Skip Header

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

Q3T108

- PSB4_BOVIN

UniProt

Q3T108 - PSB4_BOVIN

(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-4

Gene

PSMB4

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 (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei46 – 461NucleophileBy similarity

GO - Molecular functioni

  1. lipopolysaccharide binding Source: Ensembl
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
  2. 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

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Gene namesi
Name:PSMB4
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
Propeptidei1 – 4545By similarityPRO_0000239854Add
BLAST
Chaini46 – 264219Proteasome subunit beta type-4PRO_0000239855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei102 – 1021PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiQ3T108.
PRIDEiQ3T108.

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. Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000028364.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533Combined sources
Beta strandi57 – 615Combined sources
Beta strandi64 – 707Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 814Combined sources
Beta strandi87 – 904Combined sources
Turni91 – 933Combined sources
Beta strandi94 – 1018Combined sources
Helixi102 – 12221Combined sources
Helixi130 – 14617Combined sources
Beta strandi153 – 1619Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1834Combined sources
Helixi187 – 1904Combined sources
Helixi192 – 1998Combined sources
Helixi207 – 22418Combined sources
Beta strandi232 – 2387Combined sources
Beta strandi241 – 2488Combined sources
Helixi255 – 2584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.752/N46-264[»]
ProteinModelPortaliQ3T108.
SMRiQ3T108. Positions 46-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T108.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
HOGENOMiHOG000181719.
HOVERGENiHBG018194.
InParanoidiQ3T108.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG74FF1D.
TreeFamiTF106220.

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.

Q3T108-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEALLESRSG LWAGGPAPGQ FYRIPPTPGS SVDPVSALYG SPITRTQNPM
60 70 80 90 100
VTGTSVLGLK FEGGVVIAAD MLGSYGSLAR FRNISRIMRV NNSTMLGASG
110 120 130 140 150
DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP KAIHSWLTRA MYSRRSKMNP
160 170 180 190 200
LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE
210 220 230 240 250
KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLSA
260
ETNWDIAHMI SGFE
Length:264
Mass (Da):29,031
Last modified:October 11, 2005 - v1
Checksum:iB2C4029A25FCC76A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102182 mRNA. Translation: AAI02183.1.
RefSeqiNP_001029438.1. NM_001034266.2.
UniGeneiBt.53288.

Genome annotation databases

EnsembliENSBTAT00000028364; ENSBTAP00000028364; ENSBTAG00000021288.
GeneIDi506203.
KEGGibta:506203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102182 mRNA. Translation: AAI02183.1 .
RefSeqi NP_001029438.1. NM_001034266.2.
UniGenei Bt.53288.

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 2/N 46-264 [» ]
ProteinModelPortali Q3T108.
SMRi Q3T108. Positions 46-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000028364.

Protein family/group databases

MEROPSi T01.987.

Proteomic databases

PaxDbi Q3T108.
PRIDEi Q3T108.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000028364 ; ENSBTAP00000028364 ; ENSBTAG00000021288 .
GeneIDi 506203.
KEGGi bta:506203.

Organism-specific databases

CTDi 5692.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00390000000698.
HOGENOMi HOG000181719.
HOVERGENi HBG018194.
InParanoidi Q3T108.
KOi K02736.
OMAi RIMRVND.
OrthoDBi EOG74FF1D.
TreeFami TF106220.

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 Q3T108.
NextBioi 20867498.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
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. 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.
  2. "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 46-264 OF COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSB4_BOVIN
AccessioniPrimary (citable) accession number: Q3T108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 11, 2005
Last modified: November 26, 2014
This is version 77 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