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P42742

- PSB1_ARATH

UniProt

P42742 - PSB1_ARATH

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Protein

Proteasome subunit beta type-1

Gene

PBF1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

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

GO - Biological processi

  1. defense response to fungus, incompatible interaction Source: TAIR
  2. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT3G60820-MONOMER.
ARA:GQT-2159-MONOMER.
ARA:GQT-2160-MONOMER.
ReactomeiREACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit F-1
Proteasome component 5
Proteasome subunit beta type-6
TAS-F22/FAFP98
TAS-G39.20
Gene namesi
Name:PBF1
Synonyms:PRC5
Ordered Locus Names:At3g60820
ORF Names:T4C21_230
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G60820.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. cytosol Source: TAIR
  4. nucleus Source: UniProtKB-KW
  5. plasma membrane Source: TAIR
  6. proteasome complex Source: TAIR
  7. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Proteasome subunit beta type-1PRO_0000148038Add
BLAST

Proteomic databases

PaxDbiP42742.
PRIDEiP42742.

Expressioni

Tissue specificityi

Present in all tissues examined. Slightly lower levels in roots.1 Publication

Developmental stagei

Expressed at maximal levels after first day of cell growth.

Inductioni

During cell proliferation.1 Publication

Gene expression databases

ExpressionAtlasiP42742. baseline and differential.
GenevestigatoriP42742.

Interactioni

Subunit structurei

Component of the 20S core complex of the 26S proteasome. The 26S proteasome is composed of a core protease (CP), known as the 20S proteasome, capped at one or both ends by the 19S regulatory particle (RP/PA700). 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.3 Publications

Protein-protein interaction databases

BioGridi10567. 8 interactions.
IntActiP42742. 8 interactions.
MINTiMINT-8065646.

Structurei

3D structure databases

ProteinModelPortaliP42742.
SMRiP42742. Positions 8-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091081.
InParanoidiP42742.
KOiK02732.
PhylomeDBiP42742.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P42742-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTKQHANWSP YDNNGGTCVA IAGSDYCVIA ADTRMSTGYS ILSRDYSKIH
60 70 80 90 100
KLADRAVLSS SGFQADVKAL QKVLKSRHLI YQHQHNKQMS CPAMAQLLSN
110 120 130 140 150
TLYFKRFFPY YAFNVLGGLD EEGKGCVFTY DAVGSYERVG YGAQGSGSTL
160 170 180 190 200
IMPFLDNQLK SPSPLLLPKQ DSNTPLSEAE AVDLVKTVFA SATERDIYTG
210 220
DKLEIMILKA DGIKTELMDL RKD
Length:223
Mass (Da):24,644
Last modified:December 8, 2000 - v2
Checksum:iE8050079F353D4C0
GO

Sequence cautioni

The sequence CAA47753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67338 mRNA. Translation: CAA47753.1. Different initiation.
X79806 mRNA. Translation: CAA56201.1.
AF043537 mRNA. Translation: AAC32073.1.
AL162295 Genomic DNA. Translation: CAB82686.1.
CP002686 Genomic DNA. Translation: AEE80112.1.
CP002686 Genomic DNA. Translation: AEE80114.1.
AY062790 mRNA. Translation: AAL32868.1.
AY081571 mRNA. Translation: AAM10133.1.
AY086619 mRNA. Translation: AAM63678.1.
AK220787 mRNA. Translation: BAD94023.1.
Z26405 mRNA. Translation: CAA81240.1.
PIRiT47893.
RefSeqiNP_001190146.1. NM_001203217.1. [P42742-1]
NP_191641.1. NM_115946.3. [P42742-1]
UniGeneiAt.20500.
At.48789.

Genome annotation databases

EnsemblPlantsiAT3G60820.1; AT3G60820.1; AT3G60820. [P42742-1]
AT3G60820.3; AT3G60820.3; AT3G60820. [P42742-1]
GeneIDi825253.
KEGGiath:AT3G60820.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67338 mRNA. Translation: CAA47753.1 . Different initiation.
X79806 mRNA. Translation: CAA56201.1 .
AF043537 mRNA. Translation: AAC32073.1 .
AL162295 Genomic DNA. Translation: CAB82686.1 .
CP002686 Genomic DNA. Translation: AEE80112.1 .
CP002686 Genomic DNA. Translation: AEE80114.1 .
AY062790 mRNA. Translation: AAL32868.1 .
AY081571 mRNA. Translation: AAM10133.1 .
AY086619 mRNA. Translation: AAM63678.1 .
AK220787 mRNA. Translation: BAD94023.1 .
Z26405 mRNA. Translation: CAA81240.1 .
PIRi T47893.
RefSeqi NP_001190146.1. NM_001203217.1. [P42742-1 ]
NP_191641.1. NM_115946.3. [P42742-1 ]
UniGenei At.20500.
At.48789.

3D structure databases

ProteinModelPortali P42742.
SMRi P42742. Positions 8-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 10567. 8 interactions.
IntActi P42742. 8 interactions.
MINTi MINT-8065646.

Proteomic databases

PaxDbi P42742.
PRIDEi P42742.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G60820.1 ; AT3G60820.1 ; AT3G60820 . [P42742-1 ]
AT3G60820.3 ; AT3G60820.3 ; AT3G60820 . [P42742-1 ]
GeneIDi 825253.
KEGGi ath:AT3G60820.

Organism-specific databases

TAIRi AT3G60820.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091081.
InParanoidi P42742.
KOi K02732.
PhylomeDBi P42742.

Enzyme and pathway databases

BioCyci ARA:AT3G60820-MONOMER.
ARA:GQT-2159-MONOMER.
ARA:GQT-2160-MONOMER.
Reactomei REACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

PROi P42742.

Gene expression databases

ExpressionAtlasi P42742. baseline and differential.
Genevestigatori P42742.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a beta-type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an alpha-type proteasome subunit early in the cell cycle."
    Genschik P., Jamet E., Phillips G., Parmentier Y., Gigot C., Fleck J.
    Plant J. 6:537-546(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. "Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana."
    Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.
    Genetics 149:677-692(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-223.
    Strain: cv. Columbia.
  8. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Philipps G., Gigot C.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-223.
  9. "Structure and functional analyses of the 26S proteasome subunits from plants."
    Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D.
    Mol. Biol. Rep. 26:137-146(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms."
    Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.
    J. Biol. Chem. 279:6401-6413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes."
    Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.
    J. Biol. Chem. 285:25554-25569(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT.

Entry informationi

Entry nameiPSB1_ARATH
AccessioniPrimary (citable) accession number: P42742
Secondary accession number(s): P42741
, Q570C3, Q6LAD2, Q9SBI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 123 of the entry and version 2 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3