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Protein

Proteasome activator complex subunit 2

Gene

Psme2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • endopeptidase activator activity Source: MGI

GO - Biological processi

  • antigen processing and presentation of exogenous antigen Source: MGI
  • positive regulation of endopeptidase activity Source: GOC
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Psme2
Synonyms:Pa28b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 11, Chromosome 14

Organism-specific databases

MGIiMGI:1096365. Psme2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 239238Proteasome activator complex subunit 2PRO_0000161786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei10 – 101PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP97372.
PaxDbiP97372.
PRIDEiP97372.

PTM databases

iPTMnetiP97372.
PhosphoSiteiP97372.
SwissPalmiP97372.

Expressioni

Inductioni

By interferon gamma.

Gene expression databases

BgeeiP97372.
CleanExiMM_PSME2.
ExpressionAtlasiP97372. baseline and differential.
GenevisibleiP97372. MM.

Interactioni

Subunit structurei

Heterodimer of PSME1 and PSME2, which forms a hexameric ring.

Protein-protein interaction databases

BioGridi202433. 1 interaction.
IntActiP97372. 4 interactions.
MINTiMINT-1856584.
STRINGi10090.ENSMUSP00000123798.

Structurei

3D structure databases

ProteinModelPortaliP97372.
SMRiP97372. Positions 7-66, 97-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PA28 family.Curated

Phylogenomic databases

eggNOGiKOG4470. Eukaryota.
ENOG410XQVX. LUCA.
HOGENOMiHOG000282822.
HOVERGENiHBG053745.
InParanoidiP97372.
KOiK06697.
OMAiTVPKCGF.
OrthoDBiEOG7GTT4C.
PhylomeDBiP97372.
TreeFamiTF106236.

Family and domain databases

Gene3Di1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProiIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERiPTHR10660. PTHR10660. 1 hit.
PfamiPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMiSSF47216. SSF47216. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKPCGVRLS GEARKQVDVF RQNLFQEADD FLCTFLPRKI ISLSQLLQED
60 70 80 90 100
SLNVADLSSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGYLPGNEKL
110 120 130 140 150
LALLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV
160 170 180 190 200
NAVKTKVEAF QTTISKYFSE RGDAVAKASK DTHVMDYRAL VHERDEAAYG
210 220 230
ALRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY
Length:239
Mass (Da):27,057
Last modified:January 23, 2007 - v4
Checksum:iD8BB90F78CB0DD7C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521A → P in AAC53296 (PubMed:9590240).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60329 mRNA. Translation: AAC53296.1.
AB007138 Genomic DNA. Translation: BAA28837.1.
AF060195 Genomic DNA. Translation: AAC83999.1.
AB053120 Genomic DNA. Translation: BAB47405.1.
AK012344 mRNA. Translation: BAB28175.1.
BC005680 mRNA. Translation: AAH05680.1.
BC057859 mRNA. Translation: AAH57859.1.
CCDSiCCDS49494.1.
RefSeqiNP_001025026.1. NM_001029855.1.
NP_001268401.1. NM_001281472.1.
NP_035320.1. NM_011190.3.
UniGeneiMm.371573.
Mm.440151.
Mm.441306.

Genome annotation databases

EnsembliENSMUST00000104958; ENSMUSP00000100564; ENSMUSG00000078153.
ENSMUST00000161807; ENSMUSP00000123798; ENSMUSG00000079197.
GeneIDi19188.
621823.
KEGGimmu:19188.
mmu:621823.
UCSCiuc007tzg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60329 mRNA. Translation: AAC53296.1.
AB007138 Genomic DNA. Translation: BAA28837.1.
AF060195 Genomic DNA. Translation: AAC83999.1.
AB053120 Genomic DNA. Translation: BAB47405.1.
AK012344 mRNA. Translation: BAB28175.1.
BC005680 mRNA. Translation: AAH05680.1.
BC057859 mRNA. Translation: AAH57859.1.
CCDSiCCDS49494.1.
RefSeqiNP_001025026.1. NM_001029855.1.
NP_001268401.1. NM_001281472.1.
NP_035320.1. NM_011190.3.
UniGeneiMm.371573.
Mm.440151.
Mm.441306.

3D structure databases

ProteinModelPortaliP97372.
SMRiP97372. Positions 7-66, 97-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202433. 1 interaction.
IntActiP97372. 4 interactions.
MINTiMINT-1856584.
STRINGi10090.ENSMUSP00000123798.

PTM databases

iPTMnetiP97372.
PhosphoSiteiP97372.
SwissPalmiP97372.

Proteomic databases

EPDiP97372.
PaxDbiP97372.
PRIDEiP97372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000104958; ENSMUSP00000100564; ENSMUSG00000078153.
ENSMUST00000161807; ENSMUSP00000123798; ENSMUSG00000079197.
GeneIDi19188.
621823.
KEGGimmu:19188.
mmu:621823.
UCSCiuc007tzg.1. mouse.

Organism-specific databases

CTDi5721.
621823.
MGIiMGI:1096365. Psme2.

Phylogenomic databases

eggNOGiKOG4470. Eukaryota.
ENOG410XQVX. LUCA.
HOGENOMiHOG000282822.
HOVERGENiHBG053745.
InParanoidiP97372.
KOiK06697.
OMAiTVPKCGF.
OrthoDBiEOG7GTT4C.
PhylomeDBiP97372.
TreeFamiTF106236.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69481. G2/M Checkpoints.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiP97372.
SOURCEiSearch...

Gene expression databases

BgeeiP97372.
CleanExiMM_PSME2.
ExpressionAtlasiP97372. baseline and differential.
GenevisibleiP97372. MM.

Family and domain databases

Gene3Di1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProiIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERiPTHR10660. PTHR10660. 1 hit.
PfamiPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMiSSF47216. SSF47216. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and expression of mouse proteasome activator PA28 and the related autoantigen Ki."
    Jiang H., Monaco J.J.
    Immunogenetics 46:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.BR.
  2. "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].
    Strain: 129/SvJ.
  3. "Characterization of the mouse proteasome regulator PA28b gene."
    Li Y., Chambers J., Pang J., Ngo K., Peterson P.A., Leung W.P., Yang Y.
    Immunogenetics 49:149-157(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  4. "Nucleotide sequence analysis of the ~35-kb segment containing interferon-gamma-inducible mouse proteasome activator genes."
    Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.
    Immunogenetics 53:119-129(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  6. "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: Mammary gland.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPSME2_MOUSE
AccessioniPrimary (citable) accession number: P97372
Secondary accession number(s): O35562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.