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Q9UL46 (PSME2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome activator complex subunit 2
Alternative name(s):
11S regulator complex subunit beta
Short name=REG-beta
Activator of multicatalytic protease subunit 2
Proteasome activator 28 subunit beta
Short name=PA28b
Short name=PA28beta
Gene names
Name:PSME2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Induction

By IFNG/IFN-gamma.

Sequence similarities

Belongs to the PA28 family.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityPolymorphism
   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_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 239238Proteasome activator complex subunit 2
PRO_0000161785

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.9
Modified residue101Phosphoserine Ref.7

Natural variations

Natural variant891H → P. Ref.1 Ref.2 Ref.4
Corresponds to variant rs7146672 [ dbSNP | Ensembl ].
VAR_063111

Experimental info

Sequence conflict2291N → T in BAA08205. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UL46 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 98A30D83B3F93A91

FASTA23927,402
        10         20         30         40         50         60 
MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL 

        70         80         90        100        110        120 
RAPLDIPIPD PPPKDDEMET DKQEKKEVHK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL 

       130        140        150        160        170        180 
VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK 

       190        200        210        220        230 
ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY 

« Hide

References

« Hide 'large scale' references
[1]"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], VARIANT PRO-89.
[2]"Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome."
Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K., Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A., DeMartino G.N.
FEBS Lett. 366:37-42(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-89.
[3]"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].
[4]"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], VARIANT PRO-89.
Tissue: Liver, Pancreas and Placenta.
[5]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-61; 91-115; 132-145; 155-171; 181-226 AND 232-239, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"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.
[7]"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-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF079558 Genomic DNA. Translation: AAF02218.1.
D45248 mRNA. Translation: BAA08205.1.
AL136295 Genomic DNA. No translation available.
BC004368 mRNA. Translation: AAH04368.1.
BC019885 mRNA. Translation: AAH19885.1.
BC072025 mRNA. Translation: AAH72025.1.
PIRI53518.
RefSeqNP_002809.2. NM_002818.2.
UniGeneHs.434081.
Hs.512410.

3D structure databases

ProteinModelPortalQ9UL46.
SMRQ9UL46. Positions 7-66, 97-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111693. 39 interactions.
IntActQ9UL46. 13 interactions.
MINTMINT-1478095.
STRING9606.ENSP00000216802.

PTM databases

PhosphoSiteQ9UL46.

Polymorphism databases

DMDM296453017.

2D gel databases

OGPQ9UL46.
REPRODUCTION-2DPAGEIPI00384051.

Proteomic databases

PaxDbQ9UL46.
PRIDEQ9UL46.

Protocols and materials databases

DNASU5721.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216802; ENSP00000216802; ENSG00000100911.
GeneID5721.
KEGGhsa:5721.
UCSCuc001wmj.3. human.

Organism-specific databases

CTD5721.
GeneCardsGC14M024612.
HGNCHGNC:9569. PSME2.
MIM602161. gene.
neXtProtNX_Q9UL46.
PharmGKBPA33915.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280316.
HOGENOMHOG000282822.
HOVERGENHBG053745.
KOK06697.
OMADGFQTNI.
PhylomeDBQ9UL46.
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

BgeeQ9UL46.
CleanExHS_PSME2.
GenevestigatorQ9UL46.

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. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPSME2. human.
GeneWikiPSME2.
GenomeRNAi5721.
NextBio22238.
PROQ9UL46.
SOURCESearch...

Entry information

Entry namePSME2_HUMAN
AccessionPrimary (citable) accession number: Q9UL46
Secondary accession number(s): Q15129
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 128 of the entry and version 4 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

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