Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9H7Z6

- KAT8_HUMAN

UniProt

Q9H7Z6 - KAT8_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone acetyltransferase KAT8

Gene

KAT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'.6 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei350 – 3501Proton donor/acceptor2 PublicationsCurated
Binding sitei354 – 3541Acetyl-CoA2 Publications
Binding sitei363 – 3631Acetyl-CoA2 Publications
Binding sitei432 – 4321Acetyl-CoA2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri208 – 23023C2HC-type1 PublicationAdd
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. histone acetyltransferase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. methylated histone binding Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone acetylation Source: UniProtKB
  3. histone H4-K16 acetylation Source: UniProtKB
  4. histone H4-K5 acetylation Source: UniProtKB
  5. histone H4-K8 acetylation Source: UniProtKB
  6. myeloid cell differentiation Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT8 (EC:2.3.1.484 Publications)
Alternative name(s):
Lysine acetyltransferase 8
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
Short name:
MYST-1
Short name:
hMOF
Gene namesi
Name:KAT8
Synonyms:MOF, MYST1
ORF Names:PP7073
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:17933. KAT8.

Subcellular locationi

Nucleus 2 Publications. Chromosome By similarity

GO - Cellular componenti

  1. histone acetyltransferase complex Source: UniProtKB
  2. kinetochore Source: Ensembl
  3. MLL1 complex Source: UniProtKB
  4. MSL complex Source: UniProtKB
  5. nuclear membrane Source: HPA
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi274 – 2741K → A: Abolishes histone acetyltransferase activity. 1 Publication
Mutagenesisi274 – 2741K → R: Abolishes histone acetyltransferase activity. 1 Publication
Mutagenesisi316 – 3161C → S: Strongly reduces histone acetyltransferase activity. 1 Publication
Mutagenesisi350 – 3501E → Q: Abolishes histone acetyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA38476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 458457Histone acetyltransferase KAT8PRO_0000051566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei113 – 1131N6-acetyllysine1 Publication
Modified residuei274 – 2741N6-acetyllysine; by autocatalysis5 Publications

Post-translational modificationi

Autoacetylation at Lys-274 is required for binding histone H4 with high affinity and for proper function.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H7Z6.
PaxDbiQ9H7Z6.
PRIDEiQ9H7Z6.

PTM databases

PhosphoSiteiQ9H7Z6.

Expressioni

Gene expression databases

BgeeiQ9H7Z6.
CleanExiHS_MYST1.
GenevestigatoriQ9H7Z6.

Organism-specific databases

HPAiHPA057106.

Interactioni

Subunit structurei

Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Interacts with MSL1; the interaction is direct. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KANSL1; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with the chromodomain of MORF4L1/MRG15. Interacts with ATM through the chromodomain. Interacts with KANSL1; the interaction is direct.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023092EBI-896414,EBI-8113From a different organism.
KMT2AQ031643EBI-896414,EBI-591370
RNF2Q994962EBI-896414,EBI-722416
TP53P046372EBI-896414,EBI-366083

Protein-protein interaction databases

BioGridi123914. 45 interactions.
IntActiQ9H7Z6. 12 interactions.
MINTiMINT-1897597.

Structurei

Secondary structure

1
458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi181 – 1844Combined sources
Beta strandi187 – 1904Combined sources
Helixi199 – 2035Combined sources
Beta strandi207 – 2093Combined sources
Turni211 – 2133Combined sources
Beta strandi216 – 2183Combined sources
Helixi220 – 22910Combined sources
Beta strandi236 – 2438Combined sources
Beta strandi246 – 2527Combined sources
Turni253 – 2553Combined sources
Helixi257 – 26812Combined sources
Helixi274 – 2774Combined sources
Beta strandi283 – 29210Combined sources
Beta strandi295 – 30511Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 3233Combined sources
Beta strandi325 – 3273Combined sources
Helixi328 – 34215Combined sources
Beta strandi347 – 3493Combined sources
Helixi355 – 37218Combined sources
Helixi383 – 3897Combined sources
Helixi393 – 40210Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi412 – 4154Combined sources
Helixi419 – 4279Combined sources
Turni429 – 4313Combined sources
Helixi440 – 4423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GIVX-ray1.94A174-449[»]
2PQ8X-ray1.45A174-449[»]
2Y0MX-ray2.70A174-458[»]
3QAHX-ray2.10A174-449[»]
3TOAX-ray3.00A177-458[»]
3TOBX-ray2.70A177-458[»]
4DNCX-ray2.05A/B170-458[»]
ProteinModelPortaliQ9H7Z6.
SMRiQ9H7Z6. Positions 47-169, 178-448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H7Z6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 12355ChromoAdd
BLAST
Domaini174 – 447274MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 458285Sufficient for interaction with KANSL1Add
BLAST
Regioni317 – 3193Acetyl-CoA binding2 Publications
Regioni324 – 3307Acetyl-CoA binding2 Publications

