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Protein

Proteasome subunit alpha type-3

Gene

PSMA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.2 Publications

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

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS02111-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP25788.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Gene namesi
Name:PSMA3
Synonyms:HC8, PSC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9532. PSMA3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: BHF-UCL
  • proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5684.
OpenTargetsiENSG00000100567.
PharmGKBiPA33877.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMA3.
DMDMi130859.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001240912 – 255Proteasome subunit alpha type-3Add BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei57N6-acetyllysineCombined sources1
Modified residuei206N6-acetyllysineCombined sources1
Modified residuei230N6-acetyllysineCombined sources1
Modified residuei243PhosphoserineCombined sources1
Modified residuei250PhosphoserineCombined sources1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP25788.
MaxQBiP25788.
PaxDbiP25788.
PeptideAtlasiP25788.
PRIDEiP25788.

2D gel databases

OGPiP25788.
REPRODUCTION-2DPAGEIPI00171199.

PTM databases

iPTMnetiP25788.
PhosphoSitePlusiP25788.
SwissPalmiP25788.

Expressioni

Inductioni

Down-regulated by antioxidants BO-653 and probucol. Up-regulated by bacterial lipopolysaccharides (LPS) and TNF.3 Publications

Gene expression databases

BgeeiENSG00000100567.
CleanExiHS_PSMA3.
ExpressionAtlasiP25788. baseline and differential.
GenevisibleiP25788. HS.

Organism-specific databases

HPAiHPA000905.

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 AURKB. Interacts with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B2R5503EBI-348380,EBI-10175488
Q5JPT63EBI-348380,EBI-10244213
Q5W1503EBI-348380,EBI-10248148
Q7KZQ13EBI-348380,EBI-10255941
Q9H8E53EBI-348380,EBI-10309031
Q9HAA03EBI-348380,EBI-10309885
Q9NWL93EBI-348380,EBI-10315054
ATP6V0CP274493EBI-348380,EBI-721179
BTN2A2Q8WVV53EBI-348380,EBI-8648738
C14orf159Q7Z3D63EBI-348380,EBI-2807872
C1orf105O955613EBI-348380,EBI-10191951
C1QTNF9B-AS1Q58A443EBI-348380,EBI-10243387
C4orf42Q96CW73EBI-348380,EBI-752053
C9orf106A2RU003EBI-348380,EBI-10173129
CCL28Q9NRJ33EBI-348380,EBI-7783254
CRB3Q9BUF73EBI-348380,EBI-9844372
CST2P092283EBI-348380,EBI-8832659
CTAGE5O153203EBI-348380,EBI-1050253
DMC1Q145653EBI-348380,EBI-930865
DMRT3Q9NQL93EBI-348380,EBI-9679045
FAM103A1Q9BTL33EBI-348380,EBI-744023
FAM171A2Q8N0U13EBI-348380,EBI-10264767
FAM218AQ96MZ43EBI-348380,EBI-10291578
FBXL18Q96D163EBI-348380,EBI-744419
FBXO7Q9Y3I13EBI-348380,EBI-1161222
GATA2P237693EBI-348380,EBI-2806671
GATA3P237713EBI-348380,EBI-6664760
GORASP2Q9H8Y83EBI-348380,EBI-739467
hCG_1998195Q8N7793EBI-348380,EBI-10267476
hCG_2003792A0A024R5S03EBI-348380,EBI-10188461
IQCEQ6IPM23EBI-348380,EBI-3893098
KIRREL2Q6UWL63EBI-348380,EBI-10254473
KIRREL3-AS3Q8N7Y13EBI-348380,EBI-10267656
KRTAP19-5Q3LI723EBI-348380,EBI-1048945
KRTAP26-1Q6PEX33EBI-348380,EBI-3957672
KRTAP8-1Q8IUC23EBI-348380,EBI-10261141
LASP1Q148473EBI-348380,EBI-742828
LETM1O952023EBI-348380,EBI-1052895
MDM2Q009872EBI-348380,EBI-389668
MUM1Q9H6H23EBI-348380,EBI-10307610
NPBWR2P481463EBI-348380,EBI-10210114
NPPBP168603EBI-348380,EBI-747044
OSR2Q8N2R03EBI-348380,EBI-5660512
PATL1Q86TB93EBI-348380,EBI-2562092
PMLP295902EBI-348380,EBI-295890
PRR10Q14CW73EBI-348380,EBI-10234793
PRR13Q9NZ813EBI-348380,EBI-740924
PRR3P795223EBI-348380,EBI-2803328
PSMA1P257866EBI-348380,EBI-359352
PSMA4P257894EBI-348380,EBI-359310
PSMA6P609009EBI-348380,EBI-357793
PSMA7O148186EBI-348380,EBI-603272
PSMB4P280703EBI-348380,EBI-603350
PTPN23Q9H3S73EBI-348380,EBI-724478
PWWP2BQ6NUJ53EBI-348380,EBI-10251192
RAB3IL1Q8TBN03EBI-348380,EBI-743796
RAD54L2Q9Y4B43EBI-348380,EBI-948156
RBFOX2O432513EBI-348380,EBI-746056
RBM42Q9BTD83EBI-348380,EBI-746862
RTP5Q14D333EBI-348380,EBI-10217913
RUSC1-AS1Q66K803EBI-348380,EBI-10248967
SF1Q156373EBI-348380,EBI-744603
SLAIN1Q8ND833EBI-348380,EBI-10269374
SLC22A23Q7L9D03EBI-348380,EBI-10256583
SNRPBP14678-23EBI-348380,EBI-372475
SNRPCQ5TAL43EBI-348380,EBI-10246938
SPATA8Q6RVD63EBI-348380,EBI-8635958
STX4Q128463EBI-348380,EBI-744942
STX6O437523EBI-348380,EBI-2695795
URB1-AS1Q96HZ73EBI-348380,EBI-10288943
VPS37CA5D8V63EBI-348380,EBI-2559305
ZNF366Q8N8953EBI-348380,EBI-2813661
ZNF385CQ66K413EBI-348380,EBI-10219231

