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Protein

Proteasome subunit beta type-4

Gene

PBG1

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei24 – 241NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
  2. response to cadmium ion Source: TAIR
  3. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT1G56450-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Protein family/group databases

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit G-1
Proteasome component H
Proteasome subunit beta type-7
Gene namesi
Name:PBG1
Synonyms:PRCH
Ordered Locus Names:At1g56450
ORF Names:F13N6.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G56450.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. cytosolic ribosome Source: TAIR
  3. nucleus Source: UniProtKB-SubCell
  4. proteasome complex Source: TAIR
  5. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2323By similarityPRO_0000042824Add
BLAST
Chaini24 – 246223Proteasome subunit beta type-4PRO_0000042825Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ7DLR9.
PRIDEiQ7DLR9.

Expressioni

Tissue specificityi

Ubiquitous low levels, higher expression in siliques and flowers.1 Publication

Gene expression databases

GenevestigatoriQ7DLR9.

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

BioGridi27323. 1 interaction.
IntActiQ7DLR9. 1 interaction.
STRINGi3702.AT1G56450.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ7DLR9.
SMRiQ7DLR9. Positions 24-233.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000181719.
InParanoidiQ7DLR9.
KOiK02736.
OMAiRIMRVND.
PhylomeDBiQ7DLR9.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7DLR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTFSVPIDN GDSMKIAEEE SQRTLYPYVT GTSIVAIKYK DGVLMASDMG
60 70 80 90 100
GSYGSTLRYK NIERVKAIGK HSLLGASGEI SDFQEILRYL DELTLNDNMW
110 120 130 140 150
DDGNSLGPKE IHNYLTRVMY NRRNKFNPLW NTLVLGGVKN GKSYLGMVSM
160 170 180 190 200
IGVSFEDDHV ATGFGNHLAR PILRDEWHAD LSFEDGVKLL EKCMRVLLYR
210 220 230 240
DRSAINKLQI AKITEEGVTV SQPYSLKTYW EFSSFHNPTA GAAGSW
Length:246
Mass (Da):27,651
Last modified:November 21, 2005 - v2
Checksum:i295B7CB39C6C66D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341I → V in AAC32074 (PubMed:9611183).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043538 mRNA. Translation: AAC32074.1.
AC058785 Genomic DNA. Translation: AAG51500.1.
CP002684 Genomic DNA. Translation: AEE33397.1.
AF378880 mRNA. Translation: AAK55683.1.
AY045596 mRNA. Translation: AAK73954.1.
AY052739 mRNA. Translation: AAK96453.1.
AK221762 mRNA. Translation: BAD93840.1.
Y13696 mRNA. Translation: CAA74030.1.
PIRiD96606.
T51986.
RefSeqiNP_176040.1. NM_104523.3.
UniGeneiAt.399.

Genome annotation databases

EnsemblPlantsiAT1G56450.1; AT1G56450.1; AT1G56450.
GeneIDi842098.
KEGGiath:AT1G56450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043538 mRNA. Translation: AAC32074.1.
AC058785 Genomic DNA. Translation: AAG51500.1.
CP002684 Genomic DNA. Translation: AEE33397.1.
AF378880 mRNA. Translation: AAK55683.1.
AY045596 mRNA. Translation: AAK73954.1.
AY052739 mRNA. Translation: AAK96453.1.
AK221762 mRNA. Translation: BAD93840.1.
Y13696 mRNA. Translation: CAA74030.1.
PIRiD96606.
T51986.
RefSeqiNP_176040.1. NM_104523.3.
UniGeneiAt.399.

3D structure databases

ProteinModelPortaliQ7DLR9.
SMRiQ7DLR9. Positions 24-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27323. 1 interaction.
IntActiQ7DLR9. 1 interaction.
STRINGi3702.AT1G56450.1-P.

Protein family/group databases

MEROPSiT01.987.

Proteomic databases

PaxDbiQ7DLR9.
PRIDEiQ7DLR9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G56450.1; AT1G56450.1; AT1G56450.
GeneIDi842098.
KEGGiath:AT1G56450.

Organism-specific databases

GeneFarmi5117.
TAIRiAT1G56450.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000181719.
InParanoidiQ7DLR9.
KOiK02736.
OMAiRIMRVND.
PhylomeDBiQ7DLR9.

Enzyme and pathway databases

BioCyciARA:AT1G56450-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiQ7DLR9.

Gene expression databases

GenevestigatoriQ7DLR9.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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 (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-246.
    Strain: cv. Columbia.
  7. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT.

Entry informationi

Entry nameiPSB4_ARATH
AccessioniPrimary (citable) accession number: Q7DLR9
Secondary accession number(s): O23718, Q9C7X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2005
Last sequence update: November 21, 2005
Last modified: March 31, 2015
This is version 85 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

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.