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Protein

Proteasome subunit beta type-7

Gene

PSMB7

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.1)
Gene namesi
Name:PSMB7
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4343Removed in mature formBy similarityPRO_0000329062Add
BLAST
Chaini44 – 277234Proteasome subunit beta type-7PRO_0000329063Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiQ2TBP0.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB10.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003990.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 516Combined sources
Beta strandi54 – 596Combined sources
Beta strandi63 – 7311Combined sources
Beta strandi77 – 815Combined sources
Beta strandi84 – 918Combined sources
Helixi92 – 11322Combined sources
Helixi119 – 13214Combined sources
Turni133 – 1353Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1716Combined sources
Helixi174 – 18310Combined sources
Helixi191 – 1955Combined sources
Helixi197 – 20812Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi230 – 2334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75I/W44-277[»]
ProteinModelPortaliQ2TBP0.
SMRiQ2TBP0. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2TBP0.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ2TBP0.
KOiK02739.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

Q2TBP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVSVYERP VGGFSFDNCR RNAVLEADFA KKGYKLPTAR KTGTTIAGVV
60 70 80 90 100
YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ
110 120 130 140 150
LISSNLELHS LSTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG
160 170 180 190 200
PHLYSIYPHG STDKLPYVTM GSGSLAAMAV FEDKFRPDME EEEAKKLVSE
210 220 230 240 250
AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PYSVPNKKGT RFGRYRCEKG
260 270
TNAVLTEKVT TLEIEVLEET VQTMDTS
Length:277
Mass (Da):30,009
Last modified:January 24, 2006 - v1
Checksum:iC3DE3CB1782AEBB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109868 mRNA. Translation: AAI09869.1.
RefSeqiNP_001033616.1. NM_001038527.2.
UniGeneiBt.56882.

Genome annotation databases

GeneIDi511207.
KEGGibta:511207.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109868 mRNA. Translation: AAI09869.1.
RefSeqiNP_001033616.1. NM_001038527.2.
UniGeneiBt.56882.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75I/W44-277[»]
ProteinModelPortaliQ2TBP0.
SMRiQ2TBP0. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003990.

Protein family/group databases

MEROPSiT01.A02.

Proteomic databases

PRIDEiQ2TBP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi511207.
KEGGibta:511207.

Organism-specific databases

CTDi5695.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ2TBP0.
KOiK02739.

Miscellaneous databases

EvolutionaryTraceiQ2TBP0.
NextBioi20869822.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  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 44-277 OF COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSB7_BOVIN
AccessioniPrimary (citable) accession number: Q2TBP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: January 24, 2006
Last modified: January 7, 2015
This is version 70 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.