Skip Header

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

Proteasome subunit beta type-1

Gene

Psmb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.1By similarity)
Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain
Gene namesi
Name:Psmb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:104884. Psmb1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002596241 – 27By similarityAdd BLAST27
ChainiPRO_000014803128 – 240Proteasome subunit beta type-1Add BLAST213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Glycosylationi57O-linked (GlcNAc)1 Publication1
Modified residuei61PhosphoserineBy similarity1
Modified residuei67PhosphoserineBy similarity1
Modified residuei149PhosphotyrosineCombined sources1
Modified residuei161PhosphoserineBy similarity1
Modified residuei203N6-acetyllysineBy similarity1
Glycosylationi208O-linked (GlcNAc)1 Publication1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO09061.
PaxDbiO09061.
PeptideAtlasiO09061.
PRIDEiO09061.

PTM databases

iPTMnetiO09061.
PhosphoSitePlusiO09061.
SwissPalmiO09061.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000014769.
ExpressionAtlasiO09061. baseline and differential.
GenevisibleiO09061. MM.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, PubMed:22341445). Interacts with SERPINB2 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi202418. 4 interactors.
IntActiO09061. 6 interactors.
MINTiMINT-1856820.
STRINGi10090.ENSMUSP00000014913.

Structurei

Secondary structure

1240
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 43Combined sources6
Beta strandi48 – 53Combined sources6
Beta strandi56 – 58Combined sources3
Beta strandi61 – 65Combined sources5
Beta strandi70 – 72Combined sources3
Beta strandi74 – 83Combined sources10
Helixi85 – 106Combined sources22
Helixi112 – 124Combined sources13
Turni125 – 128Combined sources4
Beta strandi133 – 137Combined sources5
Beta strandi142 – 144Combined sources3
Beta strandi146 – 151Combined sources6
Beta strandi157 – 159Combined sources3
Beta strandi161 – 166Combined sources6
Helixi169 – 179Combined sources11
Helixi195 – 212Combined sources18
Beta strandi213 – 215Combined sources3
Beta strandi218 – 226Combined sources9
Beta strandi229 – 236Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.902/L/Z/n28-240[»]
3UNEX-ray3.202/L/Z/n28-240[»]
3UNFX-ray2.90L/Z28-240[»]
3UNHX-ray3.20L/Z28-240[»]
5L65X-ray2.90L/Z123-137[»]
L/Z144-159[»]
5L66X-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L67X-ray2.60L/Z123-137[»]
L/Z144-159[»]
5L68X-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L69X-ray2.70L/Z123-137[»]
L/Z144-159[»]
5L6AX-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L6BX-ray2.60L/Z123-137[»]
L/Z144-159[»]
5L6CX-ray2.60L/Z123-137[»]
L/Z144-159[»]
ProteinModelPortaliO09061.
SMRiO09061.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0179. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000075035.
HOGENOMiHOG000091081.
HOVERGENiHBG000961.
InParanoidiO09061.
KOiK02732.
OMAiQNPLMNG.
OrthoDBiEOG091G0FUK.
PhylomeDBiO09061.
TreeFamiTF106218.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O09061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSTAAYRDV ERELGMGPHG SAGPVQLRFS PYAFNGGTVL AIAGEDFSIV
60 70 80 90 100
ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK
110 120 130 140 150
MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS
160 170 180 190 200
FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLTLDRAMR
210 220 230 240
LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD
Length:240
Mass (Da):26,372
Last modified:July 1, 1997 - v1
Checksum:i22ADBC6ACB3A8D31
GO

Sequence cautioni

The sequence CAA56702 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60824 mRNA. Translation: AAB37251.1.
X80686 mRNA. Translation: CAA56701.1.
X80686 mRNA. Translation: CAA56702.1. Different initiation.
AK077520 mRNA. Translation: BAC36841.1.
BC018351 mRNA. Translation: AAH18351.1.
CCDSiCCDS28411.1.
RefSeqiNP_035315.1. NM_011185.3.
UniGeneiMm.32912.

Genome annotation databases

EnsembliENSMUST00000014913; ENSMUSP00000014913; ENSMUSG00000014769.
GeneIDi19170.
KEGGimmu:19170.
UCSCiuc008aol.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60824 mRNA. Translation: AAB37251.1.
X80686 mRNA. Translation: CAA56701.1.
X80686 mRNA. Translation: CAA56702.1. Different initiation.
AK077520 mRNA. Translation: BAC36841.1.
BC018351 mRNA. Translation: AAH18351.1.
CCDSiCCDS28411.1.
RefSeqiNP_035315.1. NM_011185.3.
UniGeneiMm.32912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.902/L/Z/n28-240[»]
3UNEX-ray3.202/L/Z/n28-240[»]
3UNFX-ray2.90L/Z28-240[»]
3UNHX-ray3.20L/Z28-240[»]
5L65X-ray2.90L/Z123-137[»]
L/Z144-159[»]
5L66X-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L67X-ray2.60L/Z123-137[»]
L/Z144-159[»]
5L68X-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L69X-ray2.70L/Z123-137[»]
L/Z144-159[»]
5L6AX-ray2.80L/Z123-137[»]
L/Z144-159[»]
5L6BX-ray2.60L/Z123-137[»]
L/Z144-159[»]
5L6CX-ray2.60L/Z123-137[»]
L/Z144-159[»]
ProteinModelPortaliO09061.
SMRiO09061.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202418. 4 interactors.
IntActiO09061. 6 interactors.
MINTiMINT-1856820.
STRINGi10090.ENSMUSP00000014913.

PTM databases

iPTMnetiO09061.
PhosphoSitePlusiO09061.
SwissPalmiO09061.

Proteomic databases

EPDiO09061.
PaxDbiO09061.
PeptideAtlasiO09061.
PRIDEiO09061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014913; ENSMUSP00000014913; ENSMUSG00000014769.
GeneIDi19170.
KEGGimmu:19170.
UCSCiuc008aol.1. mouse.

Organism-specific databases

CTDi5689.
MGIiMGI:104884. Psmb1.

Phylogenomic databases

eggNOGiKOG0179. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000075035.
HOGENOMiHOG000091081.
HOVERGENiHBG000961.
InParanoidiO09061.
KOiK02732.
OMAiQNPLMNG.
OrthoDBiEOG091G0FUK.
PhylomeDBiO09061.
TreeFamiTF106218.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiPR:O09061.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000014769.
ExpressionAtlasiO09061. baseline and differential.
GenevisibleiO09061. MM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPSB1_MOUSE
AccessioniPrimary (citable) accession number: O09061
Secondary accession number(s): Q62038, Q62039
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: March 15, 2017
This is version 150 of the entry and version 1 of the sequence. See 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.