Full text data of PSMG2
PSMG2
(HCCA3, PAC2, TNFSF5IP1)
[Confidence: low (only semi-automatic identification from reviews)]
Proteasome assembly chaperone 2; PAC-2 (Hepatocellular carcinoma-susceptibility protein 3; Tumor necrosis factor superfamily member 5-induced protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome assembly chaperone 2; PAC-2 (Hepatocellular carcinoma-susceptibility protein 3; Tumor necrosis factor superfamily member 5-induced protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q969U7
ID PSMG2_HUMAN Reviewed; 264 AA.
AC Q969U7; B0YJB3; Q6IAH4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 90.
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; Synonyms=HCCA3, PAC2, TNFSF5IP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11854909;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-264.
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 [7]
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 [8]
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 [9]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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,
CC promotes assembly of the proteasome alpha subunits into the
CC heteroheptameric alpha ring and prevents alpha ring dimerization.
CC -!- SUBUNIT: Forms a heterodimer with PSMG1. The PSMG1-PSMG2
CC heterodimer interacts directly with the PSMA5 and PSMA7 proteasome
CC alpha subunits.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in lung,
CC brain and colon. Moderately expressed in muscle, stomach, spleen
CC and heart. Weakly expressed in small intestine, pancreas and
CC liver. Highly expressed in hepatocellular carcinomas with low
CC levels in surrounding liver tissue.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation.
CC -!- SIMILARITY: Belongs to the PSMG2 family.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF276707; AAK69439.2; -; mRNA.
DR EMBL; EF445040; ACA06090.1; -; Genomic_DNA.
DR EMBL; AK057005; BAG51841.1; -; mRNA.
DR EMBL; CH471113; EAX01540.1; -; Genomic_DNA.
DR EMBL; BC013356; AAH13356.1; -; mRNA.
DR EMBL; CR457181; CAG33462.1; -; mRNA.
DR EMBL; BR000237; FAA00023.1; -; mRNA.
DR RefSeq; NP_064617.2; NM_020232.4.
DR RefSeq; NP_671692.1; NM_147163.1.
DR UniGene; Hs.464652; -.
DR ProteinModelPortal; Q969U7; -.
DR IntAct; Q969U7; 4.
DR MINT; MINT-6176023; -.
DR STRING; 9606.ENSP00000325919; -.
DR BindingDB; Q969U7; -.
DR PhosphoSite; Q969U7; -.
DR DMDM; 74731063; -.
DR PaxDb; Q969U7; -.
DR PRIDE; Q969U7; -.
DR DNASU; 56984; -.
DR Ensembl; ENST00000317615; ENSP00000325919; ENSG00000128789.
DR GeneID; 56984; -.
DR KEGG; hsa:56984; -.
DR UCSC; uc002krg.3; human.
DR CTD; 56984; -.
DR GeneCards; GC18P012684; -.
DR HGNC; HGNC:24929; PSMG2.
DR HPA; HPA041517; -.
DR HPA; HPA046741; -.
DR MIM; 609702; gene.
DR neXtProt; NX_Q969U7; -.
DR PharmGKB; PA162400246; -.
DR eggNOG; NOG282678; -.
DR HOGENOM; HOG000046033; -.
DR HOVERGEN; HBG059464; -.
DR InParanoid; Q969U7; -.
DR KO; K11876; -.
DR OMA; QWKMPSS; -.
DR OrthoDB; EOG7BKCW2; -.
DR PhylomeDB; Q969U7; -.
DR ChiTaRS; PSMG2; human.
DR GenomeRNAi; 56984; -.
DR NextBio; 62663; -.
DR PRO; PR:Q969U7; -.
DR ArrayExpress; Q969U7; -.
DR Bgee; Q969U7; -.
DR CleanEx; HS_PSMG2; -.
DR Genevestigator; Q969U7; -.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; IEA:Ensembl.
DR GO; GO:0043248; P:proteasome assembly; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2.
DR InterPro; IPR016562; Proteasome_assmbl_chp_2_euk.
DR Pfam; PF09754; PAC2; 1.
DR PIRSF; PIRSF010044; UCP010044; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Nucleus; Reference proteome.
FT CHAIN 1 264 Proteasome assembly chaperone 2.
