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Q02724 (ULP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-like-specific protease 1

EC=3.4.22.68
Gene names
Name:ULP1
Ordered Locus Names:YPL020C
ORF Names:LPB11C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.3

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 cleavage 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.

Sequence similarities

Belongs to the peptidase C48 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 621620Ubiquitin-like-specific protease 1
PRO_0000101731

Regions

Region432 – 621190Protease

Sites

Active site5141
Active site5311
Active site5801

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue211Phosphoserine Ref.5
Modified residue251Phosphoserine Ref.5
Modified residue1791Phosphothreonine Ref.5 Ref.6
Modified residue2641Phosphoserine Ref.6

Secondary structure

........................................ 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02724 [UniParc].

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

FASTA62172,378
        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 

« Hide

References

« Hide '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. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"A new protease required for cell-cycle progression in yeast."
Li S.J., Hochstrasser M.
Nature 398:246-251(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25 AND THR-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND SER-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 401-621 IN COMPLEX WITH SMT3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36624 Genomic DNA. Translation: AAB68167.1.
BK006949 Genomic DNA. Translation: DAA11408.1.
PIRS63462.
RefSeqNP_015305.1. NM_001183834.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUVX-ray1.60A403-621[»]
2HKPX-ray2.10A403-621[»]
2HL8X-ray2.00A403-621[»]
2HL9X-ray1.90A403-621[»]
ProteinModelPortalQ02724.
SMRQ02724. Positions 403-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36157. 255 interactions.
DIPDIP-4041N.
IntActQ02724. 13 interactions.
MINTMINT-421115.
STRING4932.YPL020C.

Protein family/group databases

MEROPSC48.001.

Proteomic databases

MaxQBQ02724.
PaxDbQ02724.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL020C; YPL020C; YPL020C.
GeneID856087.
KEGGsce:YPL020C.

Organism-specific databases

CYGDYPL020c.
SGDS000005941. ULP1.

Phylogenomic databases

eggNOGCOG5160.
GeneTreeENSGT00530000062941.
HOGENOMHOG000141768.
KOK08592.
OMAPRRWLND.
OrthoDBEOG7ZKSMM.

Enzyme and pathway databases

BioCycYEAST:G3O-33938-MONOMER.
BRENDA3.4.22.68. 984.

Gene expression databases

GenevestigatorQ02724.

Family and domain databases

InterProIPR003653. Peptidase_C48.
[Graphical view]
PfamPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02724.
NextBio981107.

Entry information

Entry nameULP1_YEAST
AccessionPrimary (citable) accession number: Q02724
Secondary accession number(s): D6W3Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references