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P25789 (PSA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-4

EC=3.4.25.1
Alternative name(s):
Macropain subunit C9
Multicatalytic endopeptidase complex subunit C9
Proteasome component C9
Proteasome subunit L
Gene names
Name:PSMA4
Synonyms:HC9, PSC9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

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 with HTLV-1 TAX protein favors NFKB1 activation.

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-body By similarity. Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

Induction

Down-regulated by antioxidants BO-653 and probucol. Ref.8

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasmic mRNA processing body

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome core complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome core complex, alpha-subunit complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12376572PubMed 14733938PubMed 15225636PubMed 15887188PubMed 17948026. Source: IntAct

threonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P25789-1)

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.
Isoform 2 (identifier: P25789-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Proteasome subunit alpha type-4
PRO_0000124103

Amino acid modifications

Modified residue131Phosphoserine Ref.10 Ref.12
Modified residue751Phosphoserine Ref.9
Modified residue1271N6-acetyllysine Ref.11
Modified residue1761N6-acetyllysine Ref.11

Natural variations

Alternative sequence1 – 7171Missing in isoform 2.
VSP_043102

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 7867422B1B31F3B9

FASTA26129,484
        10         20         30         40         50         60 
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF 

        70         80         90        100        110        120 
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA 

       130        140        150        160        170        180 
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK 

       190        200        210        220        230        240 
EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH 

       250        260 
EEEEAKAERE KKEKEQKEKD K 

« Hide

Isoform 2 [UniParc].

Checksum: 0F5AC7AC01335F6A
Show »

FASTA19021,365

References

« Hide 'large scale' references
[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] (ISOFORM 1).
[3]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: Blood, Brain, Lung, 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 18-39.
[7]"Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome."
Rousset R., Desbois C., Bantignies F., Jalinot P.
Nature 381:328-331(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTLV-1 TAX.
[8]"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.
[9]"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-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-127 AND LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00763 mRNA. Translation: BAA00660.1.
BT009784 mRNA. Translation: AAP88786.1.
AC027228 Genomic DNA. No translation available.
CH471136 Genomic DNA. Translation: EAW99163.1.
CH471136 Genomic DNA. Translation: EAW99164.1.
BC005361 mRNA. Translation: AAH05361.1.
BC022445 mRNA. Translation: AAH22445.1.
BC022817 mRNA. Translation: AAH22817.2.
BC047667 mRNA. Translation: AAH47667.1.
BC093069 mRNA. Translation: AAH93069.1.
CCDSCCDS10303.1. [P25789-1]
CCDS45319.1. [P25789-2]
PIRSNHUC9. S15972.
RefSeqNP_001096137.1. NM_001102667.1. [P25789-1]
NP_001096138.1. NM_001102668.1. [P25789-2]
NP_002780.1. NM_002789.4. [P25789-1]
UniGeneHs.251531.

3D structure databases

ProteinModelPortalP25789.
SMRP25789. Positions 2-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111658. 83 interactions.
DIPDIP-29365N.
IntActP25789. 19 interactions.
MINTMINT-5002513.
STRING9606.ENSP00000044462.

Chemistry

ChEMBLCHEMBL2364701.

Protein family/group databases

MEROPST01.973.

PTM databases

PhosphoSiteP25789.

Polymorphism databases

DMDM130861.

2D gel databases

UCD-2DPAGEP25789.

Proteomic databases

MaxQBP25789.
PaxDbP25789.
PRIDEP25789.

Protocols and materials databases

DNASU5685.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000044462; ENSP00000044462; ENSG00000041357. [P25789-1]
ENST00000413382; ENSP00000402118; ENSG00000041357. [P25789-2]
ENST00000559082; ENSP00000453887; ENSG00000041357. [P25789-1]
GeneID5685.
KEGGhsa:5685.
UCSCuc002bdu.4. human. [P25789-1]

Organism-specific databases

CTD5685.
GeneCardsGC15P078832.
HGNCHGNC:9533. PSMA4.
HPACAB004973.
MIM176846. gene.
neXtProtNX_P25789.
PharmGKBPA33878.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091085.
HOVERGENHBG003005.
InParanoidP25789.
KOK02728.
OMAKQEYKDD.
PhylomeDBP25789.
TreeFamTF106209.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP25789.
BgeeP25789.
CleanExHS_PSMA4.
GenevestigatorP25789.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMA4. human.
GeneWikiPSMA4.
GenomeRNAi5685.
NextBio22078.
PROP25789.
SOURCESearch...

Entry information

Entry namePSA4_HUMAN
AccessionPrimary (citable) accession number: P25789
Secondary accession number(s): D3DW86 expand/collapse secondary AC list , Q53XP2, Q567Q5, Q8TBD1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM