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Protein

Histone acetyltransferase KAT6B

Gene

KAT6B

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei599 – 5991Proton donor/acceptorBy similarity
Binding sitei603 – 6031Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri457 – 47923C2HC-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6B (EC:2.3.1.48By similarity)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name:
MYST-4
Gene namesi
Name:KAT6B
Synonyms:MYST4
ORF Names:QflA-12408
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17841784Histone acetyltransferase KAT6BPRO_0000051576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei523 – 5231N6-acetyllysine; by autocatalysisBy similarity
Modified residuei746 – 7461N6-acetyllysineBy similarity
Modified residuei750 – 7501N6-acetyllysineBy similarity
Modified residuei752 – 7521N6-acetyllysineBy similarity

Post-translational modificationi

Autoacetylation at Lys-523 is required for proper function.By similarity

Keywords - PTMi

Acetylation

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. Interacts with RUNX1 and RUNX2.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8WML3.
SMRiQ8WML3. Positions 426-698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 17674H15PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 697275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 42565Negatively regulates HAT activityBy similarityAdd
BLAST
Regioni426 – 716291CatalyticBy similarityAdd
BLAST
Regioni460 – 716257Interaction with BRPF1By similarityAdd
BLAST
Regioni564 – 5685Acetyl-CoA bindingBy similarity
Regioni573 – 5797Acetyl-CoA bindingBy similarity
Regioni1271 – 1784514Interaction with RUNX1 and RUNX2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi778 – 81841Poly-GluAdd
BLAST
Compositional biasi918 – 9214Poly-Glu
Compositional biasi1065 – 108521Poly-GluAdd
BLAST
Compositional biasi1120 – 11289Poly-Glu
Compositional biasi1305 – 1474170Ser-richAdd
BLAST
Compositional biasi1672 – 1772101Met-richAdd
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.Curated
Contains 1 C2HC-type zinc finger.Curated
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri213 – 27260PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri269 – 32052PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri457 – 47923C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOVERGENiHBG052563.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR016024. ARM-type_fold.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WML3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ
60 70 80 90 100
LELSVQDGSV LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK STKESRGSCN
110 120 130 140 150
DLRNVDWNKL LRRAIEGLEE PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ
160 170 180 190 200
RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD GKGAPQYPSA FPSSLPPVSL
210 220 230 240 250
LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC GSSGHPSCLK
260 270 280 290 300
FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC
310 320 330 340 350
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK
360 370 380 390 400
QRLLSVTSDE GSMNAFTGRG SPDTEIKINI KQESADVNVI GNKDVVTEED
410 420 430 440 450
LDVFKQAQEL SWEKIECESG VEDCGRYPSV IEFGKYEIQT WYSSPYPQEY
460 470 480 490 500
ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG WFHPPANEIY RRKDLSVFEV
510 520 530 540 550
DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN DEKGCHLVGY
560 570 580 590 600
FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK
610 620 630 640 650
PLSDLGRLSY LAYWKSVILE YLYHHHERHI SIKAISRATG MCPHDIATTL
660 670 680 690 700
QHLHMIDKRD GGFVIIRREK LILSHMEKLK TCSRANELDP DSLRWTPILI
710 720 730 740 750
SNAAVSEEER EAEKEAERLM EQASCWEKEE QEVLSTRANS RQSPAKVQSK
760 770 780 790 800
NKYLHSPESR PVTGERGQLL ELSKESSEEE EEEEEDEEEE DEEEEEEEEE
810 820 830 840 850
DEEEEEEEEE EEEEEEEENI QSSPPRLTKP QSVAIKRKRP FVLKKKRGRK
860 870 880 890 900
RRRINSSVTT ETISETTEVL NEPFDNSDEE RPMPQLEPTC EIEVEEDGRK
910 920 930 940 950
PVLRKAFQHQ PGKKRQTEEE EGKDNHCFKN ADPCRNNMND DSRNLKEGSK
960 970 980 990 1000
DNPEPLKCKQ AWPKGTKRGL SKWRQNKERK TGFKLNLYTP PETPLEPDEQ
1010 1020 1030 1040 1050
VTVEEQKETS EGKTSPTPIS IEEEAKEAGE ALLPQEENRR QETCAPVSPN
1060 1070 1080 1090 1100
TSPGEKPEDD LIKPEEEEEE EEEEEEEEGE EEEEEGGNVE KDPDGAKSQE
1110 1120 1130 1140 1150
KEEPEISPEK EDSARLDDHE EEEEEDEEPS HNEDHDADDE DDSHMESAEV
1160 1170 1180 1190 1200
EKEELPRESF KEVLENEEAF LDLNVQPSHS NPEVLMDCGV DLTASCNSEP
1210 1220 1230 1240 1250
KELAGDPEAV PESDEEPPPG EQAQKQDQKN SKEVDTEFKE GNPATMEIDS
1260 1270 1280 1290 1300
ETVQAVQSLT QESSEQDDTF QDCAETQEAC RSLQNYTRAD QSPQIATTLD
1310 1320 1330 1340 1350
DCQQSDHSSP VSSVHSHPGQ SVRSVNSPSV PALENSYAQI SPDQSAISVP
1360 1370 1380 1390 1400
SLQNMETSPM MDVPSVSDHS QQVVDSGFSD LGSIESTTEN YENPSSYDST
1410 1420 1430 1440 1450
MGGSICGNGS SQNSCSYSNL TSSSLTQSSC AVTQQMSNIS GSCSMLQQTS
1460 1470 1480 1490 1500
ISSPPTCSVK SPQGCVVERP PSSSQQLAQC SMAANFTPPM QLAEIPETGN
1510 1520 1530 1540 1550
ANIGLYERMG QSDFGAGHYP QPSATFSLAK LQQLTNTLID HSLPYSHSAA
1560 1570 1580 1590 1600
VTSYANSASL STPLSNTGLV QLSQSPHSVP GGPQAQATMT PPPNLTPPPM
1610 1620 1630 1640 1650
NLPPPLLQRN MAASNIGISH SQRLQTQIAS KGHVSMRTKS ASLSPAAATH
1660 1670 1680 1690 1700
QSQIYGRSQT VAMQGPARTL TMQRGMNMSV NLMPAPAYNV NSVNMNMNTL
1710 1720 1730 1740 1750
NAMNGYSMSQ PMMNSGYHSN HGYMNQTPQY PMQMQMGMMG TQPYAQQPMQ
1760 1770 1780
TPPHGNMMYT APGHHGYMNT GMSKQSLNGS YMRR
Length:1,784
Mass (Da):200,154
Last modified:March 1, 2002 - v1
Checksum:iF5A93EB283D3AE17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB061870 mRNA. Translation: BAB72094.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB061870 mRNA. Translation: BAB72094.1.

3D structure databases

ProteinModelPortaliQ8WML3.
SMRiQ8WML3. Positions 426-698.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052563.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR016024. ARM-type_fold.
IPR002717. HAT_MYST-type.
IPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiKAT6B_MACFA
AccessioniPrimary (citable) accession number: Q8WML3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.