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Q9H7Z6 (KAT8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.17 Ref.20 Ref.22

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.6 Ref.20 Ref.22

Subunit structure

Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Interacts with MSL1; the interaction is direct. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KANSL1; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, 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.17 Ref.18 Ref.20 Ref.22

Subcellular location

Nucleus. Chromosome By similarity Ref.6 Ref.17.

Post-translational modification

Autoacetylation at Lys-274 is required for proper function. Ref.20 Ref.21 Ref.22 Ref.23

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 processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Acyltransferase
Chromatin regulator
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H4-K16 acetylation

Inferred from direct assay Ref.17. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.17. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.17. Source: UniProtKB

histone acetylation

Inferred from direct assay PubMed 11742995. Source: UniProtKB

myeloid cell differentiation

Inferred from direct assay PubMed 11742995. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11742995. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11742995PubMed 11965546. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.10. Source: UniProtKB

MSL complex

Inferred from direct assay Ref.17. Source: UniProtKB

histone acetyltransferase complex

Inferred from direct assay Ref.17. Source: UniProtKB

kinetochore

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11742995. Source: UniProtKB

   Molecular_functionacetyltransferase activity

Inferred from direct assay PubMed 11742995. Source: UniProtKB

histone acetyltransferase activity

Inferred from direct assay PubMed 11742995. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylated histone binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11965546Ref.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

HHF2P023092EBI-896414,EBI-8113From a different organism.
KMT2AQ031643EBI-896414,EBI-591370
RNF2Q994962EBI-896414,EBI-722416
TP53P046372EBI-896414,EBI-366083

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 → GGWGAAVCRGRWGSVSIWTGRSQGLLIAVT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 458457Histone acetyltransferase KAT8
PRO_0000051566

Regions

Domain69 – 12355Chromo
Zinc finger208 – 23023C2HC-type
Region174 – 458285Sufficient for interaction with KANSL1
Region324 – 3307Acetyl-CoA binding

Sites

Active site2741 Ref.22 Ref.23
Active site3501Proton donor/acceptor Probable
Binding site3191Acetyl-CoA
Binding site3541Acetyl-CoA
Binding site3631Acetyl-CoA
Binding site4321Acetyl-CoA

Amino acid modifications

Modified residue21N-acetylalanine Ref.15 Ref.19
Modified residue1131N6-acetyllysine Ref.16
Modified residue2741N6-acetyllysine; by autocatalysis Ref.20 Ref.21 Ref.22 Ref.23

Natural variations

Alternative sequence438 – 45821VDSVC…KLSKK → GGWGAAVCRGRWGSVSIWTG RSQGLLIAVT in isoform 2.
VSP_014579

Experimental info

Mutagenesis2741K → A: Abolishes histone acetyltransferase activity. Ref.22
Mutagenesis3161C → S: Strongly reduces histone acetyltransferase activity. Ref.22
Mutagenesis3501E → Q: Abolishes histone acetyltransferase activity. Ref.22
Sequence conflict2221S → T in AAL55762. Ref.7
Sequence conflict2491Y → H in BAB14827. Ref.1
Sequence conflict3721I → N in BAB14827. Ref.1
Isoform 2:
Sequence conflict4541I → M in AAH37773. Ref.4

Secondary structure

....................................................... 458
Helix Strand Turn

Details...

Sequences

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

Last modified July 5, 2005. Version 2.
Checksum: 66C474BE5B90E8E3

FASTA45852,403
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 69AA4F8800E687E0
Show »

FASTA46753,085

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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: IDENTIFICATION OF MSL COMPLEX COMPONENTS, IDENTIFICATION BY MASS SPECTROMETRY.
[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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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.
[18]"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.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 170-458 IN COMPLEX WITH MSL1, ACETYLATION AT LYS-274, FUNCTION IN MSL AND NSL COMPLEX, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KANSL1; MSL1 AND MSL3.
[21]"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.
[22]"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-458 IN COMPLEX WITH MSL1; ZINC ION AND ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-274, INTERACTION WITH KANSL1; MSL1 AND MSL3, MUTAGENESIS OF LYS-274; CYS-316 AND GLU-350.
[23]"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. expand/collapse author list , 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.
CCDSCCDS10706.1. [Q9H7Z6-1]
CCDS45468.1. [Q9H7Z6-2]
RefSeqNP_115564.2. NM_032188.2. [Q9H7Z6-1]
NP_892003.2. NM_182958.2. [Q9H7Z6-2]
UniGeneHs.533803.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GIVX-ray1.94A174-449[»]
2PQ8X-ray1.45A174-449[»]
2Y0MX-ray2.70A174-458[»]
3QAHX-ray2.10A174-449[»]
3TOAX-ray3.00A177-458[»]
3TOBX-ray2.70A177-458[»]
4DNCX-ray2.05A/B170-458[»]
ProteinModelPortalQ9H7Z6.
SMRQ9H7Z6. Positions 47-169, 178-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123914. 43 interactions.
IntActQ9H7Z6. 12 interactions.
MINTMINT-1897597.

Chemistry

BindingDBQ9H7Z6.
ChEMBLCHEMBL1932912.

PTM databases

PhosphoSiteQ9H7Z6.

Polymorphism databases

DMDM68565938.

Proteomic databases

MaxQBQ9H7Z6.
PaxDbQ9H7Z6.
PRIDEQ9H7Z6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
GeneID84148.
KEGGhsa:84148.
UCSCuc002eax.3. human. [Q9H7Z6-2]
uc002eay.3. human. [Q9H7Z6-1]

Organism-specific databases

CTD84148.
GeneCardsGC16P031130.
HGNCHGNC:17933. KAT8.
HPAHPA057106.
MIM609912. gene.
neXtProtNX_Q9H7Z6.
PharmGKBPA38476.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5027.
HOVERGENHBG053268.
InParanoidQ9H7Z6.
KOK11308.
OMADGRDHKI.
PhylomeDBQ9H7Z6.
TreeFamTF317619.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressQ9H7Z6.
BgeeQ9H7Z6.
CleanExHS_MYST1.
GenevestigatorQ9H7Z6.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKAT8. human.
EvolutionaryTraceQ9H7Z6.
GeneWikiMYST1.
GenomeRNAi84148.
NextBio73476.
PROQ9H7Z6.
SOURCESearch...

Entry information

Entry nameKAT8_HUMAN
AccessionPrimary (citable) accession number: Q9H7Z6
Secondary accession number(s): A8K4Z1 expand/collapse secondary AC list , 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: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM