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Protein

Proteasome subunit alpha type-2

Gene

PSMA2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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).By similarity

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-BTA-1169091. Activation of NF-kappaB in B cells.
R-BTA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-BTA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-BTA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-BTA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-BTA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-BTA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-BTA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-BTA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-BTA-195253. Degradation of beta-catenin by the destruction complex.
R-BTA-202424. Downstream TCR signaling.
R-BTA-2467813. Separation of Sister Chromatids.
R-BTA-2871837. FCERI mediated NF-kB activation.
R-BTA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-BTA-350562. Regulation of ornithine decarboxylase (ODC).
R-BTA-382556. ABC-family proteins mediated transport.
R-BTA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-BTA-4608870. Asymmetric localization of PCP proteins.
R-BTA-4641257. Degradation of AXIN.
R-BTA-4641258. Degradation of DVL.
R-BTA-5358346. Hedgehog ligand biogenesis.
R-BTA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-BTA-5607764. CLEC7A (Dectin-1) signaling.
R-BTA-5610780. Degradation of GLI1 by the proteasome.
R-BTA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-BTA-5632684. Hedgehog 'on' state.
R-BTA-5658442. Regulation of RAS by GAPs.
R-BTA-5668541. TNFR2 non-canonical NF-kB pathway.
R-BTA-5676590. NIK-->noncanonical NF-kB signaling.
R-BTA-5687128. MAPK6/MAPK4 signaling.
R-BTA-5689603. UCH proteinases.
R-BTA-5689880. Ub-specific processing proteases.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-BTA-68949. Orc1 removal from chromatin.
R-BTA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-BTA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-BTA-69481. G2/M Checkpoints.
R-BTA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-BTA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-BTA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-BTA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1By similarity)
Gene namesi
Name:PSMA2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 4

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002398652 – 234Proteasome subunit alpha type-2Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei6PhosphotyrosineBy similarity1
Modified residuei7PhosphoserineBy similarity1
Modified residuei14PhosphoserineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei24PhosphotyrosineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei76PhosphotyrosineBy similarity1
Modified residuei171N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylated on tyrosine residues; which may be important for nuclear import.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3T0Y5.
PeptideAtlasiQ3T0Y5.
PRIDEiQ3T0Y5.

Expressioni

Gene expression databases

BgeeiENSBTAG00000000990.

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 PSMB7.1 Publication

Protein-protein interaction databases

BioGridi195708. 3 interactors.
STRINGi9913.ENSBTAP00000001309.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi20 – 30Combined sources11
Beta strandi35 – 39Combined sources5
Beta strandi44 – 49Combined sources6
Beta strandi55 – 57Combined sources3
Beta strandi64 – 78Combined sources15
Helixi80 – 101Combined sources22
Helixi107 – 120Combined sources14
Turni121 – 123Combined sources3
Beta strandi131 – 139Combined sources9
Beta strandi141 – 149Combined sources9
Beta strandi155 – 164Combined sources10
Helixi167 – 177Combined sources11
Helixi184 – 196Combined sources13
Beta strandi205 – 214Combined sources10
Beta strandi217 – 220Combined sources4
Helixi223 – 230Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75B/P2-234[»]
ProteinModelPortaliQ3T0Y5.
SMRiQ3T0Y5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T0Y5.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ3T0Y5.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
TreeFamiTF106207.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
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.

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

Q3T0Y5-1 [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 LTPTEVKDYL AAIA
Length:234
Mass (Da):25,899
Last modified:January 23, 2007 - v3
Checksum:i63CB56A233583836
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102206 mRNA. Translation: AAI02207.1.
RefSeqiNP_001029834.1. NM_001034662.2.
UniGeneiBt.49020.

Genome annotation databases

EnsembliENSBTAT00000001309; ENSBTAP00000001309; ENSBTAG00000000990.
GeneIDi539141.
KEGGibta:539141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102206 mRNA. Translation: AAI02207.1.
RefSeqiNP_001029834.1. NM_001034662.2.
UniGeneiBt.49020.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75B/P2-234[»]
ProteinModelPortaliQ3T0Y5.
SMRiQ3T0Y5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi195708. 3 interactors.
STRINGi9913.ENSBTAP00000001309.

Protein family/group databases

MEROPSiT01.972.

Proteomic databases

PaxDbiQ3T0Y5.
PeptideAtlasiQ3T0Y5.
PRIDEiQ3T0Y5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000001309; ENSBTAP00000001309; ENSBTAG00000000990.
GeneIDi539141.
KEGGibta:539141.

Organism-specific databases

CTDi5683.

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ3T0Y5.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
TreeFamiTF106207.

Enzyme and pathway databases

ReactomeiR-BTA-1169091. Activation of NF-kappaB in B cells.
R-BTA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-BTA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-BTA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-BTA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-BTA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-BTA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-BTA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-BTA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-BTA-195253. Degradation of beta-catenin by the destruction complex.
R-BTA-202424. Downstream TCR signaling.
R-BTA-2467813. Separation of Sister Chromatids.
R-BTA-2871837. FCERI mediated NF-kB activation.
R-BTA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-BTA-350562. Regulation of ornithine decarboxylase (ODC).
R-BTA-382556. ABC-family proteins mediated transport.
R-BTA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-BTA-4608870. Asymmetric localization of PCP proteins.
R-BTA-4641257. Degradation of AXIN.
R-BTA-4641258. Degradation of DVL.
R-BTA-5358346. Hedgehog ligand biogenesis.
R-BTA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-BTA-5607764. CLEC7A (Dectin-1) signaling.
R-BTA-5610780. Degradation of GLI1 by the proteasome.
R-BTA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-BTA-5632684. Hedgehog 'on' state.
R-BTA-5658442. Regulation of RAS by GAPs.
R-BTA-5668541. TNFR2 non-canonical NF-kB pathway.
R-BTA-5676590. NIK-->noncanonical NF-kB signaling.
R-BTA-5687128. MAPK6/MAPK4 signaling.
R-BTA-5689603. UCH proteinases.
R-BTA-5689880. Ub-specific processing proteases.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-BTA-68949. Orc1 removal from chromatin.
R-BTA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-BTA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-BTA-69481. G2/M Checkpoints.
R-BTA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-BTA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-BTA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-BTA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ3T0Y5.

Gene expression databases

BgeeiENSBTAG00000000990.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
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 nameiPSA2_BOVIN
AccessioniPrimary (citable) accession number: Q3T0Y5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: March 15, 2017
This is version 99 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.