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Protein

Proteasome subunit alpha type-5

Gene

Psma5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, 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 alpha type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain zeta chain
Multicatalytic endopeptidase complex zeta chain
Proteasome zeta chain
Gene namesi
Name:Psma5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1347009. Psma5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241181 – 241Proteasome subunit alpha type-5Add BLAST241

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei16PhosphoserineBy similarity1
Modified residuei55PhosphothreonineBy similarity1
Modified residuei56PhosphoserineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Glycosylationi198O-linked (GlcNAc)1 Publication1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9Z2U1.
MaxQBiQ9Z2U1.
PaxDbiQ9Z2U1.
PRIDEiQ9Z2U1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U1.

PTM databases

iPTMnetiQ9Z2U1.
PhosphoSitePlusiQ9Z2U1.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000068749.
ExpressionAtlasiQ9Z2U1. baseline and differential.
GenevisibleiQ9Z2U1. MM.

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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.2 Publications

Protein-protein interaction databases

BioGridi204993. 3 interactors.
IntActiQ9Z2U1. 6 interactors.
MINTiMINT-1856766.
STRINGi10090.ENSMUSP00000088057.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Helixi22 – 31Combined sources10
Beta strandi37 – 42Combined sources6
Beta strandi45 – 51Combined sources7
Helixi61 – 63Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi74 – 80Combined sources7
Helixi82 – 103Combined sources22
Helixi109 – 117Combined sources9
Turni118 – 121Combined sources4
Beta strandi125 – 127Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi139 – 146Combined sources8
Beta strandi151 – 156Combined sources6
Beta strandi162 – 171Combined sources10
Helixi174 – 184Combined sources11
Helixi191 – 205Combined sources15
Turni212 – 214Combined sources3
Beta strandi215 – 220Combined sources6
Beta strandi222 – 224Combined sources3
Helixi231 – 238Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90D/R/f/t1-241[»]
3UNEX-ray3.20D/R/f/t1-241[»]
3UNFX-ray2.90D/R1-241[»]
3UNHX-ray3.20D/R1-241[»]
ProteinModelPortaliQ9Z2U1.
SMRiQ9Z2U1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0176. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U1.
KOiK02729.
OMAiSGAYFEW.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ9Z2U1.
TreeFamiTF106211.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2U1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV
60 70 80 90 100
EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW
110 120 130 140 150
FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG
160 170 180 190 200
PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI
210 220 230 240
ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I
Length:241
Mass (Da):26,411
Last modified:May 1, 1999 - v1
Checksum:i5610CDA00469120A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019661 mRNA. Translation: AAC69149.1.
BC010709 mRNA. Translation: AAH10709.1.
BC083342 mRNA. Translation: AAH83342.1.
CCDSiCCDS17755.1.
RefSeqiNP_036097.1. NM_011967.3.
UniGeneiMm.208883.

Genome annotation databases

EnsembliENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749.
GeneIDi26442.
KEGGimmu:26442.
UCSCiuc008qyq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019661 mRNA. Translation: AAC69149.1.
BC010709 mRNA. Translation: AAH10709.1.
BC083342 mRNA. Translation: AAH83342.1.
CCDSiCCDS17755.1.
RefSeqiNP_036097.1. NM_011967.3.
UniGeneiMm.208883.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90D/R/f/t1-241[»]
3UNEX-ray3.20D/R/f/t1-241[»]
3UNFX-ray2.90D/R1-241[»]
3UNHX-ray3.20D/R1-241[»]
ProteinModelPortaliQ9Z2U1.
SMRiQ9Z2U1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204993. 3 interactors.
IntActiQ9Z2U1. 6 interactors.
MINTiMINT-1856766.
STRINGi10090.ENSMUSP00000088057.

PTM databases

iPTMnetiQ9Z2U1.
PhosphoSitePlusiQ9Z2U1.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U1.

Proteomic databases

EPDiQ9Z2U1.
MaxQBiQ9Z2U1.
PaxDbiQ9Z2U1.
PRIDEiQ9Z2U1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749.
GeneIDi26442.
KEGGimmu:26442.
UCSCiuc008qyq.1. mouse.

Organism-specific databases

CTDi5686.
MGIiMGI:1347009. Psma5.

Phylogenomic databases

eggNOGiKOG0176. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U1.
KOiK02729.
OMAiSGAYFEW.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ9Z2U1.
TreeFamiTF106211.

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

PROiQ9Z2U1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000068749.
ExpressionAtlasiQ9Z2U1. baseline and differential.
GenevisibleiQ9Z2U1. MM.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSA5_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 154 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, 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.