Full text data of PSMC6
PSMC6
(SUG2)
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4; Proteasome 26S subunit ATPase 6; Proteasome subunit p42)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4; Proteasome 26S subunit ATPase 6; Proteasome subunit p42)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00021926
IPI00021926 26S protease regulatory subunit S10 26S protease regulatory subunit S10 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00021926 26S protease regulatory subunit S10 26S protease regulatory subunit S10 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P62333
ID PRS10_HUMAN Reviewed; 389 AA.
AC P62333; B2R975; P49719; Q6IBU3; Q92524;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=26S protease regulatory subunit 10B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE AltName: Full=Proteasome 26S subunit ATPase 6;
DE AltName: Full=Proteasome subunit p42;
GN Name=PSMC6; Synonyms=SUG2;
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].
RC TISSUE=Aorta;
RX PubMed=8674546; DOI=10.1016/0014-5793(96)00489-9;
RA Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.;
RT "cDNA cloning of p42, a shared subunit of two proteasome regulatory
RT proteins, reveals a novel member of the AAA protein family.";
RL FEBS Lett. 387:184-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Y., Benezra R.;
RT "Human SUG2.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [8]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
RA Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
RA Hisamatsu H., Tanaka K., Slaughter C.A.;
RT "Identification, purification, and characterization of a PA700-
RT dependent activator of the proteasome.";
RL J. Biol. Chem. 271:3112-3118(1996).
RN [9]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-206, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex.
CC -!- SUBUNIT: Found in the multi-protein complexes: the 26S proteasome
CC (formed from the 20S proteasome and PA700), and the modulator.
CC PA700 consists of 28 subunits arranged to form a cylinder-shaped
CC complex by four stacked rings, each containing seven subunits.
CC Interacts with PAAF1.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=3; IntAct=EBI-357669, EBI-357598;
CC P17980:PSMC3; NbExp=5; IntAct=EBI-357669, EBI-359720;
CC P43686:PSMC4; NbExp=3; IntAct=EBI-357669, EBI-743997;
CC P62195:PSMC5; NbExp=8; IntAct=EBI-357669, EBI-357745;
CC O00233:PSMD9; NbExp=5; IntAct=EBI-357669, EBI-750973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- CAUTION: Alternative initiation from an upstream conserved
CC methionine cannot be fully excluded but is not experimentally
CC supported while initiation from the displayed methionine is
CC supported by PubMed:17323924.
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DR EMBL; D78275; BAA11338.1; -; mRNA.
DR EMBL; AF006305; AAB61616.1; -; mRNA.
DR EMBL; BT006843; AAP35489.1; -; mRNA.
DR EMBL; CR456709; CAG32990.1; -; mRNA.
DR EMBL; AK313670; BAG36422.1; -; mRNA.
DR EMBL; CH471078; EAW65645.1; -; Genomic_DNA.
DR EMBL; BC005390; AAH05390.1; -; mRNA.
DR PIR; S71316; S71316.
DR RefSeq; NP_002797.3; NM_002806.3.
DR UniGene; Hs.156171; -.
DR ProteinModelPortal; P62333; -.
DR SMR; P62333; 19-379.
DR DIP; DIP-38150N; -.
DR IntAct; P62333; 30.
DR MINT; MINT-5001174; -.
DR STRING; 9606.ENSP00000401802; -.
DR PhosphoSite; P62333; -.
DR DMDM; 51702772; -.
DR REPRODUCTION-2DPAGE; IPI00021926; -.
DR PaxDb; P62333; -.
DR PeptideAtlas; P62333; -.
DR PRIDE; P62333; -.
DR DNASU; 5706; -.
DR Ensembl; ENST00000606149; ENSP00000475721; ENSG00000100519.
DR GeneID; 5706; -.
DR KEGG; hsa:5706; -.
DR UCSC; uc010tqx.2; human.
DR CTD; 5706; -.
DR GeneCards; GC14P053173; -.
DR H-InvDB; HIX0011661; -.
DR HGNC; HGNC:9553; PSMC6.
DR HPA; HPA042823; -.
DR MIM; 602708; gene.
DR neXtProt; NX_P62333; -.
DR PharmGKB; PA33898; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62333; -.
DR KO; K03064; -.
DR OrthoDB; EOG7TF78Z; -.
DR PhylomeDB; P62333; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMC6; -.
DR GenomeRNAi; 5706; -.
DR NextBio; 22170; -.
DR PRO; PR:P62333; -.
DR ArrayExpress; P62333; -.
DR Bgee; P62333; -.
DR CleanEx; HS_PSMC6; -.
DR Genevestigator; P62333; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; TAS:UniProtKB.
