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O42726

- UBP2_KLULA

UniProt

O42726 - UBP2_KLULA

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Protein

Ubiquitin carboxyl-terminal hydrolase 2

Gene
UBP2, KLLA0E02376g
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.

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 sitei707 – 7071Nucleophile By similarity
Active sitei1153 – 11531Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.003.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP2
Ordered Locus Names:KLLA0E02376g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome E

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12201220Ubiquitin carboxyl-terminal hydrolase 2PRO_0000080587Add
BLAST

Proteomic databases

PRIDEiO42726.

Interactioni

Protein-protein interaction databases

STRINGi28985.O42726.

Structurei

3D structure databases

ProteinModelPortaliO42726.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini698 – 1202505USPAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG275561.
HOGENOMiHOG000094458.
KOiK11849.
OMAiHRGEASY.
OrthoDBiEOG7327X3.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR025305. UCH_repeat_domain.
[Graphical view]
PfamiPF13446. RPT. 2 hits.
PF00443. 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.

O42726-1 [UniParc]FASTAAdd to Basket

« Hide

MMASQEPALE LNGEQRDSVS ETAEVLRSKS LESFSDLVDD GKTLLYGDIS     50
KSFPFKTCDR ILDDIRISPW FLKKFGSSVM KQPMLQYSRE RQQLQPWNLV 100
HLIDQVNLRS RYDYDSMTCP GKNTISVMFA LLVDPNFTPN DFDDIDKFPE 150
YFFHLKITVK RRSYLENFNR HVGITHYHVL EPESLHPFDK RDIFIMEEKD 200
CRLVDQSIFV SADTNKLILV EIIKPEFNSE NLAEYRTAKI EERYKNACQE 250
FDLLNPDDIP SQAECLKTLF MIFKNPLQRK SANSEFKIIS RDSVALNSQI 300
NTDWLTTMFD FSLQKTAVED NVQSGEEYKP PDLVDYITDF KVRGIREAYT 350
RKSMEVVLIG KQSMLLENEL GTEKKTVAKC FSNQHFSASH TWWFNILNHQ 400
HIEPFPYDIN YHFINLSVAF KYIDKDIIKN YETQIALDQE NISHYFDALQ 450
YVTNAKGSYQ LIAYCGKQDV VGYEDLNNAL QVFGLDPTDI DASLLDANTM 500
IEYYNSHLLR SSDNQRKDLR NALRVLGKYL GSQKMLFLVE YEPYYNVQQA 550
YTLLKVDETV DDDIIQTAYT INIADAPGLK KDYDRAIFTI ALDRRSIFLL 600
NVLTDECPEF AQYYNCTDIS YDEALNIIEI DMNASDDVIL EVFQKKWSHG 650
IMTGPDYLLK LKMALQNIGF TRNSKLINHF LDTGIVDVSC LPVATWPAGI 700
NNVGNTCYLN SLLQFFFTIK PLRDFILNYD DDSAKLLDAS EYHSRRRIGG 750
REVSKQEELR SVQFVYHLRD LFNDMIHTNS RCVTPTKELV YLAFAPSNVE 800
VEFGDDTVAQ KELIDLTTDV VEDPTDTTRH LASCDDDIIM CQSPVALPEH 850
KTSSEAGTQQ YSVQVAKISA DQLENTLEIG RQQDVTECIG NVLAQLEIAS 900
EPLSLEDDLE QNDLVKQLFY GRIKQDLIPV NDEASVRTKY ERFLSLLVNT 950
GDHPKDIYDA LDFYFQNDYL NLEEYGDVKR TVSISELPAV LQIQIQRVYY 1000
DREKFMPFKS IEPLPFGETL YMDRYMATED PKLLAEIQQN AELKQKLQDL 1050
KQRQRKLLSQ NEIGLTLKSS LIETKKFLQS GTLKAHDIDA DNIPSSIAYI 1100
DILINNIDEE LKSLFNKITD LETTISQQFS EFKHIGYSLF AVFIHRGEAS 1150
YGHYWVYIKD HTKNGIWRKY NDDSVTEVPQ SEVFNFTEGN TATPYFLVYV 1200
REGQEQETIE PLKRILQQQE 1220
Length:1,220
Mass (Da):141,120
Last modified:September 27, 2004 - v2
Checksum:i7362B30C368B4A47
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti646 – 6505KWSHG → EMESR in AAB94074. 1 Publication
Sequence conflicti1009 – 102214KSIEP…ETLYM → QVYRAATFRRKRCTW in AAB94074. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022776 Genomic DNA. Translation: AAB94074.1.
CR382125 Genomic DNA. Translation: CAG99142.1.
PIRiT30529.
RefSeqiXP_454055.1. XM_454055.1.

Genome annotation databases

GeneIDi2894270.
KEGGikla:KLLA0E02377g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022776 Genomic DNA. Translation: AAB94074.1 .
CR382125 Genomic DNA. Translation: CAG99142.1 .
PIRi T30529.
RefSeqi XP_454055.1. XM_454055.1.

3D structure databases

ProteinModelPortali O42726.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 28985.O42726.

Protein family/group databases

MEROPSi C19.003.

Proteomic databases

PRIDEi O42726.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2894270.
KEGGi kla:KLLA0E02377g.

Phylogenomic databases

eggNOGi NOG275561.
HOGENOMi HOG000094458.
KOi K11849.
OMAi HRGEASY.
OrthoDBi EOG7327X3.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR025305. UCH_repeat_domain.
[Graphical view ]
Pfami PF13446. RPT. 2 hits.
PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBP2_KLULA
AccessioniPrimary (citable) accession number: O42726
Secondary accession number(s): Q6CPT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 27, 2004
Last modified: September 3, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3