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-6

Gene

PSMA6

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

  • endopeptidase activity Source: UniProtKB
  • NF-kappaB binding Source: BHF-UCL
  • purine ribonucleoside triphosphate binding Source: BHF-UCL
  • RNA binding Source: UniProtKB
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciZFISH:HS02161-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.
SIGNORiP60900.

Protein family/group databases

MEROPSiT01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-6 (EC:3.4.25.1)
Alternative name(s):
27 kDa prosomal protein
Short name:
PROS-27
Short name:
p27K
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain
Gene namesi
Name:PSMA6
Synonyms:PROS27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9535. PSMA6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • myofibril Source: BHF-UCL
  • nuclear matrix Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • polysome Source: BHF-UCL
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: BHF-UCL
  • sarcomere Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5687.
MalaCardsiPSMA6.
OpenTargetsiENSG00000100902.
PharmGKBiPA33880.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

DMDMi46397659.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241301 – 246Proteasome subunit alpha type-6Add BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi5O-linked (GlcNAc)By similarity1
Modified residuei17PhosphoserineCombined sources1
Modified residuei63PhosphoserineCombined sources1
Modified residuei64PhosphoserineCombined sources1
Modified residuei102N6-acetyllysineCombined sources1
Modified residuei104N6-acetyllysineCombined sources1
Modified residuei159PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP60900.
MaxQBiP60900.
PaxDbiP60900.
PeptideAtlasiP60900.
PRIDEiP60900.
TopDownProteomicsiP60900-1. [P60900-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00029623.
SWISS-2DPAGEP60900.
UCD-2DPAGEP60900.

PTM databases

iPTMnetiP60900.
PhosphoSitePlusiP60900.
SwissPalmiP60900.

Expressioni

Gene expression databases

BgeeiENSG00000100902.
CleanExiHS_PSMA6.
ExpressionAtlasiP60900. baseline and differential.
GenevisibleiP60900. HS.

Organism-specific databases

HPAiHPA003049.

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. Interacts with ALKBH4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
C19orf57Q0VDD73EBI-357793,EBI-741210
CADM1Q9BY673EBI-357793,EBI-5652260
KRTAP4-2Q9BYR53EBI-357793,EBI-10172511
LIMD2Q9BT233EBI-357793,EBI-2805292
PSMA2P257875EBI-357793,EBI-603262
PSMA3P257889EBI-357793,EBI-348380
PSMA4P257894EBI-357793,EBI-359310
PSMA7O1481811EBI-357793,EBI-603272
RNF170Q96K193EBI-357793,EBI-2130336
RTP5Q14D333EBI-357793,EBI-10217913
TRIM39Q9HCM93EBI-357793,EBI-739510
UCHL5Q9Y5K54EBI-357793,EBI-1051183
ZBTB44Q8NCP53EBI-357793,EBI-5658292

GO - Molecular functioni

  • NF-kappaB binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111660. 141 interactors.
DIPiDIP-29367N.
IntActiP60900. 54 interactors.
MINTiMINT-5001118.
STRINGi9606.ENSP00000261479.

Chemistry databases

BindingDBiP60900.

