Q92993 (KAT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT5
EC=2.3.1.48

Alternative name(s):
60 kDa Tat-interactive protein
Short name=Tip60
Histone acetyltransferase HTATIP
Short name=HIV-1 Tat interactive protein
Lysine acetyltransferase 5
cPLA(2)-interacting protein

Gene names

Name:	KAT5
Synonyms:	HTATIP, TIP60

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	513 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Directly acetylates and activates ATM. In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation. Ref.14 Ref.18 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.30
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.10
Subunit structure	Interacts with the cytoplasmic tail of APP and APBB1/FE65 By similarity. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Interacts with ATM. Interacts with PHF17. Interacts with HIV-1 Tat. Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Ref.1 Ref.2 Ref.9 Ref.11 Ref.12 Ref.16 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.27 Ref.30
Subcellular location	Nucleus › nucleolus. Cytoplasm › perinuclear region. Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies. Ref.2 Ref.16 Ref.26 Ref.28
Post-translational modification	Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies. Ref.28 Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. Phosphorylated form has a higher activity. Ref.15 Ubiquitinated by MDM2, leading to its proteasome-dependent degradation. Ref.13 Autoacetylation at Lys-327 is required for proper function By similarity.
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.
Sequence caution	The sequence AAB02683.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Growth regulation Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from direct assay Ref.20. Source: UniProtKB androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB double-strand break repair Inferred from mutant phenotype Ref.11. Source: UniProtKB histone acetylation Inferred from direct assay Ref.11. Source: UniProtKB negative regulation of interleukin-2 production Inferred from direct assay PubMed 17360565. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17360565. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.20. Source: UniProtKB regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Piccolo NuA4 histone acetyltransferase complex Inferred from direct assay Ref.20. Source: UniProtKB chromatin Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara nucleolus Inferred from direct assay Ref.26. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB histone acetyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Inferred from direct assay Ref.20. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	3	EBI-399080,EBI-930964
CBX8	Q9HC52	2	EBI-399080,EBI-712912
DLEU1	O43261	2	EBI-399080,EBI-710057
GADD45G	O95257	2	EBI-399080,EBI-448202
KIAA1377	Q9P2H0	2	EBI-399080,EBI-473176
PTPN4	P29074	2	EBI-399080,EBI-710431
TP53	P04637	3	EBI-399080,EBI-366083

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92993-1)

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: Q92993-2)

Also known as: PLIP;

The sequence of this isoform differs from the canonical sequence as follows:
     96-147: Missing.

Isoform 3 (identifier: Q92993-3)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ

Isoform 4 (identifier: Q92993-4)

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: V → VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
     96-147: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 513

513

Histone acetyltransferase KAT5

PRO_0000051580

Regions

Zinc finger

261 – 283

23

C2HC-type

Region

377 – 383

7

Acetyl-CoA binding

Sites

Active site

327

1

By similarity

Active site

369

1

Nucleophile By similarity

Binding site

372

1

Acetyl-CoA

Binding site

407

1

Acetyl-CoA

Amino acid modifications

Modified residue

52

1

N6-acetyllysine Ref.32

Modified residue

86

1

Phosphoserine Ref.15

Modified residue

90

1

Phosphoserine; by CDK1 Ref.15

Modified residue

327

1

N6-acetyllysine; by autocatalysis By similarity

Cross-link

430

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28

Cross-link

451

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28

Natural variations

Alternative sequence

4

1

V → VVSPVPGAGRREPGEVGRAR GPPVADPGVALSPQ in isoform 3 and isoform 4.

VSP_009104

Alternative sequence

96 – 147

52

Missing in isoform 2 and isoform 4.

VSP_007438

Natural variant

78

1

P → T.
Corresponds to variant rs11541271 [ dbSNP | Ensembl ].

VAR_059456

Experimental info

Mutagenesis

86

1

S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced activity. Ref.15

Mutagenesis

90

1

S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced activity. Ref.15

Mutagenesis

254

1

L → A: Does not affect phosphorylation; when associated with A-257. Ref.15

Mutagenesis

257

1

L → A: Does not affect phosphorylation; when associated with A-254. Ref.15

Mutagenesis

380

1

G → A: Loss of function. Does not affect phosphorylation. Ref.15

Mutagenesis

430

1

K → R: Abrogates sumoylation. Ref.28

Mutagenesis

451

1

K → R: Abrogates sumoylation. Ref.28

Sequence conflict

382

1

G → R in AAB18236. Ref.1

Sequence conflict

382

1

G → R in AAB02683. Ref.1

Isoform 3:

