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UniProtKB/Swiss-Prot entry P25787


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PSA2_HUMAN
Primary accession number P25787
Secondary accession number Q9BU45
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Proteasome subunit alpha type-2
Synonyms EC 3.4.25.1
Proteasome component C3
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Gene name
Name: PSMA2
Synonyms: PSC3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0167-4781(91)90090-9; PubMed=2025653 [NCBI, ExPASy, EBI, Israel, Japan]
Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.;
"Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes).";
Biochim. Biophys. Acta 1089:95-102(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 5-39; 71-84; 93-113 AND 178-196, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 5-14.
DOI=10.1006/bbrc.1994.2876; PubMed=7811265 [NCBI, ExPASy, EBI, Israel, Japan]
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24 AND TYR-98, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-229, AND MASS SPECTROMETRY.
TISSUE=Pituitary adenoma;
DOI=10.1016/j.ab.2006.05.024; PubMed=16777052 [NCBI, ExPASy, EBI, Israel, Japan]
Zhan X., Desiderio D.M.;
"Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry.";
Anal. Biochem. 354:279-289(2006).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57 AND TYR-76, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
VARIANT [LARGE SCALE ANALYSIS] VAL-110.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: 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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.
  • CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad specificity.
  • SUBUNIT: 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.
  • INTERACTION:
    O60921:HUS1; NbExp=1; IntAct=EBI-603262, EBI-1056174;
    P22392:NME2; NbExp=1; IntAct=EBI-603262, EBI-713693;
    P25789:PSMA4; NbExp=3; IntAct=EBI-603262, EBI-359310;
    O14818:PSMA7; NbExp=1; IntAct=EBI-603262, EBI-603272;
    Q15008:PSMD6; NbExp=1; IntAct=EBI-603262, EBI-359701;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • PTM: Phosphorylated on tyrosine residues; which may be important for nuclear import (By similarity).
  • SIMILARITY: Belongs to the peptidase T1A family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D00760; BAA00657.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002900; AAH02900.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047697; AAH47697.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15970; SNHUC3.
RefSeq NP_002778.1; -.
UniGene Hs.333786
3D structure databases
HSSP P23639; 1RYP. [HSSP ENTRY / PDB]
ModBase P25787.
Protein-protein interaction databases
IntAct P25787; -.
Protein family/group databases
MEROPS T01.972; -.
PTM databases
PhosphoSite P25787; -.
Enzyme and pathway databases
Reactome REACT_11045; Signaling by Wnt.
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
REACT_6185; HIV Infection.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
2D gel databases
OGP P25787; -.
REPRODUCTION-2DPAGE IPI00219622; -.
Organism-specific databases
H-InvDB HIX0025313; -.
HGNC HGNC:9531; PSMA2.
GenAtlas PSMA2.
HPA HPA008188; -.
MIM 176842; gene. [NCBI / EBI]
PharmGKB PA33876; -.
GeneCards P25787.
Gene expression databases
ArrayExpress P25787; -.
CleanEx HS_PSMA2; -.
GermOnline ENSG00000106588; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005839; Cellular component: proteasome core complex (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004298; Molecular function: threonine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR001353; Proteasome_A_B_su.
IPR000426; Proteasome_alpha_CS.
Graphical view of domain structure.
Pfam PF00227; Proteasome; 1.
Pfam graphical view of domain structure.
PROSITE PS00388; PROTEASOME_A; 1.
BLOCKS P25787.
ProtoNet P25787.
Proteomic databases
PeptideAtlas P25787; -.
Genome annotation databases
Ensembl ENSG00000106588; Homo sapiens. [Contig view]
GeneID 5683; -.
KEGG hsa:5683; -.
Phylogenomic databases
HOGENOM P25787; -.
HOVERGEN P25787; -.
Other
LinkHub P25787; -.
NextBio 22068; -.
SOURCE PSMA2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Nitration; Nucleus; Phosphoprotein; Polymorphism; Protease; Proteasome; Threonine protease.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   234  233     Proteasome subunit alpha type-2. PRO_0000124077
MOD_RES   2     2        N-acetylalanine (By similarity). 
MOD_RES   24    24        Phosphotyrosine. 
MOD_RES   57    57        Phosphotyrosine. 
MOD_RES   76    76        Phosphotyrosine. 
MOD_RES   98    98        Phosphotyrosine. 
MOD_RES   121   121        Phosphotyrosine (By similarity). 
MOD_RES   229   229        Nitrated tyrosine. 
VARIANT   110   110  1     L -> V (in a colorectal cancer sample; somatic mutation). VAR_036278 
Sequence information
Length: 234 AA [This is the length of the unprocessed precursor] Molecular weight: 25899 Da [This is the MW of the unprocessed precursor] CRC64: 63CB56A233583836 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER 

        70         80         90        100        110        120 
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE 

       130        140        150        160        170        180 
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE 

       190        200        210        220        230 
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA 

P25787 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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