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 12Combined sources5
Helixi23 – 34Combined sources12
Beta strandi38 – 42Combined sources5
Beta strandi49 – 53Combined sources5
Beta strandi59 – 61Combined sources3
Helixi63 – 65Combined sources3
Beta strandi68 – 73Combined sources6
Beta strandi76 – 82Combined sources7
Helixi84 – 105Combined sources22
Helixi111 – 125Combined sources15
Beta strandi128 – 131Combined sources4
Beta strandi135 – 144Combined sources10
Turni145 – 147Combined sources3
Beta strandi148 – 154Combined sources7
Beta strandi156 – 158Combined sources3
Beta strandi163 – 169Combined sources7
Helixi172 – 185Combined sources14
Helixi187 – 189Combined sources3
Beta strandi191 – 193Combined sources3
Helixi194 – 206Combined sources13
Helixi212 – 214Combined sources3
Beta strandi215 – 219Combined sources5
Helixi232 – 243Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60A/O2-245[»]
4R67X-ray2.89A/O/c/q2-245[»]
5A0Qelectron microscopy3.50A/O1-246[»]
5GJQelectron microscopy4.50B/h1-246[»]
5GJRelectron microscopy3.50B/h1-246[»]
5L4Gelectron microscopy4.02A/N1-246[»]
5LE5X-ray1.80G/U1-246[»]
5LEXX-ray2.20G/U1-246[»]
5LEYX-ray1.90G/U1-246[»]
5LEZX-ray2.19G/U1-246[»]
5LF0X-ray2.41G/U1-246[»]
5LF1X-ray2.00G/U1-246[»]
5LF3X-ray2.10G/U1-246[»]
5LF4X-ray1.99G/U1-246[»]
5LF6X-ray2.07G/U1-246[»]
5LF7X-ray2.00G/U1-246[»]
5T0Celectron microscopy3.80AG/BG2-246[»]
5T0Gelectron microscopy4.40G2-246[»]
5T0Helectron microscopy6.80G2-246[»]
5T0Ielectron microscopy8.00G2-246[»]
5T0Jelectron microscopy8.00G2-246[»]
ProteinModelPortaliP60900.
SMRiP60900.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0182. Eukaryota.
ENOG410XR7X. LUCA.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
HOVERGENiHBG107363.
InParanoidiP60900.
KOiK02730.
PhylomeDBiP60900.
TreeFamiTF106210.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
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 (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P60900-1) [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
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI
60 70 80 90 100
VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN
110 120 130 140 150
WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ
160 170 180 190 200
VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT
210 220 230 240
CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD
Length:246
Mass (Da):27,399
Last modified:April 13, 2004 - v1
Checksum:i94D1FD3C0A7CC72A
GO
Isoform 2 (identifier: P60900-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MSRGSSAGFDRHITIFSPEGRLYQV → MAGLRR

Note: No experimental confirmation available.
Show »
Length:227
Mass (Da):25,290
Checksum:i436E2FE91E1BCDE8
GO
Isoform 3 (identifier: P60900-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Note: No experimental confirmation available.
Show »
Length:167
Mass (Da):18,816
Checksum:iF46774830B65E327
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59K → C in CAA43964 (PubMed:1888762).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0545861 – 79Missing in isoform 3. 1 PublicationAdd BLAST79
Alternative sequenceiVSP_0545871 – 25MSRGS…RLYQV → MAGLRR in isoform 2. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59417 mRNA. Translation: CAA42052.1.
CR456944 mRNA. Translation: CAG33225.1.
AK298920 mRNA. Translation: BAG61026.1.
AK302008 mRNA. Translation: BAG63411.1.
AK313011 mRNA. Translation: BAG35846.1.
AK316223 mRNA. Translation: BAH14594.1.
AL121594 Genomic DNA. No translation available.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65876.1.
CH471078 Genomic DNA. Translation: EAW65877.1.
BC002979 mRNA. Translation: AAH02979.1.
BC017882 mRNA. Translation: AAH17882.1.
BC022354 mRNA. Translation: AAH22354.1.
BC023659 mRNA. Translation: AAH23659.1.
BC070137 mRNA. Translation: AAH70137.1.
X61972 mRNA. Translation: CAA43964.1.
CCDSiCCDS61437.1. [P60900-2]
CCDS61438.1. [P60900-3]
CCDS9655.1. [P60900-1]
PIRiS30274.
RefSeqiNP_001269161.1. NM_001282232.1. [P60900-3]
NP_001269162.1. NM_001282233.1. [P60900-3]
NP_001269163.1. NM_001282234.1. [P60900-2]
NP_002782.1. NM_002791.2. [P60900-1]
XP_016876957.1. XM_017021468.1. [P60900-3]
UniGeneiHs.446260.

