Full text data of PSMC5
PSMC5
(SUG1)
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6; Proteasome 26S subunit ATPase 5; Proteasome subunit p45; Thyroid hormone receptor-interacting protein 1; TRIP1; p45/SUG)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6; Proteasome 26S subunit ATPase 5; Proteasome subunit p45; Thyroid hormone receptor-interacting protein 1; TRIP1; p45/SUG)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00023919
IPI00023919 Similar to 26S protease regulatory subunit 8 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 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
IPI00023919 Similar to 26S protease regulatory subunit 8 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 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
P62195
ID PRS8_HUMAN Reviewed; 406 AA.
AC P62195; A8K3Z3; A8K763; O35051; O43208; P47210; P52915; P52916;
read moreDT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=26S protease regulatory subunit 8;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE AltName: Full=Proteasome 26S subunit ATPase 5;
DE AltName: Full=Proteasome subunit p45;
DE AltName: Full=Thyroid hormone receptor-interacting protein 1;
DE Short=TRIP1;
DE AltName: Full=p45/SUG;
GN Name=PSMC5; Synonyms=SUG1;
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] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=7729537; DOI=10.1016/0014-5793(95)00304-R;
RA Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N.,
RA Slaughter C.A., Noda C., Tanaka K.;
RT "cDNA cloning of a new putative ATPase subunit p45 of the human 26S
RT proteasome, a homolog of yeast transcriptional factor Sug1p.";
RL FEBS Lett. 363:151-156(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7776974; DOI=10.1210/me.9.2.243;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence
RT of thyroid hormone for interaction with the thyroid hormone
RT receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
RC TISSUE=Lung carcinoma;
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 127-406.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [7]
RP INTERACTION WITH NDC80.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome
RT and modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [8]
RP INTERACTION WITH NDC80.
RX PubMed=10409732;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
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 ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS 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 [13]
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).
RN [14]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, AND STRUCTURE BY NMR
RP OF 320-395.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of a domain of 26s proteasome regulatory subunit 8
RT from Homo sapiens. Northeast structural genomics consortium target ID
RT HR3102A.";
RL Submitted (JAN-2010) to the PDB data bank.
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-60.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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: Interacts, in vitro, with the thyroid hormone receptor
CC (in a thyroid hormone T3-dependent manner) and with retinoid X
CC receptor (RXR) (By similarity). Interacts with NDC80. Interacts
CC with PAAF1. Interacts with TRIM5. Component of a complex with
CC USP49 and RUVBL1.
CC -!- INTERACTION:
CC P03255-1:- (xeno); NbExp=2; IntAct=EBI-357745, EBI-6692439;
CC P11275:Camk2a (xeno); NbExp=4; IntAct=EBI-357745, EBI-2640645;
CC P08413:Camk2b (xeno); NbExp=3; IntAct=EBI-357745, EBI-916155;
CC P19447:ERCC3; NbExp=4; IntAct=EBI-357745, EBI-1183307;
CC Q9BRP4:PAAF1; NbExp=2; IntAct=EBI-357745, EBI-1056358;
CC Q53GL0:PLEKHO1; NbExp=9; IntAct=EBI-357745, EBI-949945;
CC P35998:PSMC2; NbExp=10; IntAct=EBI-357745, EBI-359710;
CC P43686:PSMC4; NbExp=11; IntAct=EBI-357745, EBI-743997;
CC P62333:PSMC6; NbExp=8; IntAct=EBI-357745, EBI-357669;
CC Q13200:PSMD2; NbExp=9; IntAct=EBI-357745, EBI-357648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62195-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62195-2; Sequence=VSP_045441;
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; D44467; BAA07919.1; -; mRNA.
DR EMBL; L38810; AAC41735.1; -; mRNA.
DR EMBL; AK290758; BAF83447.1; -; mRNA.
DR EMBL; AK291878; BAF84567.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94270.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94271.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94272.1; -; Genomic_DNA.
DR EMBL; BC001932; AAH01932.1; -; mRNA.
DR EMBL; BC002367; AAH02367.3; -; mRNA.
DR EMBL; AF035309; AAB88187.1; -; mRNA.
DR PIR; S60343; S60343.
DR PIR; S65536; S65536.
DR RefSeq; NP_001186092.1; NM_001199163.1.
DR RefSeq; NP_002796.4; NM_002805.5.
DR UniGene; Hs.79387; -.
DR PDB; 2KRK; NMR; -; A=320-395.
DR PDB; 3KW6; X-ray; 2.10 A; A=318-395.
DR PDBsum; 2KRK; -.
DR PDBsum; 3KW6; -.
DR ProteinModelPortal; P62195; -.
DR SMR; P62195; 27-396.
DR IntAct; P62195; 42.
DR MINT; MINT-5004394; -.
DR STRING; 9606.ENSP00000310572; -.
DR PhosphoSite; P62195; -.
DR DMDM; 49065819; -.
DR PaxDb; P62195; -.
DR PRIDE; P62195; -.
DR DNASU; 5705; -.
DR Ensembl; ENST00000310144; ENSP00000310572; ENSG00000087191.
DR Ensembl; ENST00000375812; ENSP00000364970; ENSG00000087191.
DR Ensembl; ENST00000580864; ENSP00000462495; ENSG00000087191.
DR Ensembl; ENST00000581882; ENSP00000463938; ENSG00000087191.
DR GeneID; 5705; -.
DR KEGG; hsa:5705; -.
DR UCSC; uc002jcb.3; human.
DR CTD; 5705; -.
DR GeneCards; GC17P061904; -.
DR HGNC; HGNC:9552; PSMC5.
DR HPA; HPA017871; -.
DR MIM; 601681; gene.
DR neXtProt; NX_P62195; -.
DR PharmGKB; PA33897; -.
DR eggNOG; COG1222; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62195; -.
DR KO; K03066; -.
DR OMA; VMGTKKV; -.
DR PhylomeDB; P62195; -.
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 ChiTaRS; PSMC5; human.
DR EvolutionaryTrace; P62195; -.
DR GeneWiki; PSMC5; -.
DR GenomeRNAi; 5705; -.
DR NextBio; 22166; -.
DR PRO; PR:P62195; -.
DR ArrayExpress; P62195; -.
DR Bgee; P62195; -.
DR CleanEx; HS_PSMC5; -.
DR Genevestigator; P62195; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031595; C:nuclear proteasome complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
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:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
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:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus;
KW Polymorphism; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 26S protease regulatory subunit 8.
FT /FTId=PRO_0000084721.
FT NP_BIND 190 197 ATP (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 222 222 N6-acetyllysine.
FT VAR_SEQ 1 8 Missing (in isoform 2).
FT /FTId=VSP_045441.
FT VARIANT 60 60 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035901.
FT VARIANT 258 258 R -> W (in dbSNP:rs11543211).
FT /FTId=VAR_048119.
FT CONFLICT 61 61 E -> R (in Ref. 1; BAA07919).
FT CONFLICT 127 128 LP -> ML (in Ref. 6; AAB88187).
FT CONFLICT 266 266 D -> S (in Ref. 2; AAC41735).
FT CONFLICT 272 272 T -> Q (in Ref. 2; AAC41735).
FT CONFLICT 300 300 I -> M (in Ref. 2; AAC41735).
FT HELIX 322 333
FT STRAND 336 338
FT HELIX 344 349
FT HELIX 356 372
FT STRAND 376 378
FT HELIX 380 391
SQ SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
//
ID PRS8_HUMAN Reviewed; 406 AA.
AC P62195; A8K3Z3; A8K763; O35051; O43208; P47210; P52915; P52916;
read moreDT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=26S protease regulatory subunit 8;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE AltName: Full=Proteasome 26S subunit ATPase 5;
DE AltName: Full=Proteasome subunit p45;
DE AltName: Full=Thyroid hormone receptor-interacting protein 1;
DE Short=TRIP1;
DE AltName: Full=p45/SUG;
GN Name=PSMC5; Synonyms=SUG1;
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] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=7729537; DOI=10.1016/0014-5793(95)00304-R;
RA Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N.,
RA Slaughter C.A., Noda C., Tanaka K.;
RT "cDNA cloning of a new putative ATPase subunit p45 of the human 26S
RT proteasome, a homolog of yeast transcriptional factor Sug1p.";
RL FEBS Lett. 363:151-156(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7776974; DOI=10.1210/me.9.2.243;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence
RT of thyroid hormone for interaction with the thyroid hormone
RT receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
RC TISSUE=Lung carcinoma;
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 127-406.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [7]
RP INTERACTION WITH NDC80.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome
RT and modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [8]
RP INTERACTION WITH NDC80.
RX PubMed=10409732;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
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 ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND MASS 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 [13]
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).
RN [14]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in
RT complex with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, AND STRUCTURE BY NMR
RP OF 320-395.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of a domain of 26s proteasome regulatory subunit 8
RT from Homo sapiens. Northeast structural genomics consortium target ID
RT HR3102A.";
RL Submitted (JAN-2010) to the PDB data bank.
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-60.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
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: Interacts, in vitro, with the thyroid hormone receptor
CC (in a thyroid hormone T3-dependent manner) and with retinoid X
CC receptor (RXR) (By similarity). Interacts with NDC80. Interacts
CC with PAAF1. Interacts with TRIM5. Component of a complex with
CC USP49 and RUVBL1.
CC -!- INTERACTION:
CC P03255-1:- (xeno); NbExp=2; IntAct=EBI-357745, EBI-6692439;
CC P11275:Camk2a (xeno); NbExp=4; IntAct=EBI-357745, EBI-2640645;
CC P08413:Camk2b (xeno); NbExp=3; IntAct=EBI-357745, EBI-916155;
CC P19447:ERCC3; NbExp=4; IntAct=EBI-357745, EBI-1183307;
CC Q9BRP4:PAAF1; NbExp=2; IntAct=EBI-357745, EBI-1056358;
CC Q53GL0:PLEKHO1; NbExp=9; IntAct=EBI-357745, EBI-949945;
CC P35998:PSMC2; NbExp=10; IntAct=EBI-357745, EBI-359710;
CC P43686:PSMC4; NbExp=11; IntAct=EBI-357745, EBI-743997;
CC P62333:PSMC6; NbExp=8; IntAct=EBI-357745, EBI-357669;
CC Q13200:PSMD2; NbExp=9; IntAct=EBI-357745, EBI-357648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62195-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62195-2; Sequence=VSP_045441;
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; D44467; BAA07919.1; -; mRNA.
DR EMBL; L38810; AAC41735.1; -; mRNA.
DR EMBL; AK290758; BAF83447.1; -; mRNA.
DR EMBL; AK291878; BAF84567.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94270.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94271.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94272.1; -; Genomic_DNA.
DR EMBL; BC001932; AAH01932.1; -; mRNA.
DR EMBL; BC002367; AAH02367.3; -; mRNA.
DR EMBL; AF035309; AAB88187.1; -; mRNA.
DR PIR; S60343; S60343.
DR PIR; S65536; S65536.
DR RefSeq; NP_001186092.1; NM_001199163.1.
DR RefSeq; NP_002796.4; NM_002805.5.
DR UniGene; Hs.79387; -.
DR PDB; 2KRK; NMR; -; A=320-395.
DR PDB; 3KW6; X-ray; 2.10 A; A=318-395.
DR PDBsum; 2KRK; -.
DR PDBsum; 3KW6; -.
DR ProteinModelPortal; P62195; -.
DR SMR; P62195; 27-396.
DR IntAct; P62195; 42.
DR MINT; MINT-5004394; -.
DR STRING; 9606.ENSP00000310572; -.
DR PhosphoSite; P62195; -.
DR DMDM; 49065819; -.
DR PaxDb; P62195; -.
DR PRIDE; P62195; -.
DR DNASU; 5705; -.
DR Ensembl; ENST00000310144; ENSP00000310572; ENSG00000087191.
DR Ensembl; ENST00000375812; ENSP00000364970; ENSG00000087191.
DR Ensembl; ENST00000580864; ENSP00000462495; ENSG00000087191.
DR Ensembl; ENST00000581882; ENSP00000463938; ENSG00000087191.
DR GeneID; 5705; -.
DR KEGG; hsa:5705; -.
DR UCSC; uc002jcb.3; human.
DR CTD; 5705; -.
DR GeneCards; GC17P061904; -.
DR HGNC; HGNC:9552; PSMC5.
DR HPA; HPA017871; -.
DR MIM; 601681; gene.
DR neXtProt; NX_P62195; -.
DR PharmGKB; PA33897; -.
DR eggNOG; COG1222; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P62195; -.
DR KO; K03066; -.
DR OMA; VMGTKKV; -.
DR PhylomeDB; P62195; -.
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 ChiTaRS; PSMC5; human.
DR EvolutionaryTrace; P62195; -.
DR GeneWiki; PSMC5; -.
DR GenomeRNAi; 5705; -.
DR NextBio; 22166; -.
DR PRO; PR:P62195; -.
DR ArrayExpress; P62195; -.
DR Bgee; P62195; -.
DR CleanEx; HS_PSMC5; -.
DR Genevestigator; P62195; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031595; C:nuclear proteasome complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
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:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
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:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus;
KW Polymorphism; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 406 26S protease regulatory subunit 8.
FT /FTId=PRO_0000084721.
FT NP_BIND 190 197 ATP (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 222 222 N6-acetyllysine.
FT VAR_SEQ 1 8 Missing (in isoform 2).
FT /FTId=VSP_045441.
FT VARIANT 60 60 R -> Q (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035901.
FT VARIANT 258 258 R -> W (in dbSNP:rs11543211).
FT /FTId=VAR_048119.
FT CONFLICT 61 61 E -> R (in Ref. 1; BAA07919).
FT CONFLICT 127 128 LP -> ML (in Ref. 6; AAB88187).
FT CONFLICT 266 266 D -> S (in Ref. 2; AAC41735).
FT CONFLICT 272 272 T -> Q (in Ref. 2; AAC41735).
FT CONFLICT 300 300 I -> M (in Ref. 2; AAC41735).
FT HELIX 322 333
FT STRAND 336 338
FT HELIX 344 349
FT HELIX 356 372
FT STRAND 376 378
FT HELIX 380 391
SQ SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
//
MIM
601681
*RECORD*
*FIELD* NO
601681
*FIELD* TI
*601681 PROTEASOME 26S SUBUNIT, ATPase, 5; PSMC5
;;THYROID HORMONE RECEPTOR INTERACTOR 1; TRIP1
read more*FIELD* TX
DESCRIPTION
PSMC5 is a member of the AAA (ATPases Associated with diverse cellular
Activities) gene family (Hoyle et al., 1997).
GENE FAMILY
Members of the AAA gene family are most similar throughout an
approximately 230-amino acid ATPase domain (the AAA domain), and related
genes have been described in organisms as distant as archaebacteria and
eubacteria. All the known AAA proteins contain either 1 or 2 AAA
domains, and the family can be subdivided into 2 groups on this basis.
It appears that 2-domain AAA proteins (e.g., NSF, 601633) are associated
with membrane functions. In eukaryotes, the 1-domain AAA proteins such
as PSMC5 appear to be involved largely in the regulatory subunit of the
26S protease (summary by Hoyle et al., 1997).
CLONING
Lee et al. (1995) used the yeast interaction trap, a version of the
yeast 2-hybrid system, to identify proteins that specifically interact
with the ligand-binding domain of rat thyroid hormone receptor-beta
(THRB; 190160). They isolated HeLa cell cDNAs encoding several different
thyroid hormone receptor (TR)-interacting proteins (TRIPs), including
TRIP1 (PSMC5). TRIP1 strongly interacted with rat Thrb only in the
presence of thyroid hormone. It also showed a ligand-dependent
interaction with retinoid X receptor-alpha (RXRA; 180245), but did not
interact with the glucocorticoid receptor (NR3C1; 138040) under any
condition. The deduced 406-amino acid TRIP1 protein shares a high degree
of sequence similarity with the yeast transcriptional coactivator SUG1.
TRIP1 contains an AAA domain that is positioned toward the C terminus,
which is typical in the AAA family. Lee et al. (1995) found that TRIP1
is ubiquitously expressed as an approximately 1.4-kb transcript.
GENE FUNCTION
Lee et al. (1995) showed that TRIP1 can functionally substitute for Sug1
in yeast, and that both proteins interact in vitro with the TR and with
the transcriptional activation domains of yeast GAL4 and herpes virus
VP16.
MAPPING
By PCR amplification of a partial sequence of PSMC5 in a panel of human
monochromosomal cell hybrids, Hoyle et al. (1997) demonstrated that the
PSMC5 gene is located on chromosome 17. By fluorescence in situ
hybridization (FISH), they refined the localization to chromosome
17q24-q25. Tanahashi et al. (1998) mapped the PSMC5 gene to chromosome
17q23.1-q23.3 by FISH.
*FIELD* RF
1. Hoyle, J.; Tan, K. H.; Fisher, E. M. C.: Localization of genes
encoding two human one-domain members of the AAA family: PSMC5 (the
thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the
Tat-binding protein, TBP1). Hum. Genet. 99: 285-288, 1997.
2. Lee, J. W.; Choi, H.-S.; Gyuris, J.; Brent, R.; Moore, D. D.:
Two classes of proteins dependent on either the presence or absence
of thyroid hormone for interaction with the thyroid hormone receptor. Molec.
Endocr. 9: 243-254, 1995.
3. Lee, J. W.; Ryan, F.; Swaffield, J. C.; Johnston, S. A.; Moore,
D. D.: Interaction of thyroid-hormone receptor with a conserved transcriptional
mediator. Nature 374: 91-94, 1995.