DR GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1 389 26S protease regulatory subunit 10B.
FT /FTId=PRO_0000084732.
FT NP_BIND 174 181 ATP (Potential).
FT MOD_RES 72 72 N6-acetyllysine.
FT MOD_RES 206 206 N6-acetyllysine.
FT CONFLICT 276 276 I -> T (in Ref. 1; BAA11338).
SQ SEQUENCE 389 AA; 44173 MW; B26421295742CACD CRC64;
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD
FVVQEDFMKA VRKVADSKKL ESKLDYKPV
//
ID PRS10_HUMAN Reviewed; 389 AA.
AC P62333; B2R975; P49719; Q6IBU3; Q92524;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=26S protease regulatory subunit 10B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE AltName: Full=Proteasome 26S subunit ATPase 6;
DE AltName: Full=Proteasome subunit p42;
GN Name=PSMC6; Synonyms=SUG2;
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].
RC TISSUE=Aorta;
RX PubMed=8674546; DOI=10.1016/0014-5793(96)00489-9;
RA Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.;
RT "cDNA cloning of p42, a shared subunit of two proteasome regulatory
RT proteins, reveals a novel member of the AAA protein family.";
RL FEBS Lett. 387:184-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Y., Benezra R.;
RT "Human SUG2.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [8]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
RA Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
RA Hisamatsu H., Tanaka K., Slaughter C.A.;
RT "Identification, purification, and characterization of a PA700-
RT dependent activator of the proteasome.";
RL J. Biol. Chem. 271:3112-3118(1996).
RN [9]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates
RT proteasome activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human
RT 26S proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-206, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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: The 26S protease is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the
CC 26S complex.
CC -!- SUBUNIT: Found in the multi-protein complexes: the 26S proteasome
CC (formed from the 20S proteasome and PA700), and the modulator.
CC PA700 consists of 28 subunits arranged to form a cylinder-shaped
CC complex by four stacked rings, each containing seven subunits.
CC Interacts with PAAF1.
CC -!- INTERACTION:
CC P62191:PSMC1; NbExp=3; IntAct=EBI-357669, EBI-357598;
CC P17980:PSMC3; NbExp=5; IntAct=EBI-357669, EBI-359720;
CC P43686:PSMC4; NbExp=3; IntAct=EBI-357669, EBI-743997;
CC P62195:PSMC5; NbExp=8; IntAct=EBI-357669, EBI-357745;
CC O00233:PSMD9; NbExp=5; IntAct=EBI-357669, EBI-750973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- CAUTION: Alternative initiation from an upstream conserved
CC methionine cannot be fully excluded but is not experimentally
CC supported while initiation from the displayed methionine is
CC supported by PubMed:17323924.
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DR EMBL; D78275; BAA11338.1; -; mRNA.
DR EMBL; AF006305; AAB61616.1; -; mRNA.
DR EMBL; BT006843; AAP35489.1; -; mRNA.
DR EMBL; CR456709; CAG32990.1; -; mRNA.
DR EMBL; AK313670; BAG36422.1; -; mRNA.
DR EMBL; CH471078; EAW65645.1; -; Genomic_DNA.
DR EMBL; BC005390; AAH05390.1; -; mRNA.
DR PIR; S71316; S71316.
DR RefSeq; NP_002797.3; NM_002806.3.
DR UniGene; Hs.156171; -.
DR ProteinModelPortal; P62333; -.
DR SMR; P62333; 19-379.
DR DIP; DIP-38150N; -.
DR IntAct; P62333; 30.
DR MINT; MINT-5001174; -.
DR STRING; 9606.ENSP00000401802; -.
DR PhosphoSite; P62333; -.
DR DMDM; 51702772; -.
DR REPRODUCTION-2DPAGE; IPI00021926; -.
DR PaxDb; P62333; -.
DR PeptideAtlas; P62333; -.
DR PRIDE; P62333; -.
DR DNASU; 5706; -.
DR Ensembl; ENST00000606149; ENSP00000475721; ENSG00000100519.
DR GeneID; 5706; -.
DR KEGG; hsa:5706; -.
DR UCSC; uc010tqx.2; human.
DR CTD; 5706; -.
DR GeneCards; GC14P053173; -.
DR H-InvDB; HIX0011661; -.
DR HGNC; HGNC:9553; PSMC6.
DR HPA; HPA042823; -.
DR MIM; 602708; gene.
DR neXtProt; NX_P62333; -.
DR PharmGKB; PA33898; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62333; -.
DR KO; K03064; -.
DR OrthoDB; EOG7TF78Z; -.
DR PhylomeDB; P62333; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMC6; -.
DR GenomeRNAi; 5706; -.
