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Protein

Proteasome subunit alpha type-7

Gene

PSMA7

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). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.8 Publications

Catalytic activityi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • threonine-type endopeptidase activity Source: UniProtKB-KW

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
SIGNORiO14818

Protein family/group databases

MEROPSiT01.979

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7 (EC:3.4.25.11 Publication)
Alternative name(s):
Proteasome subunit RC6-1
Proteasome subunit XAPC7
Gene namesi
Name:PSMA7
Synonyms:HSPC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000101182.14
HGNCiHGNC:9536 PSMA7
MIMi606607 gene
neXtProtiNX_O14818

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi153Y → F: Displays impaired G1/S transition and S/G2 progression. 1 Publication1

Organism-specific databases

DisGeNETi5688
OpenTargetsiENSG00000101182
PharmGKBiPA33881

Chemistry databases

ChEMBLiCHEMBL3831201
DrugBankiDB07558 2-ACETYLAMINO-4-METHYL-PENTANOIC ACID [1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE

Polymorphism and mutation databases

BioMutaiPSMA7

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241421 – 248Proteasome subunit alpha type-7Add BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi130O-linked (GlcNAc) serineBy similarity1
Modified residuei153Phosphotyrosine; by ABL1 and ABL21 Publication1
Modified residuei227N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO14818
MaxQBiO14818
PaxDbiO14818
PeptideAtlasiO14818
PRIDEiO14818
ProteomicsDBi48256
48257 [O14818-2]

2D gel databases

REPRODUCTION-2DPAGEiIPI00024175
UCD-2DPAGEiO14818

PTM databases

iPTMnetiO14818
PhosphoSitePlusiO14818
SwissPalmiO14818

Expressioni

Inductioni

Down-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues.2 Publications

Gene expression databases

BgeeiENSG00000101182
CleanExiHS_PSMA7
ExpressionAtlasiO14818 baseline and differential
GenevisibleiO14818 HS

Organism-specific databases

HPAiCAB046007
CAB046008
HPA047266

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. PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (PubMed:16251969). Interacts with HIF1A. Interacts with RAB7A (PubMed:14998988). Interacts with PRKN (PubMed:15987638). Interacts with ABL1 and ABL2 (PubMed:16678104). Interacts with EMAP2 (PubMed:19362550). Interacts with MAVS (PubMed:19734229).12 Publications
(Microbial infection) Interacts with HIV-1 TAT protein.1 Publication
(Microbial infection) Interacts with hepatitis B virus X protein (HBX).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi111661, 116 interactors
CORUMiO14818
DIPiDIP-29363N
IntActiO14818, 59 interactors
MINTiO14818
STRINGi9606.ENSP00000359910

Chemistry databases

BindingDBiO14818

Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi12 – 14Combined sources3
Helixi17 – 27Combined sources11
Beta strandi32 – 36Combined sources5
Beta strandi38 – 46Combined sources9
Beta strandi52 – 54Combined sources3
Helixi56 – 59Combined sources4
Beta strandi61 – 66Combined sources6
Beta strandi69 – 75Combined sources7
Helixi77 – 98Combined sources22
Helixi104 – 117Combined sources14
Turni118 – 120Combined sources3
Beta strandi129 – 136Combined sources8
Beta strandi142 – 147Combined sources6
Beta strandi153 – 162Combined sources10
Helixi165 – 175Combined sources11
Turni178 – 181Combined sources4
Helixi184 – 196Combined sources13
Beta strandi199 – 201Combined sources3
Beta strandi202 – 212Combined sources11
Turni213 – 215Combined sources3
Beta strandi216 – 219Combined sources4
Helixi222 – 233Combined sources12
Turni234 – 237Combined sources4
Turni241 – 243Combined sources3

3D structure databases

ProteinModelPortaliO14818
SMRiO14818
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0183 Eukaryota
ENOG410XP21 LUCA
GeneTreeiENSGT00550000074753
HOGENOMiHOG000091085
HOVERGENiHBG003005
InParanoidiO14818
KOiK02731
OMAiPYTQKPA
OrthoDBiEOG091G0GX6
PhylomeDBiO14818
TreeFamiTF106212

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR035190 Proteasome_alpha7
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF40 PTHR11599:SF40, 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: O14818-1) [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
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV
60 70 80 90 100
AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED
110 120 130 140 150
PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS
160 170 180 190 200
GTYHAWKANA IGRGAKSVRE FLEKNYTDEA IETDDLTIKL VIKALLEVVQ
210 220 230 240
SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
Length:248
Mass (Da):27,887
Last modified:January 1, 1998 - v1
Checksum:i5DD0276A1C2DEF91
GO
Isoform 2 (identifier: O14818-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Show »
Length:178
Mass (Da):20,193
Checksum:iA4A7D8924670D890
GO
Isoform 3 (identifier: O14818-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-149: RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP → VGACPLACSPLAAGQSRLRHGGSCHVTSGESEN
     150-248: Missing.

Show »
Length:149
Mass (Da):16,135
Checksum:i90D6129907EDE5C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160A → S in AAC99402 (PubMed:11042152).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078692112A → D Found in patient with severe intellectual disability; unknown pathological significance. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0052811 – 70Missing in isoform 2. CuratedAdd BLAST70
Alternative sequenceiVSP_046556117 – 149RYTQS…YQTDP → VGACPLACSPLAAGQSRLRH GGSCHVTSGESEN in isoform 3. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_046557150 – 248Missing in isoform 3. 1 PublicationAdd BLAST99

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022815 mRNA Translation: AAB81515.1
AF054185 mRNA Translation: AAC99402.1
BT007165 mRNA Translation: AAP35829.1
AK312025 mRNA Translation: BAG34962.1
AL078633 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75398.1
BC004427 mRNA Translation: AAH04427.1
BI906714 mRNA No translation available.
CCDSiCCDS13489.1 [O14818-1]
PIRiPC2326
RefSeqiNP_002783.1, NM_002792.3 [O14818-1]
UniGeneiHs.233952

Genome annotation databases

EnsembliENST00000370858; ENSP00000359895; ENSG00000101182 [O14818-4]
ENST00000370861; ENSP00000359898; ENSG00000101182 [O14818-2]
ENST00000370873; ENSP00000359910; ENSG00000101182 [O14818-1]
GeneIDi5688
KEGGihsa:5688
UCSCiuc002ybx.3 human [O14818-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSA7_HUMAN
AccessioniPrimary (citable) accession number: O14818
Secondary accession number(s): B2R515
, Q5JXJ2, Q9BR53, Q9H4K5, Q9UEU8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 1, 1998
Last modified: July 18, 2018
This is version 199 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 20
    Human chromosome 20: 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

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