PSMG1_MOUSE
ID PSMG1_MOUSE Reviewed; 289 AA.
AC Q9JK23; Q8BU12;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Proteasome assembly chaperone 1;
DE AltName: Full=Down syndrome critical region protein 2 homolog;
GN Name=Psmg1 {ECO:0000312|MGI:MGI:1860263};
GN Synonyms=Dscr2 {ECO:0000312|MGI:MGI:1860263};
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] {ECO:0000305, ECO:0000312|EMBL:CAB87195.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10872820; DOI=10.1006/bbrc.2000.2726;
RA Vidal-Taboada J.M., Lu A., Pique M., Pons G., Gil J., Oliva R.;
RT "Down syndrome critical region gene 2: expression during mouse development
RT and in human cell lines indicates a function related to cell
RT proliferation.";
RL Biochem. Biophys. Res. Commun. 272:156-163(2000).
RN [2] {ECO:0000312|EMBL:BAC31197.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31197.1}, and
RC NOD {ECO:0000312|EMBL:BAC40157.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:BAC31197.1};
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 [3] {ECO:0000312|EMBL:AAH32965.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH32965.1};
RC TISSUE=Limb {ECO:0000312|EMBL:AAH60285.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH32965.1};
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 [4]
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).
CC -!- FUNCTION: Chaperone protein which promotes assembly of the 20S
CC proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2
CC heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes
CC assembly of the proteasome alpha subunits into the heteroheptameric
CC alpha ring and prevents alpha ring dimerization (By similarity).
CC {ECO:0000250|UniProtKB:O95456}.
CC -!- SUBUNIT: Forms a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer
CC interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits
CC (By similarity). {ECO:0000250|UniProtKB:O95456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95456}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:O95456}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis with moderate expression
CC in brain, liver and kidney and low levels in heart, skeletal muscle and
CC pancreas. {ECO:0000269|PubMed:10872820}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a fairly constant level throughout
CC embryonic development. {ECO:0000269|PubMed:10872820}.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation. {ECO:0000250|UniProtKB:O95456}.
CC -!- SIMILARITY: Belongs to the PSMG1 family. {ECO:0000255}.
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DR EMBL; AJ238270; CAB87195.1; -; mRNA.
DR EMBL; AK042203; BAC31197.1; -; mRNA.
DR EMBL; AK088118; BAC40157.1; -; mRNA.
DR EMBL; BC032965; AAH32965.1; -; mRNA.
DR EMBL; BC060285; AAH60285.1; -; mRNA.
DR CCDS; CCDS28352.1; -.
DR PIR; JC7279; JC7279.
DR RefSeq; NP_062410.1; NM_019537.3.
DR AlphaFoldDB; Q9JK23; -.
DR BioGRID; 207810; 15.
DR IntAct; Q9JK23; 1.
DR MINT; Q9JK23; -.
DR STRING; 10090.ENSMUSP00000023630; -.
DR iPTMnet; Q9JK23; -.
DR PhosphoSitePlus; Q9JK23; -.
DR SwissPalm; Q9JK23; -.
DR EPD; Q9JK23; -.
DR jPOST; Q9JK23; -.
DR MaxQB; Q9JK23; -.
DR PaxDb; Q9JK23; -.
DR PeptideAtlas; Q9JK23; -.
DR PRIDE; Q9JK23; -.
DR ProteomicsDB; 301865; -.
DR Antibodypedia; 23276; 219 antibodies from 34 providers.
DR DNASU; 56088; -.
DR Ensembl; ENSMUST00000023630; ENSMUSP00000023630; ENSMUSG00000022913.
DR GeneID; 56088; -.
DR KEGG; mmu:56088; -.
DR UCSC; uc008ach.1; mouse.
DR CTD; 8624; -.
DR MGI; MGI:1860263; Psmg1.
DR VEuPathDB; HostDB:ENSMUSG00000022913; -.
DR eggNOG; ENOG502QTPH; Eukaryota.
DR GeneTree; ENSGT00500000044950; -.
DR HOGENOM; CLU_083637_0_0_1; -.
DR InParanoid; Q9JK23; -.
DR OMA; FDCLQHR; -.
DR OrthoDB; 1232038at2759; -.
DR PhylomeDB; Q9JK23; -.
DR TreeFam; TF331909; -.
DR BioGRID-ORCS; 56088; 16 hits in 70 CRISPR screens.
DR ChiTaRS; Psmg1; mouse.
DR PRO; PR:Q9JK23; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JK23; protein.
DR Bgee; ENSMUSG00000022913; Expressed in otic placode and 277 other tissues.
DR ExpressionAtlas; Q9JK23; baseline and differential.
DR Genevisible; Q9JK23; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0070628; F:proteasome binding; IDA:MGI.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IMP:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:UniProtKB.
DR GO; GO:0080129; P:proteasome core complex assembly; IMP:MGI.
DR InterPro; IPR016565; Proteasome_assmbl_chp_1.
DR PANTHER; PTHR15069; PTHR15069; 1.
DR Pfam; PF16094; PAC1; 1.
DR PIRSF; PIRSF010076; Psome_chaperone-1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Endoplasmic reticulum; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT CHAIN 2..289
FT /note="Proteasome assembly chaperone 1"
FT /id="PRO_0000322547"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95456"
FT CONFLICT 39
FT /note="R -> A (in Ref. 2; BAC40157)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="I -> T (in Ref. 2; BAC40157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 33104 MW; FEB4F7FDDC020F06 CRC64;
MAATFFGEVV KAPCRAGTEE EEEEEEQSRR DTPEDREVRR QLARKREVRL LRRQTETSLE
AVLLETHPCS KFIIAVGSNA TAFLSAFVMN SGVWEEVGCA KLWNEWCRTT DTVRLSPTDV
FCVFYQLKSD PSVFLCQCSC YIAEDQQFQW LEKVFGFQPR KSMQVTVLTC RHITDYKTPE
STCSLSSPFL RALKTQTFKD ALCCPLLEQP NIVHDLSAAV LSYCQVWKIP AVLYLCYTDV
MKLDRVTVEA FKPLLSSRSL KCLVKNIPES TEILKKLMTT NEIQSNIYT
