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Protein

26S proteasome non-ATPase regulatory subunit 2

Gene

Psmd2

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

Functioni

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.By similarity

GO - Molecular functioni

GO - Biological processi

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:
26S proteasome non-ATPase regulatory subunit 2
Alternative name(s):
26S proteasome regulatory subunit RPN1
26S proteasome regulatory subunit S2
26S proteasome subunit p97
Gene namesi
Name:Psmd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1096584. Psmd2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • nucleus Source: GO_Central
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: MGI
  • proteasome regulatory particle Source: MGI
  • proteasome regulatory particle, base subcomplex Source: GO_Central
  • proteasome storage granule Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 90890826S proteasome non-ATPase regulatory subunit 2PRO_0000173811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources1 Publication
Modified residuei9 – 91PhosphothreonineCombined sources
Modified residuei20 – 201PhosphothreonineCombined sources
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei194 – 1941PhosphotyrosineBy similarity
Modified residuei361 – 3611PhosphoserineCombined sources
Modified residuei363 – 3631PhosphoserineBy similarity
Modified residuei551 – 5511N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8VDM4.
MaxQBiQ8VDM4.
PaxDbiQ8VDM4.
PRIDEiQ8VDM4.

PTM databases

iPTMnetiQ8VDM4.
PhosphoSiteiQ8VDM4.
SwissPalmiQ8VDM4.

Expressioni

Gene expression databases

BgeeiQ8VDM4.
ExpressionAtlasiQ8VDM4. baseline and differential.
GenevisibleiQ8VDM4. MM.

Interactioni

Protein-protein interaction databases

BioGridi204127. 7 interactions.
IntActiQ8VDM4. 6 interactions.
MINTiMINT-4108957.
STRINGi10090.ENSMUSP00000007212.

Structurei

3D structure databases

ProteinModelPortaliQ8VDM4.
SMRiQ8VDM4. Positions 671-772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati409 – 44234PC 1Add
BLAST
Repeati443 – 47937PC 2Add
BLAST
Repeati480 – 51435PC 3Add
BLAST
Repeati517 – 55135PC 4Add
BLAST
Repeati560 – 58930PC 5Add
BLAST
Repeati692 – 72332PC 6Add
BLAST
Repeati742 – 75716PC 7Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi623 – 64119Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the proteasome subunit S2 family.Curated
Contains 7 PC repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2005. Eukaryota.
COG5110. LUCA.
GeneTreeiENSGT00550000074983.
HOGENOMiHOG000176022.
HOVERGENiHBG001842.
InParanoidiQ8VDM4.
KOiK03028.
OMAiIVQTIME.
OrthoDBiEOG70KGNV.
PhylomeDBiQ8VDM4.
TreeFamiTF105739.

Family and domain databases

InterProiIPR016643. 26S_Psome_Rpn1.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 2 hits.
[Graphical view]
PIRSFiPIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

Q8VDM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEGGRDKTP VQSQQPSATT PSGADEKSSG KERRDAGEKD KEQELSEEDK
60 70 80 90 100
QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR
110 120 130 140 150
PHYGKLKEIY ENMAPGENKC FAADIISVLA MTMSGERECL KYRLVGSQEE
160 170 180 190 200
LASWGHEYVR HLAGEVAKEW QELDDAEKAQ REPLLTLVKE IVPYNMAHNA
210 220 230 240 250
EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR
260 270 280 290 300
CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR
310 320 330 340 350
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK
360 370 380 390 400
THLENNRFGG SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY
410 420 430 440 450
KNKDHGMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI
460 470 480 490 500
VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA GSNREDVLTL
510 520 530 540 550
LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL
560 570 580 590 600
KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY
610 620 630 640 650
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ
660 670 680 690 700
GVAVLGIALI AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS
710 720 730 740 750
NPRLNILDTL SKFSHDADPE VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ
760 770 780 790 800
YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ VAVAGLLTVL
810 820 830 840 850
VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV
860 870 880 890 900
DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL

RKNPNYDL
Length:908
Mass (Da):100,203
Last modified:March 1, 2002 - v1
Checksum:i1EE5BC93298C2208
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC021508 mRNA. Translation: AAH21508.1.
BC024830 mRNA. Translation: AAH24830.1.
BC027388 mRNA. Translation: AAH27388.1.
BC027767 mRNA. Translation: AAH27767.1.
BC027822 mRNA. Translation: AAH27822.1.
BC028851 mRNA. Translation: AAH28851.1.
BC031128 mRNA. Translation: AAH31128.1.
CCDSiCCDS28053.1.
RefSeqiNP_598862.1. NM_134101.2.
UniGeneiMm.243234.
Mm.296792.

Genome annotation databases

EnsembliENSMUST00000007212; ENSMUSP00000007212; ENSMUSG00000006998.
GeneIDi21762.
KEGGimmu:21762.
UCSCiuc007yqq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC021508 mRNA. Translation: AAH21508.1.
BC024830 mRNA. Translation: AAH24830.1.
BC027388 mRNA. Translation: AAH27388.1.
BC027767 mRNA. Translation: AAH27767.1.
BC027822 mRNA. Translation: AAH27822.1.
BC028851 mRNA. Translation: AAH28851.1.
BC031128 mRNA. Translation: AAH31128.1.
CCDSiCCDS28053.1.
RefSeqiNP_598862.1. NM_134101.2.
UniGeneiMm.243234.
Mm.296792.

3D structure databases

ProteinModelPortaliQ8VDM4.
SMRiQ8VDM4. Positions 671-772.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204127. 7 interactions.
IntActiQ8VDM4. 6 interactions.
MINTiMINT-4108957.
STRINGi10090.ENSMUSP00000007212.

PTM databases

iPTMnetiQ8VDM4.
PhosphoSiteiQ8VDM4.
SwissPalmiQ8VDM4.

Proteomic databases

EPDiQ8VDM4.
MaxQBiQ8VDM4.
PaxDbiQ8VDM4.
PRIDEiQ8VDM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007212; ENSMUSP00000007212; ENSMUSG00000006998.
GeneIDi21762.
KEGGimmu:21762.
UCSCiuc007yqq.2. mouse.

Organism-specific databases

CTDi5708.
MGIiMGI:1096584. Psmd2.

Phylogenomic databases

eggNOGiKOG2005. Eukaryota.
COG5110. LUCA.
GeneTreeiENSGT00550000074983.
HOGENOMiHOG000176022.
HOVERGENiHBG001842.
InParanoidiQ8VDM4.
KOiK03028.
OMAiIVQTIME.
OrthoDBiEOG70KGNV.
PhylomeDBiQ8VDM4.
TreeFamiTF105739.

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

ChiTaRSiPsmd2. mouse.
PROiQ8VDM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDM4.
ExpressionAtlasiQ8VDM4. baseline and differential.
GenevisibleiQ8VDM4. MM.

Family and domain databases

InterProiIPR016643. 26S_Psome_Rpn1.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamiPF01851. PC_rep. 2 hits.
[Graphical view]
PIRSFiPIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMiSSF48371. SSF48371. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: Czech II and FVB/N.
    Tissue: Colon, Eye and Mammary tumor.
  2. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, ACETYLATION AT MET-1.
  3. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPSMD2_MOUSE
AccessioniPrimary (citable) accession number: Q8VDM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 114 of the entry and version 1 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.