O95251 (KAT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT7
EC=2.3.1.48

Alternative name(s):
Histone acetyltransferase binding to ORC1
Lysine acetyltransferase 7
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2
Short name=MYST-2

Gene names

Name:	KAT7
Synonyms:	HBO1, HBOa, MYST2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Through chromatin acetylation it may regulate DNA replication and act as a coactivator of TP53-dependent transcription. Specifically represses AR-mediated transcription. Ref.1 Ref.2 Ref.8 Ref.10
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1
Subunit structure	Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of PHF15, PHF16 and PHF17. Interacts with MCM2 and ORC1L. Interacts with the androgen receptor (AR) in the presence of dihydrotestosterone. Ref.1 Ref.2 Ref.8 Ref.10
Subcellular location	Nucleus › nucleoplasm Ref.2 Ref.8 Ref.10.
Tissue specificity	Ubiquitously expressed, with highest levels in testis. Ref.1 Ref.2
Domain	The C2HC-type zinc finger is required for interaction with MCM2 and ORC1L. Ref.8 The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction By similarity. Ref.8
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Biological process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Chromatin regulator Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from direct assay Ref.10. Source: UniProtKB histone H3 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K12 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K5 acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4-K8 acetylation Inferred from direct assay Ref.10. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone acetyltransferase complex Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction Ref.10. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AR	P10275	5	EBI-473199,EBI-608057
BARD1	Q99728	2	EBI-473199,EBI-473181
KIAA1377	Q9P2H0	2	EBI-473199,EBI-473176
VIM	P08670	3	EBI-473199,EBI-353844

