Ubiquitin-like-specific protease 1 - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
Ubiquitin-like-specific protease 1
EC=3.4.22.68

Gene names

Name:	ULP1
Ordered Locus Names:	YPL020C
ORF Names:	LPB11C

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	621 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle. Ref.2
Catalytic activity	Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-\|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the formation of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
Miscellaneous	Present with 377 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the peptidase C48 family.

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Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Ref.2 Inferred from mutant phenotype. Source: SGD modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein desumoylation Ref.2 Inferred from direct assay. Source: SGD
Cellular component	nuclear pore Inferred from direct assay. Source: SGD
Molecular function	SUMO-specific protease activity Ref.2 Inferred from direct assay. Source: SGD protein binding Ref.8 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMT3	Q12306	1	EBI-20050,EBI-17490

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 621

621

Ubiquitin-like-specific protease 1

PRO_0000101731

Regions

Region

432 – 621

190

Protease

Sites

Active site

514

1

Active site

531

1

Active site

580

1

Amino acid modifications

Modified residue

21

1

Phosphoserine Ref.5 Ref.7

Modified residue

25

1

Phosphoserine Ref.5

Modified residue

48

1

Phosphoserine Ref.7 Ref.4

Modified residue

124

1

Phosphoserine Ref.7

Modified residue

179

1

Phosphothreonine Ref.5 Ref.7 Ref.6

Modified residue

183

1

Phosphoserine Ref.7 Ref.6

Modified residue

264

1

Phosphoserine Ref.7

Modified residue

308

1

Phosphoserine Ref.7

Modified residue

551

1

Phosphotyrosine Ref.7

Secondary structure

1

.

621

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q02724-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F71132817FAF0B41
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FASTA

621

72,378

        10         20         30         40         50         60 
MSVEVDKHRN TLQYHKKNPY SPLFSPISTY RCYPRVLNNP SESRRSASFS GIYKKRTNTS 

        70         80         90        100        110        120 
RFNYLNDRRV LSMEESMKDG SDRASKAGFI GGIRETLWNS GKYLWHTFVK NEPRNFDGSE 

       130        140        150        160        170        180 
VEASGNSDVE SRSSGSRSSD VPYGLRENYS SDTRKHKFDT STWALPNKRR RIESEGVGTP 

       190        200        210        220        230        240 
STSPISSLAS QKSNCDSDNS ITFSRDPFGW NKWKTSAIGS NSENNTSDQK NSYDRRQYGT 

       250        260        270        280        290        300 
AFIRKKKVAK QNINNTKLVS RAQSEEVTYL RQIFNGEYKV PKILKEERER QLKLMDMDKE 

       310        320        330        340        350        360 
KDTGLKKSII DLTEKIKTIL IENNKNRLQT RNENDDDLVF VKEKKISSLE RKHKDYLNQK 

       370        380        390        400        410        420 
LKFDRSILEF EKDFKRYNEI LNERKKIQED LKKKKEQLAK KKLVPELNEK DDDQVQKALA 

       430        440        450        460        470        480 
SRENTQLMNR DNIEITVRDF KTLAPRRWLN DTIIEFFMKY IEKSTPNTVA FNSFFYTNLS 

       490        500        510        520        530        540 
ERGYQGVRRW MKRKKTQIDK LDKIFTPINL NQSHWALGII DLKKKTIGYV DSLSNGPNAM 

       550        560        570        580        590        600 
SFAILTDLQK YVMEESKHTI GEDFDLIHLD CPQQPNGYDC GIYVCMNTLY GSADAPLDFD 

       610        620 
YKDAIRMRRF IAHLILTDAL K

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"A new protease required for cell-cycle progression in yeast." Li S.J., Hochstrasser M. Nature 398:246-251(1999) [PubMed: 10094048] [Abstract] Cited for: FUNCTION.
[3]	"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].
[4]	"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-48, MASS SPECTROMETRY.
[5]	"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-21; SER-25 AND THR-179, MASS SPECTROMETRY.
[6]	"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 THR-179 AND SER-183, MASS SPECTROMETRY.
[7]	"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-21; SER-48; SER-124; THR-179; SER-183; SER-264; SER-308 AND TYR-551, MASS SPECTROMETRY.
[8]	"Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast." Mossessova E., Lima C.D. Mol. Cell 5:865-876(2000) [PubMed: 10882122] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 401-621 IN COMPLEX WITH SMT3.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U36624 Genomic DNA. Translation: AAB68167.1.

PIR

S63462.

RefSeq

NP_015305.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EUV	X-ray	1.60	A	403-621	[»]
2HKP	X-ray	2.10	A	403-621	[»]
2HL8	X-ray	2.00	A	403-621	[»]
2HL9	X-ray	1.90	A	403-621	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4041N.

IntAct

Q02724. 17 interactions.

Protein family/group databases

MEROPS

C48.001.

Genome annotation databases

Ensembl

YPL020C. Saccharomyces cerevisiae. [Contig view]

GeneID

856087.

GenomeReviews

Gene locus YPL020C in contig U00094_GR.

KEGG

sce:YPL020C.

NMPDR

fig|4932.3.peg.6439.

Organism-specific databases

CYGD

YPL020c.

SGD

S000005941. ULP1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q02724.

OMA

Q02724. TLAPRRW.

Enzyme and pathway databases

BRENDA

3.4.22.68. 250.

Gene expression databases

GermOnline

YPL020C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003653. Peptidase_C48.
[Graphical view]

Pfam

PF02902. Peptidase_C48. 1 hit.
[Graphical view]

PROSITE

PS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981107.

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Entry information

Entry name

ULP1_YEAST

Accession

Primary (citable) accession number: Q02724

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents