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Q9D1P2

- KAT8_MOUSE

UniProt

Q9D1P2 - KAT8_MOUSE

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Protein
Histone acetyltransferase KAT8
Gene
Kat8, Mof, Myst1
Organism
Mus musculus (Mouse)
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 By similarity.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741 By similarity
Binding sitei319 – 3191Acetyl-CoA By similarity
Active sitei350 – 3501Proton donor/acceptor By similarity
Binding sitei354 – 3541Acetyl-CoA By similarity
Binding sitei363 – 3631Acetyl-CoA By similarity
Binding sitei432 – 4321Acetyl-CoA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri208 – 23023C2HC-type
Add
BLAST

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. histone acetyltransferase activity (H4-K16 specific) Source: Ensembl
  4. histone acetyltransferase activity (H4-K5 specific) Source: Ensembl
  5. histone acetyltransferase activity (H4-K8 specific) Source: Ensembl
  6. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. histone H4-K16 acetylation Source: UniProtKB
  2. histone H4-K5 acetylation Source: UniProtKB
  3. histone H4-K8 acetylation Source: UniProtKB
  4. myeloid cell differentiation Source: Ensembl
  5. negative regulation of transcription, DNA-templated Source: Ensembl
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. 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_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase KAT8 (EC:2.3.1.48)
Alternative name(s):
Lysine acetyltransferase 8
MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
Short name:
MYST-1
Gene namesi
Name:Kat8
Synonyms:Mof, Myst1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1915023. Kat8.

Subcellular locationi

Nucleus. Chromosome By similarity

GO - Cellular componenti

  1. MLL1 complex Source: UniProtKB
  2. MSL complex Source: UniProtKB
  3. histone acetyltransferase complex Source: UniProtKB
  4. kinetochore Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 458457Histone acetyltransferase KAT8
PRO_0000051567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei113 – 1131N6-acetyllysine By similarity
Modified residuei274 – 2741N6-acetyllysine; by autocatalysis By similarity

Post-translational modificationi

Autoacetylation at Lys-274 is required for proper function By similarity.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9D1P2.
PRIDEiQ9D1P2.

PTM databases

PhosphoSiteiQ9D1P2.

Expressioni

Gene expression databases

BgeeiQ9D1P2.
CleanExiMM_MYST1.
GenevestigatoriQ9D1P2.

Interactioni

Subunit structurei

Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. 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 By similarity. Interacts with MSL1; the interaction is direct.1 Publication

Protein-protein interaction databases

BioGridi212433. 21 interactions.
IntActiQ9D1P2. 16 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi59 – 657
Turni66 – 683
Beta strandi69 – 8113
Turni82 – 854
Beta strandi86 – 927
Turni94 – 963
Beta strandi102 – 1043
Turni106 – 1083
Turni112 – 1143
Beta strandi115 – 1173

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGSNMR-A50-169[»]
ProteinModelPortaliQ9D1P2.
SMRiQ9D1P2. Positions 47-169, 178-448.

Miscellaneous databases

EvolutionaryTraceiQ9D1P2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 12355Chromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 458285Sufficient for interaction with KANSL1 By similarity
Add
BLAST
Regioni324 – 3307Acetyl-CoA binding By similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.
Contains 1 chromo domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
HOVERGENiHBG053268.
InParanoidiQ9D1P2.
KOiK11308.
OMAiDGRDHKI.
OrthoDBiEOG7WHH8N.
PhylomeDBiQ9D1P2.
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.

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: Q9D1P2-1) [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

MAAQGATAAV AATTSGTVGE GEPGPGENAA VEGPARSPGR VSPPTPARGE    50
PEVTVEIGET YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL 100
DEWVDKNRLA LTKTVKDAVQ KNSEKYLSEL AEQPERKITR NQKRKHDEIN 150
HVQKTYAEMD PTTAALEKEH EAITKVKYVD KIHIGNYEID AWYFSPFPED 200
YGKQPKLWLC EYCLKYMKFE KSYRFHLGQC QWRQPPGKEI YRKSNISVYE 250
VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 300
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE 350
KPLSDLGKLS YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL 400
QSLNMVKYWK GQHVICVTPK LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH 450
KQVKLSKK 458
Length:458
Mass (Da):52,574
Last modified:June 1, 2001 - v1
Checksum:iFA25E0C8D7E46CEC
GO
Isoform 2 (identifier: Q9D1P2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-194: TYAEMDPTTA...GNYEIDAWYF → VLAPPFSGPS...LFTYEKILSL
     195-458: Missing.

Show »
Length:194
Mass (Da):21,398
Checksum:i36334369729A61C2
GO

Sequence cautioni

The sequence BAC25539.1 differs from that shown. Reason: Frameshift at position 236.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei155 – 19440TYAEM…DAWYF → VLAPPFSGPSQQSHSNSHVK AGSMPGFFSRLFTYEKILSL in isoform 2.
VSP_014580Add
BLAST
Alternative sequencei195 – 458264Missing in isoform 2.
VSP_014581Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851L → F in AAH36284. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK003264 mRNA. Translation: BAB22680.1.
AK018002 mRNA. Translation: BAC25539.1. Frameshift.
AK029350 mRNA. Translation: BAC26411.1.
AK146710 mRNA. Translation: BAE27376.1.
BC036284 mRNA. Translation: AAH36284.1.
CCDSiCCDS21885.1. [Q9D1P2-1]
RefSeqiNP_080646.1. NM_026370.1. [Q9D1P2-1]
UniGeneiMm.425492.

Genome annotation databases

EnsembliENSMUST00000033070; ENSMUSP00000033070; ENSMUSG00000030801. [Q9D1P2-1]
GeneIDi67773.
KEGGimmu:67773.
UCSCiuc009jxg.1. mouse. [Q9D1P2-2]
uc009jxh.1. mouse. [Q9D1P2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK003264 mRNA. Translation: BAB22680.1 .
AK018002 mRNA. Translation: BAC25539.1 . Frameshift.
AK029350 mRNA. Translation: BAC26411.1 .
AK146710 mRNA. Translation: BAE27376.1 .
BC036284 mRNA. Translation: AAH36284.1 .
CCDSi CCDS21885.1. [Q9D1P2-1 ]
RefSeqi NP_080646.1. NM_026370.1. [Q9D1P2-1 ]
UniGenei Mm.425492.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WGS NMR - A 50-169 [» ]
ProteinModelPortali Q9D1P2.
SMRi Q9D1P2. Positions 47-169, 178-448.
ModBasei Search...

Protein-protein interaction databases

BioGridi 212433. 21 interactions.
IntActi Q9D1P2. 16 interactions.

PTM databases

PhosphoSitei Q9D1P2.

Proteomic databases

PaxDbi Q9D1P2.
PRIDEi Q9D1P2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033070 ; ENSMUSP00000033070 ; ENSMUSG00000030801 . [Q9D1P2-1 ]
GeneIDi 67773.
KEGGi mmu:67773.
UCSCi uc009jxg.1. mouse. [Q9D1P2-2 ]
uc009jxh.1. mouse. [Q9D1P2-1 ]

Organism-specific databases

CTDi 84148.
MGIi MGI:1915023. Kat8.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000182457.
HOVERGENi HBG053268.
InParanoidi Q9D1P2.
KOi K11308.
OMAi DGRDHKI.
OrthoDBi EOG7WHH8N.
PhylomeDBi Q9D1P2.
TreeFami TF317619.

Enzyme and pathway databases

Reactomei REACT_226917. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTracei Q9D1P2.
NextBioi 325529.
PROi Q9D1P2.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1P2.
CleanExi MM_MYST1.
Genevestigatori Q9D1P2.

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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Amnion, Embryo, Head and Thymus.
  2. "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).
    Strain: FVB/N.
    Tissue: Liver.
  3. "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: INTERACTION WITH MSL1.
  4. "Solution structure of the Tudor domain from mouse hypothetical protein homologous to histone acetyltransferase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 50-169 (ISOFORM 1).

Entry informationi

Entry nameiKAT8_MOUSE
AccessioniPrimary (citable) accession number: Q9D1P2
Secondary accession number(s): Q3UIY0
, Q8BJ69, Q8BJ76, Q8CI73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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