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Protein

Proteasome subunit alpha type-4

Gene

PSMA4

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

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS00553-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.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C9
Multicatalytic endopeptidase complex subunit C9
Proteasome component C9
Proteasome subunit L
Gene namesi
Name:PSMA4
Synonyms:HC9, PSC9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9533. PSMA4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: Reactome
  • 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

DisGeNETi5685.
OpenTargetsiENSG00000041357.
PharmGKBiPA33878.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMA4.
DMDMi130861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241031 – 261Proteasome subunit alpha type-4Add BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13PhosphoserineCombined sources1
Modified residuei75PhosphoserineCombined sources1
Modified residuei127N6-acetyllysineCombined sources1
Modified residuei173PhosphoserineCombined sources1
Modified residuei176N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP25789.
MaxQBiP25789.
PaxDbiP25789.
PeptideAtlasiP25789.
PRIDEiP25789.
TopDownProteomicsiP25789-1. [P25789-1]

2D gel databases

UCD-2DPAGEP25789.

PTM databases

iPTMnetiP25789.
PhosphoSitePlusiP25789.
SwissPalmiP25789.

Expressioni

Inductioni

Down-regulated by antioxidants BO-653 and probucol.1 Publication

Gene expression databases

BgeeiENSG00000041357.
CleanExiHS_PSMA4.
ExpressionAtlasiP25789. baseline and differential.
GenevisibleiP25789. HS.

Organism-specific databases

HPAiCAB004973.
HPA055466.
HPA060613.

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. Interaction with HTLV-1 TAX protein favors NFKB1 activation.

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-359310,EBI-618309
IKZF1Q134223EBI-359310,EBI-745305
PSMA1P257863EBI-359310,EBI-359352
PSMA2P257877EBI-359310,EBI-603262
PSMA3P257884EBI-359310,EBI-348380
PSMA6P609004EBI-359310,EBI-357793
PSMA7O148188EBI-359310,EBI-603272

Protein-protein interaction databases

BioGridi111658. 102 interactors.
DIPiDIP-29365N.
IntActiP25789. 31 interactors.
MINTiMINT-5002513.
STRINGi9606.ENSP00000044462.

Chemistry databases

BindingDBiP25789.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Turni14 – 16Combined sources3
Helixi19 – 29Combined sources11
Beta strandi34 – 39Combined sources6
Beta strandi42 – 48Combined sources7
Beta strandi63 – 69Combined sources7
Beta strandi72 – 78Combined sources7
Helixi80 – 101Combined sources22
Helixi107 – 123Combined sources17
Beta strandi124 – 126Combined sources3
Beta strandi132 – 140Combined sources9
Turni141 – 143Combined sources3
Beta strandi144 – 150Combined sources7
Beta strandi156 – 165Combined sources10
Helixi168 – 178Combined sources11
Turni181 – 183Combined sources3
Helixi186 – 200Combined sources15
Beta strandi203 – 205Combined sources3
Helixi208 – 210Combined sources3
Beta strandi211 – 219Combined sources9
Beta strandi222 – 227Combined sources6
Helixi230 – 246Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60C/Q2-251[»]
4R67X-ray2.89C/Q/e/s2-251[»]
5A0Qelectron microscopy3.50C/Q1-261[»]
5GJQelectron microscopy4.50D/j1-261[»]
5GJRelectron microscopy3.50D/j1-261[»]
5L4Gelectron microscopy4.02C/P1-261[»]
5LE5X-ray1.80B/P1-261[»]
5LEXX-ray2.20B/P1-261[»]
5LEYX-ray1.90B/P1-261[»]
5LEZX-ray2.19B/P1-261[»]
5LF0X-ray2.41B/P1-261[»]
5LF1X-ray2.00B/P1-261[»]
5LF3X-ray2.10B/P1-261[»]
5LF4X-ray1.99B/P1-261[»]
5LF6X-ray2.07B/P1-261[»]
5LF7X-ray2.00B/P1-261[»]
5T0Celectron microscopy3.80AI/BI2-261[»]
5T0Gelectron microscopy4.40I2-261[»]
5T0Helectron microscopy6.80I2-261[»]
5T0Ielectron microscopy8.00I2-261[»]
5T0Jelectron microscopy8.00I2-261[»]
ProteinModelPortaliP25789.
SMRiP25789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP25789.
KOiK02728.
OMAiCNEKQRY.
OrthoDBiEOG091G0F2L.
PhylomeDBiP25789.
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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P25789-1) [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
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:May 1, 1992 - v1
Checksum:i7867422B1B31F3B9
GO
Isoform 2 (identifier: P25789-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: No experimental confirmation available.
Show »
Length:190
Mass (Da):21,365
Checksum:i0F5AC7AC01335F6A
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0431021 – 71Missing in isoform 2. 1 PublicationAdd BLAST71

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00763 mRNA. Translation: BAA00660.1.
BT009784 mRNA. Translation: AAP88786.1.
AC027228 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99163.1.
CH471136 Genomic DNA. Translation: EAW99164.1.
BC005361 mRNA. Translation: AAH05361.1.
BC022445 mRNA. Translation: AAH22445.1.
BC022817 mRNA. Translation: AAH22817.2.
BC047667 mRNA. Translation: AAH47667.1.
BC093069 mRNA. Translation: AAH93069.1.
CCDSiCCDS10303.1. [P25789-1]
CCDS45319.1. [P25789-2]
PIRiS15972. SNHUC9.
RefSeqiNP_001096137.1. NM_001102667.2. [P25789-1]
NP_001096138.1. NM_001102668.2. [P25789-2]
NP_001317605.1. NM_001330676.1.
NP_002780.1. NM_002789.5. [P25789-1]
UniGeneiHs.251531.