FT /FTId=PRO_0000322552.
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
//
ID PSMG2_HUMAN Reviewed; 264 AA.
AC Q969U7; B0YJB3; Q6IAH4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 90.
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; Synonyms=HCCA3, PAC2, TNFSF5IP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11854909;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-264.
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 [7]
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 [8]
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 [9]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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,
CC promotes assembly of the proteasome alpha subunits into the
CC heteroheptameric alpha ring and prevents alpha ring dimerization.
CC -!- SUBUNIT: Forms a heterodimer with PSMG1. The PSMG1-PSMG2
CC heterodimer interacts directly with the PSMA5 and PSMA7 proteasome
CC alpha subunits.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in lung,
CC brain and colon. Moderately expressed in muscle, stomach, spleen
CC and heart. Weakly expressed in small intestine, pancreas and
CC liver. Highly expressed in hepatocellular carcinomas with low
CC levels in surrounding liver tissue.
CC -!- PTM: Degraded by the proteasome upon completion of 20S proteasome
CC maturation.
CC -!- SIMILARITY: Belongs to the PSMG2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF276707; AAK69439.2; -; mRNA.
DR EMBL; EF445040; ACA06090.1; -; Genomic_DNA.
DR EMBL; AK057005; BAG51841.1; -; mRNA.
DR EMBL; CH471113; EAX01540.1; -; Genomic_DNA.
DR EMBL; BC013356; AAH13356.1; -; mRNA.
DR EMBL; CR457181; CAG33462.1; -; mRNA.
DR EMBL; BR000237; FAA00023.1; -; mRNA.
DR RefSeq; NP_064617.2; NM_020232.4.
DR RefSeq; NP_671692.1; NM_147163.1.
DR UniGene; Hs.464652; -.
DR ProteinModelPortal; Q969U7; -.
DR IntAct; Q969U7; 4.
DR MINT; MINT-6176023; -.
DR STRING; 9606.ENSP00000325919; -.
DR BindingDB; Q969U7; -.
DR PhosphoSite; Q969U7; -.
DR DMDM; 74731063; -.
DR PaxDb; Q969U7; -.
DR PRIDE; Q969U7; -.
DR DNASU; 56984; -.
DR Ensembl; ENST00000317615; ENSP00000325919; ENSG00000128789.
DR GeneID; 56984; -.
DR KEGG; hsa:56984; -.
DR UCSC; uc002krg.3; human.
DR CTD; 56984; -.
DR GeneCards; GC18P012684; -.
DR HGNC; HGNC:24929; PSMG2.
DR HPA; HPA041517; -.
DR HPA; HPA046741; -.
DR MIM; 609702; gene.
DR neXtProt; NX_Q969U7; -.
DR PharmGKB; PA162400246; -.
DR eggNOG; NOG282678; -.
DR HOGENOM; HOG000046033; -.
DR HOVERGEN; HBG059464; -.
DR InParanoid; Q969U7; -.
DR KO; K11876; -.
DR OMA; QWKMPSS; -.
DR OrthoDB; EOG7BKCW2; -.
DR PhylomeDB; Q969U7; -.
DR ChiTaRS; PSMG2; human.
DR GenomeRNAi; 56984; -.
DR NextBio; 62663; -.
DR PRO; PR:Q969U7; -.
DR ArrayExpress; Q969U7; -.
DR Bgee; Q969U7; -.
DR CleanEx; HS_PSMG2; -.
DR Genevestigator; Q969U7; -.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint; IEA:Ensembl.
DR GO; GO:0043248; P:proteasome assembly; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2.
DR InterPro; IPR016562; Proteasome_assmbl_chp_2_euk.
DR Pfam; PF09754; PAC2; 1.
DR PIRSF; PIRSF010044; UCP010044; 1.
PE 1: Evidence at protein level;
KW Chaperone; Complete proteome; Nucleus; Reference proteome.
FT CHAIN 1 264 Proteasome assembly chaperone 2.
FT /FTId=PRO_0000322552.