Protein-protein interaction databases

BioGridi111657. 286 interactors.
DIPiDIP-29366N.
IntActiP25788. 119 interactors.
MINTiMINT-1035201.
STRINGi9606.ENSP00000216455.

Chemistry databases

BindingDBiP25788.

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 32Combined sources11
Beta strandi37 – 42Combined sources6
Beta strandi45 – 53Combined sources9
Turni61 – 64Combined sources4
Beta strandi67 – 71Combined sources5
Beta strandi74 – 80Combined sources7
Helixi82 – 103Combined sources22
Helixi109 – 122Combined sources14
Beta strandi124 – 129Combined sources6
Beta strandi133 – 142Combined sources10
Turni143 – 145Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi158 – 167Combined sources10
Helixi170 – 177Combined sources8
Helixi182 – 184Combined sources3
Helixi187 – 201Combined sources15
Turni204 – 206Combined sources3
Beta strandi210 – 218Combined sources9
Helixi219 – 221Combined sources3
Beta strandi225 – 227Combined sources3
Helixi230 – 244Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
5A0Qelectron microscopy3.50G/U1-255[»]
5DSVX-ray3.75A/B/C/D/E/F/G/H/I/J/K/L/M/N1-255[»]
5GJQelectron microscopy4.50X/n1-255[»]
5GJRelectron microscopy3.50X/n1-255[»]
5L4Gelectron microscopy4.02G/T1-255[»]
5LE5X-ray1.80F/T1-255[»]
5LEXX-ray2.20F/T1-255[»]
5LEYX-ray1.90F/T1-255[»]
5LEZX-ray2.19F/T1-255[»]
5LF0X-ray2.41F/T1-255[»]
5LF1X-ray2.00F/T1-255[»]
5LF3X-ray2.10F/T1-255[»]
5LF4X-ray1.99F/T1-255[»]
5LF6X-ray2.07F/T1-255[»]
5LF7X-ray2.00F/T1-255[»]
5T0Celectron microscopy3.80AM/BM2-255[»]
5T0Gelectron microscopy4.40M2-255[»]
5T0Helectron microscopy6.80M2-255[»]
5T0Ielectron microscopy8.00M2-255[»]
5T0Jelectron microscopy8.00M2-255[»]
ProteinModelPortaliP25788.
SMRiP25788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0184. Eukaryota.
ENOG410XP01. LUCA.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiP25788.
KOiK02727.
OMAiMVDPSGI.
OrthoDBiEOG091G0GQL.
PhylomeDBiP25788.
TreeFamiTF106208.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25788-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV
60 70 80 90 100
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR
110 120 130 140 150
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY
160 170 180 190 200
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI
210 220 230 240 250
VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES

DDDNM
Length:255
Mass (Da):28,433
Last modified:January 23, 2007 - v2
Checksum:iA1854ED3C0650FB1
GO
Isoform 2 (identifier: P25788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-142: Missing.

