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Protein

Proteasome subunit alpha type-2

Gene

PAB1

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.

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

ReactomeiR-OSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-OSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-OSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-OSA-5632684. Hedgehog 'on' state.
R-OSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-OSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-OSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit B
20S proteasome subunit alpha-2
Gene namesi
Name:PAB1
Ordered Locus Names:Os03g0387100, LOC_Os03g26970
ORF Names:OsJ_11088Imported, OSJNBb0058G04.11
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 3, cultivar: Nipponbare

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Proteasome subunit alpha type-2PRO_0000124087Add
BLAST

Proteomic databases

PaxDbiQ10KF0.
PRIDEiQ10KF0.

Expressioni

Gene expression databases

ExpressionAtlasiQ10KF0. baseline and differential.
GenevisibleiQ10KF0. OS.

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

STRINGi39947.LOC_Os03g26970.1.

Structurei

3D structure databases

ProteinModelPortaliQ10KF0.
SMRiQ10KF0. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
InParanoidiQ10KF0.
KOiK02726.
OMAiEVAMGDS.

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.

Q10KF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA ANGVVIATEK
60 70 80 90 100
KLPSILVDET SVQKIQSLTP NIGVVYSGMG PDFRVLVRKS RKQAQQYYRL
110 120 130 140 150
YKETIPVTQL VRETAAVMQE FTQSGGVRPF GVSLLIAGYD DNGPQLYQVD
160 170 180 190 200
PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE DMELDDAIHT AILTLKEGYE
210 220 230
GQISANNIEI GIIRSDREFK VLSPAEIKDF LEEVE
Length:235
Mass (Da):25,844
Last modified:August 22, 2006 - v1
Checksum:iD98998C0BC6CD676
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026559 mRNA. Translation: BAA96830.1.
AC103551 Genomic DNA. Translation: AAT78811.1.
DP000009 Genomic DNA. Translation: ABF96319.1.
AP008209 Genomic DNA. Translation: BAF12173.1.
AP014959 Genomic DNA. Translation: BAS84482.1.
CM000140 Genomic DNA. Translation: EEE59166.1.
AK058567 mRNA. Translation: BAG86735.1.
AK101195 mRNA. Translation: BAG94950.1.
RefSeqiXP_015628148.1. XM_015772662.1.
UniGeneiOs.7900.

Genome annotation databases

EnsemblPlantsiOS03T0387100-01; OS03T0387100-01; OS03G0387100.
GeneIDi4333000.
GrameneiOS03T0387100-01; OS03T0387100-01; OS03G0387100.
KEGGiosa:4333000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026559 mRNA. Translation: BAA96830.1.
AC103551 Genomic DNA. Translation: AAT78811.1.
DP000009 Genomic DNA. Translation: ABF96319.1.
AP008209 Genomic DNA. Translation: BAF12173.1.
AP014959 Genomic DNA. Translation: BAS84482.1.
CM000140 Genomic DNA. Translation: EEE59166.1.
AK058567 mRNA. Translation: BAG86735.1.
AK101195 mRNA. Translation: BAG94950.1.
RefSeqiXP_015628148.1. XM_015772662.1.
UniGeneiOs.7900.

3D structure databases

ProteinModelPortaliQ10KF0.
SMRiQ10KF0. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os03g26970.1.

Proteomic databases

PaxDbiQ10KF0.
PRIDEiQ10KF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOS03T0387100-01; OS03T0387100-01; OS03G0387100.
GeneIDi4333000.
GrameneiOS03T0387100-01; OS03T0387100-01; OS03G0387100.
KEGGiosa:4333000.

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
InParanoidiQ10KF0.
KOiK02726.
OMAiEVAMGDS.

Enzyme and pathway databases

ReactomeiR-OSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-OSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-OSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-OSA-5632684. Hedgehog 'on' state.
R-OSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-OSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-OSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Gene expression databases

ExpressionAtlasiQ10KF0. baseline and differential.
GenevisibleiQ10KF0. OS.

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

« Hide 'large scale' publications
  1. "Primary structural features of the 20S proteasome subunits of rice (Oryza sativa)."
    Sassa H., Oguchi S., Inoue T., Hirano H.
    Gene 250:61-66(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Nipponbare.
  2. "Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species."
    The rice chromosome 3 sequencing consortium
    Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S.
    , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.
    Genome Res. 15:1284-1291(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nipponbare.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nipponbare.
  4. "The rice annotation project database (RAP-DB): 2008 update."
    The rice annotation project (RAP)
    Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: cv. Nipponbare.
  5. Cited for: GENOME REANNOTATION.
    Strain: cv. Nipponbare.
  6. "The genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Nipponbare.
  7. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
    The rice full-length cDNA consortium
    Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Nipponbare.

Entry informationi

Entry nameiPSA2_ORYSJ
AccessioniPrimary (citable) accession number: Q10KF0
Secondary accession number(s): B7E2Y8
, O22539, Q6AVF6, Q9LSU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: May 11, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.