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O95251 (KAT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence 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 JADE1, JADE2 and JADE3. 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

Nucleusnucleoplasm Ref.2 Ref.9 Ref.11.

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

Keywords
   Biological processDNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionAcyltransferase
Chromatin regulator
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from direct assay Ref.11. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

histone H4-K12 acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

histone acetyltransferase complex

Inferred from direct assay Ref.11. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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...

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:
     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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Histone acetyltransferase KAT7
PRO_0000051569

Regions

Zinc finger366 – 38823C2HC-type
Region482 – 4887Acetyl-CoA binding By similarity
Compositional bias10 – 5748Ser-rich

Sites

Active site4321 By similarity
Active site4741Nucleophile By similarity
Binding site4771Acetyl-CoA By similarity
Binding site5121Acetyl-CoA By similarity

Amino acid modifications

Modified residue501Phosphoserine Ref.14
Modified residue571Phosphoserine; by PLK1 Ref.14 Ref.15 Ref.17 Ref.20
Modified residue851Phosphothreonine; by CDK1 Ref.14 Ref.15 Ref.17
Modified residue881Phosphothreonine; by CDK1 Ref.12 Ref.14 Ref.15 Ref.17 Ref.20
Modified residue1021Phosphoserine Ref.14 Ref.17 Ref.20
Modified residue1241Phosphoserine Ref.20
Modified residue1621Phosphoserine Ref.19 Ref.20
Modified residue1641Phosphoserine Ref.20
Modified residue1991N6-acetyllysine Ref.18
Modified residue2771N6-acetyllysine By similarity
Modified residue4321N6-acetyllysine; by autocatalysis By similarity
Modified residue5061Phosphoserine Ref.19

Natural variations

Alternative sequence55 – 11359Missing in isoform 3 and isoform 5.
VSP_042552
Alternative sequence114 – 19380Missing in isoform 2, isoform 3 and isoform 5.
VSP_042553
Alternative sequence222 – 25130Missing in isoform 2, isoform 3 and isoform 4.
VSP_042554

Experimental info

Mutagenesis3711C → A: No interaction with MCM2 and ORC1L. Ref.9
Sequence conflict38 – 447Missing in BAG57945. Ref.5
Sequence conflict411R → Q in BAG57346. Ref.5

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: 8368E7C4F07D8D7C

FASTA61170,642
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 005414956B922380
Show »

FASTA50158,136
Isoform 3 [UniParc].

Checksum: EF5AA3D8E63B35D0
Show »

FASTA44251,440
Isoform 4 [UniParc].

Checksum: 30A3E4C3E47EFBED
Show »

FASTA58166,947
Isoform 5 [UniParc].

Checksum: 906F630E44BAFD2B
Show »

FASTA47255,135

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. 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] (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. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., 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. 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 (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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_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.
UniGeneHs.21907.

3D structure databases

ProteinModelPortalO95251.
SMRO95251. Positions 183-211, 340-607.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116315. 53 interactions.
DIPDIP-29697N.
IntActO95251. 30 interactions.
MINTMINT-141769.
STRING9606.ENSP00000259021.

PTM databases

PhosphoSiteO95251.

Proteomic databases

PaxDbO95251.
PRIDEO95251.

Protocols and materials databases

DNASU11143.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259021; ENSP00000259021; ENSG00000136504. [O95251-1]
ENST00000424009; ENSP00000398961; ENSG00000136504. [O95251-4]
ENST00000454930; ENSP00000413415; ENSG00000136504. [O95251-5]
ENST00000509773; ENSP00000424577; ENSG00000136504. [O95251-2]
ENST00000510819; ENSP00000423385; ENSG00000136504. [O95251-3]
GeneID11143.
KEGGhsa:11143.
UCSCuc002ipl.2. human.
uc002ipm.3. human. [O95251-1]
uc010wmb.2. human. [O95251-2]
uc010wmc.2. human. [O95251-3]

Organism-specific databases

CTD11143.
GeneCardsGC17P047867.
HGNCHGNC:17016. KAT7.
HPAHPA044470.
MIM609880. gene.
neXtProtNX_O95251.
PharmGKBPA134886407.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
HOVERGENHBG053268.
InParanoidO95251.
KOK11307.
OMAKDMSMKD.
OrthoDBEOG7WHH8N.
PhylomeDBO95251.
TreeFamTF317619.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressO95251.
BgeeO95251.
CleanExHS_MYST2.
GenevestigatorO95251.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR002717. MOZ_SAS.
IPR015880. Znf_C2H2-like.
IPR002515. Znf_C2HC.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF01530. zf-C2HC. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

GeneWikiMYST2.
GenomeRNAi11143.
NextBio42360.
PROO95251.
SOURCESearch...

Entry information

Entry nameKAT7_HUMAN
AccessionPrimary (citable) accession number: O95251
Secondary accession number(s): B3KN74 expand/collapse secondary AC list , B4DF85, B4DFB4, B4DFE0, B4DGY4, E7ER15, G5E9K7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 126 of the entry and version 1 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

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM