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Protein

Histone acetyltransferase Tip60 homolog

Gene

mys-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probable catalytic subunit of the Tip60 chromatin-remodeling complex. May acetylate nucleosomal histone H4 and H2A. Acts in the determination of vulval cell fates.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei344 – 3441Proton donor/acceptorBy similarity
Binding sitei348 – 3481Acetyl-CoABy similarity
Binding sitei357 – 3571Acetyl-CoABy similarity

GO - Molecular functioni

GO - Biological processi

  • cell fate specification Source: WormBase
  • multicellular organismal development Source: UniProtKB-KW
  • protein localization to chromatin Source: WormBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Developmental protein, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_285408. formation of the beta-catenin:TCF transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase Tip60 homolog (EC:2.3.1.48By similarity)
Alternative name(s):
Myst family histone acetyltransferase-like protein 1
Gene namesi
Name:mys-1
ORF Names:VC5.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiVC5.4; CE21225; WBGene00007029; mys-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Histone acetyltransferase Tip60 homologPRO_0000245807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-268 is required for binding histones with high affinity and for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9TYU5.

Interactioni

Protein-protein interaction databases

BioGridi44141. 12 interactions.
IntActiQ9TYU5. 18 interactions.
STRINGi6239.VC5.4.1.

Structurei

3D structure databases

ProteinModelPortaliQ9TYU5.
SMRiQ9TYU5. Positions 12-86, 169-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 446279MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 3133Acetyl-CoA bindingBy similarity
Regioni318 – 3247Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ9TYU5.
KOiK11304.
OMAiVEGHECA.
PhylomeDBiQ9TYU5.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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]

Sequencei

Sequence statusi: Complete.

Q9TYU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEPKKEIIE DENHGISKKI PTDPRQYEKV TEGCRLLVMM ASQEEERWAE
60 70 80 90 100
VISRCRAANG SIKFYVHYID CNRRLDEWVQ SDRLNLASCE LPKKGGKKGA
110 120 130 140 150
HLREENRDSN ENEGKKSGRK RKIPLLPMDD LKAESVDPLQ AISTMTSGST
160 170 180 190 200
PSLRGSMSMV GHSEDAMTRI RNVECIELGR SRIQPWYFAP YPQQLTSLDC
210 220 230 240 250
IYICEFCLKY LKSKTCLKRH MEKCAMCHPP GNQIYSHDKL SFFEIDGRKN
260 270 280 290 300
KSYAQNLCLL AKLFLDHKTL YYDTDPFLFY VLTEEDEKGH HIVGYFSKEK
310 320 330 340 350
ESAEEYNVAC ILVLPPFQKK GYGSLLIEFS YELSKIEQKT GSPEKPLSDL
360 370 380 390 400
GLLSYRSYWS MAIMKELFAF KRRHPGEDIT VQDISQSTSI KREDVVSTLQ
410 420 430 440 450
QLDLYKYYKG SYIIVISDEK RQVYEKRIEA AKKKTRINPA ALQWRPKEYG

KKRAQIMF
Length:458
Mass (Da):53,143
Last modified:May 1, 2000 - v1
Checksum:i19D7727E5B47D10B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY551963 mRNA. Translation: AAS65427.1.
FO081233 Genomic DNA. Translation: CCD70078.1.
PIRiT33814.
RefSeqiNP_504796.1. NM_072395.3.
UniGeneiCel.2062.

Genome annotation databases

EnsemblMetazoaiVC5.4.1; VC5.4.1; WBGene00007029.
VC5.4.2; VC5.4.2; WBGene00007029.
GeneIDi179096.
KEGGicel:CELE_VC5.4.
UCSCiVC5.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY551963 mRNA. Translation: AAS65427.1.
FO081233 Genomic DNA. Translation: CCD70078.1.
PIRiT33814.
RefSeqiNP_504796.1. NM_072395.3.
UniGeneiCel.2062.

3D structure databases

ProteinModelPortaliQ9TYU5.
SMRiQ9TYU5. Positions 12-86, 169-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44141. 12 interactions.
IntActiQ9TYU5. 18 interactions.
STRINGi6239.VC5.4.1.

Proteomic databases

PaxDbiQ9TYU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiVC5.4.1; VC5.4.1; WBGene00007029.
VC5.4.2; VC5.4.2; WBGene00007029.
GeneIDi179096.
KEGGicel:CELE_VC5.4.
UCSCiVC5.4. c. elegans.

Organism-specific databases

CTDi179096.
WormBaseiVC5.4; CE21225; WBGene00007029; mys-1.

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ9TYU5.
KOiK11304.
OMAiVEGHECA.
PhylomeDBiQ9TYU5.

Enzyme and pathway databases

ReactomeiREACT_285408. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

NextBioi903906.
PROiQ9TYU5.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new class of C. elegans synMuv genes implicates a Tip60/NuA4-like HAT complex as a negative regulator of Ras signaling."
    Ceol C.J., Horvitz H.R.
    Dev. Cell 6:563-576(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiTIP60_CAEEL
AccessioniPrimary (citable) accession number: Q9TYU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.