Q8BRB7 (KAT6B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1872 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Repressor Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB nucleosome assembly Inferred from electronic annotation. Source: InterPro positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MOZ/MORF histone acetyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB nucleosome Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro 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 4 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.

Isoform 3 (identifier: Q8BRB7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     209-259: PRADPIPICS...LKFCPELTAN → VSEPGGIDAL...TLQFITVAKL
     260-1872: Missing.

Isoform 4 (identifier: Q8BRB7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     284-285: DN → VR
     286-1872: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1872	1872	Histone acetyltransferase KAT6B		PRO_0000051577
Regions
	Domain	104 – 177	74	H15
	Zinc finger	214 – 273	60	PHD-type 1
	Zinc finger	270 – 321	52	PHD-type 2
	Zinc finger	567 – 589	23	C2HC-type
	Region	362 – 535	174	Negatively regulates HAT activity By similarity
	Region	536 – 826	291	Catalytic By similarity
	Region	570 – 826	257	Interaction with BRPF1 By similarity
	Region	674 – 678	5	Acetyl-CoA binding By similarity
	Region	683 – 689	7	Acetyl-CoA binding By similarity
	Region	1359 – 1872	514	Interaction with RUNX1 and RUNX2 By similarity
	Compositional bias	888 – 896	9	Poly-Glu
	Compositional bias	899 – 908	10	Poly-Glu
	Compositional bias	1008 – 1013	6	Poly-Glu
	Compositional bias	1154 – 1175	22	Poly-Glu
	Compositional bias	1209 – 1217	9	Poly-Glu
	Compositional bias	1393 – 1562	170	Ser-rich
	Compositional bias	1760 – 1860	101	Met-rich
Sites
	Active site	633	1	By similarity
	Active site	675	1	Nucleophile By similarity
	Binding site	713	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	633	1	N6-acetyllysine; by autocatalysis By similarity
	Modified residue	856	1	N6-acetyllysine By similarity
	Modified residue	860	1	N6-acetyllysine By similarity
	Modified residue	862	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	209 – 259	51	PRADP…ELTAN → VSEPGGIDALEILLFYLSLP LRRAQPVGPNPFGKHLSPQI VTLQFITVAKL in isoform 3.		VSP_014588
	Alternative sequence	260 – 1872	1613	Missing in isoform 3.		VSP_014589
	Alternative sequence	284 – 285	2	DN → VR in isoform 4.		VSP_014590
	Alternative sequence	286 – 1872	1587	Missing in isoform 4.		VSP_014591
	Alternative sequence	374 – 482	109	Missing in isoform 2.		VSP_014592
Experimental info
	Sequence conflict	1033	1	E → Q in AAF26744. Ref.1
	Sequence conflict	1418	1	V → I in AAF26744. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 2807D9D473EE22C7	FASTA	1,872	208,526
	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
	Isoform 2 [UniParc]. Checksum: 667EEDB2F43FF958	FASTA	1,763	196,867
	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 GSPDTDIKIS IKQESADVSL VGNKELVTEE DLDVFKQAQE LSWEKIECES 430 440 450 460 470 480 GVEDCGRYPS VIEFGKYEIQ TWYSSPYPQE YARLPKLYLC EFCLKYMKSK NILLRHSKKC 490 500 510 520 530 540 GWFHPPANEI YRRKDLSVFE VDGNMSKIYC QNLCLLAKLF LDHKTLYYDV EPFLFYVLTK 550 560 570 580 590 600 NDEKGCHLVG YFSKEKLCQQ KYNVSCIMIM PQHQRQGFGR FLIDFSYLLS RREGQAGSPE 610 620 630 640 650 660 KPLSDLGRLS YLAYWKSVIL EYLYRHHERH ISIKAISRAT GMCPHDIATT LQHLHMIDRR 670 680 690 700 710 720 DGRFVIIRRE KLILGHMEKL KNCSRPNELD PESLRWTPML ISNAVVSEEE REAEKEAERL 730 740 750 760 770 780 MEQASCWEKE EQEILSSRVS SRQSSAKVQS KNKYLHSPER RPVAGERGQL LELSKESSEE 790 800 810 820 830 840 EEEEEEEDDE EEEEEEEEES IQTSPPRLTK PQSVSIKRKR PFVVKKKRGR KRRRINSSVT 850 860 870 880 890 900 TETISETTEV LNEPFDNSDE ERPMPQLEPT CEIPVEEGGR KPVLRKAFPH QPGKKRQTEE 910 920 930 940 950 960 EEGEDNHFFK TAALCRKDVD DDAEHLKEGS KDNPEPLKCR QVWPKGAKRG LSKWKQSKER 970 980 990 1000 1010 1020 KTGFKLNLYT PPETPMEPED QVTIEEQKEL SEDKGSPVGM EREVTETVDA LLPQEGSRRE 1030 1040 1050 1060 1070 1080 ETGIPVSPHK SPGGKVDEED LIRGEEEGEE EGEEEGEREE QEEEEEVTTE KDLDGAKSKE 1090 1100 1110 1120 1130 1140 NPEPEISMEK EDPVHLGDHE EDEDEEEEPS HNEDHDADDE DDGHMEAANM ERGDLPRETF 1150 1160 1170 1180 1190 1200 KDALEGQEAF LDLSIQPSHS NPEVLMNCGV DLTMSCNSEP KELAGDTGTA PESDAEPPEE 1210 1220 1230 1240 1250 1260 QTQKQDQKNS DGVDAELEEG GPAAVEIDSE TAQAVQSLTQ ENREHDDTFP DCAETQEACR 1270 1280 1290 1300 1310 1320 SLQNYTHTDQ SPQIATTLDE CQQSDHSSPV SSVHSHPGQS VRSVNSPSVP ALENSYAQIS 1330 1340 1350 1360 1370 1380 PDQTAITVPP LQNMETSPMM DVPSVSDHSQ QVVDSGFSDL GSIESTTENY ENPSSYDSTM 1390 1400 1410 1420 1430 1440 GGSICGNGSS QNSCSYSSLT SSNLTQNSCA VTQQMSNISG SCSMLQQTSI SSPPTCSVKS 1450 1460 1470 1480 1490 1500 PQGCVVERPP SSSQQLAQCS MAANFTPPMQ LADIPETSNA NIGLYERMGQ SDFGAGHYPQ 1510 1520 1530 1540 1550 1560 PSATFSLAKL QQLTNTLIDH SLPYSHSAAV TSYANSASLS TPLSNTGLVQ LSQSPHSVPG 1570 1580 1590 1600 1610 1620 GPQAQATMTP PPNLTPPPMN LPPPLLQRNM AASNIGISHS QRLQTQIASK GHVSMRTKAA 1630 1640 1650 1660 1670 1680 SLSPAAATHQ SQIYGRSQTV AMQGPARTLT MQRGMNMSVN LMPAPAYNVN SVNMNMNTLN 1690 1700 1710 1720 1730 1740 AMNGYSMSQP MMNSGYHSNH GYMNQTPQYP MQMQMGMMGS QPYAQQPMQT PPHANMMYTA 1750 1760 PGHHGYMNTG MSKQSLNGSY MRR
	Isoform 3 [UniParc]. Checksum: CC9CC22D55C9BE93	FASTA	259	28,476
	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 LLPHEKDQVS EPGGIDALEI LLFYLSLPLR RAQPVGPNPF 250 GKHLSPQIVT LQFITVAKL
	Isoform 4 [UniParc]. Checksum: 2D15D7076ABB75FE	FASTA	285	31,335
	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 CGSSGHPSCL KFCPELTANV KALRWQCIEC KTCSACRVQG KNAVR

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORMS 3 AND 4), 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. , 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. , 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.
+	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. AK052307 mRNA. Translation: BAC34930.1. AK083123 mRNA. Translation: BAC38771.1. AC115122 Genomic DNA. No translation available. AC148978 Genomic DNA. No translation available. AY294423 Genomic DNA. Translation: AAQ01512.1.
IPI	IPI00123569. IPI00457388. IPI00608081. IPI00667176.
RefSeq	NP_059507.2. NM_017479.3.
UniGene	Mm.248967.
3D structure databases
ProteinModelPortal	Q8BRB7.
SMR	Q8BRB7. Positions 212-321, 536-808.
ModBase	Search...
PTM databases
PhosphoSite	Q8BRB7.
Proteomic databases
PRIDE	Q8BRB7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000069648; ENSMUSP00000066693; ENSMUSG00000021767.
GeneID	54169.
KEGG	mmu:54169.
UCSC	uc007slf.1. mouse. uc007slj.1. mouse. uc007slk.1. mouse.
Organism-specific databases
CTD	23522.
MGI	MGI:1858746. Kat6b.
Phylogenomic databases
eggNOG	COG5027.
GeneTree	ENSGT00550000074503.
HOGENOM	HOG000234365.
HOVERGEN	HBG052563.
InParanoid	Q8BRB7.
KO	K11306.
OMA	KRKRPFV.
OrthoDB	EOG4PZJ5S.
Gene expression databases
ArrayExpress	Q8BRB7.
Bgee	Q8BRB7.
Genevestigator	Q8BRB7.
GermOnline	ENSMUSG00000021767. Mus musculus.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 3.30.40.10. 1 hit. 3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR005818. Histone_H1/H5. 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]
Pfam	PF00538. Linker_histone. 1 hit. PF01853. MOZ_SAS. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00526. H15. 1 hit. SM00249. PHD. 2 hits. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS51504. H15. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	311014.
SOURCE	Search...

Entry information

Entry name

KAT6B_MOUSE

Accession

Primary (citable) accession number: Q8BRB7
Secondary accession number(s): E9QK86 , Q7TNW5, Q8BG35, Q8C441, Q9JKX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program