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   27-MAR-2024, entry version 190.
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; 227.
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; 4932-YBR058C; -.
DR   PeptideAtlas; P38237; -.
DR   EnsemblFungi; YBR058C_mRNA; YBR058C; YBR058C.
DR   GeneID; 852349; -.
DR   KEGG; sce:YBR058C; -.
DR   AGR; SGD:S000000262; -.
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; KVKYKTR; -.
DR   OrthoDB; 166948at2759; -.
DR   BioCyc; YEAST:G3O-29029-MONOMER; -.
DR   BioGRID-ORCS; 852349; 5 hits in 10 CRISPR screens.
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: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   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14298; UBA2_scUBP14_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
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; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46934; UBA-like; 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
//