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Protein

Proteasome subunit alpha type-5

Gene

PSMA5

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.

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

BioCyciZFISH:HS06984-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-6798695. Neutrophil degranulation.
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.
SIGNORiP28066.

Protein family/group databases

MEROPSiT01.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain zeta chain
Multicatalytic endopeptidase complex zeta chain
Proteasome zeta chain
Gene namesi
Name:PSMA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9534. PSMA5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5686.
OpenTargetsiENSG00000143106.
PharmGKBiPA33879.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMA5.
DMDMi38258905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241171 – 241Proteasome subunit alpha type-5Add BLAST241

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei16PhosphoserineCombined sources1
Modified residuei55PhosphothreonineCombined sources1
Modified residuei56PhosphoserineCombined sources1
Modified residuei63PhosphoserineCombined sources1
Glycosylationi198O-linked (GlcNAc)By similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP28066.
MaxQBiP28066.
PaxDbiP28066.
PeptideAtlasiP28066.
PRIDEiP28066.
TopDownProteomicsiP28066-1. [P28066-1]

2D gel databases

DOSAC-COBS-2DPAGEP28066.
REPRODUCTION-2DPAGEIPI00291922.
SWISS-2DPAGEP28066.

PTM databases

iPTMnetiP28066.
PhosphoSitePlusiP28066.
SwissPalmiP28066.

Expressioni

Tissue specificityi

Expressed in fetal brain (at protein level).1 Publication

Inductioni

Up-regulated in colon cancer cell lines. Up-regulated in fetal Down syndrome (DS) brain (at protein level). May be the target of the transcriptional activator NFE2L2.2 Publications

Gene expression databases

BgeeiENSG00000143106.
CleanExiHS_PSMA5.
ExpressionAtlasiP28066. baseline and differential.
GenevisibleiP28066. HS.

Organism-specific databases

HPAiHPA028392.
HPA028398.
HPA028441.

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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMA7O148182EBI-355475,EBI-603272

Protein-protein interaction databases

BioGridi111659. 135 interactors.
DIPiDIP-29368N.
IntActiP28066. 32 interactors.
MINTiMINT-1178571.
STRINGi9606.ENSP00000271308.

Chemistry databases

BindingDBiP28066.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 31Combined sources10
Beta strandi37 – 42Combined sources6
Beta strandi45 – 51Combined sources7
Helixi61 – 63Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi74 – 80Combined sources7
Helixi82 – 84Combined sources3
Helixi85 – 103Combined sources19
Helixi109 – 117Combined sources9
Turni118 – 121Combined sources4
Beta strandi125 – 128Combined sources4
Beta strandi133 – 135Combined sources3
Beta strandi139 – 147Combined sources9
Beta strandi150 – 156Combined sources7
Beta strandi162 – 171Combined sources10
Helixi174 – 184Combined sources11
Helixi191 – 205Combined sources15
Beta strandi214 – 220Combined sources7
Beta strandi222 – 224Combined sources3
Helixi231 – 238Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60E/S8-241[»]
4R67X-ray2.89E/S/g/u8-241[»]
5A0Qelectron microscopy3.50E/S1-241[»]
5GJQelectron microscopy4.50F/l1-241[»]
5GJRelectron microscopy3.50F/l1-241[»]
5L4Gelectron microscopy4.02E/R1-241[»]
5LE5X-ray1.80D/R1-241[»]
5LEXX-ray2.20D/R1-241[»]
5LEYX-ray1.90D/R1-241[»]
5LEZX-ray2.19D/R1-241[»]
5LF0X-ray2.41D/R1-241[»]
5LF1X-ray2.00D/R1-241[»]
5LF3X-ray2.10D/R1-241[»]
5LF4X-ray1.99D/R1-241[»]
5LF6X-ray2.07D/R1-241[»]
5LF7X-ray2.00D/R1-241[»]
5T0Celectron microscopy3.80AK/BK2-241[»]
5T0Gelectron microscopy4.40K2-241[»]
5T0Helectron microscopy6.80K2-241[»]
5T0Ielectron microscopy8.00K2-241[»]
5T0Jelectron microscopy8.00K2-241[»]
ProteinModelPortaliP28066.
SMRiP28066.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0176. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP28066.
KOiK02729.
OMAiEPGKTFH.
OrthoDBiEOG091G0GX6.
PhylomeDBiP28066.
TreeFamiTF106211.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
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.

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

Isoform 1 (identifier: P28066-1) [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
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV
60 70 80 90 100
EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW
110 120 130 140 150
FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG
160 170 180 190 200
PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI
210 220 230 240
ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I
Length:241
Mass (Da):26,411
Last modified:October 31, 2003 - v3
Checksum:i5610CDA00469120A
GO
Isoform 2 (identifier: P28066-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.

Note: No experimental confirmation available.
Show »
Length:183
Mass (Da):20,035
Checksum:i24D3C1197D3AD8A5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27A → D in CAA43962 (PubMed:1888762).Curated1
Sequence conflicti184V → L in CAA43962 (PubMed:1888762).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0462411 – 58Missing in isoform 2. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61970 mRNA. Translation: CAA43962.1.
CR456847 mRNA. Translation: CAG33128.1.
AK304448 mRNA. Translation: BAG65266.1.
AK313351 mRNA. Translation: BAG36153.1.
AL356735, AL390252 Genomic DNA. Translation: CAH70887.1.
AL390252, AL356735 Genomic DNA. Translation: CAI13171.1.
CH471122 Genomic DNA. Translation: EAW56381.1.
CH471122 Genomic DNA. Translation: EAW56383.1.
BC102018 mRNA. Translation: AAI02019.1.
BC102019 mRNA. Translation: AAI02020.1.
BC102020 mRNA. Translation: AAI02021.1.
BC103751 mRNA. Translation: AAI03752.1.
CCDSiCCDS55619.1. [P28066-2]
CCDS799.1. [P28066-1]
PIRiS17521.
RefSeqiNP_001186701.1. NM_001199772.1. [P28066-2]
NP_001186702.1. NM_001199773.1. [P28066-2]
NP_001186703.1. NM_001199774.1. [P28066-2]
NP_002781.2. NM_002790.3. [P28066-1]
UniGeneiHs.485246.

