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Q8WML3 (KAT6B_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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 KAT6B

EC=2.3.1.48
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name=MYST-4
Gene names
Name:KAT6B
Synonyms:MYST4
ORF Names:QflA-12408
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length1784 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity 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 and RUNX2 By similarity.

Subcellular location

Nucleus Probable.

Domain

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

Post-translational modification

Autoacetylated By similarity.

Autoacetylation at Lys-523 is required for proper function 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
Gene Ontology (GO)
   Biological_processhistone H3 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetylation

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

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMOZ/MORF histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleosome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

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 electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17841784Histone acetyltransferase KAT6B
PRO_0000051576

Regions

Domain103 – 17674H15
Zinc finger213 – 27260PHD-type 1
Zinc finger269 – 32052PHD-type 2
Zinc finger457 – 47923C2HC-type
Region361 – 42565Negatively regulates HAT activity By similarity
Region426 – 716291Catalytic By similarity
Region460 – 716257Interaction with BRPF1 By similarity
Region564 – 5685Acetyl-CoA binding By similarity
Region573 – 5797Acetyl-CoA binding By similarity
Region1271 – 1784514Interaction with RUNX1 and RUNX2 By similarity
Compositional bias778 – 81841Poly-Glu
Compositional bias918 – 9214Poly-Glu
Compositional bias1065 – 108521Poly-Glu
Compositional bias1120 – 11289Poly-Glu
Compositional bias1305 – 1474170Ser-rich
Compositional bias1672 – 1772101Met-rich

Sites

Active site5231 By similarity
Active site5651Nucleophile By similarity
Binding site6031Acetyl-CoA By similarity

Amino acid modifications

Modified residue5231N6-acetyllysine; by autocatalysis By similarity
Modified residue7461N6-acetyllysine By similarity
Modified residue7501N6-acetyllysine By similarity
Modified residue7521N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WML3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: F5A93EB283D3AE17

FASTA1,784200,154
        10         20         30         40         50         60 
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 

        70         80         90        100        110        120 
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK STKESRGSCN DLRNVDWNKL LRRAIEGLEE 

       130        140        150        160        170        180 
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD 

       190        200        210        220        230        240 
GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC 

       250        260        270        280        290        300 
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC 

       310        320        330        340        350        360 
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE 

       370        380        390        400        410        420 
GSMNAFTGRG SPDTEIKINI KQESADVNVI GNKDVVTEED LDVFKQAQEL SWEKIECESG 

       430        440        450        460        470        480 
VEDCGRYPSV IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG 

       490        500        510        520        530        540 
WFHPPANEIY RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN 

       550        560        570        580        590        600 
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK 

       610        620        630        640        650        660 
PLSDLGRLSY LAYWKSVILE YLYHHHERHI SIKAISRATG MCPHDIATTL QHLHMIDKRD 

       670        680        690        700        710        720 
GGFVIIRREK LILSHMEKLK TCSRANELDP DSLRWTPILI SNAAVSEEER EAEKEAERLM 

       730        740        750        760        770        780 
EQASCWEKEE QEVLSTRANS RQSPAKVQSK NKYLHSPESR PVTGERGQLL ELSKESSEEE 

       790        800        810        820        830        840 
EEEEEDEEEE DEEEEEEEEE DEEEEEEEEE EEEEEEEENI QSSPPRLTKP QSVAIKRKRP 

       850        860        870        880        890        900 
FVLKKKRGRK RRRINSSVTT ETISETTEVL NEPFDNSDEE RPMPQLEPTC EIEVEEDGRK 

       910        920        930        940        950        960 
PVLRKAFQHQ PGKKRQTEEE EGKDNHCFKN ADPCRNNMND DSRNLKEGSK DNPEPLKCKQ 

       970        980        990       1000       1010       1020 
AWPKGTKRGL SKWRQNKERK TGFKLNLYTP PETPLEPDEQ VTVEEQKETS EGKTSPTPIS 

      1030       1040       1050       1060       1070       1080 
IEEEAKEAGE ALLPQEENRR QETCAPVSPN TSPGEKPEDD LIKPEEEEEE EEEEEEEEGE 

      1090       1100       1110       1120       1130       1140 
EEEEEGGNVE KDPDGAKSQE KEEPEISPEK EDSARLDDHE EEEEEDEEPS HNEDHDADDE 

      1150       1160       1170       1180       1190       1200 
DDSHMESAEV EKEELPRESF KEVLENEEAF LDLNVQPSHS NPEVLMDCGV DLTASCNSEP 

      1210       1220       1230       1240       1250       1260 
KELAGDPEAV PESDEEPPPG EQAQKQDQKN SKEVDTEFKE GNPATMEIDS ETVQAVQSLT 

      1270       1280       1290       1300       1310       1320 
QESSEQDDTF QDCAETQEAC RSLQNYTRAD QSPQIATTLD DCQQSDHSSP VSSVHSHPGQ 

      1330       1340       1350       1360       1370       1380 
SVRSVNSPSV PALENSYAQI SPDQSAISVP SLQNMETSPM MDVPSVSDHS QQVVDSGFSD 

      1390       1400       1410       1420       1430       1440 
LGSIESTTEN YENPSSYDST MGGSICGNGS SQNSCSYSNL TSSSLTQSSC AVTQQMSNIS 

      1450       1460       1470       1480       1490       1500 
GSCSMLQQTS ISSPPTCSVK SPQGCVVERP PSSSQQLAQC SMAANFTPPM QLAEIPETGN 

      1510       1520       1530       1540       1550       1560 
ANIGLYERMG QSDFGAGHYP QPSATFSLAK LQQLTNTLID HSLPYSHSAA VTSYANSASL 

      1570       1580       1590       1600       1610       1620 
STPLSNTGLV QLSQSPHSVP GGPQAQATMT PPPNLTPPPM NLPPPLLQRN MAASNIGISH 

      1630       1640       1650       1660       1670       1680 
SQRLQTQIAS KGHVSMRTKS ASLSPAAATH QSQIYGRSQT VAMQGPARTL TMQRGMNMSV 

      1690       1700       1710       1720       1730       1740 
NLMPAPAYNV NSVNMNMNTL NAMNGYSMSQ PMMNSGYHSN HGYMNQTPQY PMQMQMGMMG 

      1750       1760       1770       1780 
TQPYAQQPMQ TPPHGNMMYT APGHHGYMNT GMSKQSLNGS YMRR 

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References

[1]"Isolation of full-length cDNA clones from macaque brain cDNA libraries."
Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Terao K., Hirai M., Sugano S., Hashimoto K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Frontal cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB061870 mRNA. Translation: BAB72094.1.

3D structure databases

ProteinModelPortalQ8WML3.
SMRQ8WML3. Positions 426-698.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052563.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR016024. ARM-type_fold.
IPR005818. Histone_H1/H5_H15.
IPR002717. MOZ_SAS.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS51504. H15. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAT6B_MACFA
AccessionPrimary (citable) accession number: Q8WML3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 73 of the entry and version 1 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