Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q06323 (PSME1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
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 hexameric ring. PSME1 can form homoheptamers. Ref.12

Induction

By IFNG/IFN-gamma.

Sequence similarities

Belongs to the PA28 family.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   Technical term3D-structure
Complete 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_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

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

nucleoplasm

Traceable author statement. Source: Reactome

proteasome activator complex

Inferred from electronic annotation. Source: InterPro

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

   Molecular_functionendopeptidase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q06323-1)

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: Q06323-2)

The sequence of this isoform differs from the canonical sequence as follows:
     224-249: AVLYDIILKNFEKLKKPRGETKGMIY → VRRQGQGRGGQRQLSQATHSLTLQARG
Note: Gene prediction based on EST data.
Isoform 3 (identifier: Q06323-3)

The sequence of this isoform differs from the canonical sequence as follows:
     224-233: AVLYDIILKN → VRRLCYMTSS
     234-249: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Proteasome activator complex subunit 1
PRO_0000161779

Natural variations

Alternative sequence224 – 24926AVLYD…KGMIY → VRRQGQGRGGQRQLSQATHS LTLQARG in isoform 2.
VSP_046880
Alternative sequence224 – 23310AVLYDIILKN → VRRLCYMTSS in isoform 3.
VSP_055166
Alternative sequence234 – 24916Missing in isoform 3.
VSP_055167
Natural variant551S → N.
Corresponds to variant rs1803830 [ dbSNP | Ensembl ].
VAR_011993
Natural variant2441T → K.
Corresponds to variant rs14930 [ dbSNP | Ensembl ].
VAR_011994

Secondary structure

............... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: D860008F47D35F97
Show »

FASTA25028,602
Isoform 3 [UniParc].

Checksum: 4B9A7BFE858CC6D9
Show »

FASTA23326,870

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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] (ISOFORM 1).
[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. expand/collapse author list , 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 1).
Tissue: Spleen.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton 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].
[9]"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].
Tissue: Muscle.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209.
Tissue: Keratinocyte.
[12]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[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]"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].
[15]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07633 mRNA. Translation: AAA16521.1.
U10360 Genomic DNA. Translation: AAA53230.1.
AF078829 Genomic DNA. Translation: AAF02217.1.
BT019337 mRNA. Translation: AAV38144.1.
AK312211 mRNA. Translation: BAG35144.1.
CR456780 mRNA. Translation: CAG33061.1.
AL136295 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66105.1.
BC000352 mRNA. Translation: AAH00352.1.
BC007503 mRNA. Translation: AAH07503.1.
AB007137 Genomic DNA. Translation: BAA28836.1.
CCDSCCDS41930.1. [Q06323-2]
CCDS9612.1. [Q06323-1]
PIRA54859.
RefSeqNP_006254.1. NM_006263.3. [Q06323-1]
UniGeneHs.75348.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVOX-ray2.80A/C/E/G/I/K/M4-63[»]
B/D/F/H/J/L/N104-242[»]
ProteinModelPortalQ06323.
SMRQ06323. Positions 4-63, 104-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111692. 59 interactions.
IntActQ06323. 20 interactions.
MINTMINT-5002728.
STRING9606.ENSP00000372155.

PTM databases

PhosphoSiteQ06323.

Polymorphism databases

DMDM1170519.

2D gel databases

DOSAC-COBS-2DPAGEQ06323.
OGPQ06323.
SWISS-2DPAGEQ06323.

Proteomic databases

MaxQBQ06323.
PaxDbQ06323.
PRIDEQ06323.

Protocols and materials databases

DNASU5720.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000206451; ENSP00000206451; ENSG00000092010. [Q06323-1]
ENST00000382708; ENSP00000372155; ENSG00000092010. [Q06323-2]
ENST00000561435; ENSP00000453976; ENSG00000092010.
GeneID5720.
KEGGhsa:5720.
UCSCuc001wmg.3. human. [Q06323-1]

Organism-specific databases

CTD5720.
GeneCardsGC14P024605.
HGNCHGNC:9568. PSME1.
HPAHPA006632.
MIM600654. gene.
neXtProtNX_Q06323.
PharmGKBPA33914.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265006.
HOGENOMHOG000282822.
HOVERGENHBG053745.
KOK06696.
OMAMINTQSE.
OrthoDBEOG7GTT4C.
PhylomeDBQ06323.
TreeFamTF106236.

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

ArrayExpressQ06323.
BgeeQ06323.
CleanExHS_PSME1.
GenevestigatorQ06323.

Family and domain databases

Gene3D1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERPTHR10660. PTHR10660. 1 hit.
PfamPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMSSF47216. SSF47216. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ06323.
GeneWikiPSME1.
GenomeRNAi5720.
NextBio22232.
PROQ06323.
SOURCESearch...

Entry information

Entry namePSME1_HUMAN
AccessionPrimary (citable) accession number: Q06323
Secondary accession number(s): A6NJG9 expand/collapse secondary AC list , H0YNE3, Q6IBM2, Q9UEF4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 140 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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