Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BRB7

- KAT6B_MOUSE

UniProt

Q8BRB7 - KAT6B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone acetyltransferase KAT6B

Gene

Kat6b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei709 – 7091Proton donor/acceptorBy similarity
Binding sitei713 – 7131Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri214 – 27360PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32152PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri567 – 58923C2HC-typeAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. histone acetylation Source: UniProtKB
  2. histone H3 acetylation Source: UniProtKB
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. nucleosome assembly Source: InterPro
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. 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_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT6B (EC:2.3.1.481 Publication)
Alternative name(s):
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4
Short name:
MYST-4
Protein querkopf
Gene namesi
Name:Kat6b
Synonyms:Myst4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1858746. Kat6b.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. nucleosome Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18721872Histone acetyltransferase KAT6BPRO_0000051577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei633 – 6331N6-acetyllysine; by autocatalysisBy similarity
Modified residuei856 – 8561N6-acetyllysine1 Publication
Modified residuei860 – 8601N6-acetyllysine1 Publication
Modified residuei862 – 8621N6-acetyllysineBy similarity

Post-translational modificationi

Autoacetylation at Lys-633 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BRB7.
PRIDEiQ8BRB7.

PTM databases

PhosphoSiteiQ8BRB7.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ8BRB7.
ExpressionAtlasiQ8BRB7. baseline.
GenevestigatoriQ8BRB7.

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

Protein-protein interaction databases

BioGridi207589. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8BRB7.
SMRiQ8BRB7. Positions 212-321, 536-808.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 17774H15PROSITE-ProRule annotationAdd
BLAST
Domaini533 – 807275MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni362 – 535174Negatively regulates HAT activityBy similarityAdd
BLAST
Regioni536 – 826291CatalyticBy similarityAdd
BLAST
Regioni570 – 826257Interaction with BRPF1By similarityAdd
BLAST
Regioni674 – 6785Acetyl-CoA bindingBy similarity
Regioni683 – 6897Acetyl-CoA bindingBy similarity
Regioni1359 – 1872514Interaction with RUNX1 and RUNX2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi888 – 8969Poly-Glu
Compositional biasi899 – 90810Poly-Glu
Compositional biasi1008 – 10136Poly-Glu
Compositional biasi1154 – 117522Poly-GluAdd
BLAST
Compositional biasi1209 – 12179Poly-Glu
Compositional biasi1393 – 1562170Ser-richAdd
BLAST
Compositional biasi1760 – 1860101Met-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 fingeri214 – 27360PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri270 – 32152PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri567 – 58923C2HC-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000234365.
HOVERGENiHBG052563.
InParanoidiQ8BRB7.
KOiK11306.
OMAiLRWTPIL.
OrthoDBiEOG7WHH8N.
TreeFamiTF106483.

