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Protein

Proteasome subunit alpha type-4

Gene

Psma4

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-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.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C9
Multicatalytic endopeptidase complex subunit C9
Proteasome component C9
Proteasome subunit L
Gene namesi
Name:Psma4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1347060. Psma4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241051 – 261Proteasome subunit alpha type-4Add BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei127N6-acetyllysineBy similarity1
Modified residuei173PhosphoserineBy similarity1
Modified residuei176N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9R1P0.
MaxQBiQ9R1P0.
PaxDbiQ9R1P0.
PeptideAtlasiQ9R1P0.
PRIDEiQ9R1P0.

PTM databases

iPTMnetiQ9R1P0.
PhosphoSitePlusiQ9R1P0.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000032301.
ExpressionAtlasiQ9R1P0. baseline and differential.
GenevisibleiQ9R1P0. 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.2 Publications

Protein-protein interaction databases

BioGridi204992. 3 interactors.
IntActiQ9R1P0. 6 interactors.
MINTiMINT-1850528.
STRINGi10090.ENSMUSP00000034848.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Helixi19 – 28Combined sources10
Beta strandi34 – 38Combined sources5
Beta strandi40 – 48Combined sources9
Beta strandi63 – 67Combined sources5
Beta strandi69 – 78Combined sources10
Helixi80 – 101Combined sources22
Helixi107 – 123Combined sources17
Beta strandi124 – 126Combined sources3
Beta strandi132 – 140Combined sources9
Turni141 – 143Combined sources3
Beta strandi144 – 150Combined sources7
Beta strandi156 – 165Combined sources10
Helixi168 – 178Combined sources11
Turni181 – 183Combined sources3
Helixi186 – 200Combined sources15
Beta strandi202 – 205Combined sources4
Helixi208 – 210Combined sources3
Beta strandi211 – 219Combined sources9
Beta strandi222 – 227Combined sources6
Helixi230 – 244Combined sources15
Beta strandi245 – 247Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90B/P/d/r1-261[»]
3UNEX-ray3.20B/P/d/r1-261[»]
3UNFX-ray2.90B/P1-261[»]
3UNHX-ray3.20B/P1-261[»]
ProteinModelPortaliQ9R1P0.
SMRiQ9R1P0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9R1P0.
KOiK02728.
OMAiCNEKQRY.
OrthoDBiEOG091G0F2L.
PhylomeDBiQ9R1P0.
TreeFamiTF106209.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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.

Q9R1P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR
60 70 80 90 100
NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ
110 120 130 140 150
YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAVKVLNKT
210 220 230 240 250
MDVSKLSAEK VEIATLTRES GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE
260
KKEKEQREKD K
Length:261
Mass (Da):29,471
Last modified:May 1, 2000 - v1
Checksum:iBB7CC8113791E13B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060093 mRNA. Translation: AAD50538.1.
AK085937 mRNA. Translation: BAC39573.1.
AK168150 mRNA. Translation: BAE40115.1.
BC001982 mRNA. Translation: AAH01982.1.
CCDSiCCDS40643.1.
RefSeqiNP_036096.1. NM_011966.3.
XP_006511261.1. XM_006511198.3.
UniGeneiMm.30270.
Mm.440582.

Genome annotation databases

EnsembliENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301.
GeneIDi26441.
KEGGimmu:26441.
UCSCiuc009pru.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060093 mRNA. Translation: AAD50538.1.
AK085937 mRNA. Translation: BAC39573.1.
AK168150 mRNA. Translation: BAE40115.1.
BC001982 mRNA. Translation: AAH01982.1.
CCDSiCCDS40643.1.
RefSeqiNP_036096.1. NM_011966.3.
XP_006511261.1. XM_006511198.3.
UniGeneiMm.30270.
Mm.440582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90B/P/d/r1-261[»]
3UNEX-ray3.20B/P/d/r1-261[»]
3UNFX-ray2.90B/P1-261[»]
3UNHX-ray3.20B/P1-261[»]
ProteinModelPortaliQ9R1P0.
SMRiQ9R1P0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204992. 3 interactors.
IntActiQ9R1P0. 6 interactors.
MINTiMINT-1850528.
STRINGi10090.ENSMUSP00000034848.

Protein family/group databases

MEROPSiT01.973.

PTM databases

iPTMnetiQ9R1P0.
PhosphoSitePlusiQ9R1P0.

Proteomic databases

EPDiQ9R1P0.
MaxQBiQ9R1P0.
PaxDbiQ9R1P0.
PeptideAtlasiQ9R1P0.
PRIDEiQ9R1P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301.
GeneIDi26441.
KEGGimmu:26441.
UCSCiuc009pru.1. mouse.

Organism-specific databases

CTDi5685.
MGIiMGI:1347060. Psma4.

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9R1P0.
KOiK02728.
OMAiCNEKQRY.
OrthoDBiEOG091G0F2L.
PhylomeDBiQ9R1P0.
TreeFamiTF106209.

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-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

ChiTaRSiPsma4. mouse.
PROiQ9R1P0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032301.
ExpressionAtlasiQ9R1P0. baseline and differential.
GenevisibleiQ9R1P0. MM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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 nameiPSA4_MOUSE
AccessioniPrimary (citable) accession number: Q9R1P0
Secondary accession number(s): Q3THT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 145 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.