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
//
MIM
609702
*RECORD*
*FIELD* NO
609702
*FIELD* TI
*609702 PROTEASOME-ASSEMBLING CHAPERONE 2; PSMG2
;;PROTEASOME ASSEMBLY CHAPERONE 2; PAC2;;
read moreTNFSF5-INDUCED PROTEIN 1; TNFSF5IP1;;
HEPATOCELLULAR CARCINOMA-ASSOCIATED PROTEIN 3; HCCA3;;
CD40 LIGAND-ACTIVATED SPECIFIC TRANSCRIPT 3; CLAST3
*FIELD* TX
CLONING
By differential display PCR to identify genes upregulated in
hepatocellular carcinoma, followed by screening a placenta cDNA library,
Wang et al. (2001) cloned TNFSF5IP1, which they called HCCA3. The
deduced 264-amino acid protein contains 2 N-glycosylation sites, 3
N-myristoylation sites, and several phosphorylation sites. Northern blot
analysis detected a 1.7-kb HCCA3 transcript in all tissues examined.
Expression was high in lung, brain, and colon, moderate in muscle,
stomach, spleen, and heart, and weak in small intestine, pancreas, and
liver. Elevated HCCA3 expression in hepatocellular carcinoma was
associated with tumor invasiveness and metastasis, but not with tumor
size, degree of differentiation, or other parameters.
Using immunofluorescence, Bahar et al. (2002) found that mouse Clast3
localized in nuclear dot-like foci in transfected mouse fibroblasts.
GENE FUNCTION
Bahar et al. (2002) found that CLAST3 expression increased in human and
mouse B cells upon activation. In synchronized mouse fibroblasts, Clast3
expression was low in G1-arrested cells and increased during S and G2-M
phases. Overexpression of Clast3 resulted in growth retardation,
polyploidy, and generation of multinucleated cells. Treatment of Clast3
transfectants with nocodazole, a spindle-damaging agent, enhanced the
incidence of multinucleated cells, suggesting that Clast3 impairs the
same checkpoint activated by nocodazole. Downregulation of Clast3
expression by antisense oligonucleotides decreased the number of cells
at G2-M phase and concomitantly increased the number of apoptotic cells.
Hirano et al. (2005) reported 2 chaperones designated
proteasome-assembling chaperone-1 (PAC1; 605296) and PAC2, that are
involved in the maturation of the mammalian 20S proteasomes. PAC1 and
PAC2 associate as heterodimers with proteasome precursors and are
degraded after formation of the 20S proteasome is completed.
Overexpression of PAC1 or PAC2 accelerates the formation of precursor
proteasomes, whereas knockdown by short interfering RNA impairs it,
resulting in poor maturation of 20S proteasomes. Furthermore, Hirano et
al. (2005) showed that the PAC complex provides a scaffold for alpha
ring formation and keeps the alpha rings competent for the subsequent
formation of half-proteasomes. Thus, Hirano et al. (2005) concluded that
their results identify a mechanism for the correct assembly of 20S
proteasomes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
TNFSF5IP1 gene to chromosome 18 (TMAP A006T17).
*FIELD* RF
1. Bahar, R.; O-Wang, J.; Kawamura, K.; Seimiya, M.; Wang, Y.; Hatano,
M.; Okada, S.; Tokuhisa, T.; Watanabe, T.; Tagawa, M.: Growth retardation,
polyploidy, and multinucleation induced by Clast3, a novel cell cycle-regulated
protein. J. Biol. Chem. 277: 40012-40019, 2002.
2. Hirano, Y.; Hendil, K. B.; Yashiroda, H.; Iemura, S.; Nagane, R.;
Hioki, Y.; Natsume, T.; Tanaka, K.; Murata, S.: A heterodimeric complex
that promotes the assembly of mammalian 20S proteasomes. Nature 437:
1381-1385, 2005.
3. Wang, Z.-X.; Hu, G.-F.; Wang, H.-Y.; Wu, M.-C.: Expression of
liver cancer associated gene HCCA3. World J. Gastroent. 7: 821-825,
2001.
