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Q01476 (UBP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 2

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene names
Name:UBP2
Ordered Locus Names:YOR124C
ORF Names:O3281, YOR3281C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1272 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. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion. Ref.7 Ref.11

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).

Subunit structure

Forms a ternary complex with RSP5 and RUP1. Interacts with FZO1. Ref.7 Ref.11

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RUP1Q122423EBI-19826,EBI-38794

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12721272Ubiquitin carboxyl-terminal hydrolase 2
PRO_0000080586

Regions

Domain736 – 1258523USP

Sites

Active site7451Nucleophile By similarity
Active site12091Proton acceptor By similarity

Amino acid modifications

Modified residue9071Phosphoserine Ref.8 Ref.9 Ref.10

Experimental info

Sequence conflict658 – 6658Missing Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q01476 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 6D106539AE5C5F3F

FASTA1,272146,355
        10         20         30         40         50         60 
MPNEDNELQK AIENHHNQLL NQDKENADRN GSVIEDLPLY GTSINQQSTP GDVDDGKHLL 

        70         80         90        100        110        120 
YPDIATNLPL KTSDRLLDDI LCDTIFLNST DPKVMQKGLQ SRGILKESML SYSTFRSSIR 

       130        140        150        160        170        180 
PNCLGSLTDQ VVFQTKSEYD SISCPKYNKI HVFQAVIFNP SLAEQQISTF DDIVKIPIYH 

       190        200        210        220        230        240 
LKVSVKVRQE LERLKKHVGV TQFHSLDHLH EYDRVDLSTF DSSDPNLLDY GIYVSDDTNK 

       250        260        270        280        290        300 
LILIEIFKPE FNSPEEHESF TADAIKKRYN AMCVKNESLD KSETPSQVDC FYTLFKIFKG 

       310        320        330        340        350        360 
PLTRKSKAEP TKTIDSGNLA LNTHLNPEWL TSKYGFQASS EIDEETNEIF TEYVPPDMVD 

       370        380        390        400        410        420 
YVNDLETRKI RESFVRKCLQ LIFWGQLSTS LLAPNSPLKN TKSVKGMSSL QTSFSTLPWF 

       430        440        450        460        470        480 
HLLGESRARI LLNSNEQTHS PLDAEPHFIN LSVSHYYTDR DIIRNYESLS SLDPENIGLY 

       490        500        510        520        530        540 
FDALTYIANR KGAYQLIAYC GKQDIIGQEA LENALLMFKI NPKECNISEL NEATLLSIYK 

       550        560        570        580        590        600 
YETSNKSQVT SNHLTNLKNA LRLLAKYTKS DKLKFYVDHE PYRALSQAYD TLSIDESVDE 

       610        620        630        640        650        660 
DIIKTAYSVK INDSPGLKLD CDRALYTIAI SKRSLDLFNF LTEECPQFSN YYGPEKLDYQ 

       670        680        690        700        710        720 
EALKLLQVNE NASDETILKI FKQKWFDENV YEPDQFLILR AALTKISIER NSTLITNFLL 

       730        740        750        760        770        780 
TGTIDPNSLP PENWPTGINN IGNTCYLNSL LQYYFSIAPL RRYVLEYQKT VENFNDHLSN 

       790        800        810        820        830        840 
SGHIRRIGGR EISRGEVERS IQFIYQLRNL FYAMVHTRER CVTPSKELAY LAFAPSNVEV 

       850        860        870        880        890        900 
EFEVEGNKVV DQTGVLSDSK KETTDDAFTT KIKDTSLIDL EMEDGLNGDV GTDANRKKNE 

       910        920        930        940        950        960 
SNDAEVSENE DTTGLTSPTR VAKISSDQLE NALEMGRQQD VTECIGNVLF QIESGSEPIR 

       970        980        990       1000       1010       1020 
YDEDNEQYDL VKQLFYGTTK QSIVPLSATN KVRTKVERFL SLLINIGDHP KDIYDAFDSY 

      1030       1040       1050       1060       1070       1080 
FKDEYLTMEE YGDVIRTVAV TTFPTILQVQ IQRVYYDRER LMPFKSIEPL PFKEVIYMDR 

      1090       1100       1110       1120       1130       1140 
YADTENPLLL AKKKETEEMK QKLKVMKNRQ RELLSRDDSG LTRKDAFLES IKLLESDTIK 

      1150       1160       1170       1180       1190       1200 
KTPLKIEAAN DVIKTLRNNV QNIDNELMKL YNDINSLEEK ISHQFDDFKE YGYSLFSVFI 

      1210       1220       1230       1240       1250       1260 
HRGEASYGHY WIYIKDRNRN GIWRKYNDET ISEVQEEEVF NFNEGNTATP YFLVYVKQGQ 

      1270 
EGDIEPLKRI LK 

« Hide

References

« Hide 'large scale' references
[1]"Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family."
Baker R.T., Tobias J.W., Varshavsky A.
J. Biol. Chem. 267:23364-23375(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"DNA sequencing and analysis of 130 kb from yeast chromosome XV."
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.
Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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. expand/collapse author list , 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.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme."
Kee Y., Lyon N., Huibregtse J.M.
EMBO J. 24:2414-2424(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RSP5 AND RUP1.
[8]"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-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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-907, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Two deubiquitylases act on mitofusin and regulate mitochondrial fusion along independent pathways."
Anton F., Dittmar G., Langer T., Escobar-Henriques M.
Mol. Cell 49:487-498(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEUBIQUITINATION OF FZO1, INTERACTION WITH FZO1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94916 Genomic DNA. Translation: AAA35190.1.
X94335 Genomic DNA. Translation: CAA64043.1.
X90518 Genomic DNA. Translation: CAA62120.1.
Z75032 Genomic DNA. Translation: CAA99323.1.
BK006948 Genomic DNA. Translation: DAA10898.1.
PIRS60999.
RefSeqNP_014767.3. NM_001183543.3.

3D structure databases

ProteinModelPortalQ01476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34519. 83 interactions.
DIPDIP-2647N.
IntActQ01476. 10 interactions.
MINTMINT-427685.
STRING4932.YOR124C.

Protein family/group databases

MEROPSC19.003.

Proteomic databases

PaxDbQ01476.
PeptideAtlasQ01476.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR124C; YOR124C; YOR124C.
GeneID854291.
KEGGsce:YOR124C.

Organism-specific databases

CYGDYOR124c.
SGDS000005650. UBP2.

Phylogenomic databases

eggNOGNOG275561.
HOGENOMHOG000094458.
KOK11849.
OMAHRGEASY.
OrthoDBEOG7327X3.

Enzyme and pathway databases

BioCycYEAST:G3O-33651-MONOMER.

Gene expression databases

GenevestigatorQ01476.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR025305. UCH_repeat_domain.
[Graphical view]
PfamPF13446. RPT. 2 hits.
PF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976278.

Entry information

Entry nameUBP2_YEAST
AccessionPrimary (citable) accession number: Q01476
Secondary accession number(s): D6W2I2, Q99357
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 129 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 XV

Yeast (Saccharomyces cerevisiae) chromosome XV: 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