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-7

Gene

PSMA7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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-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

HGNCiHGNC:9536. PSMA7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: InterPro

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

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

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)By 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.

2D gel databases

REPRODUCTION-2DPAGEIPI00024175.
UCD-2DPAGEO14818.

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

HPAiHPA047266.

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 HIV-1 TAT protein (PubMed:14550573). Interacts with hepatitis B virus X protein (HBX) (PubMed:8764072). Interacts with HIF1A. Interacts with RAB7A (PubMed:14998988). Interacts with PARK2 (PubMed:15987638). Interacts with ABL1 and ABL2 (PubMed:16678104). Interacts with EMAP2 (PubMed:19362550). Interacts with MAVS (PubMed:19734229).15 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi111661. 111 interactors.
DIPiDIP-29363N.
IntActiO14818. 41 interactors.
MINTiMINT-5000782.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60D/R2-244[»]
4R67X-ray2.89D/R/f/t2-244[»]
5A0Qelectron microscopy3.50D/R1-248[»]
5GJQelectron microscopy4.50E/k1-248[»]
5GJRelectron microscopy3.50E/k1-248[»]
5L4Gelectron microscopy4.02D/Q1-248[»]
5LE5X-ray1.80C/Q1-248[»]
5LEXX-ray2.20C/Q1-248[»]
5LEYX-ray1.90C/Q1-248[»]
5LEZX-ray2.19C/Q1-248[»]
5LF0X-ray2.41C/Q1-248[»]
5LF1X-ray2.00C/Q1-248[»]
5LF3X-ray2.10C/Q1-248[»]
5LF4X-ray1.99C/Q1-248[»]
5LF6X-ray2.07C/Q1-248[»]
5LF7X-ray2.00C/Q1-248[»]
5T0Celectron microscopy3.80AJ/BJ2-248[»]
5T0Gelectron microscopy4.40J2-248[»]
5T0Helectron microscopy6.80J2-248[»]
5T0Ielectron microscopy8.00J2-248[»]
5T0Jelectron microscopy8.00J2-248[»]
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.
OMAiIKLVIRA.
OrthoDBiEOG090A0C1B.
PhylomeDBiO14818.
TreeFamiTF106212.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
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

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. Translation: CAC04017.1.
AL078633 Genomic DNA. Translation: CAC04018.1.
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

Cross-referencesi

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. Translation: CAC04017.1.
AL078633 Genomic DNA. Translation: CAC04018.1.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60D/R2-244[»]
4R67X-ray2.89D/R/f/t2-244[»]
5A0Qelectron microscopy3.50D/R1-248[»]
5GJQelectron microscopy4.50E/k1-248[»]
5GJRelectron microscopy3.50E/k1-248[»]
5L4Gelectron microscopy4.02D/Q1-248[»]
5LE5X-ray1.80C/Q1-248[»]
5LEXX-ray2.20C/Q1-248[»]
5LEYX-ray1.90C/Q1-248[»]
5LEZX-ray2.19C/Q1-248[»]
5LF0X-ray2.41C/Q1-248[»]
5LF1X-ray2.00C/Q1-248[»]
5LF3X-ray2.10C/Q1-248[»]
5LF4X-ray1.99C/Q1-248[»]
5LF6X-ray2.07C/Q1-248[»]
5LF7X-ray2.00C/Q1-248[»]
5T0Celectron microscopy3.80AJ/BJ2-248[»]
5T0Gelectron microscopy4.40J2-248[»]
5T0Helectron microscopy6.80J2-248[»]
5T0Ielectron microscopy8.00J2-248[»]
5T0Jelectron microscopy8.00J2-248[»]
ProteinModelPortaliO14818.
SMRiO14818.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111661. 111 interactors.
DIPiDIP-29363N.
IntActiO14818. 41 interactors.
MINTiMINT-5000782.
STRINGi9606.ENSP00000359910.

Chemistry databases

BindingDBiO14818.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.979.

PTM databases

iPTMnetiO14818.
PhosphoSitePlusiO14818.
SwissPalmiO14818.

Polymorphism and mutation databases

BioMutaiPSMA7.

2D gel databases

REPRODUCTION-2DPAGEIPI00024175.
UCD-2DPAGEO14818.

Proteomic databases

EPDiO14818.
MaxQBiO14818.
PaxDbiO14818.
PeptideAtlasiO14818.
PRIDEiO14818.

Protocols and materials databases

DNASUi5688.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5688.
DisGeNETi5688.
GeneCardsiPSMA7.
HGNCiHGNC:9536. PSMA7.
HPAiHPA047266.
MIMi606607. gene.
neXtProtiNX_O14818.
OpenTargetsiENSG00000101182.
PharmGKBiPA33881.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiO14818.
KOiK02731.
OMAiIKLVIRA.
OrthoDBiEOG090A0C1B.
PhylomeDBiO14818.
TreeFamiTF106212.

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-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiO14818.

Miscellaneous databases

ChiTaRSiPSMA7. human.
GeneWikiiPSMA7.
GenomeRNAii5688.
PROiO14818.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101182.
CleanExiHS_PSMA7.
ExpressionAtlasiO14818. baseline and differential.
GenevisibleiO14818. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
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.
ProtoNetiSearch...

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: February 15, 2017
This is version 183 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. 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.