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Q5TKR9 (KAT6A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Kat6a
Synonyms:Moz, Myst3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1998 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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.

Subcellular location

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

Domain

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

Post-translational modification

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.

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Repressor
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular senescence

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

myeloid cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMOZ/MORF histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

PML body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19981998Histone acetyltransferase KAT6A
PRO_0000051574

Regions

Domain95 – 17177H15
Zinc finger199 – 25860PHD-type 1
Zinc finger255 – 30652PHD-type 2
Zinc finger536 – 55823C2HC-type
Region1 – 144144Required for activation of RUNX1-1 By similarity
Region52 – 166115Required for nuclear localization By similarity
Region144 – 662519Interaction with PML By similarity
Region312 – 662351Interaction with RUNX1-1 By similarity
Region486 – 776291Catalytic By similarity
Region505 – 808304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity By similarity
Region643 – 6475Acetyl-CoA binding By similarity
Region652 – 6587Acetyl-CoA binding By similarity
Region1510 – 1735226Interaction with PML By similarity
Region1510 – 1635126Interaction with RUNX1-2 By similarity
Region1907 – 194236Required for activation of RUNX1-2 By similarity
Compositional bias988 – 9947Poly-Glu
Compositional bias1018 – 10258Poly-Arg
Compositional bias1028 – 110679Glu-rich
Compositional bias1107 – 11137Poly-Glu
Compositional bias1141 – 116828Lys-rich
Compositional bias1231 – 12377Poly-Glu
Compositional bias1262 – 12709Poly-Glu
Compositional bias1463 – 1583121Ser-rich
Compositional bias1586 – 15905Poly-Ser
Compositional bias1593 – 169199Gln-rich
Compositional bias1665 – 16728Poly-Pro
Compositional bias1676 – 16805Poly-Pro
Compositional bias1684 – 16907Poly-Pro
Compositional bias1884 – 196481Met-rich

Sites

Active site6021 By similarity
Active site6441Nucleophile By similarity
Binding site6821Acetyl-CoA By similarity

Amino acid modifications

Modified residue1721N6-acetyllysine By similarity
Modified residue3501N6-acetyllysine By similarity
Modified residue3551N6-acetyllysine By similarity
Modified residue3691Phosphothreonine; by PKB/AKT1 By similarity
Modified residue4711Phosphoserine By similarity
Modified residue6021N6-acetyllysine; by autocatalysis By similarity
Modified residue8151N6-acetyllysine By similarity
Modified residue9001Phosphotyrosine Ref.3
Modified residue10061N6-acetyllysine By similarity
Modified residue11141Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5TKR9 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 37092EED5475855D

FASTA1,998223,331
        10         20         30         40         50         60 
MVKLANPLYT QWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRKTVLEQ LELSVKDGTI 

        70         80         90        100        110        120 
LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDNKQSVDWN KLLKRAFEGL AESGGSTLKS 

       130        140        150        160        170        180 
IERFLKSQKD VSAACGGTAA SGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAANAEGKE 

       190        200        210        220        230        240 
GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKKPEDLISC ADCGNSGHPS 

       250        260        270        280        290        300 
CLKFSPELTV RVRALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 

       310        320        330        340        350        360 
PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQSTVSK GPFSKVRTGP 

       370        380        390        400        410        420 
GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSSAPLK FNKKTKGLID GLTKFFTPSP 

       430        440        450        460        470        480 
DGRKARGEAV DYSELRIRKK GNRKSSTSHW PTDNQDGWES KQESEERLFG SQEIMTERDM 

       490        500        510        520        530        540 
ELFRDIQEQA LQKVGVTGPP DPQVRCPSVI EFGKYEIHTW YSSPYPQEYS RLPKLYLCEF 

       550        560        570        580        590        600 
CLKYMKSRTI LQQHMKKCGW FHPPANEIYR KNNISVFEVD GNVSTIYCQN LCLLAKLFLD 

       610        620        630        640        650        660 
HKTLYYDVEP FLFYVLTQND VKGCHLVGYF SKEKHCQQKY NVSCIMILPQ YQRKGYGRFL 

       670        680        690        700        710        720 
IDFSYLLSKR EGQAGSPEKP LSDLGRLSYM AYWKSVILEC LYHQNDKQIS IKKLSKLTGV 

       730        740        750        760        770        780 
CPQDITSTLH HLRMLDFRSD QFVIIRREKL IQDHMAKLQL NLRPVDVDPE CLRWTPVIVS 

       790        800        810        820        830        840 
NSVVSEEEDE EADDGEKEEP QGQERELETR ERVGKSVSRE NKDQDSSSLI ESEKKPEVKE 

       850        860        870        880        890        900 
LASSSRLSKQ ALVRDSLPAN SQPPRRGRCG RKNRKTQERF GDKDSKMLVG ETLSTSQEQY 

