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Protein

tRNA(Thr) (cytosine(32)-N(3))-methyltransferase

Gene

ABP140

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that mediates 3-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser). Binds F-actin and shows weak F-actin cross-linking activity.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + cytosine(32) in tRNA(Thr) = S-adenosyl-L-homocysteine + N(3)-methylcytosine(32) in tRNA(Thr).2 Publications
S-adenosyl-L-methionine + cytosine(32) in tRNA(Ser) = S-adenosyl-L-homocysteine + N(3)-methylcytosine(32) in tRNA(Ser).2 Publications

GO - Molecular functioni

  • actin filament binding Source: SGD
  • protein binding, bridging Source: SGD
  • tRNA (cytosine-3-)-methyltransferase activity Source: SGD

GO - Biological processi

  • actin filament bundle assembly Source: SGD
  • tRNA methylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Actin-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-33735-MONOMER.
BRENDAi2.1.1.268. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA(Thr) (cytosine(32)-N(3))-methyltransferase (EC:2.1.1.2682 Publications)
Alternative name(s):
Actin-binding protein of 140 kDa
tRNA methyltransferase of 140 kDa
Gene namesi
Name:ABP140
Synonyms:TRM140
Ordered Locus Names:YOR239W
ORF Names:YOR240W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR239W.
SGDiS000005765. ABP140.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • actin filament Source: SGD
  • actin filament bundle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 628627tRNA(Thr) (cytosine(32)-N(3))-methyltransferasePRO_0000204458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei150 – 1501PhosphothreonineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei326 – 3261PhosphoserineCombined sources
Modified residuei347 – 3471PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08641.
PeptideAtlasiQ08641.

PTM databases

iPTMnetiQ08641.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: SGD
  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi34631. 31 interactions.
DIPiDIP-4117N.
IntActiQ08641. 27 interactions.
MINTiMINT-493479.

Structurei

3D structure databases

ProteinModelPortaliQ08641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00520000055554.
HOGENOMiHOG000033747.
InParanoidiQ08641.
KOiK17053.
OMAiHEANNIV.
OrthoDBiEOG7X3R2C.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR013217. Methyltransf_12.
IPR026113. MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR22809. PTHR22809. 1 hit.
PfamiPF08242. Methyltransf_12. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by ribosomal frameshifting. AlignAdd to basket

Isoform 1 (identifier: Q08641-1) [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
MGVADLIKKF ESISKEEGDA TVDTNSSSKP LKSNDETKEL HQQESTAVPQ
60 70 80 90 100
EVDVNEEFEN EPETINSSRT AEKPLETNLP KPETNEEDEE EGSMSENKIY
110 120 130 140 150
SKGENADINV NDFQEYKEME NTGAEVLASS VEESDAIQEG VAEETEGIAT
160 170 180 190 200
PKQKENEKND ESEEESANNA SEPAEEYSQS EEDADIEQSN GKETENAENA
210 220 230 240 250
SQQANDGSTS TTTSKNKKKK NKKKNKKKRN GNVNTNANVD DSTKTGENDD
260 270 280 290 300
TTGDTTSSTT SAIQEVNDLE VVDDSCLGID QQHNREHLKA LTQDVKEETL
310 320 330 340 350
ENIAHEGRGD NTGDQNAVEK SDFEKSDTEG SRIGRDLPFE FGKRNLTEES
360 370 380 390 400
DVWDHNAWDN VEWGEEQVQQ AEEKIKEQFK HPVPEFDKKL YNENPARYWD
410 420 430 440 450
IFYKNNKENF FKDRKWLQIE FPILYASTRK DAEPVTIFEI GCGAGNTFFP
460 470 480 490 500
ILKDNENENL RIIAADFAPR AVELVKNSEQ FNPKYGHATV WDLANPDGNL
510 520 530 540 550
PDGVEPHSVD IAVMIFVFSA LAPNQWDQAM DNLHKILKPG GKIIFRDYGA
560 570 580 590 600
YDLTQVRFKK NRILEENFYV RGDGTRVYFF SEEKLREIFT KKYFLENKIG
610 620
TDRRLLVNRK RQLKMYRCWV QAVFDVPQ
Note: Produced by ribosomal frameshifting between codon Leu-277 and Gly-278.
Length:628
Mass (Da):71,486
Last modified:January 23, 2007 - v3
Checksum:i74F9CA30BC5BCABF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75147 Genomic DNA. Translation: CAA99460.1. Sequence problems.
Z75147 Genomic DNA. Translation: CAA99461.1. Sequence problems.
BK006948 Genomic DNA. Translation: DAA11008.1.
RefSeqiNP_014882.4. NM_001183658.6. [Q08641-1]

Genome annotation databases

EnsemblFungiiYOR239W; YOR239W; YOR239W. [Q08641-1]
GeneIDi854414.
KEGGisce:YOR239W.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75147 Genomic DNA. Translation: CAA99460.1. Sequence problems.
Z75147 Genomic DNA. Translation: CAA99461.1. Sequence problems.
BK006948 Genomic DNA. Translation: DAA11008.1.
RefSeqiNP_014882.4. NM_001183658.6. [Q08641-1]

3D structure databases

ProteinModelPortaliQ08641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34631. 31 interactions.
DIPiDIP-4117N.
IntActiQ08641. 27 interactions.
MINTiMINT-493479.

PTM databases

iPTMnetiQ08641.

Proteomic databases

MaxQBiQ08641.
PeptideAtlasiQ08641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR239W; YOR239W; YOR239W. [Q08641-1]
GeneIDi854414.
KEGGisce:YOR239W.

Organism-specific databases

EuPathDBiFungiDB:YOR239W.
SGDiS000005765. ABP140.

Phylogenomic databases

GeneTreeiENSGT00520000055554.
HOGENOMiHOG000033747.
InParanoidiQ08641.
KOiK17053.
OMAiHEANNIV.
OrthoDBiEOG7X3R2C.

Enzyme and pathway databases

BioCyciYEAST:G3O-33735-MONOMER.
BRENDAi2.1.1.268. 984.

Miscellaneous databases

PROiQ08641.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR013217. Methyltransf_12.
IPR026113. MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR22809. PTHR22809. 1 hit.
PfamiPF08242. Methyltransf_12. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae."
    Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.
    Yeast 12:1575-1586(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae."
    Asakura T., Sasaki T., Nagano F., Satoh A., Obaishi H., Nishioka H., Imamura H., Hotta K., Tanaka K., Nakanishi H., Takai Y.
    Oncogene 16:121-130(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-13; 39-73; 103-116; 245-287; 561-575 AND 599-609, FUNCTION, SUBCELLULAR LOCATION.
    Strain: BJ5457.
  5. "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-93; SER-321 AND SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 THR-150 AND SER-326, 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-93; SER-321; SER-326 AND THR-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Cotranslational transport of ABP140 mRNA to the distal pole of S. cerevisiae."
    Kilchert C., Spang A.
    EMBO J. 30:3567-3580(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MRNA TRANSLATION.
  10. "A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop."
    D'Silva S., Haider S.J., Phizicky E.M.
    RNA 17:1100-1110(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  11. "Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae."
    Noma A., Yi S., Katoh T., Takai Y., Suzuki T., Suzuki T.
    RNA 17:1111-1119(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiAB140_YEAST
AccessioniPrimary (citable) accession number: Q08641
Secondary accession number(s): D6W2U2, Q08644
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

N- and C-terminal domains are encoded in separate ORFs that are translated into one protein via a +1 frameshift (PubMed:9467951). ABP140 mRNA translation follows a cotranslational transport: mRNA is transported to the distal pole of the mother cell, independently of the SHE machinery, and follows a translational coupling, in which ABP140 mRNA is tethered to actin cables via its nascent protein product and is transported to the distal pole by actin retrograde flow (PubMed:21792172).2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.