PSMG1_HUMAN
ID PSMG1_HUMAN Reviewed; 288 AA.
AC O95456; B5BUN2; Q6FHA3; Q6FHD3; Q6S713;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Proteasome assembly chaperone 1;
DE Short=PAC-1;
DE AltName: Full=Chromosome 21 leucine-rich protein;
DE Short=C21-LRP;
DE AltName: Full=Down syndrome critical region protein 2;
GN Name=PSMG1; Synonyms=C21LRP, DSCR2, PAC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9784380; DOI=10.1006/bbrc.1998.9352;
RA Vidal-Taboada J.M., Sanz S., Egeo A., Scartezzini P., Oliva R.;
RT "Identification and characterization of a new gene from human chromosome 21
RT between markers D21S343 and D21S268 encoding a leucine-rich protein.";
RL Biochem. Biophys. Res. Commun. 250:547-554(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Sommer C.A., Abrao Possik P., Henrique-Silva F.;
RT "First clue of an alternative splicing event in DSCR2, a gene involved in
RT Down syndrome.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Muscle;
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 [8]
RP TISSUE SPECIFICITY.
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15590417;
RA Possik P.A., Sommer C.A., Issa Hori J., Machado-Santelli G.M., Jamur M.C.,
RA Henrique-Silva F.;
RT "DSCR2, a Down syndrome critical region protein, is localized to the
RT endoplasmic reticulum of mammalian cells.";
RL Eur. J. Histochem. 48:267-272(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15670775; DOI=10.1016/j.bbrc.2004.09.226;
RA Vesa J., Brown Y., Greenfield D., Korenberg J.R.;
RT "Molecular and cellular characterization of the Down syndrome critical
RT region protein 2.";
RL Biochem. Biophys. Res. Commun. 328:235-242(2005).
RN [11]
RP IDENTIFICATION (ISOFORM 1), FUNCTION, INTERACTION WITH PSMA5; PSMA7 AND
RP PSMG2, AND DEGRADATION BY THE PROTEASOME.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [12]
RP FUNCTION.
RX PubMed=17707236; DOI=10.1016/j.molcel.2007.06.025;
RA Le Tallec B., Barrault M.-B., Courbeyrette R., Guerois R.,
RA Marsolier-Kergoat M.-C., Peyroche A.;
RT "20S proteasome assembly is orchestrated by two distinct pairs of
RT chaperones in yeast and in mammals.";
RL Mol. Cell 27:660-674(2007).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; THR-54 AND SER-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
CC {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.
CC -!- SUBUNIT: Forms a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer
CC interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits.
CC {ECO:0000269|PubMed:16251969}.
CC -!- INTERACTION:
CC O95456; P31321: PRKAR1B; NbExp=3; IntAct=EBI-6286129, EBI-2805516;
CC O95456; Q969U7: PSMG2; NbExp=6; IntAct=EBI-6286129, EBI-723276;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95456-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95456-2; Sequence=VSP_017261;
CC -!- TISSUE SPECIFICITY: In the adult, detected in brain, colon, leukocytes,
CC breast and testis. Widely expressed in the fetus. Also expressed in a
CC variety of proliferating cell lines. {ECO:0000269|PubMed:10872820,
CC ECO:0000269|PubMed:9784380}.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation.
CC -!- SIMILARITY: Belongs to the PSMG1 family. {ECO:0000305}.
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DR EMBL; AJ006291; CAA06957.1; -; mRNA.
DR EMBL; AY463963; AAR25628.1; -; mRNA.
DR EMBL; CR541821; CAG46620.1; -; mRNA.
DR EMBL; CR541852; CAG46650.1; -; mRNA.
DR EMBL; AB451468; BAG70282.1; -; mRNA.
DR EMBL; AL163279; CAB90451.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09664.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09665.1; -; Genomic_DNA.
DR EMBL; BC003619; AAH03619.1; -; mRNA.
DR EMBL; BC010424; AAH10424.1; -; mRNA.
DR EMBL; BC011755; AAH11755.1; -; mRNA.
DR EMBL; BC012809; AAH12809.1; -; mRNA.
DR EMBL; BR000236; FAA00022.1; -; mRNA.
DR CCDS; CCDS13660.1; -. [O95456-1]
DR CCDS; CCDS13661.1; -. [O95456-2]
DR PIR; JE0290; JE0290.