DR NextBio; 22170; -.
DR PRO; PR:P62333; -.
DR ArrayExpress; P62333; -.
DR Bgee; P62333; -.
DR CleanEx; HS_PSMC6; -.
DR Genevestigator; P62333; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; TAS:UniProtKB.
DR GO; GO:0030674; F:protein binding, bridging; NAS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005937; 26S_Psome_P45.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1 389 26S protease regulatory subunit 10B.
FT /FTId=PRO_0000084732.
FT NP_BIND 174 181 ATP (Potential).
FT MOD_RES 72 72 N6-acetyllysine.
FT MOD_RES 206 206 N6-acetyllysine.
FT CONFLICT 276 276 I -> T (in Ref. 1; BAA11338).
SQ SEQUENCE 389 AA; 44173 MW; B26421295742CACD CRC64;
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD
FVVQEDFMKA VRKVADSKKL ESKLDYKPV
//
MIM
602708
*RECORD*
*FIELD* NO
602708
*FIELD* TI
*602708 PROTEASOME 26S SUBUNIT, ATPase, 6; PSMC6
*FIELD* TX
CLONING
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
read moreprotease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules (see PSMC1; 602706). DeMartino et al. (1996)
identified a protein complex that enhanced PA700 activation of the
proteasome. They found that 2 proteins, p42 (PSMC6) and p50 (PSMC3;
186852), are components of both this complex and PA700. Using the amino
acid sequence of bovine p42, Fujiwara et al. (1996) identified a human
aorta cDNA that encodes p42. The predicted 389-amino acid human p42
contains an AAA (ATPase associated with diverse cellular activities)
domain (see PSMC5; 601681).
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the PSMC6 gene to chromosome 12q15. However, Gross (2011) mapped the
PSMC6 gene to chromosome 14q22.1 based on an alignment of the PSMC6
sequence (GenBank GENBANK BC005390) with the genomic sequence (GRCh37).
*FIELD* RF
1. DeMartino, G. N.; Proske, R. J.; Moomaw, C. R.; Strong, A. A.;
Song, X.; Hisamatsu, H.; Tanaka, K.; Slaughter, C. A.: Identification,
purification, and characterization of a PA700-dependent activator
of the proteasome. J. Biol. Chem. 271: 3112-3118, 1996.
2. Fujiwara, T.; Watanabe, T. K.; Tanaka, K.; Slaughter, C. A.; DeMartino,
G. N.: cDNA cloning of p42, a shared subunit of two proteasome regulatory
proteins, reveals a novel member of the AAA protein family. FEBS
Lett. 387: 184-188, 1996.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
4. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
mgross: 02/17/2011
psherman: 6/11/1998
*RECORD*
*FIELD* NO
602708
*FIELD* TI
*602708 PROTEASOME 26S SUBUNIT, ATPase, 6; PSMC6
*FIELD* TX
CLONING
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
read moreprotease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules (see PSMC1; 602706). DeMartino et al. (1996)
identified a protein complex that enhanced PA700 activation of the
proteasome. They found that 2 proteins, p42 (PSMC6) and p50 (PSMC3;
186852), are components of both this complex and PA700. Using the amino
acid sequence of bovine p42, Fujiwara et al. (1996) identified a human
aorta cDNA that encodes p42. The predicted 389-amino acid human p42
contains an AAA (ATPase associated with diverse cellular activities)
domain (see PSMC5; 601681).
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the PSMC6 gene to chromosome 12q15. However, Gross (2011) mapped the
PSMC6 gene to chromosome 14q22.1 based on an alignment of the PSMC6
sequence (GenBank GENBANK BC005390) with the genomic sequence (GRCh37).
*FIELD* RF
1. DeMartino, G. N.; Proske, R. J.; Moomaw, C. R.; Strong, A. A.;
Song, X.; Hisamatsu, H.; Tanaka, K.; Slaughter, C. A.: Identification,
purification, and characterization of a PA700-dependent activator
of the proteasome. J. Biol. Chem. 271: 3112-3118, 1996.
2. Fujiwara, T.; Watanabe, T. K.; Tanaka, K.; Slaughter, C. A.; DeMartino,
G. N.: cDNA cloning of p42, a shared subunit of two proteasome regulatory
proteins, reveals a novel member of the AAA protein family. FEBS
Lett. 387: 184-188, 1996.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/17/2011.
4. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
analysis of a family of human 26S proteasomal ATPases. Biochem. Biophys.
Res. Commun. 243: 229-232, 1998.
*FIELD* CN
Matthew B. Gross - updated: 02/17/2011
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
mgross: 02/17/2011
psherman: 6/11/1998