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Protein

Proteasome subunit alpha type-3

Gene

PSMA3

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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.2 Publications

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Gene namesi
Name:PSMA3
Synonyms:HC8, PSC8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9532. PSMA3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: BHF-UCL
  • proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33877.

Polymorphism and mutation databases

BioMutaiPSMA3.
DMDMi130859.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 255254Proteasome subunit alpha type-3PRO_0000124091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei206 – 2061N6-acetyllysine1 Publication
Modified residuei230 – 2301N6-acetyllysine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication
Modified residuei250 – 2501Phosphoserine12 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25788.
PaxDbiP25788.
PRIDEiP25788.

2D gel databases

OGPiP25788.
REPRODUCTION-2DPAGEIPI00171199.

PTM databases

PhosphoSiteiP25788.

Expressioni

Inductioni

Down-regulated by antioxidants BO-653 and probucol. Up-regulated by bacterial lipopolysaccharides (LPS) and TNF.3 Publications

Gene expression databases

BgeeiP25788.
CleanExiHS_PSMA3.
ExpressionAtlasiP25788. baseline and differential.
GenevisibleiP25788. HS.

Organism-specific databases

HPAiHPA000905.

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 AURKB. Interacts with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B2R5503EBI-348380,EBI-10175488
Q5JPT63EBI-348380,EBI-10244213
Q5W1503EBI-348380,EBI-10248148
Q7KZQ13EBI-348380,EBI-10255941
Q9H8E53EBI-348380,EBI-10309031
Q9HAA03EBI-348380,EBI-10309885
Q9NWL93EBI-348380,EBI-10315054
ATP6V0CP274493EBI-348380,EBI-721179
BTN2A2Q8WVV53EBI-348380,EBI-8648738
C14orf159Q7Z3D63EBI-348380,EBI-2807872
C1orf105O955613EBI-348380,EBI-10191951
C1QTNF9B-AS1Q58A443EBI-348380,EBI-10243387
C4orf42Q96CW73EBI-348380,EBI-752053
C9orf106A2RU003EBI-348380,EBI-10173129
CCL28Q9NRJ33EBI-348380,EBI-7783254
CRB3Q9BUF73EBI-348380,EBI-9844372
CST2P092283EBI-348380,EBI-8832659
CTAGE5O153203EBI-348380,EBI-1050253
DMC1Q145653EBI-348380,EBI-930865
DMRT3Q9NQL93EBI-348380,EBI-9679045
FAM103A1Q9BTL33EBI-348380,EBI-744023
FAM171A2Q8N0U13EBI-348380,EBI-10264767
FAM218AQ96MZ43EBI-348380,EBI-10291578
FBXL18Q96D163EBI-348380,EBI-744419
FBXO7Q9Y3I13EBI-348380,EBI-1161222
GATA2P237693EBI-348380,EBI-2806671
GATA3P237713EBI-348380,EBI-6664760
GORASP2Q9H8Y83EBI-348380,EBI-739467
hCG_1998195Q8N7793EBI-348380,EBI-10267476
hCG_2003792A0A024R5S03EBI-348380,EBI-10188461
IQCEQ6IPM23EBI-348380,EBI-3893098
KIRREL2Q6UWL63EBI-348380,EBI-10254473
KIRREL3-AS3Q8N7Y13EBI-348380,EBI-10267656
KRTAP19-5Q3LI723EBI-348380,EBI-1048945
KRTAP26-1Q6PEX33EBI-348380,EBI-3957672
KRTAP8-1Q8IUC23EBI-348380,EBI-10261141
LASP1Q148473EBI-348380,EBI-742828
LETM1O952023EBI-348380,EBI-1052895
MDM2Q009872EBI-348380,EBI-389668
MUM1Q9H6H23EBI-348380,EBI-10307610
NPBWR2P481463EBI-348380,EBI-10210114
NPPBP168603EBI-348380,EBI-747044
OSR2Q8N2R03EBI-348380,EBI-5660512
PATL1Q86TB93EBI-348380,EBI-2562092
PMLP295902EBI-348380,EBI-295890
PRR10Q14CW73EBI-348380,EBI-10234793
PRR13Q9NZ813EBI-348380,EBI-740924
PRR3P795223EBI-348380,EBI-2803328
PSMA1P257866EBI-348380,EBI-359352
PSMA4P257894EBI-348380,EBI-359310
PSMA6P609007EBI-348380,EBI-357793
PSMA7O148186EBI-348380,EBI-603272
PSMB4P280703EBI-348380,EBI-603350
PTPN23Q9H3S73EBI-348380,EBI-724478
PWWP2BQ6NUJ53EBI-348380,EBI-10251192
RAB3IL1Q8TBN03EBI-348380,EBI-743796
RAD54L2Q9Y4B43EBI-348380,EBI-948156
RBFOX2O432513EBI-348380,EBI-746056
RBM42Q9BTD83EBI-348380,EBI-746862
RTP5Q14D333EBI-348380,EBI-10217913
RUSC1-AS1Q66K803EBI-348380,EBI-10248967
SF1Q156373EBI-348380,EBI-744603
SLAIN1Q8ND833EBI-348380,EBI-10269374
SLC22A23Q7L9D03EBI-348380,EBI-10256583
SNRPBP14678-23EBI-348380,EBI-372475
SNRPCQ5TAL43EBI-348380,EBI-10246938
SPATA8Q6RVD63EBI-348380,EBI-8635958
STX4Q128463EBI-348380,EBI-744942
STX6O437523EBI-348380,EBI-2695795
URB1-AS1Q96HZ73EBI-348380,EBI-10288943
VPS37CA5D8V63EBI-348380,EBI-2559305
ZNF366Q8N8953EBI-348380,EBI-2813661
ZNF385CQ66K413EBI-348380,EBI-10219231

