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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)DescriptionActionsGraphical viewLength
Active sitei44Nucleophile1

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003290621 – 43Removed in mature formBy similarityAdd BLAST43
ChainiPRO_000032906344 – 277Proteasome subunit beta type-7Add BLAST234

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ2TBP0.
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

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 51Combined sources6
Beta strandi54 – 59Combined sources6
Beta strandi63 – 73Combined sources11
Beta strandi77 – 81Combined sources5
Beta strandi84 – 91Combined sources8
Helixi92 – 113Combined sources22
Helixi119 – 132Combined sources14
Turni133 – 135Combined sources3
Beta strandi139 – 146Combined sources8
Beta strandi151 – 156Combined sources6
Beta strandi162 – 164Combined sources3
Beta strandi166 – 171Combined sources6
Helixi174 – 183Combined sources10
Helixi191 – 195Combined sources5
Helixi197 – 208Combined sources12
Beta strandi216 – 222Combined sources7
Beta strandi225 – 227Combined sources3
Beta strandi230 – 233Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ2TBP0.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75I/W44-277[»]
ProteinModelPortaliQ2TBP0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000003990.

Protein family/group databases

MEROPSiT01.A02.

Proteomic databases

PaxDbiQ2TBP0.
PRIDEiQ2TBP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi511207.
KEGGibta:511207.

Organism-specific databases

CTDi5695.

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ2TBP0.
KOiK02739.

Miscellaneous databases

EvolutionaryTraceiQ2TBP0.

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...

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: October 5, 2016
This is version 76 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

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 one 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.