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 611	611	Histone acetyltransferase KAT7		PRO_0000051569
Regions
	Zinc finger	366 – 388	23	C2HC-type
	Region	482 – 488	7	Acetyl-CoA binding By similarity
	Compositional bias	10 – 57	48	Ser-rich
Sites
	Active site	474	1	Nucleophile By similarity
	Binding site	477	1	Acetyl-CoA By similarity
	Binding site	512	1	Acetyl-CoA By similarity
Amino acid modifications
	Modified residue	50	1	Phosphoserine Ref.12 Ref.13 Ref.14
	Modified residue	52	1	Phosphoserine Ref.12 Ref.15
	Modified residue	53	1	Phosphoserine Ref.12 Ref.14 Ref.15
	Modified residue	56	1	Phosphoserine Ref.12 Ref.15
	Modified residue	57	1	Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	85	1	Phosphothreonine Ref.14 Ref.15 Ref.16
	Modified residue	88	1	Phosphothreonine Ref.11 Ref.14 Ref.15 Ref.16
	Modified residue	99	1	Phosphoserine Ref.9 Ref.14
	Modified residue	100	1	Phosphoserine Ref.9
	Modified residue	102	1	Phosphoserine Ref.9 Ref.14 Ref.15 Ref.16
	Modified residue	104	1	Phosphothreonine Ref.14
	Modified residue	124	1	Phosphoserine Ref.9
	Modified residue	128	1	Phosphothreonine Ref.9
	Modified residue	199	1	N6-acetyllysine Ref.17
Experimental info
	Mutagenesis	371	1	C → A: No interaction with MCM2 and ORC1L. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	O95251 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 8368E7C4F07D8D7C	FASTA	611	70,642
	10 20 30 40 50 60 MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR 70 80 90 100 110 120 NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRETKNTAD 130 140 150 160 170 180 HDESPPRTPT GNAPSSESDI DISSPNVSHD ESIAKDMSLK DSGSDLSHRP KRRRFHESYN 190 200 210 220 230 240 FNMKCPTPGC NSLGHLTGKH ERHFSISGCP LYHNLSADEC KVRAQSRDKQ IEERMLSHRQ 250 260 270 280 290 300 DDNNRHATRH QAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY GNTREPLLEN 310 320 330 340 350 360 LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW YHSPYPEEYA 370 380 390 400 410 420 RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD GKKNKIYCQN 430 440 450 460 470 480 LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY NVSCILTMPQ 490 500 510 520 530 540 YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY LHNFQGKEIS 550 560 570 580 590 600 IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK RSNSNKTMDP 610 SCLKWTPPKG T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein." Iizuka M., Stillman B. J. Biol. Chem. 274:23027-23034(1999) [PubMed: 10438470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ORC1L, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Epithelium.
[2]	"Androgen receptor interacts with a novel MYST protein, HBO1." Sharma M., Zarnegar M., Li X., Lim B., Sun Z. J. Biol. Chem. 275:35200-35208(2000) [PubMed: 10930412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AR, FUNCTION. Tissue: Prostate.
[3]	"Cloning and identifying histone acetyltransferase HBOa." Jian J., Guangtao L., Guangwei D., Yan Z., Jianhe C., Jiangang Y., Boqin Q. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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].
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid.
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[8]	"Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1." Burke T.W., Cook J.G., Asano M., Nevins J.R. J. Biol. Chem. 276:15397-15408(2001) [PubMed: 11278932] [Abstract] Cited for: INTERACTION WITH MCM2 AND ORC1L, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-371.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-100; SER-102; SER-124 AND THR-128, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed: 16387653] [Abstract] Cited for: FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN TP53-MEDIATED TRANSCRIPTION, IDENTIFICATION IN THE HBO1 COMPLEX, INTERACTION WITH MCM2, SUBCELLULAR LOCATION.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-52; SER-53; SER-56 AND SER-57, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-57, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-53; SER-57; THR-85; THR-88; SER-99; SER-102 AND THR-104, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-56; SER-57; THR-85; THR-88 AND SER-102, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-85; THR-88 AND SER-102, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF074606 mRNA. Translation: AAC99368.1. AF140360 mRNA. Translation: AAD42348.1. AF217502 mRNA. Translation: AAL56649.1. AK023890 mRNA. Translation: BAG51236.1. CH471109 Genomic DNA. Translation: EAW94658.1. BC032640 mRNA. Translation: AAH32640.1.
IPI	IPI00180764.
RefSeq	NP_001186084.1. NM_001199155.1. NP_001186085.1. NM_001199156.1. NP_001186086.1. NM_001199157.1. NP_001186087.1. NM_001199158.1. NP_008998.1. NM_007067.4.
UniGene	Hs.21907.
3D structure databases
ProteinModelPortal	O95251.
SMR	O95251. Positions 142-214, 340-607.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29697N.
IntAct	O95251. 28 interactions.
MINT	MINT-141769.
STRING	O95251.
PTM databases
PhosphoSite	O95251.
Proteomic databases
PRIDE	O95251.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259021; ENSP00000259021; ENSG00000136504.
GeneID	11143.
KEGG	hsa:11143.
UCSC	uc002ipm.1. human.
Organism-specific databases
CTD	11143.
GeneCards	GC17P047865.
H-InvDB	HIX0013964.
HGNC	HGNC:17016. KAT7.
HPA	HPA044470.
MIM	609880. gene.
neXtProt	NX_O95251.
PharmGKB	PA134886407.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12660.
GeneTree	ENSGT00550000074503.
HOGENOM	HBG631736.
HOVERGEN	HBG053268.
InParanoid	O95251.
OMA	VYSTRRV.
OrthoDB	EOG4BCDMN.
PhylomeDB	O95251.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_tf_pathway. Regulation of Androgen receptor activity.
Gene expression databases
ArrayExpress	O95251.
Bgee	O95251.
CleanEx	HS_MYST2.
Genevestigator	O95251.
GermOnline	ENSG00000136504. Homo sapiens.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. IPR015880. Znf_C2H2-like. IPR002515. Znf_C2HC. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KO	K11307.
Pfam	PF01853. MOZ_SAS. 1 hit. PF01530. zf-C2HC. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...
Other
NextBio	42360.
SOURCE	Search...

Entry information

Entry name

KAT7_HUMAN

Accession

Primary (citable) accession number: O95251
Secondary accession number(s): B3KN74

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 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.