PSMD2_MOUSE
ID PSMD2_MOUSE Reviewed; 908 AA.
AC Q8VDM4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
DE AltName: Full=26S proteasome regulatory subunit RPN1;
DE AltName: Full=26S proteasome regulatory subunit S2;
DE AltName: Full=26S proteasome subunit p97;
GN Name=Psmd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, AND ACETYLATION AT
RP MET-1.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-9, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-361, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-551, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP INTERACTION WITH RPGRIP1L.
RX PubMed=26150391; DOI=10.1083/jcb.201408060;
RA Gerhardt C., Lier J.M., Burmuehl S., Struchtrup A., Deutschmann K.,
RA Vetter M., Leu T., Reeg S., Grune T., Ruether U.;
RT "The transition zone protein Rpgrip1l regulates proteasomal activity at the
RT primary cilium.";
RL J. Cell Biol. 210:115-133(2015).
RN [8]
RP INTERACTION WITH CRY1.
RX PubMed=30500822; DOI=10.1371/journal.pbio.2006145;
RA Saran A.R., Kalinowska D., Oh S., Janknecht R., DiTacchio L.;
RT "JMJD5 links CRY1 function and proteasomal degradation.";
RL PLoS Biol. 16:E2006145-E2006145(2018).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. {ECO:0000250|UniProtKB:Q13200}.
CC -!- FUNCTION: Binds to the intracellular domain of tumor necrosis factor
CC type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside
CC the death domain of TNFR1. {ECO:0000250|UniProtKB:Q13200}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases and few additional
CC components including PSMD2 (By similarity). Interacts with RPGRIP1L
CC (PubMed:26150391). Interacts with CRY1 in a KDM8-dependent manner
CC (PubMed:30500822). {ECO:0000250|UniProtKB:Q13200,
CC ECO:0000269|PubMed:26150391, ECO:0000269|PubMed:30500822}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR EMBL; BC021508; AAH21508.1; -; mRNA.
DR EMBL; BC024830; AAH24830.1; -; mRNA.
DR EMBL; BC027388; AAH27388.1; -; mRNA.
DR EMBL; BC027767; AAH27767.1; -; mRNA.
DR EMBL; BC027822; AAH27822.1; -; mRNA.
DR EMBL; BC028851; AAH28851.1; -; mRNA.
DR EMBL; BC031128; AAH31128.1; -; mRNA.
DR CCDS; CCDS28053.1; -.
DR RefSeq; NP_598862.1; NM_134101.2.
DR AlphaFoldDB; Q8VDM4; -.
DR SMR; Q8VDM4; -.
DR BioGRID; 204127; 69.
DR IntAct; Q8VDM4; 5.
DR STRING; 10090.ENSMUSP00000007212; -.
DR iPTMnet; Q8VDM4; -.
DR PhosphoSitePlus; Q8VDM4; -.
DR SwissPalm; Q8VDM4; -.
DR EPD; Q8VDM4; -.
DR jPOST; Q8VDM4; -.
DR MaxQB; Q8VDM4; -.
DR PaxDb; Q8VDM4; -.
DR PRIDE; Q8VDM4; -.
DR ProteomicsDB; 301990; -.
DR Antibodypedia; 33807; 606 antibodies from 36 providers.
DR DNASU; 21762; -.
DR Ensembl; ENSMUST00000007212; ENSMUSP00000007212; ENSMUSG00000006998.
DR GeneID; 21762; -.
DR KEGG; mmu:21762; -.
DR UCSC; uc007yqq.2; mouse.
DR CTD; 5708; -.
DR MGI; MGI:1096584; Psmd2.
DR VEuPathDB; HostDB:ENSMUSG00000006998; -.
DR eggNOG; KOG2005; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q8VDM4; -.
DR OMA; KTVYKHM; -.
DR OrthoDB; 229956at2759; -.
DR PhylomeDB; Q8VDM4; -.
DR TreeFam; TF105739; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 21762; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Psmd2; mouse.
DR PRO; PR:Q8VDM4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8VDM4; protein.
DR Bgee; ENSMUSG00000006998; Expressed in embryonic brain and 70 other tissues.
DR ExpressionAtlas; Q8VDM4; baseline and differential.
DR Genevisible; Q8VDM4; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:MGI.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:MGI.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF11; PTHR10943:SF11; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..908
FT /note="26S proteasome non-ATPase regulatory subunit 2"
FT /id="PRO_0000173811"
FT REPEAT 409..442
FT /note="PC 1"
FT REPEAT 443..479
FT /note="PC 2"
FT REPEAT 480..514
FT /note="PC 3"
FT REPEAT 517..551
FT /note="PC 4"
FT REPEAT 560..589
FT /note="PC 5"
FT REPEAT 692..723
FT /note="PC 6"
FT REPEAT 742..757
FT /note="PC 7"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:16857966,
FT ECO:0007744|PubMed:17242355"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 194
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13200"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 908 AA; 100203 MW; 1EE5BC93298C2208 CRC64;
MEEGGRDKTP VQSQQPSATT PSGADEKSSG KERRDAGEKD KEQELSEEDK QLQDELEMLV
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKC
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKAQ
REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV
PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG
SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW
DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ
TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI
AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE
VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL
PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL
RKNPNYDL
