Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit alpha type-4

Gene

PSMA4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_274004. degradation of DVL.
REACT_276477. ER-Phagosome pathway.
REACT_280521. Activation of NF-kappaB in B cells.
REACT_282220. Asymmetric localization of PCP proteins.
REACT_290505. SCF(Skp2)-mediated degradation of p27/p21.
REACT_291730. Separation of Sister Chromatids.
REACT_293325. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_295102. CDT1 association with the CDC6:ORC:origin complex.
REACT_297209. Degradation of beta-catenin by the destruction complex.
REACT_302851. CDK-mediated phosphorylation and removal of Cdc6.
REACT_304977. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_306095. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_307496. Hedgehog ligand biogenesis.
REACT_308391. Ubiquitin-dependent degradation of Cyclin D1.
REACT_311810. Hedgehog 'on' state.
REACT_314321. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_321728. Regulation of ornithine decarboxylase (ODC).
REACT_326365. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_328795. Orc1 removal from chromatin.
REACT_329551. degradation of AXIN.
REACT_329646. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_330101. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335347. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_338497. APC/C:Cdc20 mediated degradation of Securin.
REACT_350460. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_357698. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_358073. Degradation of GLI1 by the proteasome.
REACT_362031. CLEC7A (Dectin-1) signaling.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Gene namesi
Name:PSMA4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 21

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Proteasome subunit alpha type-4PRO_0000274032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei173 – 1731PhosphoserineBy similarity
Modified residuei176 – 1761N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ3ZCK9.

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

STRINGi9913.ENSBTAP00000019203.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Helixi19 – 2810Combined sources
Beta strandi34 – 385Combined sources
Beta strandi40 – 478Combined sources
Beta strandi63 – 675Combined sources
Beta strandi69 – 7810Combined sources
Helixi80 – 10122Combined sources
Helixi107 – 12014Combined sources
Turni121 – 1233Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi132 – 1409Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 1518Combined sources
Turni152 – 1543Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi160 – 1656Combined sources
Turni166 – 1694Combined sources
Helixi170 – 1789Combined sources
Helixi186 – 19914Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi212 – 2176Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi224 – 2274Combined sources
Helixi230 – 24112Combined sources
Turni245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75C/Q1-261[»]
ProteinModelPortaliQ3ZCK9.
SMRiQ3ZCK9. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3ZCK9.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ3ZCK9.
KOiK02728.
OMAiYQVEYAQ.
OrthoDBiEOG7F512J.
TreeFamiTF106209.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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.

Q3ZCK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR
60 70 80 90 100
NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ
110 120 130 140 150
YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAIKVLNKT
210 220 230 240 250
MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE
260
KKEKEQKEKD K
Length:261
Mass (Da):29,484
Last modified:September 27, 2005 - v1
Checksum:i7867422B1B31F3B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102102 mRNA. Translation: AAI02103.1.
RefSeqiNP_001029553.1. NM_001034381.2.
UniGeneiBt.49419.

Genome annotation databases

EnsembliENSBTAT00000019203; ENSBTAP00000019203; ENSBTAG00000014440.
GeneIDi510423.
KEGGibta:510423.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102102 mRNA. Translation: AAI02103.1.
RefSeqiNP_001029553.1. NM_001034381.2.
UniGeneiBt.49419.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75C/Q1-261[»]
ProteinModelPortaliQ3ZCK9.
SMRiQ3ZCK9. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019203.

Chemistry

BindingDBiQ3ZCK9.

Protein family/group databases

MEROPSiT01.973.

Proteomic databases

PRIDEiQ3ZCK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000019203; ENSBTAP00000019203; ENSBTAG00000014440.
GeneIDi510423.
KEGGibta:510423.

Organism-specific databases

CTDi5685.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ3ZCK9.
KOiK02728.
OMAiYQVEYAQ.
OrthoDBiEOG7F512J.
TreeFamiTF106209.

Enzyme and pathway databases

ReactomeiREACT_274004. degradation of DVL.
REACT_276477. ER-Phagosome pathway.
REACT_280521. Activation of NF-kappaB in B cells.
REACT_282220. Asymmetric localization of PCP proteins.
REACT_290505. SCF(Skp2)-mediated degradation of p27/p21.
REACT_291730. Separation of Sister Chromatids.
REACT_293325. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_295102. CDT1 association with the CDC6:ORC:origin complex.
REACT_297209. Degradation of beta-catenin by the destruction complex.
REACT_302851. CDK-mediated phosphorylation and removal of Cdc6.
REACT_304977. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_306095. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_307496. Hedgehog ligand biogenesis.
REACT_308391. Ubiquitin-dependent degradation of Cyclin D1.
REACT_311810. Hedgehog 'on' state.
REACT_314321. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_321728. Regulation of ornithine decarboxylase (ODC).
REACT_326365. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_328795. Orc1 removal from chromatin.
REACT_329551. degradation of AXIN.
REACT_329646. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_330101. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335347. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_338497. APC/C:Cdc20 mediated degradation of Securin.
REACT_350460. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_357698. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_358073. Degradation of GLI1 by the proteasome.
REACT_362031. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

EvolutionaryTraceiQ3ZCK9.
NextBioi20869437.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  2. "The structure of the mammalian 20S proteasome at 2.75 A resolution."
    Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
    Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S PROTEASOME.

Entry informationi

Entry nameiPSA4_BOVIN
AccessioniPrimary (citable) accession number: Q3ZCK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: September 27, 2005
Last modified: June 24, 2015
This is version 87 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, 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

External Data

Dasty 3

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 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.