       910        920        930        940        950        960 
GECEEKSAAS RERYTEVGEQ PAAPQAQADG NPDIPKGRFS ESADLWRGQL KKSPETLKCR 

       970        980        990       1000       1010       1020 
LPEGNDRLPC CYTDGDRAVF RGFSESSEEE EEPESPRSNS PPVLTKPTLK RKKPILHRRR 

      1030       1040       1050       1060       1070       1080 
RVRKRKHHNS SVVTETISET TEVLDEPFED SDSERPMPRL EPTFEIEEEE EEEDENELFP 

      1090       1100       1110       1120       1130       1140 
RGYFHCLSSQ DILRCQASSK RTASKDEEEE EEESDDADDT PVLKPVSLLR KCDVNSASLE 

      1150       1160       1170       1180       1190       1200 
PDTSTPMKKK KGWPKGKSRK PIHWKKRPGR KPGFKLNQDI IAVSTQECIV EPIVPIKPGR 

      1210       1220       1230       1240       1250       1260 
KPRTQESEEL VEVKEGLVEE RKEEMHTEAD EEAEEEEDAA SSDIRAMSPL DSSNSPDADP 

      1270       1280       1290       1300       1310       1320 
KEPEAEEEEE KPLDDPRQSE EEPQELEEQE QEEEDEVTAE ANQNEDHDAD DEDDGHLDSL 

      1330       1340       1350       1360       1370       1380 
KTKEPEGQPA REDGTEEPGT QESFLDASIQ DSRENAKDKD ETEADSEEEQ PSHEASVGSE 

      1390       1400       1410       1420       1430       1440 
TMPGSEEDHE EDSNTKEELI ELKEEEEIPH SELDLETVQA VQSLTQEESS EHEGAYQDCE 

      1450       1460       1470       1480       1490       1500 
ETLAACQTLQ SYTHTDEDPQ MSMVEDCHAS EHNSPISSIP SHPSQSVRSV SSPSMPALES 

      1510       1520       1530       1540       1550       1560 
GYTQISPEQG SLSAPSMQNM ETSPMMDVPS VSDHSQQVVD SGFSDLGSIE STTENYENPS 

      1570       1580       1590       1600       1610       1620 
SYDSTMGSSI CGNNSSQSSC SYGGLSSSSS LTQNSCVVTQ QMASMGNSCS MLQQNSVQPA 

      1630       1640       1650       1660       1670       1680 
TNCNIKSPQT CVVERPPSNQ QPPPPPPPPP PPQQPQPQPQ QQAAPQPPPP QPQQQPPPPP 

      1690       1700       1710       1720       1730       1740 
QQQPQPPPPP QQQPPLSQCS MNNSFTAAPM IMEIPESGGT GNISIYERIP GDFGAGSYSQ 

      1750       1760       1770       1780       1790       1800 
PSATFSLAKL QQLTNTIMDP HAMPYSHSPA VTSYATSVSL SNTGLAQLAP SHPLAGTPQA 

      1810       1820       1830       1840       1850       1860 
QATMTPPPNL APTTMNLTSP LLQCNMSATN IGIPHTQRLQ GQMPVKGHIS IRSKSAPLPS 

      1870       1880       1890       1900       1910       1920 
ATAHQQQLYG RSPPAVAMQA GPRALAVQRG MNMGVNLMPT PAYNVNSMNM NTLNAMNSYR 

      1930       1940       1950       1960       1970       1980 
MTQPMMNSSY HSNPAYMNQT AQYPMQMQMG MMGSQAYTQQ PMQPNPHGNM MYTGPSHHSY 

      1990 
MNAAGVPKQS LNGPYMRR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03100194 Genomic DNA. No translation available.
AB195309 mRNA. Translation: BAD72833.1.
RefSeqNP_001094040.1. NM_001100570.1.
UniGeneRn.33802.

3D structure databases

ProteinModelPortalQ5TKR9.
SMRQ5TKR9. Positions 505-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000037279.

PTM databases

PhosphoSiteQ5TKR9.

Proteomic databases

PaxDbQ5TKR9.
PRIDEQ5TKR9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID306571.
KEGGrno:306571.
UCSCRGD:1304892. rat.

Organism-specific databases

CTD7994.
RGD1304892. Kat6a.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000234365.
HOVERGENHBG052563.
InParanoidQ5TKR9.
KOK11305.
OrthoDBEOG7WHH8N.
PhylomeDBQ5TKR9.
TreeFamTF106483.

Gene expression databases

GenevestigatorQ5TKR9.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
3.40.630.30. 1 hit.
InterProIPR016181. 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]
PfamPF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio656228.
PROQ5TKR9.

Entry information

Entry nameKAT6A_RAT
AccessionPrimary (citable) accession number: Q5TKR9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families