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Protein

tRNA acetyltransferase TAN1

Gene

TAN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable tRNA acetyltransferase required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs. Binds RNA.1 Publication

GO - Molecular functioni

  • RNA binding Source: SGD
  • transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  • tRNA modification Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30706-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA acetyltransferase TAN1 (EC:2.3.-.-)
Gene namesi
Name:TAN1
Ordered Locus Names:YGL232W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL232W.
SGDiS000003201. TAN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289tRNA acetyltransferase TAN1PRO_0000072426Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53072.
PeptideAtlasiP53072.

PTM databases

iPTMnetiP53072.

Interactioni

Protein-protein interaction databases

BioGridi33007. 35 interactions.
IntActiP53072. 2 interactions.
MINTiMINT-2492386.

Structurei

3D structure databases

ProteinModelPortaliP53072.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 259114THUMPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 THUMP domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000002365.
HOGENOMiHOG000065974.
InParanoidiP53072.
KOiK06963.
OMAiKFNVMEI.
OrthoDBiEOG77Q57P.

Family and domain databases

InterProiIPR004114. THUMP_dom.
[Graphical view]
PfamiPF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEiPS51165. THUMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53072-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEKRNRNGK DANSQNRKKF KVSSGFLDPG TSGIYATCSR RHERQAAQEL
60 70 80 90 100
QLLFEEKFQE LYGDIKEGED ESENDEKKDL SIEDQIKKEL QELKGEETGK
110 120 130 140 150
DLSSGETKKK DPLAFIDLNC ECVTFCKTRK PIVPEEFVLS IMKDLADPKN
160 170 180 190 200
MVKRTRYVQK LTPITYSCNA KMEQLIKLAN LVIGPHFHDP SNVKKNYKFA
210 220 230 240 250
VEVTRRNFNT IERMDIINQV VKLVNKEGSE FNHTVDLKNY DKLILVECFK
260 270 280
SNIGMCVVDG DYKTKYRKYN VQQLYESKFR KDEDKSVKQ
Length:289
Mass (Da):33,550
Last modified:October 1, 1996 - v1
Checksum:i0E1C8C55E70CEB28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72754 Genomic DNA. Translation: CAA96950.1.
BK006941 Genomic DNA. Translation: DAA07886.1.
PIRiS64254.
RefSeqiNP_011282.1. NM_001181098.1.

Genome annotation databases

EnsemblFungiiYGL232W; YGL232W; YGL232W.
GeneIDi852619.
KEGGisce:YGL232W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72754 Genomic DNA. Translation: CAA96950.1.
BK006941 Genomic DNA. Translation: DAA07886.1.
PIRiS64254.
RefSeqiNP_011282.1. NM_001181098.1.

3D structure databases

ProteinModelPortaliP53072.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33007. 35 interactions.
IntActiP53072. 2 interactions.
MINTiMINT-2492386.

PTM databases

iPTMnetiP53072.

Proteomic databases

MaxQBiP53072.
PeptideAtlasiP53072.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL232W; YGL232W; YGL232W.
GeneIDi852619.
KEGGisce:YGL232W.

Organism-specific databases

EuPathDBiFungiDB:YGL232W.
SGDiS000003201. TAN1.

Phylogenomic databases

GeneTreeiENSGT00390000002365.
HOGENOMiHOG000065974.
InParanoidiP53072.
KOiK06963.
OMAiKFNVMEI.
OrthoDBiEOG77Q57P.

Enzyme and pathway databases

BioCyciYEAST:G3O-30706-MONOMER.

Miscellaneous databases

NextBioi971829.
PROiP53072.

Family and domain databases

InterProiIPR004114. THUMP_dom.
[Graphical view]
PfamiPF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
PROSITEiPS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The Saccharomyces cerevisiae TAN1 gene is required for N4-acetylcytidine formation in tRNA."
    Johansson M.J., Bystroem A.S.
    RNA 10:712-719(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTAN1_YEAST
AccessioniPrimary (citable) accession number: P53072
Secondary accession number(s): D6VVA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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 one 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.