Skip Header

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

P33672

- PSB3_BOVIN

UniProt

P33672 - PSB3_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-3

Gene

PSMB3

Organism
Bos taurus (Bovine)
Status
Reviewed - 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.

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

Enzyme and pathway databases

ReactomeiREACT_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.

Protein family/group databases

MEROPSiT01.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
Proteasome chain 13
Proteasome component C10-II
Proteasome theta chain
Gene namesi
Name:PSMB3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 19

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. Golgi apparatus Source: Ensembl
  4. mitochondrion Source: Ensembl
  5. nucleus Source: UniProtKB-KW
  6. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei77 – 771N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP33672.
PRIDEiP33672.

Expressioni

Gene expression databases

ExpressionAtlasiP33672. baseline.

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

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156
Beta strandi17 – 259
Beta strandi28 – 303
Beta strandi33 – 375
Beta strandi42 – 443
Beta strandi49 – 524
Helixi57 – 7721
Beta strandi78 – 803
Helixi84 – 9613
Turni97 – 1004
Beta strandi108 – 1125
Beta strandi119 – 1246
Beta strandi130 – 1323
Beta strandi134 – 1407
Helixi143 – 15311
Helixi160 – 17415
Helixi175 – 1773
Beta strandi185 – 20016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75J/X1-205[»]
ProteinModelPortaliP33672.
SMRiP33672. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33672.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiP33672.
KOiK02735.
OMAiMDLIGCP.
OrthoDBiEOG783MWB.
TreeFamiTF106216.

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.

P33672-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY
60 70 80 90 100
IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF
110 120 130 140 150
GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCTEQMYGMC
160 170 180 190 200
ESLWEPNMDP EHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL

KARMD
Length:205
Mass (Da):22,993
Last modified:June 13, 2006 - v3
Checksum:i62551E484D5042FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891S → C AA sequence (PubMed:1510924)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102554 mRNA. Translation: AAI02555.1.
PIRiA42762.
B42762.
C42762.
D42762.
G42762.
RefSeqiNP_001029768.1. NM_001034596.2.
UniGeneiBt.44351.

Genome annotation databases

EnsembliENSBTAT00000004984; ENSBTAP00000004984; ENSBTAG00000003830.
GeneIDi533874.
KEGGibta:533874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102554 mRNA. Translation: AAI02555.1 .
PIRi A42762.
B42762.
C42762.
D42762.
G42762.
RefSeqi NP_001029768.1. NM_001034596.2.
UniGenei Bt.44351.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IRU X-ray 2.75 J/X 1-205 [» ]
ProteinModelPortali P33672.
SMRi P33672. Positions 2-205.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi T01.983.

Proteomic databases

PaxDbi P33672.
PRIDEi P33672.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000004984 ; ENSBTAP00000004984 ; ENSBTAG00000003830 .
GeneIDi 533874.
KEGGi bta:533874.

Organism-specific databases

CTDi 5691.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074820.
HOGENOMi HOG000090523.
HOVERGENi HBG004446.
InParanoidi P33672.
KOi K02735.
OMAi MDLIGCP.
OrthoDBi EOG783MWB.
TreeFami TF106216.

Enzyme and pathway databases

Reactomei 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.

Miscellaneous databases

EvolutionaryTracei P33672.
NextBioi 20876178.

Gene expression databases

ExpressionAtlasi P33672. baseline.

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 (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.
  2. "Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome."
    Dick L.R., Moomaw C.R., Pramanik B.C., DeMartino G.N., Slaughter C.A.
    Biochemistry 31:7347-7355(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 14-79; 89-114; 121-141; 160-170 AND 183-205.
  3. "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 COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSB3_BOVIN
AccessioniPrimary (citable) accession number: P33672
Secondary accession number(s): Q3T059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 13, 2006
Last modified: October 29, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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