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Q5E9K0

- PSB2_BOVIN

UniProt

Q5E9K0 - PSB2_BOVIN

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Protein

Proteasome subunit beta type-2

Gene

PSMB2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 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. This subunit has a chymotrypsin-like activity (By similarity).By similarity

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

ReactomeiREACT_203739. Degradation of beta-catenin by the destruction complex.
REACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
REACT_205897. Activation of NF-kappaB in B cells.
REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
REACT_207857. Asymmetric localization of PCP proteins.
REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_208889. degradation of AXIN.
REACT_211738. ER-Phagosome pathway.
REACT_212887. Separation of Sister Chromatids.
REACT_213030. Orc1 removal from chromatin.
REACT_215163. degradation of DVL.
REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_237530. Regulation of ornithine decarboxylase (ODC).
REACT_252463. Hedgehog ligand biogenesis.
REACT_259250. Hh ligand biogenesis disease.
REACT_269173. Degradation of GLI2 by the proteasome.
REACT_269531. GLI3 is processed to GLI3R by the proteasome.
REACT_271133. Degradation of GLI1 by the proteasome.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-2 (EC:3.4.25.1)
Gene namesi
Name:PSMB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 3

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Proteasome subunit beta type-2PRO_0000239852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5E9K0.
PRIDEiQ5E9K0.

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.

Protein-protein interaction databases

IntActiQ5E9K0. 1 interaction.
STRINGi9913.ENSBTAP00000003072.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi10 – 189Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 316Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 4911Combined sources
Helixi52 – 7120Combined sources
Helixi77 – 9216Combined sources
Beta strandi94 – 963Combined sources
Beta strandi100 – 1089Combined sources
Turni109 – 1113Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1336Combined sources
Helixi134 – 14613Combined sources
Helixi153 – 16917Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi187 – 1893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75K/Y1-201[»]
ProteinModelPortaliQ5E9K0.
SMRiQ5E9K0. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5E9K0.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
InParanoidiQ5E9K0.
KOiK02734.
OMAiHFVRGEL.
OrthoDBiEOG7N63NQ.
TreeFamiTF106219.

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.

Q5E9K0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA
60 70 80 90 100
GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLAD YLRSRTPYHV
110 120 130 140 150
NLLLAGYDEH EGPALYYMDY LAALAKAPFA AHGYGAFLTL SILDRYYTPT
160 170 180 190 200
ISREKAVELL RKCLEELQKR FILNLPTFSV RIIDRNGIHD LDNISFPKQG

S
Length:201
Mass (Da):22,896
Last modified:March 15, 2005 - v1
Checksum:i8D195EBA1DBB02DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020855 mRNA. Translation: AAX08872.1.
BT020920 mRNA. Translation: AAX08937.1.
BC102367 mRNA. Translation: AAI02368.1.
RefSeqiNP_001015615.1. NM_001015615.1.
UniGeneiBt.40863.

Genome annotation databases

EnsembliENSBTAT00000003072; ENSBTAP00000003072; ENSBTAG00000002377.
GeneIDi516919.
KEGGibta:516919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020855 mRNA. Translation: AAX08872.1 .
BT020920 mRNA. Translation: AAX08937.1 .
BC102367 mRNA. Translation: AAI02368.1 .
RefSeqi NP_001015615.1. NM_001015615.1.
UniGenei Bt.40863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IRU X-ray 2.75 K/Y 1-201 [» ]
ProteinModelPortali Q5E9K0.
SMRi Q5E9K0. Positions 1-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q5E9K0. 1 interaction.
STRINGi 9913.ENSBTAP00000003072.

Protein family/group databases

MEROPSi T01.984.

Proteomic databases

PaxDbi Q5E9K0.
PRIDEi Q5E9K0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000003072 ; ENSBTAP00000003072 ; ENSBTAG00000002377 .
GeneIDi 516919.
KEGGi bta:516919.

Organism-specific databases

CTDi 5690.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00640000091536.
HOGENOMi HOG000188743.
HOVERGENi HBG000815.
InParanoidi Q5E9K0.
KOi K02734.
OMAi HFVRGEL.
OrthoDBi EOG7N63NQ.
TreeFami TF106219.

Enzyme and pathway databases

Reactomei REACT_203739. Degradation of beta-catenin by the destruction complex.
REACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
REACT_205897. Activation of NF-kappaB in B cells.
REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
REACT_207857. Asymmetric localization of PCP proteins.
REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_208889. degradation of AXIN.
REACT_211738. ER-Phagosome pathway.
REACT_212887. Separation of Sister Chromatids.
REACT_213030. Orc1 removal from chromatin.
REACT_215163. degradation of DVL.
REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_237530. Regulation of ornithine decarboxylase (ODC).
REACT_252463. Hedgehog ligand biogenesis.
REACT_259250. Hh ligand biogenesis disease.
REACT_269173. Degradation of GLI2 by the proteasome.
REACT_269531. GLI3 is processed to GLI3R by the proteasome.
REACT_271133. Degradation of GLI1 by the proteasome.

Miscellaneous databases

EvolutionaryTracei Q5E9K0.
NextBioi 20872333.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "The structure of the mammalian 20S proteasome at 2.75 A resolution."
    Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
    Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSB2_BOVIN
AccessioniPrimary (citable) accession number: Q5E9K0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 15, 2005
Last modified: November 26, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3