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
Patti M. Sherman - updated: 8/31/2000
Patti M. Sherman - updated: 2/7/2000
Rebekah S. Rasooly - updated: 6/10/1998
*FIELD* CD
Victor A. McKusick: 2/13/1997
*FIELD* ED
carol: 02/23/2011
alopez: 9/21/2010
mcapotos: 9/12/2000
psherman: 8/31/2000
mgross: 2/8/2000
psherman: 2/7/2000
alopez: 8/4/1998
psherman: 6/10/1998
jamie: 2/18/1997
mark: 2/13/1997
*RECORD*
*FIELD* NO
601681
*FIELD* TI
*601681 PROTEASOME 26S SUBUNIT, ATPase, 5; PSMC5
;;THYROID HORMONE RECEPTOR INTERACTOR 1; TRIP1
read more*FIELD* TX
DESCRIPTION
PSMC5 is a member of the AAA (ATPases Associated with diverse cellular
Activities) gene family (Hoyle et al., 1997).
GENE FAMILY
Members of the AAA gene family are most similar throughout an
approximately 230-amino acid ATPase domain (the AAA domain), and related
genes have been described in organisms as distant as archaebacteria and
eubacteria. All the known AAA proteins contain either 1 or 2 AAA
domains, and the family can be subdivided into 2 groups on this basis.
It appears that 2-domain AAA proteins (e.g., NSF, 601633) are associated
with membrane functions. In eukaryotes, the 1-domain AAA proteins such
as PSMC5 appear to be involved largely in the regulatory subunit of the
26S protease (summary by Hoyle et al., 1997).
CLONING
Lee et al. (1995) used the yeast interaction trap, a version of the
yeast 2-hybrid system, to identify proteins that specifically interact
with the ligand-binding domain of rat thyroid hormone receptor-beta
(THRB; 190160). They isolated HeLa cell cDNAs encoding several different
thyroid hormone receptor (TR)-interacting proteins (TRIPs), including
TRIP1 (PSMC5). TRIP1 strongly interacted with rat Thrb only in the
presence of thyroid hormone. It also showed a ligand-dependent
interaction with retinoid X receptor-alpha (RXRA; 180245), but did not
interact with the glucocorticoid receptor (NR3C1; 138040) under any
condition. The deduced 406-amino acid TRIP1 protein shares a high degree
of sequence similarity with the yeast transcriptional coactivator SUG1.
TRIP1 contains an AAA domain that is positioned toward the C terminus,
which is typical in the AAA family. Lee et al. (1995) found that TRIP1
is ubiquitously expressed as an approximately 1.4-kb transcript.
GENE FUNCTION
Lee et al. (1995) showed that TRIP1 can functionally substitute for Sug1
in yeast, and that both proteins interact in vitro with the TR and with
the transcriptional activation domains of yeast GAL4 and herpes virus
VP16.
MAPPING
By PCR amplification of a partial sequence of PSMC5 in a panel of human
monochromosomal cell hybrids, Hoyle et al. (1997) demonstrated that the
PSMC5 gene is located on chromosome 17. By fluorescence in situ
hybridization (FISH), they refined the localization to chromosome
17q24-q25. Tanahashi et al. (1998) mapped the PSMC5 gene to chromosome
17q23.1-q23.3 by FISH.
*FIELD* RF
1. Hoyle, J.; Tan, K. H.; Fisher, E. M. C.: Localization of genes
encoding two human one-domain members of the AAA family: PSMC5 (the
thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the
Tat-binding protein, TBP1). Hum. Genet. 99: 285-288, 1997.
2. Lee, J. W.; Choi, H.-S.; Gyuris, J.; Brent, R.; Moore, D. D.:
Two classes of proteins dependent on either the presence or absence
of thyroid hormone for interaction with the thyroid hormone receptor. Molec.
Endocr. 9: 243-254, 1995.
3. Lee, J. W.; Ryan, F.; Swaffield, J. C.; Johnston, S. A.; Moore,
D. D.: Interaction of thyroid-hormone receptor with a conserved transcriptional
mediator. Nature 374: 91-94, 1995.
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
Patti M. Sherman - updated: 8/31/2000
Patti M. Sherman - updated: 2/7/2000
Rebekah S. Rasooly - updated: 6/10/1998
*FIELD* CD
Victor A. McKusick: 2/13/1997
*FIELD* ED
carol: 02/23/2011
alopez: 9/21/2010
mcapotos: 9/12/2000
psherman: 8/31/2000
mgross: 2/8/2000
psherman: 2/7/2000
alopez: 8/4/1998
psherman: 6/10/1998
jamie: 2/18/1997
mark: 2/13/1997