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P38237 (UBP14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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 14

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 14
Glucose-induced degradation protein 6
Ubiquitin thioesterase 14
Ubiquitin-specific-processing protease 14
Gene names
Name:UBP14
Synonyms:GID6
Ordered Locus Names:YBR058C
ORF Names:YBR0515
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length781 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in the negative regulation of gluconeogenesis. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome. Ref.5 Ref.6

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).

Subcellular location

Cytoplasm. Nucleus Ref.8.

Miscellaneous

Present with 3040 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 2 UBA domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence CAA85001.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA86402.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 781781Ubiquitin carboxyl-terminal hydrolase 14
PRO_0000080599

Regions

Domain323 – 781459USP
Domain576 – 62651UBA 1
Domain649 – 68941UBA 2
Zinc finger190 – 26273UBP-type
Compositional bias92 – 954Poly-Asn

Sites

Active site3321Nucleophile
Active site7371Proton acceptor By similarity

Experimental info

Mutagenesis3321C → A: Loss of enzyme activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P38237 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 52B421DCD4A0FCBA

FASTA78188,630
        10         20         30         40         50         60 
MAEAVLENVN VPAVVSKDEC IYCFESPYNE PLALNASPKH SLNICLNCFQ ATCNRHVPLH 

        70         80         90        100        110        120 
IRVTEYACDT IHSNYLTIAK VEKPKQENVE ENNNNKKIKL QVIETSEDDT HNTIWSLQRF 

       130        140        150        160        170        180 
NGENVPRTVL SKSTDSDISS TALEKIEKIL KAKSQDFEDK KNSWVLEIST CPHTENFQIP 

       190        200        210        220        230        240 
SKPENTVNLN QCSSCDLTQN LWLCLHCGNI GCGREQIGID GHSHALDHYR SNNNHPLAIK 

       250        260        270        280        290        300 
LGSLSSSTYD LYCYACDDET RFPDNVNLGS ALQIYGINIQ EKIADEKTLV QLQVEQNENW 

       310        320        330        340        350        360 
QFRMVDSSGK EFEKLSASKN YGCGLINLGN SCYLNSVIQS LVNGGVPNWS LDFLGSKFPL 

       370        380        390        400        410        420 
DVVYPDNNLK CQWIKLLNAM KCEPELYPNG IKPTTFKKCI GQNHQEFSSN RQQDAMEFLT 

       430        440        450        460        470        480 
FLLDLLDKKF FSSSSSGIPN PNDLVRFMME DRLQCNICGK VKYSYEPTEA IQIPLEENDE 

       490        500        510        520        530        540 
PQDMLERIKA YFEGQTIEFK CANCKEKVTA NKKPGFKSLP QTLILNPIRI RLQNWIPVKT 

       550        560        570        580        590        600 
SNELSLPGLI DRDDMLDVSS YLSQGFDPQT ENLLPDEDEN RSSFTPNQCS ISQLIEMGFT 

       610        620        630        640        650        660 
QNASVRALFN TGNQDAESAM NWLFQHMDDP DLNDPFVPPP NVPKKDKREV DEVSLTSMLS 

       670        680        690        700        710        720 
MGLNPNLCRK ALILNNGDVN RSVEWVFNNM DDDGTFPEPE VPNEEQQQKK DLGYSTAKPY 

       730        740        750        760        770        780 
ALTAVICHKG NSVHSGHYVV FIRKLVADKW KWVLYNDEKL VAADSIEDMK KNGYIYFYTR 


C 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of 24 kb on chromosome II of Saccharomyces cerevisiae."
Aljinovic G., Pohl T.M.
Yeast 11:475-479(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues."
Russell N.S., Wilkinson K.D.
Biochemistry 43:4844-4854(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-80; 120-127; 215-240; 288-303; 399-411; 430-452; 463-487; 490-500; 518-529; 540-552; 670-681; 730-743; 752-759 AND 772-780.
[5]"In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome."
Amerik A.Y., Swaminathan S., Krantz B.A., Wilkinson K.D., Hochstrasser M.
EMBO J. 16:4826-4838(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-332.
[6]"Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways."
Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D., Thumm M., Wolf D.H.
Mol. Biol. Cell 14:1652-1663(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35927 Genomic DNA. Translation: CAA85001.1. Different initiation.
Z46260 Genomic DNA. Translation: CAA86402.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07177.1.
PIRS45916.
RefSeqNP_009614.2. NM_001178406.1.

3D structure databases

ProteinModelPortalP38237.
SMRP38237. Positions 4-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32761. 131 interactions.
DIPDIP-4897N.
IntActP38237. 11 interactions.
MINTMINT-486523.
STRING4932.YBR058C.

Protein family/group databases

MEROPSC19.083.

Proteomic databases

PaxDbP38237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR058C; YBR058C; YBR058C.
GeneID852349.
KEGGsce:YBR058C.

Organism-specific databases

CYGDYBR058c.
SGDS000000262. UBP14.

Phylogenomic databases

eggNOGCOG5207.
GeneTreeENSGT00390000000874.
HOGENOMHOG000162311.
KOK11836.
OMAHRDECAY.
OrthoDBEOG74TX7J.

Enzyme and pathway databases

BioCycYEAST:G3O-29029-MONOMER.

Gene expression databases

GenevestigatorP38237.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFPIRSF016308. UBP. 1 hit.
SMARTSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971095.

Entry information

Entry nameUBP14_YEAST
AccessionPrimary (citable) accession number: P38237
Secondary accession number(s): D6VQ57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 31, 2006
Last modified: April 16, 2014
This is version 124 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 II

Yeast (Saccharomyces cerevisiae) chromosome II: 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