Reviewed, UniProtKB/Swiss-Prot P25037 (UBP1_YEAST)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 1
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 1
    Ubiquitin-specific-processing protease 1
    Deubiquitinating enzyme 1

Gene names

Name:	UBP1
Ordered Locus Names:	YDL122W
ORF Names:	D2250

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	809 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an amino-terminal extension to ubiquitin.
Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Miscellaneous	Present with 8970 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the peptidase C19 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein deubiquitination Traceable author statement. Source: SGD ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC ubiquitin-specific protease activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CPT1	P17898	1	EBI-19819,EBI-2050738
DOS2	P54858	1	EBI-19819,EBI-6042
EHT1	P38295	1	EBI-19819,EBI-20890
ERG11	P10614	1	EBI-19819,EBI-5127
ERG25	P53045	1	EBI-19819,EBI-6506
ERG5	P54781	1	EBI-19819,EBI-6563
ERP1	Q05359	1	EBI-19819,EBI-6581
ERV29	P53337	1	EBI-19819,EBI-23662
GAP1	P19145	1	EBI-19819,EBI-7314
GOT1	Q03554	1	EBI-19819,EBI-2057821
HSP30	P25619	1	EBI-19819,EBI-8563
OLE1	P21147	1	EBI-19819,EBI-2098
PHO86	P46956	1	EBI-19819,EBI-13337
PHO88	P38264	1	EBI-19819,EBI-13350
PIS1	P06197	1	EBI-19819,EBI-13458
PNO1	Q99216	1	EBI-19819,EBI-31176
SAC1	P32368	1	EBI-19819,EBI-16210
SCS7	Q03529	1	EBI-19819,EBI-16747
SHR3	Q02774	1	EBI-19819,EBI-17099
SLC1	P33333	1	EBI-19819,EBI-13494
SUR2	P38992	1	EBI-19819,EBI-18574
SWP1	Q02795	1	EBI-19819,EBI-12666
VHS3	Q08438	1	EBI-19819,EBI-30482
WBP1	P33767	1	EBI-19819,EBI-12658
YOP1	Q12402	1	EBI-19819,EBI-37092

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 809	809	Ubiquitin carboxyl-terminal hydrolase 1		PRO_0000080585
Sites
	Active site	110	1	By similarity
	Active site	689	1	By similarity
	Active site	697	1	By similarity
Amino acid modifications
	Modified residue	530	1	Phosphoserine Ref.3 Ref.6 Ref.9
	Modified residue	531	1	Phosphoserine Ref.3 Ref.6 Ref.9
	Modified residue	555	1	Phosphoserine Ref.6 Ref.9 Ref.7
	Modified residue	561	1	Phosphotyrosine Ref.9
	Modified residue	618	1	Phosphoserine Ref.6 Ref.9 Ref.7 Ref.8
	Modified residue	638	1	Phosphoserine Ref.6 Ref.9
	Modified residue	670	1	Phosphoserine Ref.6
	Modified residue	672	1	Phosphoserine Ref.5
	Modified residue	755	1	Phosphoserine Ref.6 Ref.9
	Modified residue	776	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	418	1	P → L in CAA98690. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P25037-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 8E3D0B2919E9EC9A	FASTA	809	92,753
	10 20 30 40 50 60 MDLFIESKIN SLLQFLFGSR QDFLRNFKTW SNNNNNLSIY LLIFGIVVFF YKKPDHLNYI 70 80 90 100 110 120 VESVSEMTTN FRNNNSLSRW LPRSKFTHLD EEILKRGGFI AGLVNDGNTC FMNSVLQSLA 130 140 150 160 170 180 SSRELMEFLD NNVIRTYEEI EQNEHNEEGN GQESAQDEAT HKKNTRKGGK VYGKHKKKLN 190 200 210 220 230 240 RKSSSKEDEE KSQEPDITFS VALRDLLSAL NAKYYRDKPY FKTNSLLKAM SKSPRKNILL 250 260 270 280 290 300 GYDQEDAQEF FQNILAELES NVKSLNTEKL DTTPVAKSEL PDDALVGQLN LGEVGTVYIP 310 320 330 340 350 360 TEQIDPNSIL HDKSIQNFTP FKLMTPLDGI TAERIGCLQC GENGGIRYSV FSGLSLNLPN 370 380 390 400 410 420 ENIGSTLKLS QLLSDWSKPE IIEGVECNRC ALTAAHSHLF GQLKEFEKKP EGSIPEKPIN 430 440 450 460 470 480 AVKDRVHQIE EVLAKPVIDD EDYKKLHTAN MVRKCSKSKQ ILISRPPPLL SIHINRSVFD 490 500 510 520 530 540 PRTYMIRKNN SKVLFKSRLN LAPWCCDINE INLDARLPMS KKEKAAQQDS SEDENIGGEY 550 560 570 580 590 600 YTKLHERFEQ EFEDSEEEKE YDDAEGNYAS HYNHTKDISN YDPLNGEVDG VTSDDEDEYI 610 620 630 640 650 660 EETDALGNTI KKRIIEHSDV ENENVKDNEE LQEIDNVSLD EPKINVEDQL ETSSDEEDVI 670 680 690 700 710 720 PAPPINYARS FSTVPATPLT YSLRSVIVHY GTHNYGHYIA FRKYRGCWWR ISDETVYVVD 730 740 750 760 770 780 EAEVLSTPGV FMLFYEYDFD EETGKMKDDL EAIQSNNEED DEKEQEQKGV QEPKESQEQG 790 800 EGEEQEEGQE QMKFERTEDH RDISGKDVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae." Tobias J.W., Varshavsky A. J. Biol. Chem. 266:12021-12028(1991) [PubMed: 2050695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-531, MASS SPECTROMETRY.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, MASS SPECTROMETRY.
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-531; SER-555; SER-618; SER-638; SER-670 AND SER-755, MASS SPECTROMETRY.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555 AND SER-618, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618 AND SER-776, MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-531; SER-555; TYR-561; SER-618; SER-638 AND SER-755, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M63484 Genomic DNA. Translation: AAA35189.1. Z74170 Genomic DNA. Translation: CAA98690.1.
PIR	S67665.
3D structure databases
HSSP	HSSP built from PDB template 1NB8 based on UniProtKB Q93009.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25037. 57 interactions.
Protein family/group databases
MEROPS	C19.002.
Proteomic databases
PeptideAtlas	P25037.
Genome annotation databases
Ensembl	YDL122W. Saccharomyces cerevisiae. [Contig view]
GenomeReviews	Gene locus YDL122W in contig Z71256_GR.
KEGG	sce:YDL122W.
Organism-specific databases
CYGD	YDL122w.
SGD	S000002280. UBP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P25037.
Enzyme and pathway databases
BRENDA	3.1.2.15. 250.
Gene expression databases
ArrayExpress	P25037.
GermOnline	YDL122W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBP1_YEAST

Accession

Primary (citable) accession number: P25037
Secondary accession number(s): Q07543

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)