O95251 (KAT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| 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.9 Ref.11 |
| 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.9 Ref.11 |
| Subcellular location | |
| 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.9 The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction By similarity. Ref.9 |
| Post-translational modification | Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior Phosphorylation at Thr-85 and Thr-88 by CDK1. Autoacetylation at Lys-432 is required for proper function By similarity. |
| Sequence similarities | Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger. |
Ontologies
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 |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O95251-1) 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: O95251-2) The sequence of this isoform differs from the canonical sequence as follows: 114-193: Missing. 222-251: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 3 (identifier: O95251-3) The sequence of this isoform differs from the canonical sequence as follows: 55-113: Missing. 114-193: Missing. 222-251: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 4 (identifier: O95251-4) The sequence of this isoform differs from the canonical sequence as follows: 37-43: Missing. 222-251: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 5 (identifier: O95251-5) The sequence of this isoform differs from the canonical sequence as follows: 55-113: Missing. 114-193: Missing. | ||||||
| Note: No experimental confirmation available. |
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 | 432 | 1 | By similarity | ||||||
| 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.14 | ||||||
| Modified residue | 57 | 1 | Phosphoserine; by PLK1 Ref.14 Ref.15 Ref.16 Ref.19 | ||||||
| Modified residue | 85 | 1 | Phosphothreonine; by CDK1 Ref.14 Ref.15 Ref.16 | ||||||
| Modified residue | 88 | 1 | Phosphothreonine; by CDK1 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 | ||||||
| Modified residue | 102 | 1 | Phosphoserine Ref.14 Ref.16 Ref.19 | ||||||
| Modified residue | 124 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 162 | 1 | Phosphoserine Ref.18 Ref.19 | ||||||
| Modified residue | 164 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 199 | 1 | N6-acetyllysine Ref.17 | ||||||
| Modified residue | 432 | 1 | N6-acetyllysine; by autocatalysis By similarity | ||||||
| Modified residue | 506 | 1 | Phosphoserine Ref.18 | ||||||
Natural variations | |||||||||
| Alternative sequence | 37 – 43 | 7 | Missing in isoform 4. | VSP_045835 | |||||
| Alternative sequence | 55 – 113 | 59 | Missing in isoform 3 and isoform 5. | VSP_042552 | |||||
| Alternative sequence | 114 – 193 | 80 | Missing in isoform 2, isoform 3 and isoform 5. | VSP_042553 | |||||
| Alternative sequence | 222 – 251 | 30 | Missing in isoform 2, isoform 3 and isoform 4. | VSP_042554 | |||||
Experimental info | |||||||||
| Mutagenesis | 371 | 1 | C → A: No interaction with MCM2 and ORC1L. Ref.9 | ||||||
| Sequence conflict | 41 | 1 | R → Q in BAG57346. Ref.5 | ||||||
Sequences
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References
| « Hide '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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1). |
| [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] (ISOFORM 1). |
| [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). Tissue: Brain, Cerebellum and Thyroid. |
| [6] | "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. Nusbaum C.Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [7] | 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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "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 1). Tissue: Lymph. |
| [9] | "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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MCM2 AND ORC1L, DOMAIN, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-371. |
| [10] | "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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [11] | "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] [Europe PMC] [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. |
| [12] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney. |
| [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-57; THR-85; THR-88 AND SER-102, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "Role for Plk1 phosphorylation of Hbo1 in regulation of replication licensing." Wu Z.Q., Liu X. Proc. Natl. Acad. Sci. U.S.A. 105:1919-1924(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-57 BY PLK1, PHOSPHORYLATION AT THR-85 AND THR-88 BY CDK1. |
| [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] [Europe PMC] [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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, MASS SPECTROMETRY. |
| [18] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-506, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [19] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-88; SER-102; SER-124; SER-162 AND SER-164, 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. AK293976 mRNA. Translation: BAG57346.1. AK294014 mRNA. Translation: BAG57375.1. AK294052 mRNA. Translation: BAG57401.1. AK294836 mRNA. Translation: BAG57945.1. AC015795 Genomic DNA. No translation available. AC027801 Genomic DNA. No translation available. CH471109 Genomic DNA. Translation: EAW94658.1. CH471109 Genomic DNA. Translation: EAW94659.1. BC032640 mRNA. Translation: AAH32640.1. |
| IPI | IPI00180764. IPI00792061. IPI00909215. IPI00909397. |
| 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. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-29697N. |
| IntAct | O95251. 28 interactions. |
| MINT | MINT-141769. |
| STRING | 9606.ENSP00000259021. |
PTM databases | |
| PhosphoSite | O95251. |
Proteomic databases | |
| PaxDb | O95251. |
| PRIDE | O95251. |
Protocols and materials databases | |
| DNASU | 11143. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000259021; ENSP00000259021; ENSG00000136504. ENST00000424009; ENSP00000398961; ENSG00000136504. ENST00000454930; ENSP00000413415; ENSG00000136504. ENST00000509773; ENSP00000424577; ENSG00000136504. ENST00000510819; ENSP00000423385; ENSG00000136504. |
| GeneID | 11143. |
| KEGG | hsa:11143. |
| UCSC | uc002ipl.2. human. |
Organism-specific databases | |
| CTD | 11143. |
| GeneCards | GC17P047867. |
| HGNC | HGNC:17016. KAT7. |
| HPA | HPA044470. |
| MIM | 609880. gene. |
| neXtProt | NX_O95251. |
| PharmGKB | PA134886407. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG5027. |
| HOGENOM | HOG000182457. |
| HOVERGEN | HBG053268. |
| InParanoid | O95251. |
| KO | K11307. |
| OMA | SPNASHD. |
| 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 | |
| Gene3D | 3.40.630.30. 1 hit. |
| InterPro | IPR016181. Acyl_CoA_acyltransferase. IPR002717. MOZ_SAS. IPR015880. Znf_C2H2-like. IPR002515. Znf_C2HC. [Graphical view] |
| 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 | |
| GenomeRNAi | 11143. |
| NextBio | 42360. |
| SOURCE | Search... |
Entry information
| Entry name | KAT7_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O95251 Secondary accession number(s): B3KN74 G5E9K7 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
