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Protein

Proteasome subunit alpha type-3

Gene

PSMA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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). 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 2.5 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • endopeptidase activity Source: GO_Central
  • threonine-type endopeptidase activity Source: UniProtKB-KW
  • ubiquitin protein ligase binding Source: ARUK-UCL

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP25788

Protein family/group databases

MEROPSiT01.977
MoonDBiP25788 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.11 Publication)
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

EuPathDBiHostDB:ENSG00000100567.12
HGNCiHGNC:9532 PSMA3
MIMi176843 gene
176845 gene
neXtProtiNX_P25788

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi5684
OpenTargetsiENSG00000100567
PharmGKBiPA33877

Chemistry databases

ChEMBLiCHEMBL3831201

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
ProteomicsDBi54290
54291 [P25788-2]

2D gel databases

OGPiP25788
REPRODUCTION-2DPAGEiIPI00171199

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 Expressed in 232 organ(s), highest expression level in adenohypophysis
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 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. Interacts with AURKB. Interacts with CDKN1A (PubMed:11350925). Interacts with MDM2 and RB1 (PubMed:16337594). Interacts with the C-terminus of TBXA2R isoform 2 (PubMed:17499743). Interacts with DNAJB2 (PubMed:15936278).11 Publications
(Microbial infection) Interacts with HIV-1 Tat protein.1 Publication
(Microbial infection) Interacts with hepatitis C virus (HCV) F protein.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus EBNA3 proteins.1 Publication

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
C1orf105O955613EBI-348380,EBI-10191951
C4orf42Q96CW73EBI-348380,EBI-752053
C9orf106A2RU003EBI-348380,EBI-10173129
CCL28Q9NRJ33EBI-348380,EBI-7783254
CRB3Q9BUF73EBI-348380,EBI-9844372
CST2P092283EBI-348380,EBI-8832659
CTAGE5O153203EBI-348380,EBI-1050253
DGLUCYQ7Z3D63EBI-348380,EBI-2807872
DMC1Q145656EBI-348380,EBI-930865
DMRT3Q9NQL93EBI-348380,EBI-9679045
FAM171A2Q8N0U13EBI-348380,EBI-10264767
FAM218AQ96MZ43EBI-348380,EBI-10291578
FBXL18Q96D163EBI-348380,EBI-744419
FBXO7Q9Y3I16EBI-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
PCOTHQ58A443EBI-348380,EBI-10243387
PMLP295902EBI-348380,EBI-295890
PRR10Q14CW73EBI-348380,EBI-10234793
PRR13Q9NZ813EBI-348380,EBI-740924
PRR3P795223EBI-348380,EBI-2803328
PSMA1P2578613EBI-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
RAMMETQ9BTL33EBI-348380,EBI-744023
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
ZNF385CQ66K414EBI-348380,EBI-8651919
ZNF688A0A0S2Z5X43EBI-348380,EBI-16429014

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111657, 290 interactors
CORUMiP25788
DIPiDIP-29366N
IntActiP25788, 121 interactors
MINTiP25788
STRINGi9606.ENSP00000216455

Chemistry databases

BindingDBiP25788

Structurei

Secondary structure

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiIIYLVHD
OrthoDBiEOG091G0GQL
PhylomeDBiP25788
TreeFamiTF106208

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 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

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

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V4X5G3V4X5_HUMAN
Proteasome endopeptidase complex
PSMA3
180Annotation score:
G3V5N4G3V5N4_HUMAN
Proteasome subunit alpha type-3
PSMA3
54Annotation score:
G3V3W4G3V3W4_HUMAN
Proteasome subunit alpha type-3
PSMA3
36Annotation score:
H0YJ03H0YJ03_HUMAN
Proteasome subunit alpha type-3
PSMA3
83Annotation score:

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

Similar proteinsi

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[»]
5LN3electron microscopy6.80G1-255[»]
5M32electron microscopy3.80F/T1-255[»]
5T0Celectron microscopy3.80AM/BM2-255[»]
5T0Gelectron microscopy4.40M2-255[»]
5T0Helectron microscopy6.80M2-255[»]
5T0Ielectron microscopy8.00M2-255[»]
5T0Jelectron microscopy8.00M2-255[»]
5VFOelectron microscopy3.50M/m2-246[»]
5VFPelectron microscopy4.20M/m2-246[»]
5VFQelectron microscopy4.20M/m2-246[»]
5VFRelectron microscopy4.90M/m2-246[»]
5VFSelectron microscopy3.60M/m2-246[»]
5VFTelectron microscopy7.00M/m2-246[»]
5VFUelectron microscopy5.80M/m2-246[»]
6AVOelectron microscopy3.80J/Q1-255[»]
ProteinModelPortaliP25788
SMRiP25788
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111657, 290 interactors
CORUMiP25788
DIPiDIP-29366N
IntActiP25788, 121 interactors
MINTiP25788
STRINGi9606.ENSP00000216455

Chemistry databases

BindingDBiP25788
ChEMBLiCHEMBL3831201

Protein family/group databases

MEROPSiT01.977
MoonDBiP25788 Predicted

PTM databases

iPTMnetiP25788
PhosphoSitePlusiP25788
SwissPalmiP25788

Polymorphism and mutation databases

BioMutaiPSMA3
DMDMi130859

2D gel databases

OGPiP25788
REPRODUCTION-2DPAGEiIPI00171199

Proteomic databases

EPDiP25788
MaxQBiP25788
PaxDbiP25788
PeptideAtlasiP25788
PRIDEiP25788
ProteomicsDBi54290
54291 [P25788-2]

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
EuPathDBiHostDB:ENSG00000100567.12
GeneCardsiPSMA3
H-InvDBiHIX0155215
HGNCiHGNC:9532 PSMA3
HPAiHPA000905
MIMi176843 gene
176845 gene
neXtProtiNX_P25788
OpenTargetsiENSG00000100567
PharmGKBiPA33877
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP25788

Miscellaneous databases

GeneWikiiPSMA3
GenomeRNAii5684
PROiPR:P25788
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100567 Expressed in 232 organ(s), highest expression level in adenohypophysis
CleanExiHS_PSMA3
ExpressionAtlasiP25788 baseline and differential
GenevisibleiP25788 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 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
ProtoNetiSearch...

Entry informationi

Entry nameiPSA3_HUMAN
AccessioniPrimary (citable) accession number: P25788
Secondary accession number(s): B2RCK6
, Q86U83, Q8N1D8, Q9BS70
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 216 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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