PSMG2_MOUSE
ID PSMG2_MOUSE Reviewed; 264 AA.
AC Q9EST4; Q3TII5; Q3UXH7; Q8C1R5; Q91YJ0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Proteasome assembly chaperone 2;
DE AltName: Full=CD40 ligand-activated specific transcript 3;
DE AltName: Full=Tumor necrosis factor superfamily member 5-induced protein 1;
GN Name=Psmg2 {ECO:0000312|MGI:MGI:1922901};
GN Synonyms=Clast3 {ECO:0000312|EMBL:BAB11962.1},
GN Tnfsf5ip1 {ECO:0000312|MGI:MGI:1922901};
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:BAB11962.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12147697; DOI=10.1074/jbc.m205345200;
RA Bahar R., O-Wang J., Kawamura K., Seimiya M., Wang Y., Hatano M., Okada S.,
RA Tokuhisa T., Watanabe T., Tagawa M.;
RT "Growth retardation, polyploidy, and multinucleation induced by Clast3, a
RT novel cell cycle-regulated protein.";
RL J. Biol. Chem. 277:40012-40019(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC36869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36869.1}, and
RC DBA/2J {ECO:0000312|EMBL:BAE39861.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC36869.1},
RC Embryonic gonad {ECO:0000312|EMBL:BAE22586.1},
RC Testis {ECO:0000312|EMBL:BAC25130.2}, and
RC Thymic lymphoma {ECO:0000312|EMBL:BAE39861.1};
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:0000305, ECO:0000312|EMBL:AAH16606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH16606.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH16606.1};
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=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 PSMG1. 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:Q969U7}.
CC -!- SUBUNIT: Forms a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer
CC interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits
CC (By similarity). {ECO:0000250|UniProtKB:Q969U7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12147697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12147697};
CC IsoId=Q9EST4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q9EST4-2; Sequence=VSP_052692, VSP_052693;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9EST4-3; Sequence=VSP_052691;
CC -!- DEVELOPMENTAL STAGE: Expression is elevated in proliferating cells and
CC down-regulated in cells undergoing growth arrest. During the cell
CC cycle, expression is low in G1-arrested cells, increases during S phase
CC and remains high at G2-M phase. {ECO:0000269|PubMed:12147697}.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation. {ECO:0000250|UniProtKB:Q969U7}.
CC -!- SIMILARITY: Belongs to the PSMG2 family. {ECO:0000255}.
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DR EMBL; AB031387; BAB11962.1; -; mRNA.
DR EMBL; AK006069; BAC25130.2; -; mRNA.
DR EMBL; AK077569; BAC36869.1; -; mRNA.
DR EMBL; AK135578; BAE22586.1; -; mRNA.
DR EMBL; AK167840; BAE39861.1; -; mRNA.
DR EMBL; BC016606; AAH16606.1; -; mRNA.
DR CCDS; CCDS29324.1; -. [Q9EST4-1]
DR CCDS; CCDS89268.1; -. [Q9EST4-3]
DR RefSeq; NP_598899.1; NM_134138.1. [Q9EST4-1]
DR AlphaFoldDB; Q9EST4; -.
DR SMR; Q9EST4; -.
DR BioGRID; 223192; 5.
DR STRING; 10090.ENSMUSP00000025418; -.
DR iPTMnet; Q9EST4; -.
DR PhosphoSitePlus; Q9EST4; -.
DR SwissPalm; Q9EST4; -.
DR EPD; Q9EST4; -.
DR jPOST; Q9EST4; -.
DR MaxQB; Q9EST4; -.
DR PaxDb; Q9EST4; -.
DR PeptideAtlas; Q9EST4; -.
DR PRIDE; Q9EST4; -.
DR ProteomicsDB; 301992; -. [Q9EST4-1]
DR ProteomicsDB; 301993; -. [Q9EST4-2]
DR ProteomicsDB; 301994; -. [Q9EST4-3]
DR Antibodypedia; 21950; 265 antibodies from 26 providers.
DR DNASU; 107047; -.
DR Ensembl; ENSMUST00000025418; ENSMUSP00000025418; ENSMUSG00000024537. [Q9EST4-1]
DR Ensembl; ENSMUST00000235799; ENSMUSP00000157785; ENSMUSG00000024537. [Q9EST4-3]
DR GeneID; 107047; -.
DR KEGG; mmu:107047; -.
DR UCSC; uc008fms.1; mouse. [Q9EST4-2]
DR UCSC; uc008fmt.1; mouse. [Q9EST4-1]
DR CTD; 56984; -.
DR MGI; MGI:1922901; Psmg2.
DR VEuPathDB; HostDB:ENSMUSG00000024537; -.
DR eggNOG; KOG3112; Eukaryota.
DR GeneTree; ENSGT00390000018415; -.
DR HOGENOM; CLU_062640_1_0_1; -.
DR InParanoid; Q9EST4; -.
DR OMA; WKEHTGE; -.
DR OrthoDB; 1522470at2759; -.
DR PhylomeDB; Q9EST4; -.
DR TreeFam; TF105397; -.
DR BioGRID-ORCS; 107047; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Psmg2; mouse.
DR PRO; PR:Q9EST4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9EST4; protein.
DR Bgee; ENSMUSG00000024537; Expressed in otic placode and 254 other tissues.
DR Genevisible; Q9EST4; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0043248; P:proteasome assembly; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR Gene3D; 3.40.50.10900; -; 2.
DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2.
DR InterPro; IPR016562; Proteasome_assmbl_chp_2_euk.
DR InterPro; IPR038389; PSMG2_sf.
DR PANTHER; PTHR12970; PTHR12970; 1.
DR Pfam; PF09754; PAC2; 1.
DR PIRSF; PIRSF010044; UCP010044; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..264
FT /note="Proteasome assembly chaperone 2"
FT /id="PRO_0000322553"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q969U7"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052691"
FT VAR_SEQ 97..161
FT /note="YKSKSFCEKLLAWVESSGCARIIVLSSSHSYHRNDAQLRSTPFRYLLTPCLQ
FT KSVQNKIKSLNWL -> VSMLAFLSSLMYGDRTQSLALRIKTNFIILFYILRKGLDLIK
FT NFIIFQVCYYHFIFILKEIVDYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052692"
FT VAR_SEQ 162..264
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052693"
FT CONFLICT 34
FT /note="L -> Q (in Ref. 3; AAH16606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29524 MW; 572AC760EDD7537E CRC64;
MFVPCGESVP DLTNFTLLMP AVSVGNVGQL AIDLIISTLN MCKIGYFYTD CLVPMVGNNP
YATEEENSNE LSINTEVYSL PSKKLVVLQL RSIFIKYKSK SFCEKLLAWV ESSGCARIIV
LSSSHSYHRN DAQLRSTPFR YLLTPCLQKS VQNKIKSLNW LEMEKSRCIP EMSDSEFCIR
IPGGGITKTL YDESCSKEIQ MAVLLKFVSE GDNIPDAVSL VEYLNEWLQI IKPCNDGPMA
SALPWKIPSS WRLLFGSGLP PALF
