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P25037 (UBP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 1

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 1
Ubiquitin thioesterase 1
Ubiquitin-specific-processing protease 1
Gene names
Name:UBP1
Ordered Locus Names:YDL122W
ORF Names:D2250
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to 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).

Miscellaneous

Present with 8970 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 809809Ubiquitin carboxyl-terminal hydrolase 1
PRO_0000080585

Regions

Domain101 – 738638USP

Sites

Active site1101Nucleophile By similarity
Active site6971Proton acceptor By similarity

Amino acid modifications

Modified residue5301Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue5311Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue5551Phosphoserine Ref.5 Ref.8
Modified residue6181Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue6381Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue6521Phosphothreonine Ref.8
Modified residue6531Phosphoserine Ref.8
Modified residue6541Phosphoserine Ref.8
Modified residue6701Phosphoserine Ref.5
Modified residue7551Phosphoserine Ref.5 Ref.7 Ref.8

Experimental info

Sequence conflict4181L → P in AAA35189. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25037 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 07BA266FB43C2C04

FASTA80992,769
        10         20         30         40         50         60 
MDLFIESKIN SLLQFLFGSR QDFLRNFKTW SNNNNNLSIY LLIFGIVVFF YKKPDHLNYI 

        70         80         90        100        110        120 
VESVSEMTTN FRNNNSLSRW LPRSKFTHLD EEILKRGGFI AGLVNDGNTC FMNSVLQSLA 

       130        140        150        160        170        180 
SSRELMEFLD NNVIRTYEEI EQNEHNEEGN GQESAQDEAT HKKNTRKGGK VYGKHKKKLN 

       190        200        210        220        230        240 
RKSSSKEDEE KSQEPDITFS VALRDLLSAL NAKYYRDKPY FKTNSLLKAM SKSPRKNILL 

       250        260        270        280        290        300 
GYDQEDAQEF FQNILAELES NVKSLNTEKL DTTPVAKSEL PDDALVGQLN LGEVGTVYIP 

       310        320        330        340        350        360 
TEQIDPNSIL HDKSIQNFTP FKLMTPLDGI TAERIGCLQC GENGGIRYSV FSGLSLNLPN 

       370        380        390        400        410        420 
ENIGSTLKLS QLLSDWSKPE IIEGVECNRC ALTAAHSHLF GQLKEFEKKP EGSIPEKLIN 

       430        440        450        460        470        480 
AVKDRVHQIE EVLAKPVIDD EDYKKLHTAN MVRKCSKSKQ ILISRPPPLL SIHINRSVFD 

       490        500        510        520        530        540 
PRTYMIRKNN SKVLFKSRLN LAPWCCDINE INLDARLPMS KKEKAAQQDS SEDENIGGEY 

       550        560        570        580        590        600 
YTKLHERFEQ EFEDSEEEKE YDDAEGNYAS HYNHTKDISN YDPLNGEVDG VTSDDEDEYI 

       610        620        630        640        650        660 
EETDALGNTI KKRIIEHSDV ENENVKDNEE LQEIDNVSLD EPKINVEDQL ETSSDEEDVI 

       670        680        690        700        710        720 
PAPPINYARS FSTVPATPLT YSLRSVIVHY GTHNYGHYIA FRKYRGCWWR ISDETVYVVD 

       730        740        750        760        770        780 
EAEVLSTPGV FMLFYEYDFD EETGKMKDDL EAIQSNNEED DEKEQEQKGV QEPKESQEQG 

       790        800 
EGEEQEEGQE QMKFERTEDH RDISGKDVN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae."
Tobias J.W., Varshavsky A.
J. Biol. Chem. 266:12021-12028(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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-530; SER-531; SER-555; SER-618; SER-638; SER-670 AND SER-755, 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 SER-530; SER-531; SER-618; SER-638 AND SER-755, 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-530; SER-531; SER-555; SER-618; SER-638; THR-652; SER-653; SER-654 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63484 Genomic DNA. Translation: AAA35189.1.
Z74170 Genomic DNA. Translation: CAA98690.1.
BK006938 Genomic DNA. Translation: DAA11738.1.
PIRS67665.
RefSeqNP_010161.1. NM_001180181.1.

3D structure databases

ProteinModelPortalP25037.
SMRP25037. Positions 657-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31941. 107 interactions.
IntActP25037. 23 interactions.
MINTMINT-2788387.
STRING4932.YDL122W.

Protein family/group databases

MEROPSC19.002.

Proteomic databases

MaxQBP25037.
PaxDbP25037.
PeptideAtlasP25037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL122W; YDL122W; YDL122W.
GeneID851435.
KEGGsce:YDL122W.

Organism-specific databases

SGDS000002280. UBP1.

Phylogenomic databases

eggNOGNOG259866.
HOGENOMHOG000093934.
KOK11870.
OMAFMLFYEY.
OrthoDBEOG7HB5JX.

Enzyme and pathway databases

BioCycYEAST:G3O-29521-MONOMER.

Gene expression databases

GenevestigatorP25037.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968666.

Entry information

Entry nameUBP1_YEAST
AccessionPrimary (citable) accession number: P25037
Secondary accession number(s): D6VRM8, Q07543
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 5, 2010
Last modified: May 14, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries