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Protein

Proteasome subunit alpha type-7

Gene

Psma7

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.PROSITE-ProRule annotation

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-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

MEROPSiT01.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7 (EC:3.4.25.1By similarity)
Alternative name(s):
Proteasome subunit RC6-1
Gene namesi
Name:Psma7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1347070. Psma7.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
  • postsynapse Source: SynGO
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: InterPro

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241431 – 248Proteasome subunit alpha type-7Add BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi130O-linked (GlcNAc) serine1 Publication1
Modified residuei153Phosphotyrosine; by ABL1 and ABL2By similarity1
Modified residuei227N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9Z2U0.
MaxQBiQ9Z2U0.
PaxDbiQ9Z2U0.
PRIDEiQ9Z2U0.

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2U0.

PTM databases

iPTMnetiQ9Z2U0.
PhosphoSitePlusiQ9Z2U0.
SwissPalmiQ9Z2U0.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues.1 Publication

Gene expression databases

BgeeiENSMUSG00000027566.
ExpressionAtlasiQ9Z2U0. baseline and differential.
GenevisibleiQ9Z2U0. 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). PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By similarity). Interacts with HIF1A (By similarity). Interacts with RAB7A (By similarity). Interacts with PRKN (By similarity). Interacts with ABL1 and ABL2 (By similarity). Interacts with EMAP2 (By similarity). Interacts with MAVS (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204995. 4 interactors.
IntActiQ9Z2U0. 5 interactors.
MINTiMINT-1856843.
STRINGi10090.ENSMUSP00000029082.

Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 27Combined sources11
Beta strandi32 – 36Combined sources5
Beta strandi38 – 45Combined sources8
Beta strandi52 – 54Combined sources3
Turni56 – 59Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi66 – 75Combined sources10
Helixi77 – 97Combined sources21
Beta strandi98 – 100Combined sources3
Helixi104 – 117Combined sources14
Beta strandi120 – 122Combined sources3
Beta strandi129 – 136Combined sources8
Beta strandi142 – 147Combined sources6
Beta strandi153 – 162Combined sources10
Helixi165 – 175Combined sources11
Turni178 – 181Combined sources4
Helixi184 – 195Combined sources12
Turni196 – 198Combined sources3
Beta strandi199 – 201Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi207 – 215Combined sources9
Beta strandi217 – 219Combined sources3
Helixi222 – 236Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90C/Q/e/s1-248[»]
3UNEX-ray3.20C/Q/e/s1-248[»]
3UNFX-ray2.90C/Q1-248[»]
3UNHX-ray3.20C/Q1-248[»]
ProteinModelPortaliQ9Z2U0.
SMRiQ9Z2U0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U0.
KOiK02731.
OMAiIKLVIRA.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ9Z2U0.
TreeFamiTF106212.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
SMARTiView protein in SMART
SM00948. Proteasome_A_N. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z2U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKDI VVLGVEKKSV
60 70 80 90 100
AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED
110 120 130 140 150
PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS
160 170 180 190 200
GTYHAWKANA IGRGAKSVRE FLEKNYTDDA IETDDLTIKL VIKALLEVVQ
210 220 230 240
SGGKNIELAV MRRDQPLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
Length:248
Mass (Da):27,855
Last modified:May 1, 1999 - v1
Checksum:iE2C8D607D8E2BC9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019662 mRNA. Translation: AAC69150.1.
BC008222 mRNA. Translation: AAH08222.1.
CCDSiCCDS17166.1.
RefSeqiNP_036099.1. NM_011969.2.
UniGeneiMm.21728.

Genome annotation databases

EnsembliENSMUST00000029082; ENSMUSP00000029082; ENSMUSG00000027566.
GeneIDi26444.
KEGGimmu:26444.
UCSCiuc008oib.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019662 mRNA. Translation: AAC69150.1.
BC008222 mRNA. Translation: AAH08222.1.
CCDSiCCDS17166.1.
RefSeqiNP_036099.1. NM_011969.2.
UniGeneiMm.21728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90C/Q/e/s1-248[»]
3UNEX-ray3.20C/Q/e/s1-248[»]
3UNFX-ray2.90C/Q1-248[»]
3UNHX-ray3.20C/Q1-248[»]
ProteinModelPortaliQ9Z2U0.
SMRiQ9Z2U0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204995. 4 interactors.
IntActiQ9Z2U0. 5 interactors.
MINTiMINT-1856843.
STRINGi10090.ENSMUSP00000029082.

Protein family/group databases

MEROPSiT01.979.

PTM databases

iPTMnetiQ9Z2U0.
PhosphoSitePlusiQ9Z2U0.
SwissPalmiQ9Z2U0.

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2U0.

Proteomic databases

EPDiQ9Z2U0.
MaxQBiQ9Z2U0.
PaxDbiQ9Z2U0.
PRIDEiQ9Z2U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029082; ENSMUSP00000029082; ENSMUSG00000027566.
GeneIDi26444.
KEGGimmu:26444.
UCSCiuc008oib.2. mouse.

Organism-specific databases

CTDi5688.
MGIiMGI:1347070. Psma7.

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U0.
KOiK02731.
OMAiIKLVIRA.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ9Z2U0.
TreeFamiTF106212.

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

PROiPR:Q9Z2U0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027566.
ExpressionAtlasiQ9Z2U0. baseline and differential.
GenevisibleiQ9Z2U0. MM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
SMARTiView protein in SMART
SM00948. Proteasome_A_N. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPSA7_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2U0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: May 10, 2017
This is version 145 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.