Skip Header

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

Q2TBX6

- PSB1_BOVIN

UniProt

Q2TBX6 - PSB1_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-1

Gene

PSMB1

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.

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

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1)
Gene namesi
Name:PSMB1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  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
Propeptidei1 – 2828By similarityPRO_0000259622Add
BLAST
Chaini29 – 241213Proteasome subunit beta type-1PRO_0000239853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi58 – 581O-linked (GlcNAc)By similarity
Modified residuei150 – 1501PhosphotyrosineBy similarity
Modified residuei204 – 2041N6-acetyllysineBy similarity
Glycosylationi209 – 2091O-linked (GlcNAc)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ2TBX6.
PRIDEiQ2TBX6.

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

IntActiQ2TBX6. 1 interaction.
STRINGi9913.ENSBTAP00000010108.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 457Combined sources
Beta strandi48 – 547Combined sources
Beta strandi57 – 593Combined sources
Beta strandi62 – 665Combined sources
Beta strandi71 – 755Combined sources
Beta strandi78 – 847Combined sources
Helixi86 – 10722Combined sources
Helixi113 – 12513Combined sources
Turni126 – 1294Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi158 – 16710Combined sources
Helixi170 – 18011Combined sources
Helixi196 – 21318Combined sources
Beta strandi219 – 2279Combined sources
Beta strandi230 – 2378Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.751/M29-241[»]
ProteinModelPortaliQ2TBX6.
SMRiQ2TBX6. Positions 29-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2TBX6.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091081.
HOVERGENiHBG000961.
InParanoidiQ2TBX6.
KOiK02732.

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.

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

Q2TBX6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSSVAAYSG AGRDLAMEPH SSVGPLQLRF SPYAFNGGTV LAIAGEDFSI
60 70 80 90 100
VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL
110 120 130 140 150
KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY
160 170 180 190 200
SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM
210 220 230 240
RLVKDVFISA AERDVYTGDA LKVCIVTKEG IRGETVPLRK D
Length:241
Mass (Da):26,246
Last modified:January 24, 2006 - v1
Checksum:i8682655C19CF2ACD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109494 mRNA. Translation: AAI09495.1.
RefSeqiNP_001033628.1. NM_001038539.2.
UniGeneiBt.7040.

Genome annotation databases

GeneIDi514237.
KEGGibta:514237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109494 mRNA. Translation: AAI09495.1 .
RefSeqi NP_001033628.1. NM_001038539.2.
UniGenei Bt.7040.

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 1/M 29-241 [» ]
ProteinModelPortali Q2TBX6.
SMRi Q2TBX6. Positions 29-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q2TBX6. 1 interaction.
STRINGi 9913.ENSBTAP00000010108.

Proteomic databases

PaxDbi Q2TBX6.
PRIDEi Q2TBX6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 514237.
KEGGi bta:514237.

Organism-specific databases

CTDi 5689.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091081.
HOVERGENi HBG000961.
InParanoidi Q2TBX6.
KOi K02732.

Miscellaneous databases

EvolutionaryTracei Q2TBX6.
NextBioi 20871244.

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. 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 29-241 OF COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSB1_BOVIN
AccessioniPrimary (citable) accession number: Q2TBX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 24, 2006
Last modified: November 26, 2014
This is version 69 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