*FIELD* CN
Ada Hamosh - updated: 11/8/2005
*FIELD* CD
Patricia A. Hartz: 11/8/2005
*FIELD* ED
joanna: 05/07/2009
carol: 10/28/2008
alopez: 11/8/2005
mgross: 11/8/2005
*RECORD*
*FIELD* NO
609702
*FIELD* TI
*609702 PROTEASOME-ASSEMBLING CHAPERONE 2; PSMG2
;;PROTEASOME ASSEMBLY CHAPERONE 2; PAC2;;
read moreTNFSF5-INDUCED PROTEIN 1; TNFSF5IP1;;
HEPATOCELLULAR CARCINOMA-ASSOCIATED PROTEIN 3; HCCA3;;
CD40 LIGAND-ACTIVATED SPECIFIC TRANSCRIPT 3; CLAST3
*FIELD* TX
CLONING
By differential display PCR to identify genes upregulated in
hepatocellular carcinoma, followed by screening a placenta cDNA library,
Wang et al. (2001) cloned TNFSF5IP1, which they called HCCA3. The
deduced 264-amino acid protein contains 2 N-glycosylation sites, 3
N-myristoylation sites, and several phosphorylation sites. Northern blot
analysis detected a 1.7-kb HCCA3 transcript in all tissues examined.
Expression was high in lung, brain, and colon, moderate in muscle,
stomach, spleen, and heart, and weak in small intestine, pancreas, and
liver. Elevated HCCA3 expression in hepatocellular carcinoma was
associated with tumor invasiveness and metastasis, but not with tumor
size, degree of differentiation, or other parameters.
Using immunofluorescence, Bahar et al. (2002) found that mouse Clast3
localized in nuclear dot-like foci in transfected mouse fibroblasts.
GENE FUNCTION
Bahar et al. (2002) found that CLAST3 expression increased in human and
mouse B cells upon activation. In synchronized mouse fibroblasts, Clast3
expression was low in G1-arrested cells and increased during S and G2-M
phases. Overexpression of Clast3 resulted in growth retardation,
polyploidy, and generation of multinucleated cells. Treatment of Clast3
transfectants with nocodazole, a spindle-damaging agent, enhanced the
incidence of multinucleated cells, suggesting that Clast3 impairs the
same checkpoint activated by nocodazole. Downregulation of Clast3
expression by antisense oligonucleotides decreased the number of cells
at G2-M phase and concomitantly increased the number of apoptotic cells.
Hirano et al. (2005) reported 2 chaperones designated
proteasome-assembling chaperone-1 (PAC1; 605296) and PAC2, that are
involved in the maturation of the mammalian 20S proteasomes. PAC1 and
PAC2 associate as heterodimers with proteasome precursors and are
degraded after formation of the 20S proteasome is completed.
Overexpression of PAC1 or PAC2 accelerates the formation of precursor
proteasomes, whereas knockdown by short interfering RNA impairs it,
resulting in poor maturation of 20S proteasomes. Furthermore, Hirano et
al. (2005) showed that the PAC complex provides a scaffold for alpha
ring formation and keeps the alpha rings competent for the subsequent
formation of half-proteasomes. Thus, Hirano et al. (2005) concluded that
their results identify a mechanism for the correct assembly of 20S
proteasomes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
TNFSF5IP1 gene to chromosome 18 (TMAP A006T17).
*FIELD* RF
1. Bahar, R.; O-Wang, J.; Kawamura, K.; Seimiya, M.; Wang, Y.; Hatano,
M.; Okada, S.; Tokuhisa, T.; Watanabe, T.; Tagawa, M.: Growth retardation,
polyploidy, and multinucleation induced by Clast3, a novel cell cycle-regulated
protein. J. Biol. Chem. 277: 40012-40019, 2002.
2. Hirano, Y.; Hendil, K. B.; Yashiroda, H.; Iemura, S.; Nagane, R.;
Hioki, Y.; Natsume, T.; Tanaka, K.; Murata, S.: A heterodimeric complex
that promotes the assembly of mammalian 20S proteasomes. Nature 437:
1381-1385, 2005.
3. Wang, Z.-X.; Hu, G.-F.; Wang, H.-Y.; Wu, M.-C.: Expression of
liver cancer associated gene HCCA3. World J. Gastroent. 7: 821-825,
2001.
*FIELD* CN
Ada Hamosh - updated: 11/8/2005
*FIELD* CD
Patricia A. Hartz: 11/8/2005
*FIELD* ED
joanna: 05/07/2009
carol: 10/28/2008
alopez: 11/8/2005
mgross: 11/8/2005