Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9XI05

- PSB3A_ARATH

UniProt

Q9XI05 - PSB3A_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proteasome subunit beta type-3-A

Gene

PBC1

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. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT1G21720-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_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3-A (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit C-1
Proteasome component T
Gene namesi
Name:PBC1
Synonyms:PRCT
Ordered Locus Names:At1g21720
ORF Names:F8K7.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G21720.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. nucleus Source: UniProtKB-KW
  3. proteasome complex Source: TAIR
  4. proteasome core complex Source: InterPro
  5. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 204203Proteasome subunit beta type-3-APRO_0000148065Add
BLAST

Proteomic databases

PaxDbiQ9XI05.
PRIDEiQ9XI05.

Expressioni

Gene expression databases

GenevestigatoriQ9XI05.

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

BioGridi24015. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9XI05.
SMRiQ9XI05. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000090523.
InParanoidiQ9XI05.
KOiK02735.
OMAiMDLIGCP.
PhylomeDBiQ9XI05.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9XI05-1) [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
MSIFEYNGSA VVAMVGKNCF AIASDRRLGV QLQTIATDFQ RISKIHDRVF
60 70 80 90 100
IGLSGLATDV QTLYQRLVFR HKLYQLREER DMKPETFASL VSAILYEKRF
110 120 130 140 150
GPYLCQPVIA GLGDDDKPFI CTMDSIGAKE LAKDFVVSGT ASESLYGACE
160 170 180 190 200
AMYKPDMEAE ELFETISQAL LSSVDRDCLS GWGGHVYIVT PTEIKERILK

GRMD
Length:204
Mass (Da):22,798
Last modified:February 9, 2010 - v2
Checksum:iB52E22CDB3EDA467
GO
Isoform 2 (identifier: Q9XI05-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-2: S → Q

Note: May be due to intron retention. No experimental confirmation available.

Show »
Length:204
Mass (Da):22,839
Checksum:iE1CD9513D8D2F3B9
GO

Sequence cautioni

The sequence AAC32068.1 differs from that shown. Reason: Frameshift at position 41.
The sequence CAA73616.1 differs from that shown. Reason: Frameshift at position 41.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81G → V in AAM62756. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 21S → Q in isoform 2. 1 PublicationVSP_016143

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13173 mRNA. Translation: CAA73616.1. Frameshift.
AF043532 mRNA. Translation: AAC32068.1. Frameshift.
AC007727 Genomic DNA. Translation: AAD41426.1.
CP002684 Genomic DNA. Translation: AEE30146.1.
AY065070 mRNA. Translation: AAL38246.1.
AY114628 mRNA. Translation: AAM47947.1.
AF344327 mRNA. Translation: AAK06878.1.
AK226397 mRNA. Translation: BAE98543.1.
AY085532 mRNA. Translation: AAM62756.1.
PIRiF86350.
RefSeqiNP_564149.1. NM_102021.2. [Q9XI05-1]
UniGeneiAt.11467.

Genome annotation databases

EnsemblPlantsiAT1G21720.1; AT1G21720.1; AT1G21720. [Q9XI05-1]
GeneIDi838776.
KEGGiath:AT1G21720.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13173 mRNA. Translation: CAA73616.1 . Frameshift.
AF043532 mRNA. Translation: AAC32068.1 . Frameshift.
AC007727 Genomic DNA. Translation: AAD41426.1 .
CP002684 Genomic DNA. Translation: AEE30146.1 .
AY065070 mRNA. Translation: AAL38246.1 .
AY114628 mRNA. Translation: AAM47947.1 .
AF344327 mRNA. Translation: AAK06878.1 .
AK226397 mRNA. Translation: BAE98543.1 .
AY085532 mRNA. Translation: AAM62756.1 .
PIRi F86350.
RefSeqi NP_564149.1. NM_102021.2. [Q9XI05-1 ]
UniGenei At.11467.

3D structure databases

ProteinModelPortali Q9XI05.
SMRi Q9XI05. Positions 2-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 24015. 1 interaction.

Proteomic databases

PaxDbi Q9XI05.
PRIDEi Q9XI05.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G21720.1 ; AT1G21720.1 ; AT1G21720 . [Q9XI05-1 ]
GeneIDi 838776.
KEGGi ath:AT1G21720.

Organism-specific databases

TAIRi AT1G21720.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000090523.
InParanoidi Q9XI05.
KOi K02735.
OMAi MDLIGCP.
PhylomeDBi Q9XI05.

Enzyme and pathway databases

BioCyci ARA:AT1G21720-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_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Gene expression databases

Genevestigatori Q9XI05.

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. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  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] (ISOFORM 1), GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. "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(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] (ISOFORMS 1 AND 2).
    Strain: cv. Columbia.
  6. "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 (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  7. "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] (ISOFORM 1).
  8. "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.
  9. "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.
  10. "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, CLEAVAGE OF INITIATOR METHIONINE.

Entry informationi

Entry nameiPSB3A_ARATH
AccessioniPrimary (citable) accession number: Q9XI05
Secondary accession number(s): O23707
, Q0WWF5, Q8LEA7, Q8VZC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 9, 2010
Last modified: October 29, 2014
This is version 110 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