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.
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]
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]
SUPFAMiSSF55729. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BRB7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVKLANPLYT EWILEAVQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ
60 70 80 90 100
LELSVQDGSV LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK PTKGSKGPPC
110 120 130 140 150
NDLRNVDWNK LLKRAIEGLE EPNGSSLKNI EKYLRSQSDL TGTTNHPAFQ
160 170 180 190 200
QRLRLGAKRA VNNGRLLKEG PQYRVNSGSS DGKGAPQYPS AFPSSLPPVS
210 220 230 240 250
LLPHEKDQPR ADPIPICSFC LGTKESNREK KPEELLSCAD CGSSGHPSCL
260 270 280 290 300
KFCPELTANV KALRWQCIEC KTCSACRVQG KNADNMLFCD SCDRGFHMEC
310 320 330 340 350
CDPPLSRMPK GMWICQVCRP KKKGRKLLHE KAAQIKRRYA KPIGRPKNKL
360 370 380 390 400
KQRLLSVTSD EGSMSAFTGR GSPGRGQKTK VSTTPSSGHA ASGKHSSSRL
410 420 430 440 450
AVTDPTRPGA TTKTTTSSTY ISASTLKVNK KTKGLIDGLT KFFTPSPDGR
460 470 480 490 500
RSRGEIIDFS KHYRPRKKVS QKQSCTSHVL ATDTDIKISI KQESADVSLV
510 520 530 540 550
GNKELVTEED LDVFKQAQEL SWEKIECESG VEDCGRYPSV IEFGKYEIQT
560 570 580 590 600
WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG WFHPPANEIY
610 620 630 640 650
RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN
660 670 680 690 700
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR
710 720 730 740 750
REGQAGSPEK PLSDLGRLSY LAYWKSVILE YLYRHHERHI SIKAISRATG
760 770 780 790 800
MCPHDIATTL QHLHMIDRRD GRFVIIRREK LILGHMEKLK NCSRPNELDP
810 820 830 840 850
ESLRWTPMLI SNAVVSEEER EAEKEAERLM EQASCWEKEE QEILSSRVSS
860 870 880 890 900
RQSSAKVQSK NKYLHSPERR PVAGERGQLL ELSKESSEEE EEEEEEDDEE
910 920 930 940 950
EEEEEEEESI QTSPPRLTKP QSVSIKRKRP FVVKKKRGRK RRRINSSVTT
960 970 980 990 1000
ETISETTEVL NEPFDNSDEE RPMPQLEPTC EIPVEEGGRK PVLRKAFPHQ
1010 1020 1030 1040 1050
PGKKRQTEEE EGEDNHFFKT AALCRKDVDD DAEHLKEGSK DNPEPLKCRQ
1060 1070 1080 1090 1100
VWPKGAKRGL SKWKQSKERK TGFKLNLYTP PETPMEPEDQ VTIEEQKELS
1110 1120 1130 1140 1150
EDKGSPVGME REVTETVDAL LPQEGSRREE TGIPVSPHKS PGGKVDEEDL
1160 1170 1180 1190 1200
IRGEEEGEEE GEEEGEREEQ EEEEEVTTEK DLDGAKSKEN PEPEISMEKE
1210 1220 1230 1240 1250
DPVHLGDHEE DEDEEEEPSH NEDHDADDED DGHMEAANME RGDLPRETFK
1260 1270 1280 1290 1300
DALEGQEAFL DLSIQPSHSN PEVLMNCGVD LTMSCNSEPK ELAGDTGTAP
1310 1320 1330 1340 1350
ESDAEPPEEQ TQKQDQKNSD GVDAELEEGG PAAVEIDSET AQAVQSLTQE
1360 1370 1380 1390 1400
NREHDDTFPD CAETQEACRS LQNYTHTDQS PQIATTLDEC QQSDHSSPVS
1410 1420 1430 1440 1450
SVHSHPGQSV RSVNSPSVPA LENSYAQISP DQTAITVPPL QNMETSPMMD
1460 1470 1480 1490 1500
VPSVSDHSQQ VVDSGFSDLG SIESTTENYE NPSSYDSTMG GSICGNGSSQ
1510 1520 1530 1540 1550
NSCSYSSLTS SNLTQNSCAV TQQMSNISGS CSMLQQTSIS SPPTCSVKSP
1560 1570 1580 1590 1600
QGCVVERPPS SSQQLAQCSM AANFTPPMQL ADIPETSNAN IGLYERMGQS
1610 1620 1630 1640 1650
DFGAGHYPQP SATFSLAKLQ QLTNTLIDHS LPYSHSAAVT SYANSASLST
1660 1670 1680 1690 1700
PLSNTGLVQL SQSPHSVPGG PQAQATMTPP PNLTPPPMNL PPPLLQRNMA
1710 1720 1730 1740 1750
ASNIGISHSQ RLQTQIASKG HVSMRTKAAS LSPAAATHQS QIYGRSQTVA
1760 1770 1780 1790 1800
MQGPARTLTM QRGMNMSVNL MPAPAYNVNS VNMNMNTLNA MNGYSMSQPM
1810 1820 1830 1840 1850
MNSGYHSNHG YMNQTPQYPM QMQMGMMGSQ PYAQQPMQTP PHANMMYTAP
1860 1870
GHHGYMNTGM SKQSLNGSYM RR
Length:1,872
Mass (Da):208,526
Last modified:July 27, 2011 - v3
Checksum:i2807D9D473EE22C7
GO
Isoform 2 (identifier: Q8BRB7-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,763
Mass (Da):196,867
Checksum:i667EEDB2F43FF958
GO

Sequence cautioni

The sequence BAC33305.1 differs from that shown. Reason: Probable intron retention.Curated
The sequence BAC34930.1 differs from that shown. Reason: Probable intron retention.Curated
The sequence BAC38771.1 differs from that shown. Reason: Probable intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1033 – 10331E → Q in AAF26744. (PubMed:10821753)Curated
Sequence conflicti1418 – 14181V → I in AAF26744. (PubMed:10821753)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei374 – 482109Missing in isoform 2. 1 PublicationVSP_014592Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS59615.1. [Q8BRB7-2]
RefSeqiNP_059507.2. NM_017479.3. [Q8BRB7-2]
XP_006519331.1. XM_006519268.1. [Q8BRB7-1]
XP_006519333.1. XM_006519270.1. [Q8BRB7-2]
UniGeneiMm.248967.

Genome annotation databases

EnsembliENSMUST00000069648; ENSMUSP00000066693; ENSMUSG00000021767. [Q8BRB7-1]
ENSMUST00000182405; ENSMUSP00000138377; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182855; ENSMUSP00000138511; ENSMUSG00000021767. [Q8BRB7-2]
ENSMUST00000182964; ENSMUSP00000138421; ENSMUSG00000021767. [Q8BRB7-1]
GeneIDi54169.
KEGGimmu:54169.
UCSCiuc007slg.2. mouse. [Q8BRB7-2]
uc007slk.1. mouse. [Q8BRB7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS59615.1. [Q8BRB7-2 ]
RefSeqi NP_059507.2. NM_017479.3. [Q8BRB7-2 ]
XP_006519331.1. XM_006519268.1. [Q8BRB7-1 ]
XP_006519333.1. XM_006519270.1. [Q8BRB7-2 ]
UniGenei Mm.248967.

3D structure databases

ProteinModelPortali Q8BRB7.
SMRi Q8BRB7. Positions 212-321, 536-808.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207589. 1 interaction.

PTM databases

PhosphoSitei Q8BRB7.

Proteomic databases

MaxQBi Q8BRB7.
PRIDEi Q8BRB7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069648 ; ENSMUSP00000066693 ; ENSMUSG00000021767 . [Q8BRB7-1 ]
ENSMUST00000182405 ; ENSMUSP00000138377 ; ENSMUSG00000021767 . [Q8BRB7-2 ]
ENSMUST00000182855 ; ENSMUSP00000138511 ; ENSMUSG00000021767 . [Q8BRB7-2 ]
ENSMUST00000182964 ; ENSMUSP00000138421 ; ENSMUSG00000021767 . [Q8BRB7-1 ]
GeneIDi 54169.
KEGGi mmu:54169.
UCSCi uc007slg.2. mouse. [Q8BRB7-2 ]
uc007slk.1. mouse. [Q8BRB7-1 ]

Organism-specific databases

CTDi 23522.
MGIi MGI:1858746. Kat6b.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000234365.
HOVERGENi HBG052563.
InParanoidi Q8BRB7.
KOi K11306.
OMAi LRWTPIL.
OrthoDBi EOG7WHH8N.
TreeFami TF106483.

Enzyme and pathway databases

Reactomei REACT_226917. HATs acetylate histones.

Miscellaneous databases

NextBioi 311014.
PROi Q8BRB7.
SOURCEi Search...

Gene expression databases

Bgeei Q8BRB7.
ExpressionAtlasi Q8BRB7. baseline.
Genevestigatori Q8BRB7.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.30.40.10. 1 hit.
3.40.630.30. 1 hit.
InterProi IPR016181. 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 ]
Pfami PF00538. Linker_histone. 1 hit.
PF01853. MOZ_SAS. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00526. H15. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS51504. H15. 1 hit.
PS51726. MYST_HAT. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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.

Entry informationi

Entry nameiKAT6B_MOUSE
AccessioniPrimary (citable) accession number: Q8BRB7
Secondary accession number(s): E9QK86
, Q7TNW5, Q8BG35, Q8C441, Q9JKX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 108 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3