DR RefSeq; NP_003711.1; NM_003720.3. [O95456-1]
DR RefSeq; NP_982257.1; NM_203433.2. [O95456-2]
DR AlphaFoldDB; O95456; -.
DR BioGRID; 114179; 64.
DR CORUM; O95456; -.
DR IntAct; O95456; 25.
DR MINT; O95456; -.
DR STRING; 9606.ENSP00000329915; -.
DR BindingDB; O95456; -.
DR ChEMBL; CHEMBL3885624; -.
DR GlyGen; O95456; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95456; -.
DR PhosphoSitePlus; O95456; -.
DR BioMuta; PSMG1; -.
DR EPD; O95456; -.
DR jPOST; O95456; -.
DR MassIVE; O95456; -.
DR MaxQB; O95456; -.
DR PaxDb; O95456; -.
DR PeptideAtlas; O95456; -.
DR PRIDE; O95456; -.
DR ProteomicsDB; 50890; -. [O95456-1]
DR ProteomicsDB; 50891; -. [O95456-2]
DR Antibodypedia; 23276; 219 antibodies from 34 providers.
DR DNASU; 8624; -.
DR Ensembl; ENST00000331573.8; ENSP00000329915.3; ENSG00000183527.12. [O95456-1]
DR Ensembl; ENST00000380900.2; ENSP00000370286.2; ENSG00000183527.12. [O95456-2]
DR GeneID; 8624; -.
DR KEGG; hsa:8624; -.
DR MANE-Select; ENST00000331573.8; ENSP00000329915.3; NM_003720.4; NP_003711.1.
DR UCSC; uc002yxi.5; human. [O95456-1]
DR CTD; 8624; -.
DR DisGeNET; 8624; -.
DR GeneCards; PSMG1; -.
DR HGNC; HGNC:3043; PSMG1.
DR HPA; ENSG00000183527; Tissue enhanced (testis).
DR MIM; 605296; gene.
DR neXtProt; NX_O95456; -.
DR OpenTargets; ENSG00000183527; -.
DR PharmGKB; PA162400229; -.
DR VEuPathDB; HostDB:ENSG00000183527; -.
DR eggNOG; ENOG502QTPH; Eukaryota.
DR GeneTree; ENSGT00500000044950; -.
DR HOGENOM; CLU_083637_0_0_1; -.
DR InParanoid; O95456; -.
DR OMA; FDCLQHR; -.
DR OrthoDB; 1232038at2759; -.
DR PhylomeDB; O95456; -.
DR TreeFam; TF331909; -.
DR PathwayCommons; O95456; -.
DR SignaLink; O95456; -.
DR BioGRID-ORCS; 8624; 430 hits in 1085 CRISPR screens.
DR GeneWiki; DSCR2; -.
DR GenomeRNAi; 8624; -.
DR Pharos; O95456; Tbio.
DR PRO; PR:O95456; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; O95456; protein.
DR Bgee; ENSG00000183527; Expressed in left testis and 98 other tissues.
DR ExpressionAtlas; O95456; baseline and differential.
DR Genevisible; O95456; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR GO; GO:0080129; P:proteasome core complex assembly; IBA:GO_Central.
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; Alternative splicing; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..288
FT /note="Proteasome assembly chaperone 1"
FT /id="PRO_0000080018"
FT REGION 13..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 132..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19054851, ECO:0000303|Ref.2"
FT /id="VSP_017261"
FT VARIANT 166
FT /note="I -> V (in dbSNP:rs8131611)"
FT /id="VAR_054014"
FT CONFLICT 4
FT /note="T -> S (in Ref. 3; CAG46650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32854 MW; 2D4A84485C290839 CRC64;
MAATFFGEVV KAPCRAGTED EEEEEEGRRE TPEDREVRLQ LARKREVRLL RRQTKTSLEV
SLLEKYPCSK FIIAIGNNAV AFLSSFVMNS GVWEEVGCAK LWNEWCRTTD TTHLSSTEAF
CVFYHLKSNP SVFLCQCSCY VAEDQQYQWL EKVFGSCPRK NMQITILTCR HVTDYKTSES
TGSLPSPFLR ALKTQNFKDS ACCPLLEQPN IVHDLPAAVL SYCQVWKIPA ILYLCYTDVM
KLDLITVEAF KPILSTRSLK GLVKNIPQST EILKKLMTTN EIQSNIYT
