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Q8BRB7 (KAT6B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Protein querkopf
Gene names
Name:Kat6b
Synonyms:Myst4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1872 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity By similarity. Involved in cerebral cortex development. Ref.1

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1

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.

Tissue specificity

Ubiquitously expressed. Ref.1

Developmental stage

Strongly expressed in the ventricular zone of the developing cerebral cortex. Ref.1

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-633 is required for proper function By similarity.

Disruption phenotype

Mice have a low body weight, craniofacial abnormalities, and defects in cortex development. Mice carrying a gene trap insertion in the gene, produces approximately 5% of the normal amount of mRNA. The hypomorphic mutant displays a number of defects that mirror SBBYSS syndrome, although the phenotype is milder. Mice are of normal size at birth but fail to thrive and have brain developmental defects as well as craniofacial defects. Observed abnormalities include short and narrow palpebral fissures, low set ears, and malocclusion. Similar to individuals with SBBYSS, mice carrying the gene trap insertion have long, slender feet and disproportionally long first digits. Ref.1 Ref.5

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.

Sequence caution

The sequence BAC33305.1 differs from that shown. Reason: Probable intron retention.

The sequence BAC34930.1 differs from that shown. Reason: Probable intron retention.

The sequence BAC38771.1 differs from that shown. Reason: Probable intron retention.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Repressor
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BRB7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BRB7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     374-482: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18721872Histone acetyltransferase KAT6B
PRO_0000051577

Regions

Domain104 – 17774H15
Zinc finger214 – 27360PHD-type 1
Zinc finger270 – 32152PHD-type 2
Zinc finger567 – 58923C2HC-type
Region362 – 535174Negatively regulates HAT activity By similarity
Region536 – 826291Catalytic By similarity
Region570 – 826257Interaction with BRPF1 By similarity
Region674 – 6785Acetyl-CoA binding By similarity
Region683 – 6897Acetyl-CoA binding By similarity
Region1359 – 1872514Interaction with RUNX1 and RUNX2 By similarity
Compositional bias888 – 8969Poly-Glu
Compositional bias899 – 90810Poly-Glu
Compositional bias1008 – 10136Poly-Glu
Compositional bias1154 – 117522Poly-Glu
Compositional bias1209 – 12179Poly-Glu
Compositional bias1393 – 1562170Ser-rich
Compositional bias1760 – 1860101Met-rich

Sites

Active site6331 By similarity
Active site6751Nucleophile By similarity
Binding site7131Acetyl-CoA By similarity

Amino acid modifications

Modified residue6331N6-acetyllysine; by autocatalysis By similarity
Modified residue8561N6-acetyllysine Ref.6
Modified residue8601N6-acetyllysine Ref.6
Modified residue8621N6-acetyllysine By similarity

Natural variations

Alternative sequence374 – 482109Missing in isoform 2.
VSP_014592

Experimental info

Sequence conflict10331E → Q in AAF26744. Ref.1
Sequence conflict14181V → I in AAF26744. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 2807D9D473EE22C7

FASTA1,872208,526
        10         20         30         40         50         60 
MVKLANPLYT EWILEAVQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV 

        70         80         90        100        110        120 
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK PTKGSKGPPC NDLRNVDWNK LLKRAIEGLE 

       130        140        150        160        170        180 
EPNGSSLKNI EKYLRSQSDL TGTTNHPAFQ QRLRLGAKRA VNNGRLLKEG PQYRVNSGSS 

       190        200        210        220        230        240 
DGKGAPQYPS AFPSSLPPVS LLPHEKDQPR ADPIPICSFC LGTKESNREK KPEELLSCAD 

       250        260        270        280        290        300 
CGSSGHPSCL KFCPELTANV KALRWQCIEC KTCSACRVQG KNADNMLFCD SCDRGFHMEC 

       310        320        330        340        350        360 
CDPPLSRMPK GMWICQVCRP KKKGRKLLHE KAAQIKRRYA KPIGRPKNKL KQRLLSVTSD 

       370        380        390        400        410        420 
EGSMSAFTGR GSPGRGQKTK VSTTPSSGHA ASGKHSSSRL AVTDPTRPGA TTKTTTSSTY 

