P38237 (UBP14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UBP14
Synonyms:	GID6
Ordered Locus Names:	YBR058C
ORF Names:	YBR0515

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Sequence caution	The sequence CAA85001.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA86402.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of gluconeogenesis Inferred from mutant phenotype Ref.6. Source: SGD proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.6. Source: SGD protein deubiquitination Traceable author statement PubMed 8982460. Source: SGD
Cellular_component	cytoplasm Inferred by curator PubMed 8982460. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from direct assay PubMed 19410548. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 781	781	Ubiquitin carboxyl-terminal hydrolase 14		PRO_0000080599
Regions
	Domain	576 – 626	51	UBA 1
	Domain	649 – 689	41	UBA 2
	Zinc finger	190 – 262	73	UBP-type
	Compositional bias	92 – 95	4	Poly-Asn
Sites
	Active site	332	1	Nucleophile
	Active site	737	1	Proton acceptor By similarity
Experimental info
	Mutagenesis	332	1	C → A: Loss of enzyme activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P38237 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 52B421DCD4A0FCBA	FASTA	781	88,630
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	S45916.
RefSeq	NP_009614.2. NM_001178406.1.
3D structure databases
ProteinModelPortal	P38237.
SMR	P38237. Positions 4-780.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4897N.
IntAct	P38237. 11 interactions.
MINT	MINT-486523.
STRING	4932.YBR058C.
Protein family/group databases
MEROPS	C19.083.
Proteomic databases
PaxDb	P38237.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR058C; YBR058C; YBR058C.
GeneID	852349.
KEGG	sce:YBR058C.
Organism-specific databases
CYGD	YBR058c.
SGD	S000000262. UBP14.
Phylogenomic databases
eggNOG	COG5207.
GeneTree	ENSGT00390000000874.
HOGENOM	HOG000162311.
KO	K11836.
OMA	AESAMNW.
OrthoDB	EOG470XRN.
Gene expression databases
Genevestigator	P38237.
GermOnline	YBR058C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR009060. UBA-like. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. IPR016652. Ubiquitinyl_hydrolase. IPR013083. Znf_RING/FYVE/PHD. IPR001607. Znf_UBP. [Graphical view]
Pfam	PF00627. UBA. 2 hits. PF00443. UCH. 1 hit. PF02148. zf-UBP. 1 hit. [Graphical view]
PIRSF	PIRSF016308. UBP. 1 hit.
SMART	SM00165. UBA. 2 hits. SM00290. ZnF_UBP. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit.
PROSITE	PS50030. UBA. 2 hits. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50271. ZF_UBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971095.

Entry information

Entry name

UBP14_YEAST

Accession

Primary (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 3, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program