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Reviewed, UniProtKB/Swiss-Prot P35127 (UBL1_YEAST)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin carboxyl-terminal hydrolase YUH1
    EC=3.4.19.12
Alternative name(s):
    Ubiquitin thioesterase
Gene names
Name: YUH1
Ordered Locus Names: YJR099W
ORF Names: J1941
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Ubiquitin-protein hydrolase is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin.

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sequence similarities

Belongs to the peptidase C12 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred by curator. Source: SGD

   Molecular functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin thiolesterase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Ubiquitin carboxyl-terminal hydrolase YUH1
PRO_0000211073

Regions

Region43 – 6018Ubiquitin binding 1 Potential
Region175 – 1839Ubiquitin binding 2 Potential

Sites

Active site901Nucleophile Ref.4
Active site1661Proton donor Ref.4
Active site1811Proton donor Ref.4
Site841Transition state stabilizer

Amino acid modifications

Modified residue1861Phosphoserine Ref.3

Secondary structure

................................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35127-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: D239FEE25798B395

FASTA23626,385
        10         20         30         40         50         60 
MSGENRAVVP IESNPEVFTN FAHKLGLKNE WAYFDIYSLT EPELLAFLPR PVKAIVLLFP 

        70         80         90        100        110        120 
INEDRKSSTS QQITSSYDVI WFKQSVKNAC GLYAILHSLS NNQSLLEPGS DLDNFLKSQS 

       130        140        150        160        170        180 
DTSSSKNRFD DVTTDQFVLN VIKENVQTFS TGQSEAPEAT ADTNLHYITY VEENGGIFEL 

       190        200        210        220        230 
DGRNLSGPLY LGKSDPTATD LIEQELVRVR VASYMENANE EDVLNFAMLG LGPNWE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a yeast ubiquitin-protein cleaving activity in Escherichia coli."
Miller H.I., Henzel W.J., Ridgway J.B., Kuang W.-J., Chisholm V., Liu C.-C.
Biotechnology (N.Y.) 7:698-704(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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-186, MASS SPECTROMETRY.
[4]"Structural basis for the specificity of ubiquitin C-terminal hydrolases."
Johnston S.C., Riddle S.M., Cohen R.E., Hill C.P.
EMBO J. 18:3877-3887(1999) [PubMed: 10406793] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UBIQUITIN, ACTIVE SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z49599 Genomic DNA. Translation: CAA89629.1.
PIRS51332.
RefSeqNP_012633.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CMXX-ray2.25A/C1-235[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5052N.
IntActP35127. 3 interactions.

Protein family/group databases

MEROPSC12.002.

Genome annotation databases

EnsemblYJR099W. Saccharomyces cerevisiae. [Contig view]
GeneID853562.
GenomeReviewsGene locus YJR099W in contig Y13136_GR.
KEGGsce:YJR099W.
NMPDRfig|4932.3.peg.3607.

Organism-specific databases

CYGDYJR099w.
SGDS000003860. YUH1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP35127.
OMAP35127. GRCVELD.

Enzyme and pathway databases

BRENDA3.4.19.12. 250.

Gene expression databases

ArrayExpressP35127.
GermOnlineYJR099W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001578. Peptidase_C12.
[Graphical view]
Gene3DG3DSA:3.40.532.10. Peptidase_C12. 1 hit.
PANTHERPTHR10589. Peptidase_C12. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
ProDomPD350662. Peptidase_C12. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio974317.

Entry information

Entry nameUBL1_YEAST
AccessionPrimary (citable) accession number: P35127
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome X

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents