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Q9LIP2 (PSB5B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-5-B

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit E-2
Proteasome epsilon-2 chain
Gene names
Name:PBE2
Ordered Locus Names:At3g26340
ORF Names:F20C19.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5757Removed in mature form By similarity
PRO_0000042826
Chain58 – 273216Proteasome subunit beta type-5-B
PRO_0000042827

Sites

Active site581Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LIP2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FAE197B491BDE6A7

FASTA27329,485
        10         20         30         40         50         60 
MKLDTSGLET TMPVIGFGSN SEMLDGFSSA PSFDLPRTTD FDGFQKKAVE MVKPAKGTTT 

        70         80         90        100        110        120 
LAFIFKEGVM VAADSRASMG GYISSQSVKK IIEINPYMLG TMAGGAADCQ FWHRNLGIKC 

       130        140        150        160        170        180 
RLHELANKRR ISVSGASKLL ANMLYSYRGM GLSVGTMIAG WDETGPGLYY VDNEGGRLKG 

       190        200        210        220        230        240 
DRFSVGSGSP YAYGVLDSGY KFDMSVEEAS ELARRSIYHA TFRDGASGGV ASVYHVGPQG 

       250        260        270 
WTKLSGDDVG ELHYHYYPVA PITAEHVMEE AAE 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[4]"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].
[5]"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.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP001298 Genomic DNA. Translation: BAB02194.1.
CP002686 Genomic DNA. Translation: AEE77147.1.
AY125569 mRNA. Translation: AAM78079.1.
AF439846 mRNA. Translation: AAL27514.1.
AY085678 mRNA. Translation: AAM62897.1.
RefSeqNP_189265.1. NM_113541.3.
UniGeneAt.6729.

3D structure databases

ProteinModelPortalQ9LIP2.
SMRQ9LIP2. Positions 58-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7569. 3 interactions.
IntActQ9LIP2. 2 interactions.
STRING3702.AT3G26340.1-P.

Protein family/group databases

MEROPST01.A10.

Proteomic databases

PaxDbQ9LIP2.
PRIDEQ9LIP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G26340.1; AT3G26340.1; AT3G26340.
GeneID822238.
KEGGath:AT3G26340.

Organism-specific databases

TAIRAT3G26340.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091082.
InParanoidQ9LIP2.
KOK02737.
OMATMCAGVT.
PhylomeDBQ9LIP2.

Enzyme and pathway databases

BioCycARA:AT3G26340-MONOMER.

Gene expression databases

GenevestigatorQ9LIP2.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB5B_ARATH
AccessionPrimary (citable) accession number: Q9LIP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names