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) [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	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	Nucleus › nucleoplasm 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 process	DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
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.11. Source: UniProtKB 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-dependent Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone acetyltransferase complex Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	histone acetyltransferase activity Inferred from electronic annotation. Source: 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...

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

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 005414956B922380	FASTA	501	58,136
	10 20 30 40 50 60 MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQDSSPVR 70 80 90 100 110 120 NLQSFGTEEP AYSTRRVTRS QQQPTPVTPK KYPLRQTRSS GSETEQVVDF SDRGHLTGKH 130 140 150 160 170 180 ERHFSISGCP LYHNLSADEC KAPTERQLRY KEKVAELRKK RNSGLSKEQK EKYMEHRQTY 190 200 210 220 230 240 GNTREPLLEN LTSEYDLDLF RRAQARASED LEKLRLQGQI TEGSNMIKTI AFGRYELDTW 250 260 270 280 290 300 YHSPYPEEYA RLGRLYMCEF CLKYMKSQTI LRRHMAKCVW KHPPGDEIYR KGSISVFEVD 310 320 330 340 350 360 GKKNKIYCQN LCLLAKLFLD HKTLYYDVEP FLFYVMTEAD NTGCHLIGYF SKEKNSFLNY 370 380 390 400 410 420 NVSCILTMPQ YMRQGYGKML IDFSYLLSKV EEKVGSPERP LSDLGLISYR SYWKEVLLRY 430 440 450 460 470 480 LHNFQGKEIS IKEISQETAV NPVDIVSTLQ ALQMLKYWKG KHLVLKRQDL IDEWIAKEAK 490 500 RSNSNKTMDP SCLKWTPPKG T
	Isoform 3 [UniParc]. Checksum: EF5AA3D8E63B35D0	FASTA	442	51,440
	10 20 30 40 50 60 MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQGHLTGK 70 80 90 100 110 120 HERHFSISGC PLYHNLSADE CKAPTERQLR YKEKVAELRK KRNSGLSKEQ KEKYMEHRQT 130 140 150 160 170 180 YGNTREPLLE NLTSEYDLDL FRRAQARASE DLEKLRLQGQ ITEGSNMIKT IAFGRYELDT 190 200 210 220 230 240 WYHSPYPEEY ARLGRLYMCE FCLKYMKSQT ILRRHMAKCV WKHPPGDEIY RKGSISVFEV 250 260 270 280 290 300 DGKKNKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVMTEA DNTGCHLIGY FSKEKNSFLN 310 320 330 340 350 360 YNVSCILTMP QYMRQGYGKM LIDFSYLLSK VEEKVGSPER PLSDLGLISY RSYWKEVLLR 370 380 390 400 410 420 YLHNFQGKEI SIKEISQETA VNPVDIVSTL QALQMLKYWK GKHLVLKRQD LIDEWIAKEA 430 440 KRSNSNKTMD PSCLKWTPPK GT
	Isoform 4 [UniParc]. Checksum: 706E5CC8E8FC59D4	FASTA	574	66,120
	10 20 30 40 50 60 MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRSSA RLSQSSQDSS PVRNLQSFGT 70 80 90 100 110 120 EEPAYSTRRV TRSQQQPTPV TPKKYPLRQT RSSGSETEQV VDFSDRETKN TADHDESPPR 130 140 150 160 170 180 TPTGNAPSSE SDIDISSPNV SHDESIAKDM SLKDSGSDLS HRPKRRRFHE SYNFNMKCPT 190 200 210 220 230 240 PGCNSLGHLT GKHERHFSIS GCPLYHNLSA DECKAPTERQ LRYKEKVAEL RKKRNSGLSK 250 260 270 280 290 300 EQKEKYMEHR QTYGNTREPL LENLTSEYDL DLFRRAQARA SEDLEKLRLQ GQITEGSNMI 310 320 330 340 350 360 KTIAFGRYEL DTWYHSPYPE EYARLGRLYM CEFCLKYMKS QTILRRHMAK CVWKHPPGDE 370 380 390 400 410 420 IYRKGSISVF EVDGKKNKIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVMT EADNTGCHLI 430 440 450 460 470 480 GYFSKEKNSF LNYNVSCILT MPQYMRQGYG KMLIDFSYLL SKVEEKVGSP ERPLSDLGLI 490 500 510 520 530 540 SYRSYWKEVL LRYLHNFQGK EISIKEISQE TAVNPVDIVS TLQALQMLKY WKGKHLVLKR 550 560 570 QDLIDEWIAK EAKRSNSNKT MDPSCLKWTP PKGT
	Isoform 5 [UniParc]. Checksum: 906F630E44BAFD2B	FASTA	472	55,135
	10 20 30 40 50 60 MPRRKRNAGS SSDGTEDSDF STDLEHTDSS ESDGTSRRSA RVTRSSARLS QSSQGHLTGK 70 80 90 100 110 120 HERHFSISGC PLYHNLSADE CKVRAQSRDK QIEERMLSHR QDDNNRHATR HQAPTERQLR 130 140 150 160 170 180 YKEKVAELRK KRNSGLSKEQ KEKYMEHRQT YGNTREPLLE NLTSEYDLDL FRRAQARASE 190 200 210 220 230 240 DLEKLRLQGQ ITEGSNMIKT IAFGRYELDT WYHSPYPEEY ARLGRLYMCE FCLKYMKSQT 250 260 270 280 290 300 ILRRHMAKCV WKHPPGDEIY RKGSISVFEV DGKKNKIYCQ NLCLLAKLFL DHKTLYYDVE 310 320 330 340 350 360 PFLFYVMTEA DNTGCHLIGY FSKEKNSFLN YNVSCILTMP QYMRQGYGKM LIDFSYLLSK 370 380 390 400 410 420 VEEKVGSPER PLSDLGLISY RSYWKEVLLR YLHNFQGKEI SIKEISQETA VNPVDIVSTL 430 440 450 460 470 QALQMLKYWK GKHLVLKRQD LIDEWIAKEA KRSNSNKTMD PSCLKWTPPK GT

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] [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. , 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. , 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. , 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, 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 , B4DF85, B4DFB4, B4DFE0, B4DGY4, E7ER15, G5E9K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 116 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.