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O42726 (UBP2_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 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:KLLA0E02376g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length1220 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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 C19 family.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12201220Ubiquitin carboxyl-terminal hydrolase 2
PRO_0000080587

Regions

Domain698 – 1202505USP

Sites

Active site7071Nucleophile By similarity
Active site11531Proton acceptor By similarity

Experimental info

Sequence conflict646 – 6505KWSHG → EMESR in AAB94074. Ref.1
Sequence conflict1009 – 102214KSIEP…ETLYM → QVYRAATFRRKRCTW in AAB94074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O42726 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 7362B30C368B4A47

FASTA1,220141,120
        10         20         30         40         50         60 
MMASQEPALE LNGEQRDSVS ETAEVLRSKS LESFSDLVDD GKTLLYGDIS KSFPFKTCDR 

        70         80         90        100        110        120 
ILDDIRISPW FLKKFGSSVM KQPMLQYSRE RQQLQPWNLV HLIDQVNLRS RYDYDSMTCP 

       130        140        150        160        170        180 
GKNTISVMFA LLVDPNFTPN DFDDIDKFPE YFFHLKITVK RRSYLENFNR HVGITHYHVL 

       190        200        210        220        230        240 
EPESLHPFDK RDIFIMEEKD CRLVDQSIFV SADTNKLILV EIIKPEFNSE NLAEYRTAKI 

       250        260        270        280        290        300 
EERYKNACQE FDLLNPDDIP SQAECLKTLF MIFKNPLQRK SANSEFKIIS RDSVALNSQI 

       310        320        330        340        350        360 
NTDWLTTMFD FSLQKTAVED NVQSGEEYKP PDLVDYITDF KVRGIREAYT RKSMEVVLIG 

       370        380        390        400        410        420 
KQSMLLENEL GTEKKTVAKC FSNQHFSASH TWWFNILNHQ HIEPFPYDIN YHFINLSVAF 

       430        440        450        460        470        480 
KYIDKDIIKN YETQIALDQE NISHYFDALQ YVTNAKGSYQ LIAYCGKQDV VGYEDLNNAL 

       490        500        510        520        530        540 
QVFGLDPTDI DASLLDANTM IEYYNSHLLR SSDNQRKDLR NALRVLGKYL GSQKMLFLVE 

       550        560        570        580        590        600 
YEPYYNVQQA YTLLKVDETV DDDIIQTAYT INIADAPGLK KDYDRAIFTI ALDRRSIFLL 

       610        620        630        640        650        660 
NVLTDECPEF AQYYNCTDIS YDEALNIIEI DMNASDDVIL EVFQKKWSHG IMTGPDYLLK 

       670        680        690        700        710        720 
LKMALQNIGF TRNSKLINHF LDTGIVDVSC LPVATWPAGI NNVGNTCYLN SLLQFFFTIK 

       730        740        750        760        770        780 
PLRDFILNYD DDSAKLLDAS EYHSRRRIGG REVSKQEELR SVQFVYHLRD LFNDMIHTNS 

       790        800        810        820        830        840 
RCVTPTKELV YLAFAPSNVE VEFGDDTVAQ KELIDLTTDV VEDPTDTTRH LASCDDDIIM 

       850        860        870        880        890        900 
CQSPVALPEH KTSSEAGTQQ YSVQVAKISA DQLENTLEIG RQQDVTECIG NVLAQLEIAS 

       910        920        930        940        950        960 
EPLSLEDDLE QNDLVKQLFY GRIKQDLIPV NDEASVRTKY ERFLSLLVNT GDHPKDIYDA 

       970        980        990       1000       1010       1020 
LDFYFQNDYL NLEEYGDVKR TVSISELPAV LQIQIQRVYY DREKFMPFKS IEPLPFGETL 

      1030       1040       1050       1060       1070       1080 
YMDRYMATED PKLLAEIQQN AELKQKLQDL KQRQRKLLSQ NEIGLTLKSS LIETKKFLQS 

      1090       1100       1110       1120       1130       1140 
GTLKAHDIDA DNIPSSIAYI DILINNIDEE LKSLFNKITD LETTISQQFS EFKHIGYSLF 

      1150       1160       1170       1180       1190       1200 
AVFIHRGEAS YGHYWVYIKD HTKNGIWRKY NDDSVTEVPQ SEVFNFTEGN TATPYFLVYV 

      1210       1220 
REGQEQETIE PLKRILQQQE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of KIUBP2, a ubiquitin hydrolase gene of Kluyveromyces lactis that can suppress a ts-mutation in CBF2, a gene encoding a centromeric protein of Saccharomyces cerevisiae."
Winkler A.A., Korstanje R., Zonneveld B.J.M., Hooykaas P.J.J., Steensma H.Y.
Curr. Genet. 38:17-22(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC MYA-539 / JBD100.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF022776 Genomic DNA. Translation: AAB94074.1.
CR382125 Genomic DNA. Translation: CAG99142.1.
PIRT30529.
RefSeqXP_454055.1. XM_454055.1.

3D structure databases

ProteinModelPortalO42726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.O42726.

Protein family/group databases

MEROPSC19.003.

Proteomic databases

PRIDEO42726.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2894270.
KEGGkla:KLLA0E02377g.

Phylogenomic databases

eggNOGNOG275561.
HOGENOMHOG000094458.
KOK11849.
OMAHRGEASY.
OrthoDBEOG7327X3.

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...

Entry information

Entry nameUBP2_KLULA
AccessionPrimary (citable) accession number: O42726
Secondary accession number(s): Q6CPT4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 27, 2004
Last modified: April 16, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries