Q9H7Z6 (KAT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT8
EC=2.3.1.48

Alternative name(s):
Lysine acetyltransferase 8
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
Short name=MYST-1
Short name=hMOF

Gene names

Name:	KAT8
Synonyms:	MOF, MYST1
ORF Names:	PP7073

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Ref.9 Ref.11 Ref.16
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.6
Subunit structure	Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with the chromodomain of MORF4L1/MRG15. Interacts with ATM through the chromodomain. Interacts with KANSL1; the interaction is direct. Ref.9 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17
Subcellular location	Nucleus. Chromosome By similarity Ref.6 Ref.16.
Post-translational modification	Autoacetylation at Lys-274 is required for proper function.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger. Contains 1 chromo domain.
Sequence caution	The sequence AAL55762.1 differs from that shown. Reason: Probable cloning artifact. The sequence AAL56648.1 differs from that shown. Reason: Frameshift at positions 23, 26 and 52.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H4-K16 acetylation Inferred from direct assay Ref.16. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.16. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.16. Source: UniProtKB myeloid cell differentiation Inferred from direct assay PubMed 11742995. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11742995. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 11742995PubMed 11965546. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from direct assay Ref.10. Source: UniProtKB MSL complex Inferred from direct assay Ref.16. Source: UniProtKB kinetochore Inferred from electronic annotation. Source: Compara
Molecular_function	histone acetyltransferase activity Inferred from direct assay PubMed 11742995. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylated histone residue binding Inferred from direct assay Ref.10. Source: UniProtKB transcription factor binding Inferred from direct assay PubMed 11742995PubMed 11965546. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MLL	Q03164	3	EBI-896414,EBI-591370
RNF2	Q99496	2	EBI-896414,EBI-722416

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H7Z6-1)

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: Q9H7Z6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     438-458: VDSVCLKWAPPKHKQVKLSKK → GGWGAAVCRGRWGSVSMWTGRSQGLLIAVT

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Histone acetyltransferase KAT8

PRO_0000051566

Regions

Domain

69 – 123

55

Chromo

Zinc finger

208 – 230

23

C2HC-type

Region

174 – 458

285

Sufficient for interaction with KANSL1

Region

324 – 330

7

Acetyl-CoA binding

Sites

Active site

274

1

Ref.19

Active site

316

1

Nucleophile By similarity

Binding site

319

1

Acetyl-CoA

Binding site

354

1

Acetyl-CoA

Amino acid modifications

Modified residue

37

1

Phosphoserine By similarity

Modified residue

42

1

Phosphoserine By similarity

Modified residue

113

1

N6-acetyllysine Ref.15

Modified residue

274

1

N6-acetyllysine; by autocatalysis Ref.18 Ref.19

Natural variations

Alternative sequence

438 – 458

21

VDSVC…KLSKK → GGWGAAVCRGRWGSVSMWTG RSQGLLIAVT in isoform 2.

VSP_014579

Experimental info

Sequence conflict

222

1

S → T in AAL55762. Ref.7

Sequence conflict

249

1

Y → H in BAB14827. Ref.1

Sequence conflict

372

1

I → N in BAB14827. Ref.1

Isoform 2:

Sequence conflict

454

1

M → I in CAH56416. Ref.8

Secondary structure

1

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458

Helix Strand Turn

Details...

Beta strand

181 – 184

4

Beta strand

187 – 190

4

Helix

199 – 203

5

Beta strand

207 – 209

3

Turn

211 – 213

3

Beta strand

216 – 218

3

Helix

220 – 229

10

Beta strand

236 – 243

8

Beta strand

246 – 252

7

Turn

253 – 255

3

Helix

257 – 268

12

Helix

274 – 277

4

Beta strand

283 – 292

10

Beta strand

295 – 305

11

Beta strand

312 – 315

4

Beta strand

317 – 319

3

Helix

321 – 323

3

Beta strand

325 – 327

3

Helix

328 – 342

15

Beta strand

347 – 349

3

Helix

355 – 372

18

Helix

383 – 389

7

Helix

393 – 402

10

Beta strand

406 – 409

4

Beta strand

412 – 415

4

Helix

419 – 427

9

Turn

429 – 431

3

Helix

440 – 442

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 66C474BE5B90E8E3	FASTA	458	52,403
	10 20 30 40 50 60 MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE PEVTVEIGET 70 80 90 100 110 120 YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ 130 140 150 160 170 180 KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD 190 200 210 220 230 240 KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI 250 260 270 280 290 300 YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 310 320 330 340 350 360 YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS 370 380 390 400 410 420 YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK 430 440 450 LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK
	Isoform 2 [UniParc]. Checksum: 69AA4F8800E393E0	FASTA	467	53,103
	10 20 30 40 50 60 MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE PEVTVEIGET 70 80 90 100 110 120 YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ 130 140 150 160 170 180 KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD 190 200 210 220 230 240 KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI 250 260 270 280 290 300 YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 310 320 330 340 350 360 YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS 370 380 390 400 410 420 YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK 430 440 450 460 LVEEHLKSAQ YKKPPITGGW GAAVCRGRWG SVSMWTGRSQ GLLIAVT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryo.
[2]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[5]	"Structure and function of the human MYST family: MOZ2, MYST1 and MYST2." Borrow J., Housman D.E. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-458 (ISOFORM 1).
[6]	"A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF." Neal K.C., Pannuti A., Smith E.R., Lucchesi J.C. Biochim. Biophys. Acta 1490:170-174(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-458 (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. Tissue: Heart.
[7]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-458 (ISOFORM 1).
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-458 (ISOFORM 2). Tissue: Uterus.
[9]	"MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation." Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M. J. Biol. Chem. 277:50860-50866(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MORF4L1, FUNCTION.
[10]	"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF." Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G. Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[11]	"Involvement of human MOF in ATM function." Gupta A., Sharma G.G., Young C.S.H., Agarwal M., Smith E.R., Paull T.T., Lucchesi J.C., Khanna K.K., Ludwig T., Pandita T.K. Mol. Cell. Biol. 25:5292-5305(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATM, FUNCTION.
[12]	"A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16." Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C. Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION OF MSL COMPLEX COMPONENTS.
[13]	Erratum Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C. Mol. Cell. Biol. 26:387-387(2006)
[14]	"Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila." Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M., Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M., Stunnenberg H.G., Saumweber H., Akhtar A. Mol. Cell 21:811-823(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KANSL1.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, MASS SPECTROMETRY.
[16]	"Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex." Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C. J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
[17]	"The nonspecific lethal complex is a transcriptional regulator in Drosophila." Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H., Kadlec J., Fraterman S., Luscombe N.M., Akhtar A. Mol. Cell 38:827-841(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KANSL1.
[18]	"Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274." Sun B., Guo S., Tang Q., Li C., Zeng R., Xiong Z., Zhong C., Ding J. Cell Res. 21:1262-1266(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 174-449 IN COMPLEX WITH ACETYL COENZYME A, ACETYLATION AT LYS-274.
[19]	"MYST protein acetyltransferase activity requires active site lysine autoacetylation." Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J., Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J., Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A., Johnson F.B. , Berger S.L., Sternglanz R., McMahon S.B., Cote J., Marmorstein R. EMBO J. 31:58-70(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 177-458, ACTIVE SITE, ACETYLATION AT LYS-274.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK021872 mRNA. Translation: BAB13924.1.
AK024102 mRNA. Translation: BAB14827.1.
AK291106 mRNA. Translation: BAF83795.1.
AC009088 Genomic DNA. No translation available.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52157.1.
CH471192 Genomic DNA. Translation: EAW52158.1.
BC037773 mRNA. Translation: AAH37773.1.
AF217501 mRNA. Translation: AAL56648.1. Frameshift.
AF260665 mRNA. Translation: AAF72665.2.
AF289578 mRNA. Translation: AAL55762.1. Sequence problems.
AL050395 mRNA. Translation: CAH56416.1.

IPI

IPI00217660.
IPI00550352.

RefSeq

NP_115564.2. NM_032188.2.
NP_892003.2. NM_182958.2.

UniGene

Hs.533803.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GIV	X-ray	1.94	A	174-449	[»]
2PQ8	X-ray	1.45	A	174-449	[»]
2Y0M	X-ray	2.70	A	174-458	[»]
3QAH	X-ray	2.10	A	174-449	[»]
3TOA	X-ray	3.00	A	177-458	[»]
3TOB	X-ray	2.70	A	177-458	[»]
4DNC	X-ray	2.05	A/B	170-458	[»]

ProteinModelPortal

Q9H7Z6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H7Z6. 8 interactions.

MINT

MINT-1897597.

PTM databases

PhosphoSite

Q9H7Z6.

Polymorphism databases

DMDM

68565938.

Proteomic databases

PaxDb

Q9H7Z6.

PRIDE

Q9H7Z6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000219797; ENSP00000219797; ENSG00000103510.
ENST00000448516; ENSP00000406037; ENSG00000103510.

GeneID

84148.

KEGG

hsa:84148.

UCSC

uc002eax.3. human.
uc002eay.3. human.

Organism-specific databases

CTD

84148.

GeneCards

GC16P031130.

HGNC

HGNC:17933. KAT8.

MIM

609912. gene.

neXtProt

NX_Q9H7Z6.

PharmGKB

PA38476.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5027.

HOVERGEN

HBG053268.

InParanoid

Q9H7Z6.

KO

K11308.

OrthoDB

EOG4933HQ.

PhylomeDB

Q9H7Z6.

Gene expression databases

ArrayExpress

Q9H7Z6.

Bgee

Q9H7Z6.

CleanEx

HS_MYST1.

Genevestigator

Q9H7Z6.

GermOnline

ENSG00000103510. Homo sapiens.

Family and domain databases

Gene3D

3.40.630.30. 1 hit.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]

Pfam

PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. False negative.
PS50013. CHROMO_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9H7Z6.

ChEMBL

CHEMBL1932912.

ChiTaRS

KAT8. human.

EvolutionaryTrace

Q9H7Z6.

GenomeRNAi

84148.

NextBio

73476.

SOURCE

Search...

Entry information

Entry name

KAT8_HUMAN

Accession

Primary (citable) accession number: Q9H7Z6
Secondary accession number(s): A8K4Z1 , G5E9P2, Q659G0, Q7LC17, Q8IY59, Q8WYB4, Q8WZ14, Q9HAC5, Q9NR35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.