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Protein

Proteasome subunit alpha type-6

Gene

Psma6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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).2 Publications

Catalytic activityi

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

GO - Molecular functioni

  • NF-kappaB binding Source: MGI
  • RNA binding Source: BHF-UCL
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-382556. ABC-family proteins mediated transport.
R-MMU-446652. Interleukin-1 family signaling.
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-5689603. UCH proteinases.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-MMU-8939236. RUNX1 regulates transcription of genes involved in differentiation of HSCs.
R-MMU-8941858. Regulation of RUNX3 expression and activity.
R-MMU-8948751. Regulation of PTEN stability and activity.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-6 (EC:3.4.25.1By similarity)
Alternative name(s):
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain
Gene namesi
Name:Psma6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1347006. Psma6.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241311 – 246Proteasome subunit alpha type-6Add BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5O-linked (GlcNAc) serine1 Publication1
Modified residuei17PhosphoserineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Modified residuei64PhosphoserineBy similarity1
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei104N6-acetyllysineCombined sources1
Modified residuei159PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9QUM9.
MaxQBiQ9QUM9.
PaxDbiQ9QUM9.
PeptideAtlasiQ9QUM9.
PRIDEiQ9QUM9.
TopDownProteomicsiQ9QUM9.

2D gel databases

COMPLUYEAST-2DPAGEiQ9QUM9.
REPRODUCTION-2DPAGEiQ9QUM9.

PTM databases

iPTMnetiQ9QUM9.
PhosphoSitePlusiQ9QUM9.
SwissPalmiQ9QUM9.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000021024.
ExpressionAtlasiQ9QUM9. baseline and differential.
GenevisibleiQ9QUM9. MM.

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 (PubMed:16857966, PubMed:22341445). Interacts with ALKBH4 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204994. 2 interactors.
CORUMiQ9QUM9.
IntActiQ9QUM9. 7 interactors.
MINTiMINT-1856833.
STRINGi10090.ENSMUSP00000021412.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 12Combined sources3
Helixi23 – 32Combined sources10
Helixi33 – 35Combined sources3
Beta strandi38 – 43Combined sources6
Beta strandi45 – 53Combined sources9
Turni63 – 65Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi73 – 82Combined sources10
Helixi84 – 105Combined sources22
Helixi111 – 127Combined sources17
Beta strandi128 – 131Combined sources4
Beta strandi135 – 144Combined sources10
Turni145 – 147Combined sources3
Beta strandi148 – 154Combined sources7
Beta strandi156 – 158Combined sources3
Beta strandi160 – 169Combined sources10
Helixi172 – 184Combined sources13
Helixi191 – 206Combined sources16
Turni212 – 214Combined sources3
Beta strandi215 – 223Combined sources9
Helixi232 – 242Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90G/U/i/w1-246[»]
3UNEX-ray3.20G/U/i/w1-246[»]
3UNFX-ray2.90G/U1-246[»]
3UNHX-ray3.20G/U1-246[»]
ProteinModelPortaliQ9QUM9.
SMRiQ9QUM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0182. Eukaryota.
ENOG410XR7X. LUCA.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
HOVERGENiHBG107363.
InParanoidiQ9QUM9.
KOiK02730.
OMAiYGYEITP.
OrthoDBiEOG091G0GSR.
PhylomeDBiQ9QUM9.
TreeFamiTF106210.

Family and domain databases

CDDicd03754. proteasome_alpha_type_6. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
IPR034642. Proteasome_subunit_alpha6.
PANTHERiPTHR11599:SF98. PTHR11599:SF98. 1 hit.
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.

Q9QUM9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI
60 70 80 90 100
VTQKKVPDKL LDSSTVTHLF KITESIGCVM TGMTADSRSQ VQRARYEAAN
110 120 130 140 150
WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ
160 170 180 190 200
VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT
210 220 230 240
CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD
Length:246
Mass (Da):27,372
Last modified:May 1, 2000 - v1
Checksum:i6DF57BE87FA48D32
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133P → T in BAE36518 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60288 mRNA. Translation: AAF21459.1.
AF060087 mRNA. Translation: AAD50532.1.
AK088143 mRNA. Translation: BAC40169.1.
AK152915 mRNA. Translation: BAE31592.1.
AK161662 mRNA. Translation: BAE36518.1.
BC086685 mRNA. Translation: AAH86685.1.
CCDSiCCDS25917.1.
RefSeqiNP_036098.1. NM_011968.3.
UniGeneiMm.30210.

Genome annotation databases

EnsembliENSMUST00000021412; ENSMUSP00000021412; ENSMUSG00000021024.
GeneIDi26443.
KEGGimmu:26443.
UCSCiuc007noq.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiPSA6_MOUSE
AccessioniPrimary (citable) accession number: Q9QUM9
Secondary accession number(s): Q0VGS3, Q3TT07, Q3U6Y2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: September 27, 2017
This is version 153 of the entry and version 1 of the sequence. See 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