EC 3.4.25.1
Proteasome component C2
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome nu chain
30 kDa prosomal protein
PROS-30

Gene name

	Name:	PSMA1
	Synonyms:	PROS30, PSC2

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=10.1016/0378-1119(92)90098-A; PubMed=1398136 [NCBI, ExPASy, EBI, Israel, Japan] Silva-Pereira I., Bey F., Coux O., Scherrer K.; "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes."; Gene 120:235-242(1992).
[2]	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).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4838(91)90020-Z; PubMed=1888762 [NCBI, ExPASy, EBI, Israel, Japan] DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.; "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."; Biochim. Biophys. Acta 1079:29-38(1991).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). TISSUE=Bone marrow, Brain, Ovary, Placenta, and Prostate; 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).
[5]	PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[6]	PROTEIN SEQUENCE OF 63-82. 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).
[7]	ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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]	UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-115 AND LYS-208, AND MASS SPECTROMETRY. DOI=10.1021/pr800468j; PubMed=18781797 [NCBI, ExPASy, EBI, Israel, Japan] Meierhofer D., Wang X., Huang L., Kaiser P.; "Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry."; J. Proteome Res. 7:4566-4576(2008).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

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.
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:
P25789:PSMA4; NbExp=1; IntAct=EBI-359352, EBI-359310;
O14818:PSMA7; NbExp=3; IntAct=EBI-359352, EBI-603272;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Short

Isoform ID P25786-1

This is the isoform sequence displayed in this entry.

Name Long

Isoform ID P25786-2

Features which should be applied to build the isoform sequence: VSP_005279.
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

M64992; AAA92734.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00759; BAA00656.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X61969; CAA43961.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002577; AAH02577.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005932; AAH05932.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008472; AAH08472.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009576; AAH09576.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015105; AAH15105.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015356; AAH15356.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022372; AAH22372.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00016832; -.
IPI00472442; -.

PIR

JC1445; JC1445.

RefSeq

NP_002777.1; -.
NP_683877.1; -.

UniGene

Hs.102798

3D structure databases

HSSP

P40302; 1RYP. [HSSP ENTRY / PDB]

SMR

P25786; 4-241.

ModBase

P25786.

Protein-protein interaction databases

IntAct

P25786; 44.

Protein family/group databases

MEROPS

T01.976; -.

PTM databases

PhosphoSite

P25786; -.

Enzyme and pathway databases

BRENDA

3.4.25.1; 247.

Reactome

REACT_11045; Signaling by Wnt.
REACT_13; Metabolism of amino acids.
REACT_13635; Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
REACT_578; Apoptosis.
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

Aarhus/Ghent-2DPAGE

2223; IEF.

OGP

P25786; -.

REPRODUCTION-2DPAGE

IPI00016832; -.

Organism-specific databases

GC11M014482; -.

HIX0009467; -.

HGNC:9530; PSMA1.

602854; gene. [NCBI / EBI]

PharmGKB

PA33875; -.

Gene expression databases

P25786; -.

P25786; -.

HS_PSMA1; -.

ENSG00000129084; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005844;	Cellular component: polysome (traceable author statement from ProtInc).
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:0003723;	Molecular function: RNA binding (traceable author statement from ProtInc).
GO:0004298;	Molecular function: threonine-type endopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
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_alpha_beta_su.
IPR000426; Proteasome_asu_CS.
Graphical view of domain structure.

Pfam

PF00227; Proteasome; 1.
PF10584; Proteasome_A_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00388; PROTEASOME_A; 1.

Proteomic databases

PRIDE

P25786; -.

Genome annotation databases

Ensembl

ENSG00000129084; Homo sapiens. [Contig view]

GeneID

5682; -.

KEGG

hsa:5682; -.

Phylogenomic databases

HOVERGEN

P25786; -.

OMA

P25786; YAVEAMK.

Other

22062; -.

PSMA1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Protease; Proteasome; Threonine protease; Ubl conjugation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 263`	`263`	`Proteasome subunit alpha type-1.`	`PRO_0000124060`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`MOD_RES`	`14 14`		`Phosphoserine.`
`CROSSLNK`	`115 115`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`CROSSLNK`	`208 208`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`VAR_SEQ`	`1 1`		`M -> MQLSKVK (in isoform Long).`	`VSP_005279`
`CONFLICT`	`37 37`		`G -> V (in Ref. 4; AAH05932).`

Sequence information

Length: 263 AA [This is the length of the unprocessed precursor]

Molecular weight: 29556 Da [This is the MW of the unprocessed precursor]

CRC64: 3F159C5BCEFE8DED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ 

        70         80         90        100        110        120 
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT 

       130        140        150        160        170        180 
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM 

       190        200        210        220        230        240 
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP 

       250        260 
QRKAQPAQPA DEPAEKADEP MEH

P25786 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools