UBP14_YEAST
ID UBP14_YEAST Reviewed; 781 AA.
AC P38237; D6VQ57;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE EC=3.4.19.12 {ECO:0000269|PubMed:9305625};
DE AltName: Full=Deubiquitinating enzyme 14;
DE AltName: Full=Glucose-induced degradation protein 6;
DE AltName: Full=Ubiquitin thioesterase 14;
DE AltName: Full=Ubiquitin-specific-processing protease 14;
GN Name=UBP14; Synonyms=GID6 {ECO:0000303|PubMed:12686616};
GN OrderedLocusNames=YBR058C; ORFNames=YBR0515;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7597852; DOI=10.1002/yea.320110511;
RA Aljinovic G., Pohl T.M.;
RT "Sequence and analysis of 24 kb on chromosome II of Saccharomyces
RT cerevisiae.";
RL Yeast 11:475-479(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 56-80; 120-127; 215-240; 288-303; 399-411; 430-452;
RP 463-487; 490-500; 518-529; 540-552; 670-681; 730-743; 752-759 AND 772-780.
RX PubMed=15096053; DOI=10.1021/bi035626r;
RA Russell N.S., Wilkinson K.D.;
RT "Identification of a novel 29-linked polyubiquitin binding protein, Ufd3,
RT using polyubiquitin chain analogues.";
RL Biochemistry 43:4844-4854(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-332.
RX PubMed=9305625; DOI=10.1093/emboj/16.16.4826;
RA Amerik A.Y., Swaminathan S., Krantz B.A., Wilkinson K.D., Hochstrasser M.;
RT "In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates
RT rates of protein degradation by the proteasome.";
RL EMBO J. 16:4826-4838(1997).
RN [6]
RP FUNCTION.
RX PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
RA Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
RA Thumm M., Wolf D.H.;
RT "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
RT Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
RT genes and indicates the existence of two degradation pathways.";
RL Mol. Biol. Cell 14:1652-1663(2003).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Required for the adaptation to the presence of glucose in the
CC growth medium; mediates the degradation of enzymes involved in
CC gluconeogenesis when cells are shifted to glucose-containing medium
CC (PubMed:12686616). Required for proteasome-dependent catabolite
CC degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616).
CC Accelerates proteasomal breakdown of ubiquitinated proteins as it
CC disassembles free ubiquitin chains that would compete with
CC ubiquitinated proteins to bind to the proteasome (PubMed:9305625).
CC {ECO:0000269|PubMed:12686616, ECO:0000269|PubMed:9305625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:9305625};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA85001.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA86402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z35927; CAA85001.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z46260; CAA86402.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07177.1; -; Genomic_DNA.
DR PIR; S45916; S45916.
DR RefSeq; NP_009614.2; NM_001178406.1.
DR AlphaFoldDB; P38237; -.
DR SMR; P38237; -.
DR BioGRID; 32761; 223.
DR DIP; DIP-4897N; -.
DR IntAct; P38237; 17.
DR MINT; P38237; -.
DR STRING; 4932.YBR058C; -.
DR MEROPS; C19.083; -.
DR iPTMnet; P38237; -.
DR MaxQB; P38237; -.
DR PaxDb; P38237; -.
DR PRIDE; P38237; -.
DR EnsemblFungi; YBR058C_mRNA; YBR058C; YBR058C.
DR GeneID; 852349; -.
DR KEGG; sce:YBR058C; -.
DR SGD; S000000262; UBP14.
DR VEuPathDB; FungiDB:YBR058C; -.
DR eggNOG; KOG0944; Eukaryota.
DR GeneTree; ENSGT00940000156053; -.
DR HOGENOM; CLU_009884_1_0_1; -.
DR InParanoid; P38237; -.
DR OMA; FDERQAV; -.
DR BioCyc; YEAST:G3O-29029-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P38237; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38237; protein.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:SGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR CDD; cd14298; UBA2_scUBP14_like; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR033864; UBA2_scUBP14-like.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nucleus;
KW Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..781
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000080599"
FT DOMAIN 323..781
FT /note="USP"
FT DOMAIN 576..626
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 649..689
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 169..279
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:9305625"
FT ACT_SITE 737
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MUTAGEN 332
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:9305625"
SQ SEQUENCE 781 AA; 88630 MW; 52B421DCD4A0FCBA CRC64;
MAEAVLENVN VPAVVSKDEC IYCFESPYNE PLALNASPKH SLNICLNCFQ ATCNRHVPLH
IRVTEYACDT IHSNYLTIAK VEKPKQENVE ENNNNKKIKL QVIETSEDDT HNTIWSLQRF
NGENVPRTVL SKSTDSDISS TALEKIEKIL KAKSQDFEDK KNSWVLEIST CPHTENFQIP
SKPENTVNLN QCSSCDLTQN LWLCLHCGNI GCGREQIGID GHSHALDHYR SNNNHPLAIK
LGSLSSSTYD LYCYACDDET RFPDNVNLGS ALQIYGINIQ EKIADEKTLV QLQVEQNENW
QFRMVDSSGK EFEKLSASKN YGCGLINLGN SCYLNSVIQS LVNGGVPNWS LDFLGSKFPL
DVVYPDNNLK CQWIKLLNAM KCEPELYPNG IKPTTFKKCI GQNHQEFSSN RQQDAMEFLT
FLLDLLDKKF FSSSSSGIPN PNDLVRFMME DRLQCNICGK VKYSYEPTEA IQIPLEENDE
PQDMLERIKA YFEGQTIEFK CANCKEKVTA NKKPGFKSLP QTLILNPIRI RLQNWIPVKT
SNELSLPGLI DRDDMLDVSS YLSQGFDPQT ENLLPDEDEN RSSFTPNQCS ISQLIEMGFT
QNASVRALFN TGNQDAESAM NWLFQHMDDP DLNDPFVPPP NVPKKDKREV DEVSLTSMLS
MGLNPNLCRK ALILNNGDVN RSVEWVFNNM DDDGTFPEPE VPNEEQQQKK DLGYSTAKPY
ALTAVICHKG NSVHSGHYVV FIRKLVADKW KWVLYNDEKL VAADSIEDMK KNGYIYFYTR
C
