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P28024

- PSB4_XENLA

UniProt

P28024 - PSB4_XENLA

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Protein
Proteasome subunit beta type-4
Gene
psmb4
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 – 241Nucleophile By similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

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):
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Gene namesi
Name:psmb4
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6253413. psmb4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei‹1 – 23›23 Reviewed prediction
PRO_0000026587Add
BLAST
Chaini24 – 242219Proteasome subunit beta type-4
PRO_0000026588Add
BLAST

Proteomic databases

PRIDEiP28024.

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.

Structurei

3D structure databases

ProteinModelPortaliP28024.
SMRiP28024. Positions 24-240.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

HOVERGENiHBG018194.

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: Fragment.

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

P28024-1 [UniParc]FASTAAdd to Basket

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ESVARGTAPG ELHCFPGAGP VRHTLNPMVT GTSVLGVKFD GGVIIAADML    50
GSYGSLARFR NISRIMKVNE NTILGASGDY ADYQYLKQVI DQMVIDEELV 100
GDGHNYSPKA IHSWLTRVMY NRRSKMNPLW NTVVIGGFYN GESFLGYVDK 150
LGVAYEAPTI ATGFGAYLAQ PLLREVTENK ATLSKEEARQ LVDRCMKVLY 200
YRDARSYNRF EITTVTESGV EVEGPLSSET NWEIAHLISG FE 242
Length:242
Mass (Da):26,759
Last modified:December 15, 1998 - v2
Checksum:iDCEB9D1A13C61D3E
GO

Sequence cautioni

The sequence CAA44593.1 differs from that shown. Reason: Erroneous initiation.

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62709 mRNA. Translation: CAA44593.1. Different initiation.
PIRiS17568.
UniGeneiXl.4728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62709 mRNA. Translation: CAA44593.1 . Different initiation.
PIRi S17568.
UniGenei Xl.4728.

3D structure databases

ProteinModelPortali P28024.
SMRi P28024. Positions 24-240.
ModBasei Search...

Protein family/group databases

MEROPSi T01.987.

Proteomic databases

PRIDEi P28024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Xenbasei XB-GENE-6253413. psmb4.

Phylogenomic databases

HOVERGENi HBG018194.

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

  1. "Cloning and sequence analysis of pituitary cDNA encoding the beta-subunit of Xenopus proteasome."
    van Riel M.C.H.M., Martens G.J.M.
    FEBS Lett. 291:37-40(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.

Entry informationi

Entry nameiPSB4_XENLA
AccessioniPrimary (citable) accession number: P28024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 15, 1998
Last modified: June 11, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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