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Q09682

- PSA3_SCHPO

UniProt

Q09682 - PSA3_SCHPO

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Protein

Probable proteasome subunit alpha type-3

Gene

SPAC13C5.01c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasome-mediated ubiquitin-dependent protein catabolic process Source: PomBase
  2. regulation of mitotic cell cycle Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_188566. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_188568. ER-Phagosome pathway.
REACT_188587. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215320. Orc1 removal from chromatin.
REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proteasome subunit alpha type-3 (EC:3.4.25.1)
Gene namesi
ORF Names:SPAC13C5.01c, SPAC31A2.17c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC13C5.01c.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
  3. 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 – 248248Probable proteasome subunit alpha type-3PRO_0000124115Add
BLAST

Proteomic databases

MaxQBiQ09682.
PaxDbiQ09682.

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

BioGridi280594. 6 interactions.
MINTiMINT-4694020.
STRINGi4896.SPAC13C5.01c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09682.
SMRiQ09682. Positions 2-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
InParanoidiQ09682.
KOiK02728.
OMAiKQEYKDD.
OrthoDBiEOG7SBP0C.
PhylomeDBiQ09682.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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.

Q09682-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRSYDSRTT IFSPEGRLYQ VEYALEAINH AGVALGIVAK DGIVLAAEKK
60 70 80 90 100
VTSKLLEQEE SAEKLYHIGD NMLCAVAGLT ADANILINYA RRVGQQYLQT
110 120 130 140 150
FNEEMPCEQL VRRVCDLKQG YTQYGGLRPF GVSFLYAGWD HIRGYQLFQS
160 170 180 190 200
NPSGNYGSWQ ANSIGGNSTS VQSLMRQEYK DDINLDEASA MAVKFLSKTL
210 220 230 240
DSNSLTHEKI EFATITKDTT KNKMVCKIWK SDEINEVLNK YQETQRQS
Length:248
Mass (Da):27,925
Last modified:November 1, 1995 - v1
Checksum:i66C32773C5D10781
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAA90475.1.
PIRiS58093.
RefSeqiXP_001713040.1. XM_001712988.2.

Genome annotation databases

EnsemblFungiiSPAC13C5.01c.1; SPAC13C5.01c.1:pep; SPAC13C5.01c.
GeneIDi3361518.
KEGGispo:SPAC13C5.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAA90475.1 .
PIRi S58093.
RefSeqi XP_001713040.1. XM_001712988.2.

3D structure databases

ProteinModelPortali Q09682.
SMRi Q09682. Positions 2-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 280594. 6 interactions.
MINTi MINT-4694020.
STRINGi 4896.SPAC13C5.01c-1.

Protein family/group databases

MEROPSi T01.973.

Proteomic databases

MaxQBi Q09682.
PaxDbi Q09682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC13C5.01c.1 ; SPAC13C5.01c.1:pep ; SPAC13C5.01c .
GeneIDi 3361518.
KEGGi spo:SPAC13C5.01c.

Organism-specific databases

PomBasei SPAC13C5.01c.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091085.
InParanoidi Q09682.
KOi K02728.
OMAi KQEYKDD.
OrthoDBi EOG7SBP0C.
PhylomeDBi Q09682.

Enzyme and pathway databases

Reactomei REACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_188566. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_188568. ER-Phagosome pathway.
REACT_188587. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215320. Orc1 removal from chromatin.
REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Miscellaneous databases

NextBioi 20811560.
PROi Q09682.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

Entry informationi

Entry nameiPSA3_SCHPO
AccessioniPrimary (citable) accession number: Q09682
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 115 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