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Protein

Probable proteasome subunit alpha type-5

Gene

pup2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_282727. Orc1 removal from chromatin.
REACT_294541. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_308182. SCF-beta-TrCP mediated degradation of Emi1.
REACT_310263. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_327472. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_329750. ER-Phagosome pathway.
REACT_331986. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_349687. Cross-presentation of soluble exogenous antigens (endosomes).

Protein family/group databases

MEROPSiT01.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proteasome subunit alpha type-5 (EC:3.4.25.1)
Gene namesi
Name:pup2
ORF Names:SPAC323.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC323.02c.
PomBaseiSPAC323.02c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nucleus Source: PomBase
  • proteasome core complex Source: GO_Central
  • proteasome core complex, alpha-subunit complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Probable proteasome subunit alpha type-5PRO_0000124128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UT97.
PaxDbiQ9UT97.
PRIDEiQ9UT97.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel (By similarity).By similarity

Protein-protein interaction databases

BioGridi279634. 6 interactions.
IntActiQ9UT97. 3 interactions.
MINTiMINT-4709913.
STRINGi4896.SPAC323.02c-1.

Structurei

3D structure databases

ProteinModelPortaliQ9UT97.
SMRiQ9UT97. Positions 6-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
InParanoidiQ9UT97.
KOiK02729.
OMAiKLDQHNV.
OrthoDBiEOG7SBP0C.
PhylomeDBiQ9UT97.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UT97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFMTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKDAVVLGV
60 70 80 90 100
EKRLTSPLME SHSVEKLFEI DSHIGCAISG LTADARTIIE HARVQTQNHR
110 120 130 140 150
FTYDEPQGIE STTQSICDLA LRFGEGEDGE ERIMSRPFGV ALLIAGIDEH
160 170 180 190 200
GPQLYHSEPS GTYFRYEAKA IGSGSEPAKS ELVKEFHKDM TLEEAEVLIL
210 220 230 240
KVLRQVMEEK LDSKNVQLAK VTAEGGFHIY NDEEMADAVA REQQRMD
Length:247
Mass (Da):27,573
Last modified:May 1, 2000 - v1
Checksum:i713E1AB3A3ADE658
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB53405.1.
PIRiT38639.
RefSeqiNP_594372.1. NM_001019793.2.

Genome annotation databases

EnsemblFungiiSPAC323.02c.1; SPAC323.02c.1:pep; SPAC323.02c.
GeneIDi2543205.
KEGGispo:SPAC323.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB53405.1.
PIRiT38639.
RefSeqiNP_594372.1. NM_001019793.2.

3D structure databases

ProteinModelPortaliQ9UT97.
SMRiQ9UT97. Positions 6-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279634. 6 interactions.
IntActiQ9UT97. 3 interactions.
MINTiMINT-4709913.
STRINGi4896.SPAC323.02c-1.

Protein family/group databases

MEROPSiT01.975.

Proteomic databases

MaxQBiQ9UT97.
PaxDbiQ9UT97.
PRIDEiQ9UT97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC323.02c.1; SPAC323.02c.1:pep; SPAC323.02c.
GeneIDi2543205.
KEGGispo:SPAC323.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAC323.02c.
PomBaseiSPAC323.02c.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
InParanoidiQ9UT97.
KOiK02729.
OMAiKLDQHNV.
OrthoDBiEOG7SBP0C.
PhylomeDBiQ9UT97.

Enzyme and pathway databases

ReactomeiREACT_282727. Orc1 removal from chromatin.
REACT_294541. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_308182. SCF-beta-TrCP mediated degradation of Emi1.
REACT_310263. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_327472. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_329750. ER-Phagosome pathway.
REACT_331986. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_349687. Cross-presentation of soluble exogenous antigens (endosomes).

Miscellaneous databases

NextBioi20804228.
PROiQ9UT97.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPSA5_SCHPO
AccessioniPrimary (citable) accession number: Q9UT97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.