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Q9Z2U0

- PSA7_MOUSE

UniProt

Q9Z2U0 - PSA7_MOUSE

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Protein

Proteasome subunit alpha type-7

Gene

Psma7

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions (By similarity). The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions (By similarity). Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Protein family/group databases

MEROPSiT01.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7 (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit RC6-1
Gene namesi
Name:Psma7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1347070. Psma7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
  5. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Proteasome subunit alpha type-7PRO_0000124143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi130 – 1301O-linked (GlcNAc)1 Publication
Modified residuei153 – 1531Phosphotyrosine; by ABL1 and ABL2By similarity
Modified residuei227 – 2271N6-acetyllysineBy similarity

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

MaxQBiQ9Z2U0.
PaxDbiQ9Z2U0.
PRIDEiQ9Z2U0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U0.

PTM databases

PhosphoSiteiQ9Z2U0.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues.1 Publication

Gene expression databases

BgeeiQ9Z2U0.
ExpressionAtlasiQ9Z2U0. baseline and differential.
GenevestigatoriQ9Z2U0.

Interactioni

Subunit structurei

PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Interacts with HIF1A (By similarity). Interacts with RAB7A (By similarity). Interacts with PARK2 (By similarity). Interacts with EMAP2 (By similarity). Interacts with MAVS (By similarity). 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.By similarity2 Publications

Protein-protein interaction databases

BioGridi204995. 3 interactions.
IntActiQ9Z2U0. 5 interactions.
MINTiMINT-1856843.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2711Combined sources
Beta strandi32 – 365Combined sources
Beta strandi38 – 458Combined sources
Beta strandi52 – 543Combined sources
Turni56 – 594Combined sources
Beta strandi62 – 643Combined sources
Beta strandi66 – 7510Combined sources
Helixi77 – 9721Combined sources
Beta strandi98 – 1003Combined sources
Helixi104 – 11714Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi129 – 1368Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi153 – 16210Combined sources
Helixi165 – 17511Combined sources
Turni178 – 1814Combined sources
Helixi184 – 19512Combined sources
Turni196 – 1983Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi207 – 2159Combined sources
Beta strandi217 – 2193Combined sources
Helixi222 – 23615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ9Z2U0.
KOiK02731.
OMAiITRHIAG.
OrthoDBiEOG71VSTG.
PhylomeDBiQ9Z2U0.
TreeFamiTF106212.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
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.

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.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019662 mRNA. Translation: AAC69150.1 .
BC008222 mRNA. Translation: AAH08222.1 .
CCDSi CCDS17166.1.
RefSeqi NP_036099.1. NM_011969.2.
UniGenei Mm.21728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 C/Q/e/s 1-248 [» ]
3UNE X-ray 3.20 C/Q/e/s 1-248 [» ]
3UNF X-ray 2.90 C/Q 1-248 [» ]
3UNH X-ray 3.20 C/Q 1-248 [» ]
ProteinModelPortali Q9Z2U0.
SMRi Q9Z2U0. Positions 2-239.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204995. 3 interactions.
IntActi Q9Z2U0. 5 interactions.
MINTi MINT-1856843.

Protein family/group databases

MEROPSi T01.979.

PTM databases

PhosphoSitei Q9Z2U0.

2D gel databases

REPRODUCTION-2DPAGE Q9Z2U0.

Proteomic databases

MaxQBi Q9Z2U0.
PaxDbi Q9Z2U0.
PRIDEi Q9Z2U0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029082 ; ENSMUSP00000029082 ; ENSMUSG00000027566 .
GeneIDi 26444.
KEGGi mmu:26444.
UCSCi uc008oib.1. mouse.

Organism-specific databases

CTDi 5688.
MGIi MGI:1347070. Psma7.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074753.
HOGENOMi HOG000091085.
HOVERGENi HBG003005.
InParanoidi Q9Z2U0.
KOi K02731.
OMAi ITRHIAG.
OrthoDBi EOG71VSTG.
PhylomeDBi Q9Z2U0.
TreeFami TF106212.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Miscellaneous databases

NextBioi 304533.
PROi Q9Z2U0.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z2U0.
ExpressionAtlasi Q9Z2U0. baseline and differential.
Genevestigatori Q9Z2U0.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.BR.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 96-109.
    Tissue: Brain.
  4. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
    Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
    Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  6. "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag."
    Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K.
    Mol. Cell. Proteomics 11:467-477(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-130.
    Tissue: Brain and Spleen.
  7. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSA7_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 121 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

External Data

Dasty 3