       430        440        450        460        470        480 
ISASTLKVNK KTKGLIDGLT KFFTPSPDGR RSRGEIIDFS KHYRPRKKVS QKQSCTSHVL 

       490        500        510        520        530        540 
ATDTDIKISI KQESADVSLV GNKELVTEED LDVFKQAQEL SWEKIECESG VEDCGRYPSV 

       550        560        570        580        590        600 
IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG WFHPPANEIY 

       610        620        630        640        650        660 
RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN DEKGCHLVGY 

       670        680        690        700        710        720 
FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK PLSDLGRLSY 

       730        740        750        760        770        780 
LAYWKSVILE YLYRHHERHI SIKAISRATG MCPHDIATTL QHLHMIDRRD GRFVIIRREK 

       790        800        810        820        830        840 
LILGHMEKLK NCSRPNELDP ESLRWTPMLI SNAVVSEEER EAEKEAERLM EQASCWEKEE 

       850        860        870        880        890        900 
QEILSSRVSS RQSSAKVQSK NKYLHSPERR PVAGERGQLL ELSKESSEEE EEEEEEDDEE 

       910        920        930        940        950        960 
EEEEEEEESI QTSPPRLTKP QSVSIKRKRP FVVKKKRGRK RRRINSSVTT ETISETTEVL 

       970        980        990       1000       1010       1020 
NEPFDNSDEE RPMPQLEPTC EIPVEEGGRK PVLRKAFPHQ PGKKRQTEEE EGEDNHFFKT 

      1030       1040       1050       1060       1070       1080 
AALCRKDVDD DAEHLKEGSK DNPEPLKCRQ VWPKGAKRGL SKWKQSKERK TGFKLNLYTP 

      1090       1100       1110       1120       1130       1140 
PETPMEPEDQ VTIEEQKELS EDKGSPVGME REVTETVDAL LPQEGSRREE TGIPVSPHKS 

      1150       1160       1170       1180       1190       1200 
PGGKVDEEDL IRGEEEGEEE GEEEGEREEQ EEEEEVTTEK DLDGAKSKEN PEPEISMEKE 

      1210       1220       1230       1240       1250       1260 
DPVHLGDHEE DEDEEEEPSH NEDHDADDED DGHMEAANME RGDLPRETFK DALEGQEAFL 

      1270       1280       1290       1300       1310       1320 
DLSIQPSHSN PEVLMNCGVD LTMSCNSEPK ELAGDTGTAP ESDAEPPEEQ TQKQDQKNSD 

      1330       1340       1350       1360       1370       1380 
GVDAELEEGG PAAVEIDSET AQAVQSLTQE NREHDDTFPD CAETQEACRS LQNYTHTDQS 

      1390       1400       1410       1420       1430       1440 
PQIATTLDEC QQSDHSSPVS SVHSHPGQSV RSVNSPSVPA LENSYAQISP DQTAITVPPL 

      1450       1460       1470       1480       1490       1500 
QNMETSPMMD VPSVSDHSQQ VVDSGFSDLG SIESTTENYE NPSSYDSTMG GSICGNGSSQ 

      1510       1520       1530       1540       1550       1560 
NSCSYSSLTS SNLTQNSCAV TQQMSNISGS CSMLQQTSIS SPPTCSVKSP QGCVVERPPS 

      1570       1580       1590       1600       1610       1620 
SSQQLAQCSM AANFTPPMQL ADIPETSNAN IGLYERMGQS DFGAGHYPQP SATFSLAKLQ 

      1630       1640       1650       1660       1670       1680 
QLTNTLIDHS LPYSHSAAVT SYANSASLST PLSNTGLVQL SQSPHSVPGG PQAQATMTPP 

      1690       1700       1710       1720       1730       1740 
PNLTPPPMNL PPPLLQRNMA ASNIGISHSQ RLQTQIASKG HVSMRTKAAS LSPAAATHQS 

      1750       1760       1770       1780       1790       1800 
QIYGRSQTVA MQGPARTLTM QRGMNMSVNL MPAPAYNVNS VNMNMNTLNA MNGYSMSQPM 

      1810       1820       1830       1840       1850       1860 
MNSGYHSNHG YMNQTPQYPM QMQMGMMGSQ PYAQQPMQTP PHANMMYTAP GHHGYMNTGM 

      1870 
SKQSLNGSYM RR 

« Hide

Isoform 2 [UniParc].

