SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38237

- UBP14_YEAST

UniProt

P38237 - UBP14_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ubiquitin carboxyl-terminal hydrolase 14
Gene
UBP14, GID6, YBR058C, YBR0515
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

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 sitei332 – 3321Nucleophile
Active sitei737 – 7371Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri190 – 26273UBP-type
Add
BLAST

GO - Molecular functioni

  1. omega peptidase activity Source: InterPro
  2. ubiquitin-specific protease activity Source: SGD
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of gluconeogenesis Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29029-MONOMER.

Protein family/group databases

MEROPSiC19.083.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBP14
Synonyms:GID6
Ordered Locus Names:YBR058C
ORF Names:YBR0515
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR058c.
SGDiS000000262. UBP14.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi332 – 3321C → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 781781Ubiquitin carboxyl-terminal hydrolase 14
PRO_0000080599Add
BLAST

Proteomic databases

MaxQBiP38237.
PaxDbiP38237.

Expressioni

Gene expression databases

GenevestigatoriP38237.

Interactioni

Protein-protein interaction databases

BioGridi32761. 132 interactions.
DIPiDIP-4897N.
IntActiP38237. 11 interactions.
MINTiMINT-486523.
STRINGi4932.YBR058C.

Structurei

3D structure databases

ProteinModelPortaliP38237.
SMRiP38237. Positions 4-780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini323 – 781459USP
Add
BLAST
Domaini576 – 62651UBA 1
Add
BLAST
Domaini649 – 68941UBA 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 954Poly-Asn

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 2 UBA domains.
Contains 1 USP domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5207.
GeneTreeiENSGT00390000000874.
HOGENOMiHOG000162311.
KOiK11836.
OMAiAESAMNW.
OrthoDBiEOG74TX7J.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018200. 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]
PfamiPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFiPIRSF016308. UBP. 1 hit.
SMARTiSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50030. 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]

Sequencei

Sequence statusi: Complete.

P38237-1 [UniParc]FASTAAdd to Basket

« Hide

MAEAVLENVN VPAVVSKDEC IYCFESPYNE PLALNASPKH SLNICLNCFQ    50
ATCNRHVPLH IRVTEYACDT IHSNYLTIAK VEKPKQENVE ENNNNKKIKL 100
QVIETSEDDT HNTIWSLQRF NGENVPRTVL SKSTDSDISS TALEKIEKIL 150
KAKSQDFEDK KNSWVLEIST CPHTENFQIP SKPENTVNLN QCSSCDLTQN 200
LWLCLHCGNI GCGREQIGID GHSHALDHYR SNNNHPLAIK LGSLSSSTYD 250
LYCYACDDET RFPDNVNLGS ALQIYGINIQ EKIADEKTLV QLQVEQNENW 300
QFRMVDSSGK EFEKLSASKN YGCGLINLGN SCYLNSVIQS LVNGGVPNWS 350
LDFLGSKFPL DVVYPDNNLK CQWIKLLNAM KCEPELYPNG IKPTTFKKCI 400
GQNHQEFSSN RQQDAMEFLT FLLDLLDKKF FSSSSSGIPN PNDLVRFMME 450
DRLQCNICGK VKYSYEPTEA IQIPLEENDE PQDMLERIKA YFEGQTIEFK 500
CANCKEKVTA NKKPGFKSLP QTLILNPIRI RLQNWIPVKT SNELSLPGLI 550
DRDDMLDVSS YLSQGFDPQT ENLLPDEDEN RSSFTPNQCS ISQLIEMGFT 600
QNASVRALFN TGNQDAESAM NWLFQHMDDP DLNDPFVPPP NVPKKDKREV 650
DEVSLTSMLS MGLNPNLCRK ALILNNGDVN RSVEWVFNNM DDDGTFPEPE 700
VPNEEQQQKK DLGYSTAKPY ALTAVICHKG NSVHSGHYVV FIRKLVADKW 750
KWVLYNDEKL VAADSIEDMK KNGYIYFYTR C 781
Length:781
Mass (Da):88,630
Last modified:October 31, 2006 - v2
Checksum:i52B421DCD4A0FCBA
GO

Sequence cautioni

The sequence CAA85001.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA86402.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z35927 Genomic DNA. Translation: CAA85001.1. Different initiation.
Z46260 Genomic DNA. Translation: CAA86402.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07177.1.
PIRiS45916.
RefSeqiNP_009614.2. NM_001178406.1.

Genome annotation databases

EnsemblFungiiYBR058C; YBR058C; YBR058C.
GeneIDi852349.
KEGGisce:YBR058C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z35927 Genomic DNA. Translation: CAA85001.1 . Different initiation.
Z46260 Genomic DNA. Translation: CAA86402.1 . Different initiation.
BK006936 Genomic DNA. Translation: DAA07177.1 .
PIRi S45916.
RefSeqi NP_009614.2. NM_001178406.1.

3D structure databases

ProteinModelPortali P38237.
SMRi P38237. Positions 4-780.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32761. 132 interactions.
DIPi DIP-4897N.
IntActi P38237. 11 interactions.
MINTi MINT-486523.
STRINGi 4932.YBR058C.

Protein family/group databases

MEROPSi C19.083.

Proteomic databases

MaxQBi P38237.
PaxDbi P38237.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR058C ; YBR058C ; YBR058C .
GeneIDi 852349.
KEGGi sce:YBR058C.

Organism-specific databases

CYGDi YBR058c.
SGDi S000000262. UBP14.

Phylogenomic databases

eggNOGi COG5207.
GeneTreei ENSGT00390000000874.
HOGENOMi HOG000162311.
KOi K11836.
OMAi AESAMNW.
OrthoDBi EOG74TX7J.

Enzyme and pathway databases

BioCyci YEAST:G3O-29029-MONOMER.

Miscellaneous databases

NextBioi 971095.

Gene expression databases

Genevestigatori P38237.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018200. 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 ]
Pfami PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF016308. UBP. 1 hit.
SMARTi SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS50030. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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]
  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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP14_YEAST
AccessioniPrimary (citable) accession number: P38237
Secondary accession number(s): D6VQ57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 31, 2006
Last modified: September 3, 2014
This is version 126 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 3040 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi