
Modified residuei1114 – 11141Phosphoserine By similarity

Post-translational modificationi

Autoacetylated. Autoacetylation at Lys-602 is required for proper function By similarity.
Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5TKR9.
PRIDEiQ5TKR9.

PTM databases

PhosphoSiteiQ5TKR9.

Expressioni

Gene expression databases

GenevestigatoriQ5TKR9.

Interactioni

Subunit structurei

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 By similarity. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction By similarity. Interacts with RUNX2 By similarity. Interacts with p53/TP53 By similarity. Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53 By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037279.

Structurei

3D structure databases

ProteinModelPortaliQ5TKR9.
SMRiQ5TKR9. Positions 505-777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 17177H15
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 144144Required for activation of RUNX1-1 By similarity
Add
BLAST
Regioni52 – 166115Required for nuclear localization By similarity
Add
BLAST
Regioni144 – 662519Interaction with PML By similarity
Add
BLAST
Regioni312 – 662351Interaction with RUNX1-1 By similarity
Add
BLAST
Regioni486 – 776291Catalytic By similarity
Add
BLAST
Regioni505 – 808304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity By similarity
Add
BLAST
Regioni643 – 6475Acetyl-CoA binding By similarity
Regioni652 – 6587Acetyl-CoA binding By similarity
Regioni1510 – 1735226Interaction with PML By similarity
Add
BLAST
Regioni1510 – 1635126Interaction with RUNX1-2 By similarity
Add
BLAST
Regioni1907 – 194236Required for activation of RUNX1-2 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi988 – 9947Poly-Glu
Compositional biasi1018 – 10258Poly-Arg
Compositional biasi1028 – 110679Glu-rich
Add
BLAST
Compositional biasi1107 – 11137Poly-Glu
Compositional biasi1141 – 116828Lys-rich
Add
BLAST
Compositional biasi1231 – 12377Poly-Glu
Compositional biasi1262 – 12709Poly-Glu
Compositional biasi1463 – 1583121Ser-rich
Add
BLAST
Compositional biasi1586 – 15905Poly-Ser
Compositional biasi1593 – 169199Gln-rich
Add
BLAST
Compositional biasi1665 – 16728Poly-Pro
Compositional biasi1676 – 16805Poly-Pro
Compositional biasi1684 – 16907Poly-Pro
Compositional biasi1884 – 196481Met-rich
Add
BLAST

Domaini

The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression By similarity.

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ5TKR9.
KOiK11305.
OrthoDBiEOG7WHH8N.
PhylomeDBiQ5TKR9.
TreeFamiTF106483.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5TKR9-1 [UniParc]FASTAAdd to Basket

« Hide

MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ     50
LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN 100
KLLKRAFEGL AESGGSTLKS IERFLKSQKD VSAACGGTAA SGFHQQLRLA 150
IKRAVGHGRL LKDGPLYRLN TKAANAEGKE GCESLSCLPP VSLLPHEKDK 200
PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS CLKFSPELTV 250
RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK 350
GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK 400
FNKKTKGLID GLTKFFTPSP DGRKARGEAV DYSELRIRKK GNRKSSTSHW 450
PTDNQDGWES KQESEERLFG SQEIMTERDM ELFRDIQEQA LQKVGVTGPP 500
DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF CLKYMKSRTI 550
LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD 600
HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ 650
YQRKGYGRFL IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC 700
LYHQNDKQIS IKKLSKLTGV CPQDITSTLH HLRMLDFRSD QFVIIRREKL 750
IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS NSVVSEEEDE EADDGEKEEP 800
QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE LASSSRLSKQ 850
ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY 900
GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL 950
KKSPETLKCR LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS 1000
PPVLTKPTLK RKKPILHRRR RVRKRKHHNS SVVTETISET TEVLDEPFED 1050
SDSERPMPRL EPTFEIEEEE EEEDENELFP RGYFHCLSSQ DILRCQASSK 1100
RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE PDTSTPMKKK 1150
KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR 1200
KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL 1250
DSSNSPDADP KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE 1300
ANQNEDHDAD DEDDGHLDSL KTKEPEGQPA REDGTEEPGT QESFLDASIQ 1350
DSRENAKDKD ETEADSEEEQ PSHEASVGSE TMPGSEEDHE EDSNTKEELI 1400
ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE ETLAACQTLQ 1450
SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES 1500
GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE 1550
STTENYENPS SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ 1600
QMASMGNSCS MLQQNSVQPA TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP 1650
PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP QQQPQPPPPP QQQPPLSQCS 1700
MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ PSATFSLAKL 1750
QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA 1800
QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS 1850
IRSKSAPLPS ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT 1900
PAYNVNSMNM NTLNAMNSYR MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG 1950
MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY MNAAGVPKQS LNGPYMRR 1998
Length:1,998
Mass (Da):223,331
Last modified:July 5, 2005 - v2
Checksum:i37092EED5475855D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03100194 Genomic DNA. No translation available.
AB195309 mRNA. Translation: BAD72833.1.
RefSeqiNP_001094040.1. NM_001100570.1.
UniGeneiRn.33802.

Genome annotation databases

GeneIDi306571.
KEGGirno:306571.
UCSCiRGD:1304892. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03100194 Genomic DNA. No translation available.
AB195309 mRNA. Translation: BAD72833.1 .
RefSeqi NP_001094040.1. NM_001100570.1.
UniGenei Rn.33802.

3D structure databases

ProteinModelPortali Q5TKR9.
SMRi Q5TKR9. Positions 505-777.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000037279.

PTM databases

PhosphoSitei Q5TKR9.

Proteomic databases

PaxDbi Q5TKR9.
PRIDEi Q5TKR9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 306571.
KEGGi rno:306571.
UCSCi RGD:1304892. rat.

Organism-specific databases

CTDi 7994.
RGDi 1304892. Kat6a.

Phylogenomic databases

eggNOGi COG5027.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q5TKR9.
KOi K11305.
OrthoDBi EOG7WHH8N.
PhylomeDBi Q5TKR9.
TreeFami TF106483.

Enzyme and pathway databases

Reactomei REACT_198384. HATs acetylate histones.

Miscellaneous databases

NextBioi 656228.
PROi Q5TKR9.

Gene expression databases

Genevestigatori Q5TKR9.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEi PS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Cloning and characterization of a cDNA encoding histone acetyltransferase MOZ (monocytic leukemia zinc finger protein) from rat."
    Ohta K., Osada S., Nishikawa J., Nishihara T.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1998.
    Strain: Wistar.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAT6A_RAT
AccessioniPrimary (citable) accession number: Q5TKR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: September 3, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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