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Q9R1P4

- PSA1_MOUSE

UniProt

Q9R1P4 - PSA1_MOUSE

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Protein

Proteasome subunit alpha type-1

Gene

Psma1

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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. lipopolysaccharide binding Source: UniProtKB
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. immune system process Source: UniProtKB-KW
  2. negative regulation of inflammatory response to antigenic stimulus Source: UniProtKB
  3. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Immunity

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_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.

Protein family/group databases

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu chain
Gene namesi
Name:Psma1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1347005. Psma1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-KW
  3. proteasome complex Source: MGI
  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 – 263263Proteasome subunit alpha type-1PRO_0000124062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Glycosylationi110 – 1101O-linked (GlcNAc)1 Publication
Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form.

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9R1P4.
PaxDbiQ9R1P4.
PRIDEiQ9R1P4.

2D gel databases

COMPLUYEAST-2DPAGEQ9R1P4.
REPRODUCTION-2DPAGEIPI00283862.
Q9R1P4.

PTM databases

PhosphoSiteiQ9R1P4.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues. Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and colon (at the protein level).2 Publications

Gene expression databases

BgeeiQ9R1P4.
ExpressionAtlasiQ9R1P4. baseline and differential.
GenevestigatoriQ9R1P4.

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. Interacts with bacterial lipopolysaccharide (LPS). Interacts with NOTCH3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NOTCH3Q9UM472EBI-991653,EBI-1236377From a different organism.

Protein-protein interaction databases

BioGridi204991. 5 interactions.
DIPiDIP-35147N.
IntActiQ9R1P4. 20 interactions.
MINTiMINT-1856889.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi20 – 3112Combined sources
Beta strandi35 – 395Combined sources
Beta strandi41 – 499Combined sources
Beta strandi53 – 575Combined sources
Beta strandi63 – 653Combined sources
Beta strandi67 – 7610Combined sources
Helixi78 – 9821Combined sources
Beta strandi99 – 1013Combined sources
Helixi105 – 11713Combined sources
Helixi118 – 1203Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi153 – 16311Combined sources
Helixi166 – 1749Combined sources
Turni176 – 1783Combined sources
Helixi179 – 1813Combined sources
Helixi184 – 19512Combined sources
Turni196 – 1983Combined sources
Turni207 – 2093Combined sources
Beta strandi210 – 21910Combined sources
Beta strandi222 – 2243Combined sources
Turni227 – 2293Combined sources
Helixi230 – 2334Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90E/S/g/u1-263[»]
3UNEX-ray3.20E/S/g/u1-263[»]
3UNFX-ray2.90E/S1-263[»]
3UNHX-ray3.20E/S1-263[»]
ProteinModelPortaliQ9R1P4.
SMRiQ9R1P4. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiQ9R1P4.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiQ9R1P4.
TreeFamiTF106206.

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.

Q9R1P4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK
60 70 80 90 100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD
110 120 130 140 150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS
160 170 180 190 200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLDELVKH GLRALRETLP
210 220 230 240 250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP QRKAQPSQAA
260
EEPAEKADEP MEH
Length:263
Mass (Da):29,547
Last modified:May 1, 2000 - v1
Checksum:iCC791C56AFBA8043
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060088 mRNA. Translation: AAD50533.1.
AJ272019 mRNA. Translation: CAB95966.1.
AJ272272 Genomic DNA. Translation: CAB95969.1.
BC005762 mRNA. Translation: AAH05762.1.
CCDSiCCDS40094.1.
RefSeqiNP_036095.1. NM_011965.2.
UniGeneiMm.121265.

Genome annotation databases

EnsembliENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751.
GeneIDi26440.
KEGGimmu:26440.
UCSCiuc009jhy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060088 mRNA. Translation: AAD50533.1 .
AJ272019 mRNA. Translation: CAB95966.1 .
AJ272272 Genomic DNA. Translation: CAB95969.1 .
BC005762 mRNA. Translation: AAH05762.1 .
CCDSi CCDS40094.1.
RefSeqi NP_036095.1. NM_011965.2.
UniGenei Mm.121265.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 E/S/g/u 1-263 [» ]
3UNE X-ray 3.20 E/S/g/u 1-263 [» ]
3UNF X-ray 2.90 E/S 1-263 [» ]
3UNH X-ray 3.20 E/S 1-263 [» ]
ProteinModelPortali Q9R1P4.
SMRi Q9R1P4. Positions 4-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204991. 5 interactions.
DIPi DIP-35147N.
IntActi Q9R1P4. 20 interactions.
MINTi MINT-1856889.

Protein family/group databases

MEROPSi T01.976.

PTM databases

PhosphoSitei Q9R1P4.

2D gel databases

COMPLUYEAST-2DPAGE Q9R1P4.
REPRODUCTION-2DPAGE IPI00283862.
Q9R1P4.

Proteomic databases

MaxQBi Q9R1P4.
PaxDbi Q9R1P4.
PRIDEi Q9R1P4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033008 ; ENSMUSP00000033008 ; ENSMUSG00000030751 .
GeneIDi 26440.
KEGGi mmu:26440.
UCSCi uc009jhy.1. mouse.

Organism-specific databases

CTDi 5682.
MGIi MGI:1347005. Psma1.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074855.
HOGENOMi HOG000091080.
HOVERGENi HBG105373.
InParanoidi Q9R1P4.
KOi K02725.
OMAi FMKQQCL.
OrthoDBi EOG7WQ7T1.
PhylomeDBi Q9R1P4.
TreeFami TF106206.

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_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.

Miscellaneous databases

NextBioi 304517.
PROi Q9R1P4.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1P4.
ExpressionAtlasi Q9R1P4. baseline and differential.
Genevestigatori Q9R1P4.

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.A.
  2. "The mouse Psma1 gene coding for the alpha-type C2 proteasome subunit: structural and functional analysis, mapping, and colocalization with Pde3b on mouse chromosome 7."
    Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J.
    Genomics 66:313-323(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Skeletal muscle.
  3. "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-3.
    Tissue: Mammary gland.
  4. Lubec G., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  5. "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events."
    Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N.
    J. Immunol. 171:1515-1525(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPS.
  6. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  7. "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.
  8. "Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
    Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
    Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DITHIOLETHIONE.
  9. "Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated Candida albicans cells unravel an anti-inflammatory response."
    Martinez-Solano L., Reales-Calderon J.A., Nombela C., Molero G., Gil C.
    Proteomics 9:2995-3010(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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-110.
    Tissue: Brain and Spleen.
  11. "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 nameiPSA1_MOUSE
AccessioniPrimary (citable) accession number: Q9R1P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 126 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