Show »
Length:248
Mass (Da):27,647
Checksum:iE1C4F1C97EC83DAD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91I → M in AAH29402 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075259233Missing Found in a patient with Nakajo syndrome who also carries a mutation in PSMB8; unknown pathological significance; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005280136 – 142Missing in isoform 2. 2 Publications7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00762 mRNA. Translation: BAA00659.1.
BT006711 mRNA. Translation: AAP35357.1.
BT019715 mRNA. Translation: AAV38520.1.
AK315158 mRNA. Translation: BAG37603.1.
CH471061 Genomic DNA. Translation: EAW80719.1.
BC005265 mRNA. Translation: AAH05265.1.
BC029402 mRNA. Translation: AAH29402.1.
BC038990 mRNA. Translation: AAH38990.1.
CCDSiCCDS45113.1. [P25788-2]
CCDS9731.1. [P25788-1]
PIRiS15971. SNHUC8.
RefSeqiNP_002779.1. NM_002788.3. [P25788-1]
NP_687033.1. NM_152132.2. [P25788-2]
UniGeneiHs.558799.

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567. [P25788-1]
ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneIDi5684.
KEGGihsa:5684.
UCSCiuc001xdj.3. human. [P25788-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00762 mRNA. Translation: BAA00659.1.
BT006711 mRNA. Translation: AAP35357.1.
BT019715 mRNA. Translation: AAV38520.1.
AK315158 mRNA. Translation: BAG37603.1.
CH471061 Genomic DNA. Translation: EAW80719.1.
BC005265 mRNA. Translation: AAH05265.1.
BC029402 mRNA. Translation: AAH29402.1.
BC038990 mRNA. Translation: AAH38990.1.
CCDSiCCDS45113.1. [P25788-2]
CCDS9731.1. [P25788-1]
PIRiS15971. SNHUC8.
RefSeqiNP_002779.1. NM_002788.3. [P25788-1]
NP_687033.1. NM_152132.2. [P25788-2]
UniGeneiHs.558799.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
5A0Qelectron microscopy3.50G/U1-255[»]
5DSVX-ray3.75A/B/C/D/E/F/G/H/I/J/K/L/M/N1-255[»]
5GJQelectron microscopy4.50X/n1-255[»]
5GJRelectron microscopy3.50X/n1-255[»]
5L4Gelectron microscopy4.02G/T1-255[»]
5LE5X-ray1.80F/T1-255[»]
5LEXX-ray2.20F/T1-255[»]
5LEYX-ray1.90F/T1-255[»]
5LEZX-ray2.19F/T1-255[»]
5LF0X-ray2.41F/T1-255[»]
5LF1X-ray2.00F/T1-255[»]
5LF3X-ray2.10F/T1-255[»]
5LF4X-ray1.99F/T1-255[»]
5LF6X-ray2.07F/T1-255[»]
5LF7X-ray2.00F/T1-255[»]
5T0Celectron microscopy3.80AM/BM2-255[»]
5T0Gelectron microscopy4.40M2-255[»]
5T0Helectron microscopy6.80M2-255[»]
5T0Ielectron microscopy8.00M2-255[»]
5T0Jelectron microscopy8.00M2-255[»]
ProteinModelPortaliP25788.
SMRiP25788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111657. 286 interactors.
DIPiDIP-29366N.
IntActiP25788. 119 interactors.
MINTiMINT-1035201.
STRINGi9606.ENSP00000216455.

Chemistry databases

BindingDBiP25788.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.977.

PTM databases

iPTMnetiP25788.
PhosphoSitePlusiP25788.
SwissPalmiP25788.

Polymorphism and mutation databases

BioMutaiPSMA3.
DMDMi130859.

2D gel databases

OGPiP25788.
REPRODUCTION-2DPAGEIPI00171199.

Proteomic databases

EPDiP25788.
MaxQBiP25788.
PaxDbiP25788.
PeptideAtlasiP25788.
PRIDEiP25788.

Protocols and materials databases

DNASUi5684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567. [P25788-1]
ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneIDi5684.
KEGGihsa:5684.
UCSCiuc001xdj.3. human. [P25788-1]

Organism-specific databases

CTDi5684.
DisGeNETi5684.
GeneCardsiPSMA3.
H-InvDBHIX0155215.
HGNCiHGNC:9532. PSMA3.
HPAiHPA000905.
MIMi176843. gene.
176845. gene.
neXtProtiNX_P25788.
OpenTargetsiENSG00000100567.
PharmGKBiPA33877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0184. Eukaryota.
ENOG410XP01. LUCA.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiP25788.
KOiK02727.
OMAiMVDPSGI.
OrthoDBiEOG091G0GQL.
PhylomeDBiP25788.
TreeFamiTF106208.

Enzyme and pathway databases

BioCyciZFISH:HS02111-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP25788.

Miscellaneous databases

GeneWikiiPSMA3.
GenomeRNAii5684.
PROiP25788.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100567.
CleanExiHS_PSMA3.
ExpressionAtlasiP25788. baseline and differential.
GenevisibleiP25788. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPSA3_HUMAN
AccessioniPrimary (citable) accession number: P25788
Secondary accession number(s): B2RCK6
, Q86U83, Q8N1D8, Q9BS70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 194 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. 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.