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P17220

- PSA2_RAT

UniProt

P17220 - PSA2_RAT

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Protein

Proteasome subunit alpha type-2

Gene

Psma2

Organism
Rattus norvegicus (Rat)
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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.

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. response to virus Source: Ensembl
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Proteasome component C3
Gene namesi
Name:Psma2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 17

Organism-specific databases

RGDi61842. Psma2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. CytoplasmP-body By similarity
Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB
  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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211Y → F: Abolishes nuclear localization and phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 234233Proteasome subunit alpha type-2PRO_0000124079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei76 – 761PhosphotyrosineBy similarity
Modified residuei121 – 1211Phosphotyrosine1 Publication
Modified residuei171 – 1711N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues; which may be important for nuclear import.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP17220.

2D gel databases

World-2DPAGE0004:P17220.

PTM databases

PhosphoSiteiP17220.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

GenevestigatoriP17220.

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.

Protein-protein interaction databases

BioGridi248290. 5 interactions.
IntActiP17220. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP17220.
SMRiP17220. Positions 2-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074870.
HOVERGENiHBG003005.
InParanoidiP17220.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG71VSTG.
PhylomeDBiP17220.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17220-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK
60 70 80 90 100
KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV
110 120 130 140 150
YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD
160 170 180 190 200
PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE
210 220 230
GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA
Length:234
Mass (Da):25,927
Last modified:January 23, 2007 - v3
Checksum:i4ECB56A233583821
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02897 mRNA. Translation: AAA40838.1.
PIRiA34535. SNRTC3.
RefSeqiNP_058975.1. NM_017279.1.
UniGeneiRn.1617.

Genome annotation databases

EnsembliENSRNOT00000073834; ENSRNOP00000066950; ENSRNOG00000049920.
GeneIDi29669.
KEGGirno:29669.
UCSCiRGD:61842. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02897 mRNA. Translation: AAA40838.1 .
PIRi A34535. SNRTC3.
RefSeqi NP_058975.1. NM_017279.1.
UniGenei Rn.1617.

3D structure databases

ProteinModelPortali P17220.
SMRi P17220. Positions 2-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248290. 5 interactions.
IntActi P17220. 1 interaction.

Protein family/group databases

MEROPSi T01.972.

PTM databases

PhosphoSitei P17220.

2D gel databases

World-2DPAGE 0004:P17220.

Proteomic databases

PRIDEi P17220.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000073834 ; ENSRNOP00000066950 ; ENSRNOG00000049920 .
GeneIDi 29669.
KEGGi rno:29669.
UCSCi RGD:61842. rat.

Organism-specific databases

CTDi 5683.
RGDi 61842. Psma2.

Phylogenomic databases

GeneTreei ENSGT00550000074870.
HOVERGENi HBG003005.
InParanoidi P17220.
KOi K02726.
OMAi WKATALG.
OrthoDBi EOG71VSTG.
PhylomeDBi P17220.

Miscellaneous databases

NextBioi 609987.
PROi P17220.

Gene expression databases

Genevestigatori P17220.

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

  1. "Molecular cloning of cDNA for proteasomes from rat liver: primary structure of component C3 with a possible tyrosine phosphorylation site."
    Tanaka K., Fujiwara T., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.
    Biochemistry 29:3777-3785(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  2. "The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."
    Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y.
    FEBS Lett. 263:373-375(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    Tissue: Liver.
  3. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-39 AND 71-84, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  4. "Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes."
    Benedict C.M., Clawson G.A.
    Biochemistry 35:11612-11621(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, PHOSPHORYLATION AT TYR-121.

Entry informationi

Entry nameiPSA2_RAT
AccessioniPrimary (citable) accession number: P17220
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3