Genome annotation databases

EnsembliENST00000261479; ENSP00000261479; ENSG00000100902. [P60900-1]
ENST00000540871; ENSP00000444844; ENSG00000100902. [P60900-2]
ENST00000555764; ENSP00000452566; ENSG00000100902. [P60900-3]
ENST00000622405; ENSP00000479620; ENSG00000100902. [P60900-3]
GeneIDi5687.
KEGGihsa:5687.
UCSCiuc001wtd.5. human. [P60900-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59417 mRNA. Translation: CAA42052.1.
CR456944 mRNA. Translation: CAG33225.1.
AK298920 mRNA. Translation: BAG61026.1.
AK302008 mRNA. Translation: BAG63411.1.
AK313011 mRNA. Translation: BAG35846.1.
AK316223 mRNA. Translation: BAH14594.1.
AL121594 Genomic DNA. No translation available.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65876.1.
CH471078 Genomic DNA. Translation: EAW65877.1.
BC002979 mRNA. Translation: AAH02979.1.
BC017882 mRNA. Translation: AAH17882.1.
BC022354 mRNA. Translation: AAH22354.1.
BC023659 mRNA. Translation: AAH23659.1.
BC070137 mRNA. Translation: AAH70137.1.
X61972 mRNA. Translation: CAA43964.1.
CCDSiCCDS61437.1. [P60900-2]
CCDS61438.1. [P60900-3]
CCDS9655.1. [P60900-1]
PIRiS30274.
RefSeqiNP_001269161.1. NM_001282232.1. [P60900-3]
NP_001269162.1. NM_001282233.1. [P60900-3]
NP_001269163.1. NM_001282234.1. [P60900-2]
NP_002782.1. NM_002791.2. [P60900-1]
XP_016876957.1. XM_017021468.1. [P60900-3]
UniGeneiHs.446260.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60A/O2-245[»]
4R67X-ray2.89A/O/c/q2-245[»]
5A0Qelectron microscopy3.50A/O1-246[»]
5GJQelectron microscopy4.50B/h1-246[»]
5GJRelectron microscopy3.50B/h1-246[»]
5L4Gelectron microscopy4.02A/N1-246[»]
5LE5X-ray1.80G/U1-246[»]
5LEXX-ray2.20G/U1-246[»]
5LEYX-ray1.90G/U1-246[»]
5LEZX-ray2.19G/U1-246[»]
5LF0X-ray2.41G/U1-246[»]
5LF1X-ray2.00G/U1-246[»]
5LF3X-ray2.10G/U1-246[»]
5LF4X-ray1.99G/U1-246[»]
5LF6X-ray2.07G/U1-246[»]
5LF7X-ray2.00G/U1-246[»]
5T0Celectron microscopy3.80AG/BG2-246[»]
5T0Gelectron microscopy4.40G2-246[»]
5T0Helectron microscopy6.80G2-246[»]
5T0Ielectron microscopy8.00G2-246[»]
5T0Jelectron microscopy8.00G2-246[»]
ProteinModelPortaliP60900.
SMRiP60900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111660. 141 interactors.
DIPiDIP-29367N.
IntActiP60900. 54 interactors.
MINTiMINT-5001118.
STRINGi9606.ENSP00000261479.

Chemistry databases

BindingDBiP60900.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.971.

PTM databases

iPTMnetiP60900.
PhosphoSitePlusiP60900.
SwissPalmiP60900.

Polymorphism and mutation databases

DMDMi46397659.

2D gel databases

REPRODUCTION-2DPAGEIPI00029623.
SWISS-2DPAGEP60900.
UCD-2DPAGEP60900.

Proteomic databases

EPDiP60900.
MaxQBiP60900.
PaxDbiP60900.
PeptideAtlasiP60900.
PRIDEiP60900.
TopDownProteomicsiP60900-1. [P60900-1]

Protocols and materials databases

DNASUi5687.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261479; ENSP00000261479; ENSG00000100902. [P60900-1]
ENST00000540871; ENSP00000444844; ENSG00000100902. [P60900-2]
ENST00000555764; ENSP00000452566; ENSG00000100902. [P60900-3]
ENST00000622405; ENSP00000479620; ENSG00000100902. [P60900-3]
GeneIDi5687.
KEGGihsa:5687.
UCSCiuc001wtd.5. human. [P60900-1]

Organism-specific databases

CTDi5687.
DisGeNETi5687.
GeneCardsiPSMA6.
HGNCiHGNC:9535. PSMA6.
HPAiHPA003049.
MalaCardsiPSMA6.
MIMi602855. gene.
neXtProtiNX_P60900.
OpenTargetsiENSG00000100902.
PharmGKBiPA33880.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0182. Eukaryota.
ENOG410XR7X. LUCA.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
HOVERGENiHBG107363.
InParanoidiP60900.
KOiK02730.
PhylomeDBiP60900.
TreeFamiTF106210.

Enzyme and pathway databases

BioCyciZFISH:HS02161-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.
SIGNORiP60900.

Miscellaneous databases

GeneWikiiPSMA6.
GenomeRNAii5687.
PROiP60900.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100902.
CleanExiHS_PSMA6.
ExpressionAtlasiP60900. baseline and differential.
GenevisibleiP60900. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
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 nameiPSA6_HUMAN
AccessioniPrimary (citable) accession number: P60900
Secondary accession number(s): B2R7J9
, B4DQR4, B4DXJ9, P34062, Q6IB60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 30, 2016
This is version 150 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 14
    Human chromosome 14: 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.