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Reviewed, UniProtKB/Swiss-Prot Q06323 (PSME1_HUMAN)

Last modified November 25, 2008. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Proteasome activator complex subunit 1
Alternative name(s):
    Proteasome activator 28 subunit alpha
      Short name=PA28alpha
      Short name=PA28a
    Activator of multicatalytic protease subunit 1
    11S regulator complex subunit alpha
      Short name=REG-alpha
    Interferon gamma up-regulated I-5111 protein
      Short name=IGUP I-5111
Gene names
Name: PSME1
Synonyms: IFI5111
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.

Subunit structure

Heterodimer of PSME1 and PSME2, which forms a hexadimeric ring. PSME1 can form homoheptamers.

Induction

By interferon gamma.

Sequence similarities

Belongs to the PA28 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Proteasome activator complex subunit 1
PRO_0000161779

Natural variations

Natural variant551S → N: dbSNP rs1803830.
VAR_011993
Natural variant2441T → K: dbSNP rs14930.
VAR_011994

Secondary structure

............... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06323-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5E27727E5A0B0AAB

FASTA24928,723
        10         20         30         40         50         60 
MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP 

        70         80         90        100        110        120 
LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE 

       130        140        150        160        170        180 
IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE 

       190        200        210        220        230        240 
RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP 


RGETKGMIY 

« Hide

References

« Hide 'large scale' references
[1]"Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111."
Honore B., Leffers H., Madsen P., Celis J.E.
Eur. J. Biochem. 218:421-430(1993) [PubMed: 8269930] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung fibroblast.
[2]"Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease."
Realini C., Dubiel W., Pratt G., Ferrell K., Rechsteiner M.
J. Biol. Chem. 269:20727-20732(1994) [PubMed: 8051173] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[3]"Organization of the genes encoding the human proteasome activators PA28alpha and beta."
McCusker D., Wilson M., Trowsdale J.
Immunogenetics 49:438-445(1999) [PubMed: 10199920] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[6]"Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes."
Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.
J. Immunol. 160:4923-4935(1998) [PubMed: 9590240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
[7]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209.
Tissue: Keratinocyte.
[8]"The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer."
Johnston S.C., Whitby F.G., Realini C., Rechsteiner M., Hill C.P.
Protein Sci. 6:2469-2473(1997) [PubMed: 9385652] [Abstract]
Cited for: SUBUNIT.
[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: 17323924] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], INTERACTION WITH PROTEASOME.
[10]"Structure of the proteasome activator REGalpha (PA28alpha)."
Knowlton J.R., Johnston S.C., Whitby F.G., Realini C., Zhang Z., Rechsteiner M., Hill C.P.
Nature 390:639-643(1997) [PubMed: 9403698] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

L07633 mRNA. Translation: AAA16521.1.
U10360 Genomic DNA. Translation: AAA53230.1.
AF078829 Genomic DNA. Translation: AAF02217.1.
BT019337 mRNA. Translation: AAV38144.1.
BC000352 mRNA. Translation: AAH00352.1.
BC007503 mRNA. Translation: AAH07503.1.
AB007137 Genomic DNA. Translation: BAA28836.1.
PIRA54859.
RefSeqNP_006254.1.
NP_788955.1.
UniGeneHs.75348

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AVOX-ray2.80A/C/E/G/I/K/M4-63[»]
B/D/F/H/J/L/N104-242[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ06323.

PTM databases

PhosphoSiteQ06323.

2-D gel databases

SWISS-2DPAGEQ06323.
Aarhus/Ghent-2DPAGE5111. IEF.
DOSAC-COBS-2DPAGEQ06323.
OGPQ06323.
PHCI-2DPAGEQ06323.

Genome annotation databases

EnsemblENSG00000092010. Homo sapiens. [Contig view]
GeneID5720.
KEGGhsa:5720.

Organism-specific databases

H-InvDBHIX0011554.
HGNCHGNC:9568. PSME1.
HPAHPA006632.
MIM600654. gene.
PharmGKBPA33914.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ06323.

Enzyme and pathway databases

ReactomeREACT_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.

Gene expression databases

ArrayExpressQ06323.
CleanExHS_PSME1.
GermOnlineENSG00000092010. Homo sapiens.

Family and domain databases

InterProIPR003185. Proteasome_activ_REG_asu.
IPR009077. Proteasome_activ_REG_asu/bsu.
IPR003186. Proteasome_activ_REG_bsu.
[Graphical view]
Gene3DG3DSA:1.20.5.120. PA28_alpha-like. 1 hit.
G3DSA:1.20.120.180. PA28_beta. 1 hit.
PANTHERPTHR10660. Proteasome_activ_REG_asu/bsu. 1 hit.
PfamPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ06323.
NextBio22232.
SOURCESearch...

Entry information

Entry namePSME1_HUMAN
AccessionPrimary (citable) accession number: Q06323
Secondary accession number(s): Q9UEF4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents