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Q9Z2U0 (PSA7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-7

EC=3.4.25.1
Alternative name(s):
Proteasome subunit RC6-1
Gene names
Name:Psma7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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. Ref.5 Ref.7

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Detected in liver (at protein level). Ref.7

Induction

Up-regulated in liver tumor tissues. Ref.4

Post-translational modification

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

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Proteasome subunit alpha type-7
PRO_0000124143

Amino acid modifications

Modified residue1531Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue2271N6-acetyllysine By similarity
Glycosylation1301O-linked (GlcNAc) Ref.6

Secondary structure

............................................ 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Z2U0 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E2C8D607D8E2BC9C

FASTA24827,855
        10         20         30         40         50         60 
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKDI VVLGVEKKSV AKLQDERTVR 

        70         80         90        100        110        120 
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ 

       130        140        150        160        170        180 
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDDA 

       190        200        210        220        230        240 
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQPLKIL NPEEIEKYVA EIEKEKEENE 


KKKQKKAS 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure of mouse 20S proteasomes."
Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.
Immunogenetics 49:835-842(1999) [PubMed] [Europe PMC] [Abstract]
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]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019662 mRNA. Translation: AAC69150.1.
BC008222 mRNA. Translation: AAH08222.1.
CCDSCCDS17166.1.
RefSeqNP_036099.1. NM_011969.2.
UniGeneMm.21728.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9Z2U0.
SMRQ9Z2U0. Positions 2-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204995. 3 interactions.
IntActQ9Z2U0. 5 interactions.
MINTMINT-1856843.

Protein family/group databases

MEROPST01.979.

PTM databases

PhosphoSiteQ9Z2U0.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2U0.

Proteomic databases

MaxQBQ9Z2U0.
PaxDbQ9Z2U0.
PRIDEQ9Z2U0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029082; ENSMUSP00000029082; ENSMUSG00000027566.
GeneID26444.
KEGGmmu:26444.
UCSCuc008oib.1. mouse.

Organism-specific databases

CTD5688.
MGIMGI:1347070. Psma7.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074753.
HOGENOMHOG000091085.
HOVERGENHBG003005.
InParanoidQ9Z2U0.
KOK02731.
OMAITRHIAG.
OrthoDBEOG71VSTG.
PhylomeDBQ9Z2U0.
TreeFamTF106212.

Gene expression databases

ArrayExpressQ9Z2U0.
BgeeQ9Z2U0.
GenevestigatorQ9Z2U0.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304533.
PROQ9Z2U0.
SOURCESearch...

Entry information

Entry namePSA7_MOUSE
AccessionPrimary (citable) accession number: Q9Z2U0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot