PSMG2_HUMAN
ID PSMG2_HUMAN Reviewed; 264 AA.
AC Q969U7; B0YJB3; Q6IAH4; Q9NRV1; V9GYH7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Proteasome assembly chaperone 2;
DE Short=PAC-2;
DE AltName: Full=Hepatocellular carcinoma-susceptibility protein 3;
DE AltName: Full=Tumor necrosis factor superfamily member 5-induced protein 1;
GN Name=PSMG2 {ECO:0000312|EMBL:AAH13356.1};
GN Synonyms=HCCA3 {ECO:0000312|EMBL:AAK69439.2},
GN PAC2 {ECO:0000312|EMBL:FAA00023.1},
GN TNFSF5IP1 {ECO:0000312|HGNC:HGNC:24929};
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 2).
RC TISSUE=Hematopoietic stem cell;
RX PubMed=11920191; DOI=10.1038/sj/thj/6200020;
RA Gu J., Zhang Q.H., Huang Q.H., Ren S.X., Wu X.Y., Ye M., Huang C.H., Fu G.,
RA Zhou J., Niu C., Han Z.G., Chen S.J., Chen Z.;
RT "Gene expression in CD34(+) cells from normal bone marrow and leukemic
RT origins.";
RL Hematol. J. 1:206-217(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK69439.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta {ECO:0000269|PubMed:11854909};
RX PubMed=11854909; DOI=10.3748/wjg.v7.i6.821;
RA Wang Z.-X., Hu G.-F., Wang H.-Y., Wu M.-C.;
RT "Expression of liver cancer associated gene HCCA3.";
RL World J. Gastroenterol. 7:821-825(2001).
RN [3] {ECO:0000312|EMBL:EAX01540.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6] {ECO:0000312|EMBL:EAX01540.1}
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] {ECO:0000312|EMBL:AAH13356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas {ECO:0000312|EMBL:AAH13356.1};
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 [8] {ECO:0000312|EMBL:EAX01540.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-264 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [9] {ECO:0000305, ECO:0000312|EMBL:FAA00023.1}
RP IDENTIFICATION, FUNCTION, INTERACTION WITH PSMA5; PSMA7 AND PSMG1, AND
RP 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 [10] {ECO:0000305}
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP INVOLVEMENT IN PRAAS4, AND VARIANT PRAAS4 LYS-225.
RX PubMed=30664889; DOI=10.1016/j.jaci.2018.12.1012;
RA de Jesus A.A., Brehm A., VanTries R., Pillet P., Parentelli A.S.,
RA Montealegre Sanchez G.A., Deng Z., Paut I.K., Goldbach-Mansky R.,
RA Krueger E.;
RT "Novel proteasome assembly chaperone mutations in PSMG2/PAC2 cause the
RT autoinflammatory interferonopathy CANDLE/PRAAS4.";
RL J. Allergy Clin. Immunol. 143:1939-1943(2019).
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.
CC {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.
CC -!- SUBUNIT: Forms a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer
CC interacts directly with the PSMA5 and PSMA7 proteasome alpha subunits.
CC {ECO:0000269|PubMed:16251969}.
CC -!- INTERACTION:
CC Q969U7; Q15323: KRT31; NbExp=6; IntAct=EBI-723276, EBI-948001;
CC Q969U7; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-723276, EBI-945833;
CC Q969U7; O95456: PSMG1; NbExp=6; IntAct=EBI-723276, EBI-6286129;
CC Q969U7; P15884: TCF4; NbExp=3; IntAct=EBI-723276, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9EST4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969U7-2; Sequence=VSP_055721;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in lung, brain
CC and colon. Moderately expressed in muscle, stomach, spleen and heart.
CC Weakly expressed in small intestine, pancreas and liver. Highly
CC expressed in hepatocellular carcinomas with low levels in surrounding
CC liver tissue. {ECO:0000269|PubMed:11854909}.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation. {ECO:0000269|PubMed:16251969}.
CC -!- DISEASE: Proteasome-associated autoinflammatory syndrome 4 (PRAAS4)
CC [MIM:619183]: An autosomal recessive, autoinflammatory disorder
CC characterized by panniculitis and erythematous skin lesions apparent in
CC early infancy. Additional features include hepatosplenomegaly,
CC lymphadenopathy, autoimmune hemolytic anemia, fever, generalized
CC lipodystrophy, myositis, joint contractures, and mild motor and speech
CC delay. {ECO:0000269|PubMed:30664889}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PSMG2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF168712; AAF87314.1; ALT_INIT; mRNA.
DR EMBL; AF276707; AAK69439.2; -; mRNA.
DR EMBL; EF445040; ACA06090.1; -; Genomic_DNA.
DR EMBL; AK057005; BAG51841.1; -; mRNA.
DR EMBL; AP005482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471113; EAX01540.1; -; Genomic_DNA.
DR EMBL; CH471113; EAX01541.1; -; Genomic_DNA.
DR EMBL; BC013356; AAH13356.1; -; mRNA.
DR EMBL; CR457181; CAG33462.1; -; mRNA.
DR EMBL; BR000237; FAA00023.1; -; mRNA.
DR CCDS; CCDS11862.1; -. [Q969U7-1]
DR CCDS; CCDS67440.1; -. [Q969U7-2]
DR RefSeq; NP_064617.2; NM_020232.4. [Q969U7-1]
DR RefSeq; NP_671692.1; NM_147163.1. [Q969U7-2]
DR AlphaFoldDB; Q969U7; -.
DR SMR; Q969U7; -.
DR BioGRID; 121301; 68.
DR CORUM; Q969U7; -.
DR IntAct; Q969U7; 33.
DR MINT; Q969U7; -.
DR STRING; 9606.ENSP00000325919; -.
DR BindingDB; Q969U7; -.
DR ChEMBL; CHEMBL3885624; -.
DR iPTMnet; Q969U7; -.
DR PhosphoSitePlus; Q969U7; -.
DR SwissPalm; Q969U7; -.
DR BioMuta; PSMG2; -.
DR DMDM; 74731063; -.
DR EPD; Q969U7; -.
DR jPOST; Q969U7; -.
DR MassIVE; Q969U7; -.
DR MaxQB; Q969U7; -.
DR PaxDb; Q969U7; -.
DR PeptideAtlas; Q969U7; -.
DR PRIDE; Q969U7; -.
DR ProteomicsDB; 75848; -. [Q969U7-1]
DR Antibodypedia; 21950; 265 antibodies from 26 providers.
DR DNASU; 56984; -.
DR Ensembl; ENST00000317615.11; ENSP00000325919.6; ENSG00000128789.21. [Q969U7-1]
DR Ensembl; ENST00000585331.6; ENSP00000476763.1; ENSG00000128789.21. [Q969U7-2]
DR GeneID; 56984; -.
DR KEGG; hsa:56984; -.
DR MANE-Select; ENST00000317615.11; ENSP00000325919.6; NM_020232.5; NP_064617.2.
DR UCSC; uc002krg.5; human. [Q969U7-1]
DR CTD; 56984; -.
DR DisGeNET; 56984; -.
DR GeneCards; PSMG2; -.
DR HGNC; HGNC:24929; PSMG2.
DR HPA; ENSG00000128789; Low tissue specificity.
DR MalaCards; PSMG2; -.
DR MIM; 609702; gene.
DR MIM; 619183; phenotype.
DR neXtProt; NX_Q969U7; -.
DR OpenTargets; ENSG00000128789; -.
DR PharmGKB; PA162400246; -.
DR VEuPathDB; HostDB:ENSG00000128789; -.
DR eggNOG; KOG3112; Eukaryota.
DR GeneTree; ENSGT00390000018415; -.
DR HOGENOM; CLU_062640_1_1_1; -.
DR InParanoid; Q969U7; -.
DR OMA; WKEHTGE; -.
DR PhylomeDB; Q969U7; -.
DR TreeFam; TF105397; -.
DR PathwayCommons; Q969U7; -.
DR SignaLink; Q969U7; -.
DR BioGRID-ORCS; 56984; 439 hits in 1089 CRISPR screens.
DR ChiTaRS; PSMG2; human.
DR GenomeRNAi; 56984; -.
DR Pharos; Q969U7; Tbio.
DR PRO; PR:Q969U7; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q969U7; protein.
DR Bgee; ENSG00000128789; Expressed in adult organism and 207 other tissues.
DR ExpressionAtlas; Q969U7; baseline and differential.
DR Genevisible; Q969U7; HS.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IGI:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043248; P:proteasome assembly; IBA:GO_Central.
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_0000322552"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11920191"
FT /id="VSP_055721"
FT VARIANT 225
FT /note="N -> K (in PRAAS4; unknown pathological
FT significance; dbSNP:rs1323730269)"
FT /evidence="ECO:0000269|PubMed:30664889"
FT /id="VAR_085403"
FT CONFLICT 117
FT /note="R -> E (in Ref. 1; AAF87314)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> D (in Ref. 1; AAF87314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29396 MW; 7D138B81C3C20EF9 CRC64;
MFVPCGESAP DLAGFTLLMP AVSVGNVGQL AMDLIISTLN MSKIGYFYTD CLVPMVGNNP
YATTEGNSTE LSINAEVYSL PSRKLVALQL RSIFIKYKSK PFCEKLLSWV KSSGCARVIV
LSSSHSYQRN DLQLRSTPFR YLLTPSMQKS VQNKIKSLNW EEMEKSRCIP EIDDSEFCIR
IPGGGITKTL YDESCSKEIQ MAVLLKFVSE GDNIPDALGL VEYLNEWLQI LKPLSDDPTV
SASRWKIPSS WRLLFGSGLP PALF