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated
Contains 1 chromo domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri208 – 23023C2HC-type1 PublicationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOVERGENiHBG053268.
InParanoidiQ9H7Z6.
KOiK11308.
OMAiDGRDHKI.
PhylomeDBiQ9H7Z6.
TreeFamiTF317619.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H7Z6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE
60 70 80 90 100
PEVTVEIGET YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL
110 120 130 140 150
DEWVDKNRLA LTKTVKDAVQ KNSEKYLSEL AEQPERKITR NQKRKHDEIN
160 170 180 190 200
HVQKTYAEMD PTTAALEKEH EAITKVKYVD KIHIGNYEID AWYFSPFPED
210 220 230 240 250
YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI YRKSNISVYE
260 270 280 290 300
VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG
310 320 330 340 350
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE
360 370 380 390 400
KPLSDLGKLS YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL
410 420 430 440 450
QSLNMVKYWK GQHVICVTPK LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH

KQVKLSKK
Length:458
Mass (Da):52,403
Last modified:July 5, 2005 - v2
Checksum:i66C474BE5B90E8E3
GO
Isoform 2 (identifier: Q9H7Z6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-458: VDSVCLKWAPPKHKQVKLSKK → GGWGAAVCRGRWGSVSIWTGRSQGLLIAVT

Show »
Length:467
Mass (Da):53,085
Checksum:i69AA4F8800E687E0
GO

Sequence cautioni

The sequence AAL55762.1 differs from that shown. Reason: Probable cloning artifact.Curated
The sequence AAL56648.1 differs from that shown. Reason: Frameshift at positions 23, 26 and 52. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221S → T in AAL55762. (PubMed:15498874)Curated
Sequence conflicti249 – 2491Y → H in BAB14827. (PubMed:14702039)Curated
Sequence conflicti372 – 3721I → N in BAB14827. (PubMed:14702039)Curated
Isoform 2 (identifier: Q9H7Z6-2)
Sequence conflicti454 – 4541I → M in AAH37773. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei438 – 45821VDSVC…KLSKK → GGWGAAVCRGRWGSVSIWTG RSQGLLIAVT in isoform 2. 2 PublicationsVSP_014579Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021872 mRNA. Translation: BAB13924.1.
AK024102 mRNA. Translation: BAB14827.1.
AK291106 mRNA. Translation: BAF83795.1.
AC009088 Genomic DNA. No translation available.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52157.1.
CH471192 Genomic DNA. Translation: EAW52158.1.
BC037773 mRNA. Translation: AAH37773.1.
AF217501 mRNA. Translation: AAL56648.1. Frameshift.
AF260665 mRNA. Translation: AAF72665.2.
AF289578 mRNA. Translation: AAL55762.1. Sequence problems.
AL050395 mRNA. Translation: CAH56416.1.
CCDSiCCDS10706.1. [Q9H7Z6-1]
CCDS45468.1. [Q9H7Z6-2]
RefSeqiNP_115564.2. NM_032188.2. [Q9H7Z6-1]
NP_892003.2. NM_182958.2. [Q9H7Z6-2]
UniGeneiHs.533803.

Genome annotation databases

EnsembliENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
GeneIDi84148.
KEGGihsa:84148.
UCSCiuc002eax.3. human. [Q9H7Z6-2]
uc002eay.3. human. [Q9H7Z6-1]

Polymorphism databases

DMDMi68565938.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK021872 mRNA. Translation: BAB13924.1 .
AK024102 mRNA. Translation: BAB14827.1 .
AK291106 mRNA. Translation: BAF83795.1 .
AC009088 Genomic DNA. No translation available.
AC135050 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52157.1 .
CH471192 Genomic DNA. Translation: EAW52158.1 .
BC037773 mRNA. Translation: AAH37773.1 .
AF217501 mRNA. Translation: AAL56648.1 . Frameshift.
AF260665 mRNA. Translation: AAF72665.2 .
AF289578 mRNA. Translation: AAL55762.1 . Sequence problems.
AL050395 mRNA. Translation: CAH56416.1 .
CCDSi CCDS10706.1. [Q9H7Z6-1 ]
CCDS45468.1. [Q9H7Z6-2 ]
RefSeqi NP_115564.2. NM_032188.2. [Q9H7Z6-1 ]
NP_892003.2. NM_182958.2. [Q9H7Z6-2 ]
UniGenei Hs.533803.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GIV X-ray 1.94 A 174-449 [» ]
2PQ8 X-ray 1.45 A 174-449 [» ]
2Y0M X-ray 2.70 A 174-458 [» ]
3QAH X-ray 2.10 A 174-449 [» ]
3TOA X-ray 3.00 A 177-458 [» ]
3TOB X-ray 2.70 A 177-458 [» ]
4DNC X-ray 2.05 A/B 170-458 [» ]
ProteinModelPortali Q9H7Z6.
SMRi Q9H7Z6. Positions 47-169, 178-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123914. 45 interactions.
IntActi Q9H7Z6. 12 interactions.
MINTi MINT-1897597.

Chemistry

BindingDBi Q9H7Z6.
ChEMBLi CHEMBL1932912.
GuidetoPHARMACOLOGYi 2668.

PTM databases

PhosphoSitei Q9H7Z6.

Polymorphism databases

DMDMi 68565938.

Proteomic databases

MaxQBi Q9H7Z6.
PaxDbi Q9H7Z6.
PRIDEi Q9H7Z6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219797 ; ENSP00000219797 ; ENSG00000103510 . [Q9H7Z6-1 ]
ENST00000448516 ; ENSP00000406037 ; ENSG00000103510 . [Q9H7Z6-2 ]
ENST00000543774 ; ENSP00000456933 ; ENSG00000103510 . [Q9H7Z6-1 ]
GeneIDi 84148.
KEGGi hsa:84148.
UCSCi uc002eax.3. human. [Q9H7Z6-2 ]
uc002eay.3. human. [Q9H7Z6-1 ]

Organism-specific databases

CTDi 84148.
GeneCardsi GC16P031130.
HGNCi HGNC:17933. KAT8.
HPAi HPA057106.
MIMi 609912. gene.
neXtProti NX_Q9H7Z6.
PharmGKBi PA38476.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOVERGENi HBG053268.
InParanoidi Q9H7Z6.
KOi K11308.
OMAi DGRDHKI.
PhylomeDBi Q9H7Z6.
TreeFami TF317619.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi KAT8. human.
EvolutionaryTracei Q9H7Z6.
GeneWikii MYST1.
GenomeRNAii 84148.
NextBioi 73476.
PROi Q9H7Z6.
SOURCEi Search...

Gene expression databases

Bgeei Q9H7Z6.
CleanExi HS_MYST1.
Genevestigatori Q9H7Z6.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 1).
    Tissue: Embryo.
  2. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2).
    Tissue: Brain.
  5. "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] OF 6-458 (ISOFORM 1).
  6. "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF."
    Neal K.C., Pannuti A., Smith E.R., Lucchesi J.C.
    Biochim. Biophys. Acta 1490:170-174(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-458 (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Tissue: Heart.
  7. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-458 (ISOFORM 1).
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-458 (ISOFORM 2).
    Tissue: Uterus.
  9. "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation."
    Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.
    J. Biol. Chem. 277:50860-50866(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MORF4L1, FUNCTION.
  10. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  11. Cited for: INTERACTION WITH ATM, FUNCTION.
  12. "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
    Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
    Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF MSL COMPLEX COMPONENTS, IDENTIFICATION BY MASS SPECTROMETRY.
  13. Erratum
    Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
    Mol. Cell. Biol. 26:387-387(2006)
  14. "Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila."
    Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M., Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M., Stunnenberg H.G., Saumweber H., Akhtar A.
    Mol. Cell 21:811-823(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KANSL1.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
    Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
  18. "The nonspecific lethal complex is a transcriptional regulator in Drosophila."
    Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H., Kadlec J., Fraterman S., Luscombe N.M., Akhtar A.
    Mol. Cell 38:827-841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KANSL1.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "MYST histone acetyltransferase 1."
    Structural genomics consortium (SGC)
    Submitted (MAY-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 174-449 IN COMPLEX WITH ACETYL-COA AND ZINC, ACETYLATION AT LYS-274.
  21. "Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274."
    Sun B., Guo S., Tang Q., Li C., Zeng R., Xiong Z., Zhong C., Ding J.
    Cell Res. 21:1262-1266(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 174-449 IN COMPLEX WITH ZINC IONS, ACETYLATION AT LYS-274.
  22. "Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
    Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
    Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-458 IN COMPLEX WITH MSL1; ZINC ION AND ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-274, INTERACTION WITH KANSL1; MSL1 AND MSL3, MUTAGENESIS OF LYS-274; CYS-316 AND GLU-350.
  23. "Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
    Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
    Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 170-458 IN COMPLEX WITH MSL1, ACETYLATION AT LYS-274, FUNCTION IN MSL AND NSL COMPLEX, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KANSL1; MSL1 AND MSL3.
  24. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 177-458 IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, ACETYLATION AT LYS-274, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-274.

Entry informationi

Entry nameiKAT8_HUMAN
AccessioniPrimary (citable) accession number: Q9H7Z6
Secondary accession number(s): A8K4Z1
, G5E9P2, Q659G0, Q7LC17, Q8IY59, Q8WYB4, Q8WZ14, Q9HAC5, Q9NR35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 26, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3