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Protein

Ubiquitin carboxyl-terminal hydrolase 1

Gene

UBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101NucleophilePROSITE-ProRule annotation
Active sitei697 – 6971Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: SGD

GO - Biological processi

  1. protein deubiquitination Source: SGD
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-29521-MONOMER.

Protein family/group databases

MEROPSiC19.002.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP1
Ordered Locus Names:YDL122W
ORF Names:D2250
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002280. UBP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. endoplasmic reticulum Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809Ubiquitin carboxyl-terminal hydrolase 1PRO_0000080585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei530 – 5301Phosphoserine3 Publications
Modified residuei531 – 5311Phosphoserine3 Publications
Modified residuei555 – 5551Phosphoserine2 Publications
Modified residuei618 – 6181Phosphoserine3 Publications
Modified residuei638 – 6381Phosphoserine3 Publications
Modified residuei652 – 6521Phosphothreonine1 Publication
Modified residuei653 – 6531Phosphoserine1 Publication
Modified residuei654 – 6541Phosphoserine1 Publication
Modified residuei670 – 6701Phosphoserine1 Publication
Modified residuei755 – 7551Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25037.
PaxDbiP25037.
PeptideAtlasiP25037.

Expressioni

Gene expression databases

GenevestigatoriP25037.

Interactioni

Protein-protein interaction databases

BioGridi31941. 107 interactions.
IntActiP25037. 23 interactions.
MINTiMINT-2788387.
STRINGi4932.YDL122W.

Structurei

3D structure databases

ProteinModelPortaliP25037.
SMRiP25037. Positions 657-735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 738638USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiNOG259866.
HOGENOMiHOG000093934.
InParanoidiP25037.
KOiK11870.
OMAiSIHINRS.
OrthoDBiEOG7HB5JX.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLFIESKIN SLLQFLFGSR QDFLRNFKTW SNNNNNLSIY LLIFGIVVFF
60 70 80 90 100
YKKPDHLNYI VESVSEMTTN FRNNNSLSRW LPRSKFTHLD EEILKRGGFI
110 120 130 140 150
AGLVNDGNTC FMNSVLQSLA SSRELMEFLD NNVIRTYEEI EQNEHNEEGN
160 170 180 190 200
GQESAQDEAT HKKNTRKGGK VYGKHKKKLN RKSSSKEDEE KSQEPDITFS
210 220 230 240 250
VALRDLLSAL NAKYYRDKPY FKTNSLLKAM SKSPRKNILL GYDQEDAQEF
260 270 280 290 300
FQNILAELES NVKSLNTEKL DTTPVAKSEL PDDALVGQLN LGEVGTVYIP
310 320 330 340 350
TEQIDPNSIL HDKSIQNFTP FKLMTPLDGI TAERIGCLQC GENGGIRYSV
360 370 380 390 400
FSGLSLNLPN ENIGSTLKLS QLLSDWSKPE IIEGVECNRC ALTAAHSHLF
410 420 430 440 450
GQLKEFEKKP EGSIPEKLIN AVKDRVHQIE EVLAKPVIDD EDYKKLHTAN
460 470 480 490 500
MVRKCSKSKQ ILISRPPPLL SIHINRSVFD PRTYMIRKNN SKVLFKSRLN
510 520 530 540 550
LAPWCCDINE INLDARLPMS KKEKAAQQDS SEDENIGGEY YTKLHERFEQ
560 570 580 590 600
EFEDSEEEKE YDDAEGNYAS HYNHTKDISN YDPLNGEVDG VTSDDEDEYI
610 620 630 640 650
EETDALGNTI KKRIIEHSDV ENENVKDNEE LQEIDNVSLD EPKINVEDQL
660 670 680 690 700
ETSSDEEDVI PAPPINYARS FSTVPATPLT YSLRSVIVHY GTHNYGHYIA
710 720 730 740 750
FRKYRGCWWR ISDETVYVVD EAEVLSTPGV FMLFYEYDFD EETGKMKDDL
760 770 780 790 800
EAIQSNNEED DEKEQEQKGV QEPKESQEQG EGEEQEEGQE QMKFERTEDH

RDISGKDVN
Length:809
Mass (Da):92,769
Last modified:October 5, 2010 - v2
Checksum:i07BA266FB43C2C04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti418 – 4181L → P in AAA35189 (PubMed:2050695).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63484 Genomic DNA. Translation: AAA35189.1.
Z74170 Genomic DNA. Translation: CAA98690.1.
BK006938 Genomic DNA. Translation: DAA11738.1.
PIRiS67665.
RefSeqiNP_010161.1. NM_001180181.1.

Genome annotation databases

EnsemblFungiiYDL122W; YDL122W; YDL122W.
GeneIDi851435.
KEGGisce:YDL122W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63484 Genomic DNA. Translation: AAA35189.1.
Z74170 Genomic DNA. Translation: CAA98690.1.
BK006938 Genomic DNA. Translation: DAA11738.1.
PIRiS67665.
RefSeqiNP_010161.1. NM_001180181.1.

3D structure databases

ProteinModelPortaliP25037.
SMRiP25037. Positions 657-735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31941. 107 interactions.
IntActiP25037. 23 interactions.
MINTiMINT-2788387.
STRINGi4932.YDL122W.

Protein family/group databases

MEROPSiC19.002.

Proteomic databases

MaxQBiP25037.
PaxDbiP25037.
PeptideAtlasiP25037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL122W; YDL122W; YDL122W.
GeneIDi851435.
KEGGisce:YDL122W.

Organism-specific databases

SGDiS000002280. UBP1.

Phylogenomic databases

eggNOGiNOG259866.
HOGENOMiHOG000093934.
InParanoidiP25037.
KOiK11870.
OMAiSIHINRS.
OrthoDBiEOG7HB5JX.

Enzyme and pathway databases

BioCyciYEAST:G3O-29521-MONOMER.

Miscellaneous databases

NextBioi968666.

Gene expression databases

GenevestigatoriP25037.

Family and domain databases

InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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].

Entry informationi

Entry nameiUBP1_YEAST
AccessioniPrimary (citable) accession number: P25037
Secondary accession number(s): D6VRM8, Q07543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 5, 2010
Last modified: January 7, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8970 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.