Sequence conflict

32

1

V → A no nucleotide entry Ref.3

Secondary structure

1

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513

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Beta strand

28 – 34

7

Beta strand

37 – 39

3

Beta strand

43 – 47

5

Beta strand

56 – 58

3

Turn

60 – 62

3

Helix

65 – 67

3

Beta strand

235 – 237

3

Beta strand

240 – 242

3

Helix

252 – 254

3

Beta strand

260 – 262

3

Turn

264 – 266

3

Beta strand

269 – 271

3

Helix

273 – 282

10

Beta strand

289 – 296

8

Beta strand

299 – 305

7

Turn

306 – 308

3

Helix

310 – 321

12

Turn

328 – 331

4

Beta strand

336 – 345

10

Beta strand

348 – 360

13

Beta strand

365 – 368

4

Beta strand

370 – 372

3

Helix

374 – 376

3

Helix

381 – 395

15

Beta strand

400 – 402

3

Helix

408 – 425

18

Helix

441 – 448

8

Helix

452 – 461

10

Beta strand

469 – 474

6

Helix

497 – 499

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 63724F5E10B957D5	FASTA	513	58,582
	10 20 30 40 50 60 MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH 70 80 90 100 110 120 ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK 130 140 150 160 170 180 EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGAARRAV 190 200 210 220 230 240 AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH 250 260 270 280 290 300 RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS 310 320 330 340 350 360 FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE 370 380 390 400 410 420 STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ 430 440 450 460 470 480 TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI 490 500 510 VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW
	Isoform 2 (PLIP) [UniParc]. Checksum: 5A0E9324550AF246	FASTA	461	53,077
	10 20 30 40 50 60 MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH 70 80 90 100 110 120 ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVKRKVE VVSPATPVPS ETAPASVFPQ 130 140 150 160 170 180 NGAARRAVAA QPGRKRKSNC LGTDEDSQDS SDGIPSAPRM TGSLVSDRSH DDIVTRMKNI 190 200 210 220 230 240 ECIELGRHRL KPWYFSPYPQ ELTTLPVLYL CEFCLKYGRS LKCLQRHLTK CDLRHPPGNE 250 260 270 280 290 300 IYRKGTISFF EIDGRKNKSY SQNLCLLAKC FLDHKTLYYD TDPFLFYVMT EYDCKGFHIV 310 320 330 340 350 360 GYFSKEKEST EDYNVACILT LPPYQRRGYG KLLIEFSYEL SKVEGKTGTP EKPLSDLGLL 370 380 390 400 410 420 SYRSYWSQTI LEILMGLKSE SGERPQITIN EISEITSIKK EDVISTLQYL NLINYYKGQY 430 440 450 460 ILTLSEDIVD GHERAMLKRL LRIDSKCLHF TPKDWSKRGK W
	Isoform 3 [UniParc]. Checksum: 0CEB1A8E8C8D3E24	FASTA	546	61,798
	10 20 30 40 50 60 MAEVVSPVPG AGRREPGEVG RARGPPVADP GVALSPQGEI IEGCRLPVLR RNQDNEDEWP 70 80 90 100 110 120 LAEILSVKDI SGRKLFYVHY IDFNKRLDEW VTHERLDLKK IQFPKKEAKT PTKNGLPGSR 130 140 150 160 170 180 PGSPEREVPA SAQASGKTLP IPVQITLRFN LPKEREAIPG GEPDQPLSSS SCLQPNHRST 190 200 210 220 230 240 KRKVEVVSPA TPVPSETAPA SVFPQNGAAR RAVAAQPGRK RKSNCLGTDE DSQDSSDGIP 250 260 270 280 290 300 SAPRMTGSLV SDRSHDDIVT RMKNIECIEL GRHRLKPWYF SPYPQELTTL PVLYLCEFCL 310 320 330 340 350 360 KYGRSLKCLQ RHLTKCDLRH PPGNEIYRKG TISFFEIDGR KNKSYSQNLC LLAKCFLDHK 370 380 390 400 410 420 TLYYDTDPFL FYVMTEYDCK GFHIVGYFSK EKESTEDYNV ACILTLPPYQ RRGYGKLLIE 430 440 450 460 470 480 FSYELSKVEG KTGTPEKPLS DLGLLSYRSY WSQTILEILM GLKSESGERP QITINEISEI 490 500 510 520 530 540 TSIKKEDVIS TLQYLNLINY YKGQYILTLS EDIVDGHERA MLKRLLRIDS KCLHFTPKDW SKRGKW
	Isoform 4 [UniParc]. Checksum: 761BF5859BE89793	FASTA	494	56,292
	10 20 30 40 50 60 MAEVVSPVPG AGRREPGEVG RARGPPVADP GVALSPQGEI IEGCRLPVLR RNQDNEDEWP 70 80 90 100 110 120 LAEILSVKDI SGRKLFYVHY IDFNKRLDEW VTHERLDLKK IQFPKKEAKT PTKNGLPGSR 130 140 150 160 170 180 PGSPEREVKR KVEVVSPATP VPSETAPASV FPQNGAARRA VAAQPGRKRK SNCLGTDEDS 190 200 210 220 230 240 QDSSDGIPSA PRMTGSLVSD RSHDDIVTRM KNIECIELGR HRLKPWYFSP YPQELTTLPV 250 260 270 280 290 300 LYLCEFCLKY GRSLKCLQRH LTKCDLRHPP GNEIYRKGTI SFFEIDGRKN KSYSQNLCLL 310 320 330 340 350 360 AKCFLDHKTL YYDTDPFLFY VMTEYDCKGF HIVGYFSKEK ESTEDYNVAC ILTLPPYQRR 370 380 390 400 410 420 GYGKLLIEFS YELSKVEGKT GTPEKPLSDL GLLSYRSYWS QTILEILMGL KSESGERPQI 430 440 450 460 470 480 TINEISEITS IKKEDVISTL QYLNLINYYK GQYILTLSED IVDGHERAML KRLLRIDSKC 490 LHFTPKDWSK RGKW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator." Kamine J., Elangovan B., Subramanian T., Coleman D., Chinnadurai G. Virology 216:357-366(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HIV-1 TAT. Tissue: Lymphoblast.
[2]	"PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production." Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., Bonventre J.V. Mol. Cell. Biol. 21:4470-4481(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PLA2G4A, SUBCELLULAR LOCATION. Tissue: Fibroblast and Placenta.
[3]	"Identification of a larger form of the histone acetyl transferase Tip60." Legube G., Trouche D. Gene 310:161-168(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterus.
[6]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(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. , 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].
[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] (ISOFORMS 1 AND 2). Tissue: Cervix, Liver, Placenta and Testis.
[9]	"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex." Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W. J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-35; 150-177 AND 297-307, IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[10]	"Tip60 acetylates six lysines of a specific class in core histones in vitro." Kimura A., Horikoshi M. Genes Cells 3:789-800(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY IN VITRO.
[11]	"Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis." Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y. Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[12]	"Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling." Lee H.-J., Chun M., Kandror K.V. J. Biol. Chem. 276:16597-16600(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EDNRA.
[13]	"Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation." Legube G., Linares L.K., Lemercier C., Scheffner M., Khochbin S., Trouche D. EMBO J. 21:1704-1712(2002) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[14]	"MYC recruits the TIP60 histone acetyltransferase complex to chromatin." Frank S.R., Parisi T., Taubert S., Fernandez P., Fuchs M., Chan H.M., Livingston D.M., Amati B. EMBO Rep. 4:575-580(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN MYC-DEPENDENT TRANSCRIPTION.
[15]	"Tip60 acetyltransferase activity is controlled by phosphorylation." Lemercier C., Legube G., Caron C., Louwagie M., Garin J., Trouche D., Khochbin S. J. Biol. Chem. 278:4713-4718(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-86 AND SER-90, MUTAGENESIS OF SER-86; SER-90; LEU-254; LEU-257 AND GLY-380.
[16]	"Tip60 is a co-repressor for STAT3." Xiao H., Chung J., Kao H.-Y., Yang Y.-C. J. Biol. Chem. 278:11197-11204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HDAC7.
[17]	"The highly conserved and multifunctional NuA4 HAT complex." Doyon Y., Cote J. Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON NUA4 COMPLEX.
[18]	"Role of the histone acetyl transferase Tip60 in the p53 pathway." Legube G., Linares L.K., Tyteca S., Caron C., Scheffner M., Chevillard-Briet M., Trouche D. J. Biol. Chem. 279:44825-44833(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
[19]	"von Hippel-Lindau partner Jade-1 is a transcriptional co-activator associated with histone acetyltransferase activity." Panchenko M.V., Zhou M.I., Cohen H.T. J. Biol. Chem. 279:56032-56041(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PHF17.
[20]	"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans." Doyon Y., Selleck W., Lane W.S., Tan S., Cote J. Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 COMPLEX.
[21]	"E2F-dependent histone acetylation and recruitment of the Tip60 acetyltransferase complex to chromatin in late G1." Taubert S., Gorrini C., Frank S.R., Parisi T., Fuchs M., Chan H.M., Livingston D.M., Amati B. Mol. Cell. Biol. 24:4546-4556(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN E2F1-DEPENDENT TRANSCRIPTION.
[22]	"A large-scale RNAi screen in human cells identifies new components of the p53 pathway." Berns K., Hijmans E.M., Mullenders J., Brummelkamp T.R., Velds A., Heimerikx M., Kerkhoven R.M., Madiredjo M., Nijkamp W., Weigelt B., Agami R., Ge W., Cavet G., Linsley P.S., Beijersbergen R.L., Bernards R. Nature 428:431-437(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN TP53-DEPENDENT TRANSCRIPTION.
[23]	"HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses." Col E., Caron C., Chable-Bessia C., Legube G., Gazzeri S., Komatsu Y., Yoshida M., Benkirane M., Trouche D., Khochbin S. EMBO J. 24:2634-2645(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[24]	"A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM." Sun Y., Jiang X., Chen S., Fernandes N., Price B.D. Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATM, FUNCTION.
[25]	"The histidine triad protein Hint1 triggers apoptosis independent of its enzymatic activity." Weiske J., Huber O. J. Biol. Chem. 281:27356-27366(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH HINT1.
[26]	"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, SUBCELLULAR LOCATION.
[27]	"TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells." Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., Nonomura K., Hatakeyama S. Cancer Res. 68:3486-3494(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRIM68.
[28]	"Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response." Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., Wu Q., Reddy S.E. , Hu R., Huang H., Jin C., Yao X. Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-430 AND LYS-451, MUTAGENESIS OF LYS-430 AND LYS-451, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
[29]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[30]	"TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells." Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S. Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TRIM24.
[31]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[32]	"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-52, MASS SPECTROMETRY.
[33]	"The crystal structure of acetyltransferase domain of human HIV-1 TAT interacting protein in complex with acetylcoenzyme A." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 227-506 IN COMPLEX WITH ACETYL COENZYME A AND ZINC IONS.
[34]	"Solution structure of RUH-073, a pseudo chromo domain from human cDNA." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 5-78.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U74667 mRNA. Translation: AAB18236.1.
U40989 mRNA. Translation: AAB02683.1. Different initiation.
U67734 mRNA. Translation: AAD00163.1.
AY214165 Genomic DNA. Translation: AAO21130.1.
AK304664 mRNA. Translation: BAG65439.1.
AP001266 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74427.1.
CH471076 Genomic DNA. Translation: EAW74429.1.
BC000166 mRNA. Translation: AAH00166.3.
BC064912 mRNA. Translation: AAH64912.1.
BC093032 mRNA. Translation: AAH93032.1.
BC143296 mRNA. Translation: AAI43297.1.
BC117167 mRNA. Translation: AAI17168.1.

IPI

IPI00165536.
IPI00290020.
IPI00394657.
IPI00981546.

RefSeq

NP_001193762.1. NM_001206833.1.
NP_006379.2. NM_006388.3.
NP_874368.1. NM_182709.2.
NP_874369.1. NM_182710.2.

UniGene

Hs.397010.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EKO	NMR	-	A	5-78	[»]
2OU2	X-ray	2.30	A	227-506	[»]

ProteinModelPortal

Q92993.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5998N.

IntAct

Q92993. 59 interactions.

MINT

MINT-94861.

STRING

9606.ENSP00000340330.

PTM databases

PhosphoSite

Q92993.

Polymorphism databases

DMDM

30923328.

Proteomic databases

PaxDb

Q92993.

PRIDE

Q92993.

Protocols and materials databases

DNASU

10524.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341318; ENSP00000340330; ENSG00000172977.
ENST00000352980; ENSP00000344955; ENSG00000172977.
ENST00000377046; ENSP00000366245; ENSG00000172977.
ENST00000530446; ENSP00000434765; ENSG00000172977.

GeneID

10524.

KEGG

hsa:10524.

UCSC

uc001ofi.3. human.
uc001ofj.3. human.

Organism-specific databases

CTD

10524.

GeneCards

GC11P065479.

HGNC

HGNC:5275. KAT5.

HPA

HPA016953.

MIM

601409. gene.

neXtProt

NX_Q92993.

PharmGKB

PA162392746.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5027.

HOGENOM

HOG000182457.

KO

K11304.

OMA

HDDIITR.

OrthoDB

EOG4JHCFH.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpress

Q92993.

Bgee

Q92993.

CleanEx

HS_KAT5.

Genevestigator

Q92993.

GermOnline

ENSG00000172977. 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.

ProtoNet

Search...

Other

BindingDB

Q92993.

ChEMBL

CHEMBL5750.

EvolutionaryTrace

Q92993.

GenomeRNAi

10524.

NextBio

39922.

SOURCE

Search...

Entry information

Entry name

KAT5_HUMAN

Accession

Primary (citable) accession number: Q92993
Secondary accession number(s): B4E3C7 , C9JL99, O95624, Q13430, Q17RW5, Q561W3, Q6GSE8, Q9BWK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 143 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.