Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit alpha type-1

Gene

PSMA1

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

  • RNA binding Source: ProtInc
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processImmunity

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

MEROPSiT01.976

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.11 Publication)
Alternative name(s):
30 kDa prosomal protein
Short name:
PROS-30
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu chain
Gene namesi
Name:PSMA1
Synonyms:HC2, NU, PROS30, PSC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000129084.17
HGNCiHGNC:9530 PSMA1
MIMi602854 gene
neXtProtiNX_P25786

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

DisGeNETi5682
OpenTargetsiENSG00000129084
PharmGKBiPA33875

Chemistry databases

ChEMBLiCHEMBL3831201

Polymorphism and mutation databases

BioMutaiPSMA1
DMDMi130848

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001240601 – 263Proteasome subunit alpha type-1Add BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei110Phosphoserine; alternateCombined sources1
Glycosylationi110O-linked (GlcNAc) serine; alternateBy similarity1
Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei177PhosphoserineCombined sources1
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP25786
MaxQBiP25786
PaxDbiP25786
PeptideAtlasiP25786
PRIDEiP25786
ProteomicsDBi54287
54288 [P25786-2]
TopDownProteomicsiP25786-1 [P25786-1]

2D gel databases

OGPiP25786
REPRODUCTION-2DPAGEiIPI00016832

PTM databases

iPTMnetiP25786
PhosphoSitePlusiP25786
SwissPalmiP25786

Expressioni

Inductioni

Induced in breast cancer tissue (at protein level). Up-regulated in liver tumor tissues.3 Publications

Gene expression databases

BgeeiENSG00000129084
CleanExiHS_PSMA1
ExpressionAtlasiP25786 baseline and differential
GenevisibleiP25786 HS

Organism-specific databases

HPAiCAB033765
HPA037646
HPA043891

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 NOTCH3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI3Q9P2A43EBI-359352,EBI-742038
APIPQ96GX93EBI-359352,EBI-359248
BANF2Q9H503-24EBI-359352,EBI-11977289
BLZF1Q9H2G93EBI-359352,EBI-2548012
CALCOCO2Q131373EBI-359352,EBI-739580
CBSP355203EBI-359352,EBI-740135
CCDC102BQ68D865EBI-359352,EBI-10171570
CCNHP519468EBI-359352,EBI-741406
CDAP323203EBI-359352,EBI-9250559
CEP70Q8NHQ15EBI-359352,EBI-739624
CEP72Q9P2095EBI-359352,EBI-739498
EHMT2A2ABF93EBI-359352,EBI-10174566
GNPTABQ3T9063EBI-359352,EBI-1104907
GOLGA2Q083795EBI-359352,EBI-618309
HEL-S-70V9HW803EBI-359352,EBI-10175326
HOMER3Q9NSC57EBI-359352,EBI-748420
IFT20Q8IY313EBI-359352,EBI-744203
IKZF1Q134223EBI-359352,EBI-745305
IKZF3Q9UKT93EBI-359352,EBI-747204
INO80EQ8NBZ03EBI-359352,EBI-769401
KAZNQ674X7-24EBI-359352,EBI-12024294
KCTD1Q719H93EBI-359352,EBI-9027502
KCTD6Q8NC694EBI-359352,EBI-2511344
KCTD9Q7L2735EBI-359352,EBI-4397613
KRT15P190124EBI-359352,EBI-739566
KRT31Q153233EBI-359352,EBI-948001
KRT38O760155EBI-359352,EBI-1047263
KRT40Q6A1623EBI-359352,EBI-10171697
KRTAP5-9P263715EBI-359352,EBI-3958099
LDOC1O957517EBI-359352,EBI-740738
LZTS2Q9BRK43EBI-359352,EBI-741037
MAD1L1Q9Y6D93EBI-359352,EBI-742610
MAPRE1Q156915EBI-359352,EBI-1004115
MAPRE3Q9UPY84EBI-359352,EBI-726739
MID2Q9UJV3-25EBI-359352,EBI-10172526
MKRN3Q130645EBI-359352,EBI-2340269
MLH1P406923EBI-359352,EBI-744248
MRFAP1L1Q96HT84EBI-359352,EBI-748896
MTUS2Q5JR596EBI-359352,EBI-742948
NOTCH2NLQ7Z3S95EBI-359352,EBI-945833
PNMA1Q8ND905EBI-359352,EBI-302345
PNMA2Q9UL423EBI-359352,EBI-302355
PNMA5Q96PV43EBI-359352,EBI-10171633
PRDM14Q9GZV83EBI-359352,EBI-3957793
PSMA2P257878EBI-359352,EBI-603262
PSMA3P2578813EBI-359352,EBI-348380
PSMA4P257897EBI-359352,EBI-359310
PSMA7O1481814EBI-359352,EBI-603272
PSMB2P497217EBI-359352,EBI-359335
RELQ048643EBI-359352,EBI-307352
ROPN1Q9HAT05EBI-359352,EBI-1378139
SH3GLB1Q9Y3713EBI-359352,EBI-2623095
SSX2IPQ9Y2D83EBI-359352,EBI-2212028
TCF12Q990813EBI-359352,EBI-722877
TCF4P158843EBI-359352,EBI-533224
TNFAIP1Q138293EBI-359352,EBI-2505861
TNRA1L3063EBI-359352,EBI-10182881
TRAF1Q130773EBI-359352,EBI-359224
TRAF6Q9Y4K32EBI-359352,EBI-359276
TRIM10Q9UDY63EBI-359352,EBI-6427325
TRIM23P364065EBI-359352,EBI-740098
TRIM27P143735EBI-359352,EBI-719493
TRIM42Q8IWZ53EBI-359352,EBI-5235829
UBXN11Q5T1243EBI-359352,EBI-746004