Protein-protein interaction databases

BioGridi111657. 261 interactions.
IntActiP25788. 112 interactions.
MINTiMINT-1035201.
STRINGi9606.ENSP00000216455.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3211Combined sources
Beta strandi37 – 426Combined sources
Beta strandi45 – 539Combined sources
Beta strandi67 – 715Combined sources
Beta strandi74 – 807Combined sources
Helixi82 – 10322Combined sources
Helixi109 – 12113Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi133 – 14210Combined sources
Turni143 – 1453Combined sources
Beta strandi146 – 1527Combined sources
Beta strandi158 – 16710Combined sources
Helixi170 – 1778Combined sources
Turni182 – 1843Combined sources
Helixi187 – 20115Combined sources
Turni204 – 2063Combined sources
Beta strandi210 – 2189Combined sources
Helixi219 – 2213Combined sources
Beta strandi225 – 2273Combined sources
Helixi230 – 24314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
ProteinModelPortaliP25788.
SMRiP25788. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiP25788.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiP25788.
TreeFamiTF106208.

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 (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25788-1) [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
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV
60 70 80 90 100
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR
110 120 130 140 150
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY
160 170 180 190 200
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDI VKEVAKIIYI
210 220 230 240 250
VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA KESLKEEDES

DDDNM
Length:255
Mass (Da):28,433
Last modified:January 23, 2007 - v2
Checksum:iA1854ED3C0650FB1
GO
Isoform 2 (identifier: P25788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-142: Missing.

Show »
Length:248
Mass (Da):27,647
Checksum:iE1C4F1C97EC83DAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → M in AAH29402 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei136 – 1427Missing in isoform 2. 2 PublicationsVSP_005280

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00762 mRNA. Translation: BAA00659.1.
BT006711 mRNA. Translation: AAP35357.1.
BT019715 mRNA. Translation: AAV38520.1.
AK315158 mRNA. Translation: BAG37603.1.
CH471061 Genomic DNA. Translation: EAW80719.1.
BC005265 mRNA. Translation: AAH05265.1.
BC029402 mRNA. Translation: AAH29402.1.
BC038990 mRNA. Translation: AAH38990.1.
CCDSiCCDS45113.1. [P25788-2]
CCDS9731.1. [P25788-1]
PIRiS15971. SNHUC8.
RefSeqiNP_002779.1. NM_002788.3. [P25788-1]
NP_687033.1. NM_152132.2. [P25788-2]
UniGeneiHs.558799.

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567.
ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneIDi5684.
KEGGihsa:5684.
UCSCiuc001xdj.2. human. [P25788-1]
uc001xdk.2. human. [P25788-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00762 mRNA. Translation: BAA00659.1.
BT006711 mRNA. Translation: AAP35357.1.
BT019715 mRNA. Translation: AAV38520.1.
AK315158 mRNA. Translation: BAG37603.1.
CH471061 Genomic DNA. Translation: EAW80719.1.
BC005265 mRNA. Translation: AAH05265.1.
BC029402 mRNA. Translation: AAH29402.1.
BC038990 mRNA. Translation: AAH38990.1.
CCDSiCCDS45113.1. [P25788-2]
CCDS9731.1. [P25788-1]
PIRiS15971. SNHUC8.
RefSeqiNP_002779.1. NM_002788.3. [P25788-1]
NP_687033.1. NM_152132.2. [P25788-2]
UniGeneiHs.558799.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60G/U2-246[»]
4R67X-ray2.89G/U/i/w2-246[»]
ProteinModelPortaliP25788.
SMRiP25788. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111657. 261 interactions.
IntActiP25788. 112 interactions.
MINTiMINT-1035201.
STRINGi9606.ENSP00000216455.

Chemistry

BindingDBiP25788.
ChEMBLiCHEMBL2364701.

Protein family/group databases

MEROPSiT01.977.

PTM databases

PhosphoSiteiP25788.

Polymorphism and mutation databases

BioMutaiPSMA3.
DMDMi130859.

2D gel databases

OGPiP25788.
REPRODUCTION-2DPAGEIPI00171199.

Proteomic databases

MaxQBiP25788.
PaxDbiP25788.
PRIDEiP25788.

Protocols and materials databases

DNASUi5684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216455; ENSP00000216455; ENSG00000100567.
ENST00000412908; ENSP00000390491; ENSG00000100567. [P25788-2]
GeneIDi5684.
KEGGihsa:5684.
UCSCiuc001xdj.2. human. [P25788-1]
uc001xdk.2. human. [P25788-2]

Organism-specific databases

CTDi5684.
GeneCardsiGC14P058711.
H-InvDBHIX0155215.
HGNCiHGNC:9532. PSMA3.
HPAiHPA000905.
MIMi176843. gene.
176845. gene.
neXtProtiNX_P25788.
PharmGKBiPA33877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiP25788.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiP25788.
TreeFamiTF106208.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GeneWikiiPSMA3.
GenomeRNAii5684.
NextBioi22072.
PROiP25788.
SOURCEiSearch...

Gene expression databases

BgeeiP25788.
CleanExiHS_PSMA3.
ExpressionAtlasiP25788. baseline and differential.
GenevisibleiP25788. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)."
    Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.
    Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow, Pancreas and Urinary bladder.
  6. "Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
    Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
    Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 116-130.
  7. "Gene expression induced by BO-653, probucol and BHQ in human endothelial cells."
    Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H., Hamakubo T., Niki E., Kodama T., Noguchi N.
    J. Atheroscler. Thromb. 7:223-230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BO-653 AND PROBUCOL.
  8. "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome."
    Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J., Allday M.J.
    EMBO J. 20:2367-2375(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDKN1A.
  9. "Mapping and structural dissection of human 20 s proteasome using proteomic approaches."
    Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E., Monsarrat B.
    Mol. Cell. Proteomics 1:567-578(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-250.
  10. "Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes."
    Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M., Imai K.
    Scand. J. Immunol. 56:593-601(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
    Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
    FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  12. "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner."
    Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L.
    Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AURKB.
  13. "Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells."
    Touitou R., O'Nions J., Heaney J., Allday M.J.
    J. Gen. Virol. 86:1269-1277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EBNA3.
  14. "MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein."
    Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X.
    Mol. Cell 20:699-708(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDM2 AND RB1.
  15. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element."
    Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N.
    Free Radic. Res. 40:21-30(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BO-653.
  18. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  20. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  21. "Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes."
    Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N.
    Prostaglandins Other Lipid Mediat. 83:237-249(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBXA2R.
  22. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "Ubiquitin-independent degradation of hepatitis C virus F protein."
    Yuksek K., Chen W.-L., Chien D., Ou J.-H.
    J. Virol. 83:612-621(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV F PROTEIN.
  27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  33. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  34. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPSA3_HUMAN
AccessioniPrimary (citable) accession number: P25788
Secondary accession number(s): B2RCK6
, Q86U83, Q8N1D8, Q9BS70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 179 of the entry and version 2 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

External Data

Dasty 3

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 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.