Genome annotation databases

EnsembliENST00000044462; ENSP00000044462; ENSG00000041357. [P25789-1]
ENST00000413382; ENSP00000402118; ENSG00000041357. [P25789-2]
ENST00000559082; ENSP00000453887; ENSG00000041357. [P25789-1]
GeneIDi5685.
KEGGihsa:5685.
UCSCiuc002bdu.5. human. [P25789-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00763 mRNA. Translation: BAA00660.1.
BT009784 mRNA. Translation: AAP88786.1.
AC027228 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99163.1.
CH471136 Genomic DNA. Translation: EAW99164.1.
BC005361 mRNA. Translation: AAH05361.1.
BC022445 mRNA. Translation: AAH22445.1.
BC022817 mRNA. Translation: AAH22817.2.
BC047667 mRNA. Translation: AAH47667.1.
BC093069 mRNA. Translation: AAH93069.1.
CCDSiCCDS10303.1. [P25789-1]
CCDS45319.1. [P25789-2]
PIRiS15972. SNHUC9.
RefSeqiNP_001096137.1. NM_001102667.2. [P25789-1]
NP_001096138.1. NM_001102668.2. [P25789-2]
NP_001317605.1. NM_001330676.1.
NP_002780.1. NM_002789.5. [P25789-1]
UniGeneiHs.251531.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60C/Q2-251[»]
4R67X-ray2.89C/Q/e/s2-251[»]
5A0Qelectron microscopy3.50C/Q1-261[»]
5GJQelectron microscopy4.50D/j1-261[»]
5GJRelectron microscopy3.50D/j1-261[»]
5L4Gelectron microscopy4.02C/P1-261[»]
5LE5X-ray1.80B/P1-261[»]
5LEXX-ray2.20B/P1-261[»]
5LEYX-ray1.90B/P1-261[»]
5LEZX-ray2.19B/P1-261[»]
5LF0X-ray2.41B/P1-261[»]
5LF1X-ray2.00B/P1-261[»]
5LF3X-ray2.10B/P1-261[»]
5LF4X-ray1.99B/P1-261[»]
5LF6X-ray2.07B/P1-261[»]
5LF7X-ray2.00B/P1-261[»]
5T0Celectron microscopy3.80AI/BI2-261[»]
5T0Gelectron microscopy4.40I2-261[»]
5T0Helectron microscopy6.80I2-261[»]
5T0Ielectron microscopy8.00I2-261[»]
5T0Jelectron microscopy8.00I2-261[»]
ProteinModelPortaliP25789.
SMRiP25789.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111658. 102 interactors.
DIPiDIP-29365N.
IntActiP25789. 31 interactors.
MINTiMINT-5002513.
STRINGi9606.ENSP00000044462.

Chemistry databases

BindingDBiP25789.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.973.

PTM databases

iPTMnetiP25789.
PhosphoSitePlusiP25789.
SwissPalmiP25789.

Polymorphism and mutation databases

BioMutaiPSMA4.
DMDMi130861.

2D gel databases

UCD-2DPAGEP25789.

Proteomic databases

EPDiP25789.
MaxQBiP25789.
PaxDbiP25789.
PeptideAtlasiP25789.
PRIDEiP25789.
TopDownProteomicsiP25789-1. [P25789-1]

Protocols and materials databases

DNASUi5685.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000044462; ENSP00000044462; ENSG00000041357. [P25789-1]
ENST00000413382; ENSP00000402118; ENSG00000041357. [P25789-2]
ENST00000559082; ENSP00000453887; ENSG00000041357. [P25789-1]
GeneIDi5685.
KEGGihsa:5685.
UCSCiuc002bdu.5. human. [P25789-1]

Organism-specific databases

CTDi5685.
DisGeNETi5685.
GeneCardsiPSMA4.
HGNCiHGNC:9533. PSMA4.
HPAiCAB004973.
HPA055466.
HPA060613.
MIMi176846. gene.
neXtProtiNX_P25789.
OpenTargetsiENSG00000041357.
PharmGKBiPA33878.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0178. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP25789.
KOiK02728.
OMAiCNEKQRY.
OrthoDBiEOG091G0F2L.
PhylomeDBiP25789.
TreeFamiTF106209.

Enzyme and pathway databases

BioCyciZFISH:HS00553-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.

Miscellaneous databases

ChiTaRSiPSMA4. human.
GeneWikiiPSMA4.
GenomeRNAii5685.
PROiP25789.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000041357.
CleanExiHS_PSMA4.
ExpressionAtlasiP25789. baseline and differential.
GenevisibleiP25789. HS.

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...

Entry informationi

Entry nameiPSA4_HUMAN
AccessioniPrimary (citable) accession number: P25789
Secondary accession number(s): D3DW86
, Q53XP2, Q567Q5, Q8TBD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 181 of the entry and version 1 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 15
    Human chromosome 15: 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.