Checksum: 667EEDB2F43FF958
Show »

FASTA1,763196,867

References

« Hide 'large scale' references
[1]"Querkopf, a MYST family histone acetyltransferase, is required for normal cerebral cortex development."
Thomas T., Voss A.K., Chowdhury K., Gruss P.
Development 127:2537-2548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ENZYME ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-933 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo, Head, Heart and Hippocampus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Genomic sequence analysis in the mouse T-complex region."
Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 696-1872.
Strain: C57BL/6J.
[5]"Whole-exome-sequencing identifies mutations in histone acetyltransferase gene KAT6B in individuals with the Say-Barber-Biesecker variant of Ohdo syndrome."
Clayton-Smith J., O'Sullivan J., Daly S., Bhaskar S., Day R., Anderson B., Voss A.K., Thomas T., Biesecker L.G., Smith P., Fryer A., Chandler K.E., Kerr B., Tassabehji M., Lynch S.A., Krajewska-Walasek M., McKee S., Smith J. expand/collapse author list , Sweeney E., Mansour S., Mohammed S., Donnai D., Black G.
Am. J. Hum. Genet. 89:675-681(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-856 AND LYS-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222800 mRNA. Translation: AAF26744.1.
AK045188 mRNA. Translation: BAC32253.2.
AK048336 mRNA. Translation: BAC33305.1. Sequence problems.
AK052307 mRNA. Translation: BAC34930.1. Sequence problems.
AK083123 mRNA. Translation: BAC38771.1. Sequence problems.
AC115122 Genomic DNA. No translation available.
AC148978 Genomic DNA. No translation available.
AY294423 Genomic DNA. Translation: AAQ01512.1.
CCDSCCDS59615.1. [Q8BRB7-2]
RefSeqNP_059507.2. NM_017479.3. [Q8BRB7-2]
XP_006519331.1. XM_006519268.1. [Q8BRB7-1]
XP_006519333.1. XM_006519270.1. [Q8BRB7-2]
UniGeneMm.248967.

3D structure databases

ProteinModelPortalQ8BRB7.
SMRQ8BRB7. Positions 212-321, 536-808.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207589. 1 interaction.

PTM databases

PhosphoSiteQ8BRB7.

Proteomic databases

PRIDEQ8BRB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069648; ENSMUSP00000066693; ENSMUSG00000021767. [Q8BRB7-1]
ENSMUST00000182405; ENSMUSP00000138377; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182855; ENSMUSP00000138511; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182964; ENSMUSP00000138421; ENSMUSG00000021767. [Q8BRB7-1]
GeneID54169.
KEGGmmu:54169.
UCSCuc007slg.2. mouse. [Q8BRB7-2]
uc007slk.1. mouse. [Q8BRB7-1]

Organism-specific databases

CTD23522.
MGIMGI:1858746. Kat6b.

Phylogenomic databases

eggNOGCOG5027.
GeneTreeENSGT00550000074503.
HOGENOMHOG000234365.
HOVERGENHBG052563.
InParanoidQ8BRB7.
KOK11306.
OMALRWTPIL.
OrthoDBEOG7WHH8N.
TreeFamTF106483.

Gene expression databases

ArrayExpressQ8BRB7.
BgeeQ8BRB7.
GenevestigatorQ8BRB7.

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.
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]
SUPFAMSSF55729. 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...

Other

NextBio311014.
PROQ8BRB7.
SOURCESearch...

Entry information

Entry nameKAT6B_MOUSE
AccessionPrimary (citable) accession number: Q8BRB7
Secondary accession number(s): E9QK86 expand/collapse secondary AC list , Q7TNW5, Q8BG35, Q8C441, Q9JKX5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 105 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot