PSMD1_MOUSE
ID PSMD1_MOUSE Reviewed; 953 AA.
AC Q3TXS7; B2RRP8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE AltName: Full=26S proteasome regulatory subunit RPN2;
DE AltName: Full=26S proteasome regulatory subunit S1;
GN Name=Psmd1;
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=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310 AND LYS-720, AND
RP IDENTIFICATION BY MASS 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).
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:Q99460}.
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 PSMD1. Interacts with ADRM1. Interacts with ZFAND1
CC (By similarity). {ECO:0000250|UniProtKB:Q99460}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; AK153386; BAE31950.1; -; mRNA.
DR EMBL; AK159123; BAE34838.1; -; mRNA.
DR EMBL; BC138526; AAI38527.1; -; mRNA.
DR EMBL; BC138527; AAI38528.1; -; mRNA.
DR CCDS; CCDS15117.1; -.
DR RefSeq; NP_081633.1; NM_027357.2.
DR AlphaFoldDB; Q3TXS7; -.
DR SMR; Q3TXS7; -.
DR BioGRID; 213938; 61.
DR IntAct; Q3TXS7; 6.
DR MINT; Q3TXS7; -.
DR STRING; 10090.ENSMUSP00000027432; -.
DR iPTMnet; Q3TXS7; -.
DR PhosphoSitePlus; Q3TXS7; -.
DR SwissPalm; Q3TXS7; -.
DR EPD; Q3TXS7; -.
DR jPOST; Q3TXS7; -.
DR MaxQB; Q3TXS7; -.
DR PaxDb; Q3TXS7; -.
DR PeptideAtlas; Q3TXS7; -.
DR PRIDE; Q3TXS7; -.
DR ProteomicsDB; 301989; -.
DR Antibodypedia; 34412; 138 antibodies from 22 providers.
DR Ensembl; ENSMUST00000027432; ENSMUSP00000027432; ENSMUSG00000026229.
DR GeneID; 70247; -.
DR KEGG; mmu:70247; -.
DR UCSC; uc007buy.1; mouse.
DR CTD; 5707; -.
DR MGI; MGI:1917497; Psmd1.
DR VEuPathDB; HostDB:ENSMUSG00000026229; -.
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; Q3TXS7; -.
DR OMA; MIMVQQN; -.
DR OrthoDB; 235012at2759; -.
DR PhylomeDB; Q3TXS7; -.
DR TreeFam; TF105742; -.
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; 70247; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Psmd1; mouse.
DR PRO; PR:Q3TXS7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3TXS7; protein.
DR Bgee; ENSMUSG00000026229; Expressed in presomitic mesoderm and 253 other tissues.
DR ExpressionAtlas; Q3TXS7; baseline and differential.
DR Genevisible; Q3TXS7; 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: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:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
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; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..953
FT /note="26S proteasome non-ATPase regulatory subunit 1"
FT /id="PRO_0000231598"
FT REPEAT 403..436
FT /note="PC 1"
FT REPEAT 441..474
FT /note="PC 2"
FT REPEAT 476..510
FT /note="PC 3"
FT REPEAT 511..545
FT /note="PC 4"
FT REPEAT 547..580
FT /note="PC 5"
FT REPEAT 581..616
FT /note="PC 6"
FT REPEAT 617..649
FT /note="PC 7"
FT REPEAT 651..685
FT /note="PC 8"
FT REPEAT 686..726
FT /note="PC 9"
FT REPEAT 729..761
FT /note="PC 10"
FT REGION 277..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 310
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 720
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99460"
SQ SEQUENCE 953 AA; 105730 MW; 40A72A08CFC778E6 CRC64;
MITSAAGIIS LLDEEEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE
GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS
LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDPMETE
EKTASAVAGK TPDASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL
QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG
LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ
HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR
RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC
AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK
HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK
KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLSMTETCRY
QPFKPLSIGG IIILKDTSED VEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD
