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P38254 (TTL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable tubulin--tyrosine ligase PBY1

EC=6.3.2.25
Alternative name(s):
P-body-associated protein 1
Gene names
Name:PBY1
Ordered Locus Names:YBR094W
ORF Names:YBR0821
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable P-body-associated tubuline--tyrosine ligase By similarity. Ref.7

Catalytic activity

ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP + phosphate.

Cofactor

Magnesium By similarity.

Potassium By similarity.

Subcellular location

Cytoplasm. CytoplasmP-body Ref.5 Ref.7.

Miscellaneous

Present with 1770 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the tubulin--tyrosine ligase family.

Contains 1 TTL domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Potassium
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein modification process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasmic mRNA processing body

Inferred from direct assay Ref.7. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

hydrolase activity

Inferred from electronic annotation. Source: InterPro

tubulin-tyrosine ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCP1Q125173EBI-21533,EBI-38519

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753Probable tubulin--tyrosine ligase PBY1
PRO_0000212448

Regions

Domain343 – 734392TTL

Amino acid modifications

Modified residue6001Phosphoserine Ref.8

Experimental info

Sequence conflict352 – 3554HALK → TPE in CAA49508. Ref.4
Sequence conflict4501A → R in CAA55599. Ref.1
Sequence conflict4501A → R in CAA85047. Ref.2
Sequence conflict5631H → R in CAA49508. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P38254 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 925C4E4CAB6679E9

FASTA75386,353
        10         20         30         40         50         60 
MRVLITNDDG PLSDQFSPYI RPFIQHIKRN YPEWKITVCV PHVQKSWVGK AHLAGKNLTA 

        70         80         90        100        110        120 
QFIYSKVDAE DNTFWGPFIQ PQIRSENSKL PYVLNAEIPK DTIEWILIDG TPASCANIGL 

       130        140        150        160        170        180 
HLLSNEPFDL VLSGPNVGRN TSAAYITSSG TVGGAMESVI TGNTKAIAIS WAYFNGLKNV 

       190        200        210        220        230        240 
SPLLMEKASK RSLDVIKHLV KNWDPKTDLY SINIPLVESL SDDTKVYYAP IWENRWIPIF 

       250        260        270        280        290        300 
NGPHINLENS FAEIEDGNES SSISFNWAPK FGAHKDSIHY MDEYKDRTVL TDAEVIESEM 

       310        320        330        340        350        360 
ISVTPMKATF KGVNHLLGEL KLTEEENNLS KTNNLIVVSI DPMEYIYKPL THALKKYLPQ 

       370        380        390        400        410        420 
VEIVSNLPEF DNGGCEKEMK VFHYGDYEQL DMDKLMELPN NYFTNSYIYR KALIRKHFLS 

       430        440        450        460        470        480 
HTIQTYTAKN PESILKKAYL ESFTIDLDYA EFLDDALDEN WELRQELENE SQDKWWIVKP 

       490        500        510        520        530        540 
SMSDKGQGIR VFKTIEDLQA IFDSFDDEDS EAEESGNDDD ADDVNGEFMD NNKVNISQLR 

       550        560        570        580        590        600 
HFIIQEYLTN PLLLASMDNR KFHIRCYVVC RGDLQVFVYD RMLALFAAKP FVPLDPYAYS 

       610        620        630        640        650        660 
VTDLKDLECH LTNTCLQSKK KDKDSSVLEF DSIEEIPNER KSNIKEQIHS ITNDVFLAAV 

       670        680        690        700        710        720 
NVNRLNFQPL PNAFETYGVD FLIDSNYEVK LLEINAFPDF KQTGKDLKNL IDELFDDTVK 

       730        740        750 
YCVTPIFNEN RNKTDDETDP NFVKVIDYTS NGW 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a 70 kb region on the right arm of yeast chromosome II."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 10:1363-1381(1994) [PubMed: 7900426] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 450.
Strain: ATCC 204508 / S288c.
[4]Dekker P.J.T., Hoekert W., van Oosterum K., Grivell L.A.
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-753.
Strain: ATCC 26109 / X2180.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"Microtubule disruption stimulates P-body formation."
Sweet T.J., Boyer B., Hu W., Baker K.E., Coller J.
RNA 13:493-502(2007) [PubMed: 17307817] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[8]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78993 Genomic DNA. Translation: CAA55599.1.
Z35963 Genomic DNA. Translation: CAA85047.1.
X69881 Genomic DNA. Translation: CAA49508.1.
BK006936 Genomic DNA. Translation: DAA07215.2.
PIRS48261.
RefSeqNP_009652.2. NM_001178442.2.

3D structure databases

ProteinModelPortalP38254.
SMRP38254. Positions 2-317, 476-505, 672-699.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1585N.
IntActP38254. 8 interactions.
MINTMINT-409689.
STRINGP38254.

Proteomic databases

PeptideAtlasP38254.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID852391.
KEGGsce:YBR094W.
NMPDRfig|4932.3.peg.351.

Organism-specific databases

CYGDYBR094w.
SGDS000000298. PBY1.

Phylogenomic databases

eggNOGfuNOG04394.
GeneTreeEFGT00050000003168.
HOGENOMHBG324223.
OMADFKQTGD.
OrthoDBEOG4HMNJK.

Gene expression databases

ArrayExpressP38254.
GenevestigatorP38254.
GermOnlineYBR094W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013816. ATP_grasp_subdomain_2.
IPR002828. SurE-like_Pase/nucleotidase.
IPR004344. Tub_tyr_ligase.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 2 hits.
PANTHERPTHR12241. Tub_tyr_ligase. 1 hit.
PfamPF01975. SurE. 1 hit.
PF03133. TTL. 1 hit.
[Graphical view]
SUPFAMSSF64167. SurE-like_Pase/nucleotidase. 1 hit.
TIGRFAMsTIGR00087. SurE. 1 hit.
PROSITEPS51221. TTL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971210.

Entry information

Entry nameTTL_YEAST
AccessionPrimary (citable) accession number: P38254
Secondary accession number(s): D6VQ95
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

SIMILARITY comments

Index of protein domains and families