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Protein

Proteasome subunit alpha type-1

Gene

PSMA1

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. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. negative regulation of apoptotic process Source: Reactome
  12. negative regulation of canonical Wnt signaling pathway Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of canonical Wnt signaling pathway Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Immunity

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_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 ligand biogenesis disease.
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
30 kDa prosomal protein
Short name:
PROS-30
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu chain
Gene namesi
Name:PSMA1
Synonyms:HC2, NU, PROS30, PSC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9530. PSMA1.

Subcellular locationi

GO - Cellular componenti

  1. centrosome Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
  6. polysome Source: ProtInc
  7. proteasome complex Source: UniProtKB
  8. proteasome core complex Source: UniProtKB
  9. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33875.

Polymorphism and mutation databases

BioMutaiPSMA1.
DMDMi130848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Proteasome subunit alpha type-1PRO_0000124060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi110 – 1101O-linked (GlcNAc)By similarity
Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP25786.
PaxDbiP25786.
PRIDEiP25786.

2D gel databases

OGPiP25786.
REPRODUCTION-2DPAGEIPI00016832.

PTM databases

PhosphoSiteiP25786.

Expressioni

Inductioni

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

Gene expression databases

BgeeiP25786.
CleanExiHS_PSMA1.
ExpressionAtlasiP25786. baseline and differential.
GenevestigatoriP25786.

Organism-specific databases

HPAiCAB033765.
HPA037646.
HPA043891.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is 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 bacterial lipopolysaccharide (LPS) (By similarity). Interacts with NOTCH3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI3Q9P2A43EBI-359352,EBI-742038
APIPQ96GX93EBI-359352,EBI-359248
BLZF1Q9H2G93EBI-359352,EBI-2548012
CBSP355203EBI-359352,EBI-740135
CCDC102BA1A4H13EBI-359352,EBI-10171570
CCNHP519464EBI-359352,EBI-741406
CDAP323203EBI-359352,EBI-9250559
CEP70Q8NHQ13EBI-359352,EBI-739624
CEP72Q9P2095EBI-359352,EBI-739498
EHMT2A2ABF93EBI-359352,EBI-10174566
GNPTABQ3T9063EBI-359352,EBI-1104907
GOLGA2Q083793EBI-359352,EBI-618309
HEL-S-70V9HW803EBI-359352,EBI-10175326
HOMER3B2RA103EBI-359352,EBI-10175777
IFT20Q8IY313EBI-359352,EBI-744203
IKZF1Q134223EBI-359352,EBI-745305
IKZF3Q9UKT93EBI-359352,EBI-747204
INO80EQ8NBZ03EBI-359352,EBI-769401
KCTD1Q719H93EBI-359352,EBI-9027502
KCTD9Q7L2733EBI-359352,EBI-4397613
KRT15P190124EBI-359352,EBI-739566
KRT31Q153233EBI-359352,EBI-948001
KRT38O760153EBI-359352,EBI-1047263
KRT40Q6A1623EBI-359352,EBI-10171697
KRTAP5-9P263713EBI-359352,EBI-3958099
LDOC1O957515EBI-359352,EBI-740738
LZTS2Q9BRK43EBI-359352,EBI-741037
MAD1L1Q9Y6D93EBI-359352,EBI-742610
MAPRE1Q156913EBI-359352,EBI-1004115
MAPRE3Q9UPY84EBI-359352,EBI-726739
MID2Q9UJV3-23EBI-359352,EBI-10172526
MKRN3Q130643EBI-359352,EBI-2340269
MLH1P406923EBI-359352,EBI-744248
MRFAP1L1Q96HT84EBI-359352,EBI-748896
MTUS2Q5JR596EBI-359352,EBI-742948
NOTCH2NLQ7Z3S93EBI-359352,EBI-945833
PNMA1Q8ND903EBI-359352,EBI-302345
PNMA2Q9UL423EBI-359352,EBI-302355
PNMA5Q96PV43EBI-359352,EBI-10171633
PRDM14Q9GZV83EBI-359352,EBI-3957793
PSMA2P257875EBI-359352,EBI-603262
PSMA3P257886EBI-359352,EBI-348380
PSMA4P257893EBI-359352,EBI-359310
PSMA7O148189EBI-359352,EBI-603272
RELQ048643EBI-359352,EBI-307352
ROPN1Q9HAT03EBI-359352,EBI-1378139
SH3GLB1Q9Y3713EBI-359352,EBI-2623095
SSX2IPQ9Y2D83EBI-359352,EBI-2212028
TCF12Q990813EBI-359352,EBI-722877
TCF4P158843EBI-359352,EBI-533224
TNFAIP1Q138293EBI-359352,EBI-2505861
TNRA1L3063EBI-359352,EBI-10182881
TRAF1Q130773EBI-359352,EBI-359224
TRIM10Q9UDY63EBI-359352,EBI-6427325
TRIM23P364065EBI-359352,EBI-740098
TRIM27P143733EBI-359352,EBI-719493
TRIM42A1L4B63EBI-359352,EBI-10172216
UBXN11Q5T1243EBI-359352,EBI-746004

Protein-protein interaction databases

BioGridi111655. 169 interactions.
DIPiDIP-29369N.
IntActiP25786. 103 interactions.
MINTiMINT-1155600.
STRINGi9606.ENSP00000315309.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60F/T4-241[»]
4R67X-ray2.89F/T/h/v4-241[»]
ProteinModelPortaliP25786.
SMRiP25786. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiP25786.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiP25786.
TreeFamiTF106206.

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.

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

Isoform Short (identifier: P25786-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK
60 70 80 90 100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD
110 120 130 140 150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS
160 170 180 190 200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP
210 220 230 240 250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPAQPA
260
DEPAEKADEP MEH
Length:263
Mass (Da):29,556
Last modified:May 1, 1992 - v1
Checksum:i3F159C5BCEFE8DED
GO
Isoform Long (identifier: P25786-2) [UniParc]FASTAAdd to basket

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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152SP → TA in AAA92734 (PubMed:1398136).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → V.2 Publications
Corresponds to variant rs17850016 [ dbSNP | Ensembl ].
VAR_067454

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MQLSKVK in isoform Long. 1 PublicationVSP_005279

Sequence databases

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

Genome annotation databases

EnsembliENST00000396394; ENSP00000379676; ENSG00000129084. [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084. [P25786-2]
GeneIDi5682.
KEGGihsa:5682.
UCSCiuc001mlk.3. human. [P25786-1]
uc001mll.3. human. [P25786-2]

Polymorphism and mutation databases

BioMutaiPSMA1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60F/T4-241[»]
4R67X-ray2.89F/T/h/v4-241[»]
ProteinModelPortaliP25786.
SMRiP25786. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111655. 169 interactions.
DIPiDIP-29369N.
IntActiP25786. 103 interactions.
MINTiMINT-1155600.
STRINGi9606.ENSP00000315309.

Chemistry

ChEMBLiCHEMBL2364701.

PTM databases

PhosphoSiteiP25786.

Polymorphism and mutation databases

BioMutaiPSMA1.
DMDMi130848.

2D gel databases

OGPiP25786.
REPRODUCTION-2DPAGEIPI00016832.

Proteomic databases

MaxQBiP25786.
PaxDbiP25786.
PRIDEiP25786.

Protocols and materials databases

DNASUi5682.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396394; ENSP00000379676; ENSG00000129084. [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084. [P25786-2]
GeneIDi5682.
KEGGihsa:5682.
UCSCiuc001mlk.3. human. [P25786-1]
uc001mll.3. human. [P25786-2]

Organism-specific databases

CTDi5682.
GeneCardsiGC11M014526.
HGNCiHGNC:9530. PSMA1.
HPAiCAB033765.
HPA037646.
HPA043891.
MIMi602854. gene.
neXtProtiNX_P25786.
PharmGKBiPA33875.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiP25786.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiP25786.
TreeFamiTF106206.

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_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 ligand biogenesis disease.
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

ChiTaRSiPSMA1. human.
GeneWikiiProteasome_(prosome,_macropain)_subunit,_alpha_1.
GenomeRNAii5682.
NextBioi22062.
PROiP25786.
SOURCEiSearch...

Gene expression databases

BgeeiP25786.
CleanExiHS_PSMA1.
ExpressionAtlasiP25786. baseline and differential.
GenevestigatoriP25786.

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. "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."
    DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.
    Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  2. "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 SHORT).
  3. "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes."
    Silva-Pereira I., Bey F., Coux O., Scherrer K.
    Gene 120:235-242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-37.
  5. "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 SHORT).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM SHORT), VARIANT VAL-37.
    Tissue: Bone marrow, Brain, Ovary, Placenta and Prostate.
  8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "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 63-82.
  10. "Comparative proteome analysis of breast cancer and adjacent normal breast tissues in human."
    Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.
    Genomics Proteomics Bioinformatics 4:165-172(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
    Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
    Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Conserved signal peptide of Notch3 inhibits interaction with proteasome."
    Zhang Y., Jia L., Lee S.J., Wang M.M.
    Biochem. Biophys. Res. Commun. 355:245-251(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOTCH3.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. "Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics."
    Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E., Yang H.
    Breast Cancer Res. Treat. 104:21-30(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPSA1_HUMAN
AccessioniPrimary (citable) accession number: P25786
Secondary accession number(s): A8K400, Q53YE8, Q9BRV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 29, 2015
This is version 177 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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.