Protein-protein interaction databases

BioGridi111655, 200 interactors
CORUMiP25786
DIPiDIP-29369N
IntActiP25786, 234 interactors
MINTiP25786
STRINGi9606.ENSP00000414359

Chemistry databases

BindingDBiP25786

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Beta strandi9 – 11Combined sources3
Beta strandi15 – 18Combined sources4
Helixi20 – 31Combined sources12
Beta strandi35 – 39Combined sources5
Beta strandi41 – 49Combined sources9
Beta strandi53 – 57Combined sources5
Beta strandi63 – 67Combined sources5
Beta strandi70 – 76Combined sources7
Helixi78 – 99Combined sources22
Helixi105 – 117Combined sources13
Helixi118 – 121Combined sources4
Beta strandi122 – 124Combined sources3
Beta strandi130 – 138Combined sources9
Beta strandi141 – 147Combined sources7
Beta strandi149 – 151Combined sources3
Beta strandi154 – 162Combined sources9
Helixi165 – 175Combined sources11
Helixi176 – 181Combined sources6
Helixi184 – 196Combined sources13
Turni207 – 209Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi219 – 224Combined sources6
Helixi226 – 229Combined sources4
Helixi230 – 233Combined sources4

3D structure databases

ProteinModelPortaliP25786
SMRiP25786
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0863 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000074855
HOGENOMiHOG000091080
HOVERGENiHBG105373
InParanoidiP25786
KOiK02725
OMAiFMKQQCL
OrthoDBiEOG091G0DNK
PhylomeDBiP25786
TreeFamiTF106206

Family and domain databases

CDDicd03749 proteasome_alpha_type_1, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR035144 Proteasome_alpha1
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF12 PTHR11599:SF12, 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 Short (identifier: P25786-1) [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
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK
60 70 80 90 100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD
110 120 130 140 150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS
160 170 180 190 200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP
210 220 230 240 250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPAQPA
260
DEPAEKADEP MEH
Length:263
Mass (Da):29,556
Last modified:May 1, 1992 - v1
Checksum:i3F159C5BCEFE8DED
GO
Isoform Long (identifier: P25786-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQLSKVK

Show »
Length:269
Mass (Da):30,239
Checksum:iDB7435F82890F923
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15SP → TA in AAA92734 (PubMed:1398136).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06745437G → V2 PublicationsCorresponds to variant dbSNP:rs17850016Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0052791M → MQLSKVK in isoform Long. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61969 mRNA Translation: CAA43961.1
D00759 mRNA Translation: BAA00656.1
M64992 mRNA Translation: AAA92734.1
BT006647 mRNA Translation: AAP35293.1
AK290765 mRNA Translation: BAF83454.1
CH471064 Genomic DNA Translation: EAW68479.1
BC002577 mRNA Translation: AAH02577.1
BC005932 mRNA Translation: AAH05932.1
BC008472 mRNA Translation: AAH08472.1
BC009576 mRNA Translation: AAH09576.1
BC015105 mRNA Translation: AAH15105.1
BC015356 mRNA Translation: AAH15356.1
BC022372 mRNA Translation: AAH22372.1
CCDSiCCDS31431.1 [P25786-2]
CCDS7816.1 [P25786-1]
PIRiJC1445
RefSeqiNP_002777.1, NM_002786.3 [P25786-1]
NP_683877.1, NM_148976.2 [P25786-2]
UniGeneiHs.102798

Genome annotation databases

EnsembliENST00000396394; ENSP00000379676; ENSG00000129084 [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084 [P25786-2]
GeneIDi5682
KEGGihsa:5682
UCSCiuc001mlk.4 human [P25786-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSA1_HUMAN
AccessioniPrimary (citable) accession number: P25786
Secondary accession number(s): A8K400, Q53YE8, Q9BRV9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 18, 2018
This is version 213 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 11
    Human chromosome 11: 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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health