Genome annotation databases

EnsembliENST00000271308; ENSP00000271308; ENSG00000143106. [P28066-1]
ENST00000538610; ENSP00000440618; ENSG00000143106. [P28066-2]
GeneIDi5686.
KEGGihsa:5686.
UCSCiuc001dxn.4. human. [P28066-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61970 mRNA. Translation: CAA43962.1.
CR456847 mRNA. Translation: CAG33128.1.
AK304448 mRNA. Translation: BAG65266.1.
AK313351 mRNA. Translation: BAG36153.1.
AL356735, AL390252 Genomic DNA. Translation: CAH70887.1.
AL390252, AL356735 Genomic DNA. Translation: CAI13171.1.
CH471122 Genomic DNA. Translation: EAW56381.1.
CH471122 Genomic DNA. Translation: EAW56383.1.
BC102018 mRNA. Translation: AAI02019.1.
BC102019 mRNA. Translation: AAI02020.1.
BC102020 mRNA. Translation: AAI02021.1.
BC103751 mRNA. Translation: AAI03752.1.
CCDSiCCDS55619.1. [P28066-2]
CCDS799.1. [P28066-1]
PIRiS17521.
RefSeqiNP_001186701.1. NM_001199772.1. [P28066-2]
NP_001186702.1. NM_001199773.1. [P28066-2]
NP_001186703.1. NM_001199774.1. [P28066-2]
NP_002781.2. NM_002790.3. [P28066-1]
UniGeneiHs.485246.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60E/S8-241[»]
4R67X-ray2.89E/S/g/u8-241[»]
5A0Qelectron microscopy3.50E/S1-241[»]
5GJQelectron microscopy4.50F/l1-241[»]
5GJRelectron microscopy3.50F/l1-241[»]
5L4Gelectron microscopy4.02E/R1-241[»]
5LE5X-ray1.80D/R1-241[»]
5LEXX-ray2.20D/R1-241[»]
5LEYX-ray1.90D/R1-241[»]
5LEZX-ray2.19D/R1-241[»]
5LF0X-ray2.41D/R1-241[»]
5LF1X-ray2.00D/R1-241[»]
5LF3X-ray2.10D/R1-241[»]
5LF4X-ray1.99D/R1-241[»]
5LF6X-ray2.07D/R1-241[»]
5LF7X-ray2.00D/R1-241[»]
5T0Celectron microscopy3.80AK/BK2-241[»]
5T0Gelectron microscopy4.40K2-241[»]
5T0Helectron microscopy6.80K2-241[»]
5T0Ielectron microscopy8.00K2-241[»]
5T0Jelectron microscopy8.00K2-241[»]
ProteinModelPortaliP28066.
SMRiP28066.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111659. 135 interactors.
DIPiDIP-29368N.
IntActiP28066. 32 interactors.
MINTiMINT-1178571.
STRINGi9606.ENSP00000271308.

Chemistry databases

BindingDBiP28066.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.975.

PTM databases

iPTMnetiP28066.
PhosphoSitePlusiP28066.
SwissPalmiP28066.

Polymorphism and mutation databases

BioMutaiPSMA5.
DMDMi38258905.

2D gel databases

DOSAC-COBS-2DPAGEP28066.
REPRODUCTION-2DPAGEIPI00291922.
SWISS-2DPAGEP28066.

Proteomic databases

EPDiP28066.
MaxQBiP28066.
PaxDbiP28066.
PeptideAtlasiP28066.
PRIDEiP28066.
TopDownProteomicsiP28066-1. [P28066-1]

Protocols and materials databases

DNASUi5686.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271308; ENSP00000271308; ENSG00000143106. [P28066-1]
ENST00000538610; ENSP00000440618; ENSG00000143106. [P28066-2]
GeneIDi5686.
KEGGihsa:5686.
UCSCiuc001dxn.4. human. [P28066-1]

Organism-specific databases

CTDi5686.
DisGeNETi5686.
GeneCardsiPSMA5.
HGNCiHGNC:9534. PSMA5.
HPAiHPA028392.
HPA028398.
HPA028441.
MIMi176844. gene.
neXtProtiNX_P28066.
OpenTargetsiENSG00000143106.
PharmGKBiPA33879.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0176. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074958.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP28066.
KOiK02729.
OMAiEPGKTFH.
OrthoDBiEOG091G0GX6.
PhylomeDBiP28066.
TreeFamiTF106211.

Enzyme and pathway databases

BioCyciZFISH:HS06984-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-6798695. Neutrophil degranulation.
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.
SIGNORiP28066.

Miscellaneous databases

ChiTaRSiPSMA5. human.
GeneWikiiPSMA5.
GenomeRNAii5686.
PROiP28066.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143106.
CleanExiHS_PSMA5.
ExpressionAtlasiP28066. baseline and differential.
GenevisibleiP28066. HS.

Family and domain databases

CDDicd03753. proteasome_alpha_type_5. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR033812. Proteasome_alpha_type_5.
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 nameiPSA5_HUMAN
AccessioniPrimary (citable) accession number: P28066
Secondary accession number(s): B2R8F6
, B4E2V4, Q3T1C1, Q6IBF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 31, 2003
Last modified: November 30, 2016
This is version 187 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.