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Protein

Proteasome subunit alpha type-4

Gene

PSMA4

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).3 Publications

Catalytic activityi

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

GO - Molecular functioni

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-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.973

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.11 Publication)
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

EuPathDBiHostDB:ENSG00000041357.15
HGNCiHGNC:9533 PSMA4
MIMi176846 gene
neXtProtiNX_P25789

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

DisGeNETi5685
OpenTargetsiENSG00000041357
PharmGKBiPA33878

Chemistry databases

ChEMBLiCHEMBL3831201

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
ProteomicsDBi54292
54293 [P25789-2]
TopDownProteomicsiP25789-1 [P25789-1]

2D gel databases

UCD-2DPAGEiP25789

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 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 PSMB7.5 Publications
(Microbial infection) Interaction with HTLV-1 TAX protein favors NFKB1 activation.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111658, 107 interactors
CORUMiP25789
DIPiDIP-29365N
IntActiP25789, 39 interactors
MINTiP25789
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 strandi152 – 154Combined sources3
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

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
OMAiMSKTMDS
OrthoDBiEOG091G0F2L
PhylomeDBiP25789
TreeFamiTF106209

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR000426 Proteasome_asu_N
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR034647 Proteasome_subunit_alpha4
PANTHERiPTHR11599:SF13 PTHR11599:SF13, 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.

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 [P25789-1]
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

Similar proteinsi

Entry informationi

Entry nameiPSA4_HUMAN
AccessioniPrimary (citable) accession number: P25789
Secondary accession number(s): D3DW86
, Q53XP2, Q567Q5, Q8TBD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 18, 2018
This is version 200 of the entry and version 1 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. 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

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