Full text data of PSMC3
PSMC3
(TBP1)
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5; Proteasome 26S subunit ATPase 3; Proteasome subunit P50; Tat-binding protein 1; TBP-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5; Proteasome 26S subunit ATPase 3; Proteasome subunit P50; Tat-binding protein 1; TBP-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00018398
IPI00018398 PSMC3 protein 26S protease regulatory subunit 6A, subunit S10 in membrane 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
IPI00018398 PSMC3 protein 26S protease regulatory subunit 6A, subunit S10 in membrane 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
P17980
ID PRS6A_HUMAN Reviewed; 439 AA.
AC P17980; B2R8V1; Q3B757; Q3B865; Q53HU5; Q6GPG8; Q6IBS1; Q96HD3;
read moreDT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=26S protease regulatory subunit 6A;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
DE AltName: Full=Proteasome 26S subunit ATPase 3;
DE AltName: Full=Proteasome subunit P50;
DE AltName: Full=Tat-binding protein 1;
DE Short=TBP-1;
GN Name=PSMC3; Synonyms=TBP1;
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].
RX PubMed=8419915; DOI=10.1073/pnas.90.1.138;
RA Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R.,
RA Rosen C.A.;
RT "The type 1 human immunodeficiency virus Tat binding protein is a
RT transcriptional activator belonging to an additional family of
RT evolutionarily conserved genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Peripheral nerve;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-439.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, AND INTERACTION WITH HIV-1 TAT.
RX PubMed=2194290; DOI=10.1126/science.2194290;
RA Nelbock P., Dillion P.J., Perkins A., Rosen C.A.;
RT "A cDNA for a protein that interacts with the human immunodeficiency
RT virus Tat transactivator.";
RL Science 248:1650-1653(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
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 [8]
RP PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294;
RP 309-327; 335-344; 351-362; 372-386 AND 398-409, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS
RP SPECTROMETRY.
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 [12]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and
RT inducible SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
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 (By similarity). In case of HIV-1 infection,
CC suppresses Tat-mediated transactivation.
CC -!- SUBUNIT: May form a heterodimer with a related family member.
CC Interacts with PAAF1. Interacts with HIV-1 Tat.
CC -!- INTERACTION:
CC P03255-1:- (xeno); NbExp=2; IntAct=EBI-359720, EBI-6692439;
CC P62333:PSMC6; NbExp=5; IntAct=EBI-359720, EBI-357669;
CC O00233:PSMD9; NbExp=4; IntAct=EBI-359720, EBI-750973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC Cytoplasm, P-body (By similarity). Note=Colocalizes with TRIM5 in
CC the cytoplasmic bodies (By similarity).
CC -!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07805.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AK313518; BAG36298.1; -; mRNA.
DR EMBL; CH471064; EAW67916.1; -; Genomic_DNA.
DR EMBL; BC008713; AAH08713.4; -; mRNA.
DR EMBL; BC073165; AAH73165.3; -; mRNA.
DR EMBL; BC106920; AAI06921.1; -; mRNA.
DR EMBL; BC107804; AAI07805.1; ALT_INIT; mRNA.
DR EMBL; AK222485; BAD96205.1; -; mRNA.
DR EMBL; M34079; AAA36666.1; -; mRNA.
DR EMBL; CR456731; CAG33012.1; -; mRNA.
DR PIR; A34832; A34832.
DR RefSeq; NP_002795.2; NM_002804.4.
DR RefSeq; XP_005253078.1; XM_005253021.1.
DR UniGene; Hs.250758; -.
DR ProteinModelPortal; P17980; -.
DR SMR; P17980; 52-439.
DR DIP; DIP-27555N; -.
DR IntAct; P17980; 25.
DR MINT; MINT-1149785; -.
DR STRING; 9606.ENSP00000298852; -.
DR PhosphoSite; P17980; -.
DR DMDM; 20532406; -.
DR REPRODUCTION-2DPAGE; IPI00018398; -.
DR PaxDb; P17980; -.
DR PeptideAtlas; P17980; -.
DR PRIDE; P17980; -.
DR DNASU; 5702; -.
DR Ensembl; ENST00000298852; ENSP00000298852; ENSG00000165916.
DR GeneID; 5702; -.
DR KEGG; hsa:5702; -.
DR UCSC; uc001nfh.2; human.
DR CTD; 5702; -.
DR GeneCards; GC11M047440; -.
DR HGNC; HGNC:9549; PSMC3.
DR HPA; HPA006065; -.
DR MIM; 186852; gene.
DR neXtProt; NX_P17980; -.
DR PharmGKB; PA33894; -.
DR eggNOG; COG1222; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P17980; -.
DR KO; K03065; -.
DR OMA; ATELNHE; -.
DR OrthoDB; EOG7TMZRN; -.
DR PhylomeDB; P17980; -.
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; PSMC3; human.
DR GeneWiki; PSMC3; -.
DR GenomeRNAi; 5702; -.
DR NextBio; 22154; -.
DR PMAP-CutDB; P17980; -.
DR PRO; PR:P17980; -.
DR ArrayExpress; P17980; -.
DR Bgee; P17980; -.
DR CleanEx; HS_PSMC3; -.
DR Genevestigator; P17980; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor 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:0001824; P:blastocyst development; IEA:Ensembl.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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; Host-virus interaction; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 439 26S protease regulatory subunit 6A.
FT /FTId=PRO_0000084698.
FT NP_BIND 227 234 ATP (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 9 9 Phosphoserine.
FT MUTAGEN 233 233 K->H: Loss of function.
FT MUTAGEN 289 289 D->A: Loss of function.
FT CONFLICT 356 356 M -> T (in Ref. 5; BAD96205).
FT CONFLICT 409 409 R -> A (in Ref. 6; AAA36666).
SQ SEQUENCE 439 AA; 49204 MW; 0E443465DDDEBB0B CRC64;
MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS EIKIMKSEVL
RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD PNDQEEDGAN IDLDSQRKGK
CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL VGVNKDSYLI LETLPTEYDS RVKAMEVDER
PTEQYSDIGG LDKQIQELVE AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC
AAQTKATFLK LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR KIEFPMPNEE
ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC VEAGMIALRR GATELTHEDY
MEGILEVQAK KKANLQYYA
//
ID PRS6A_HUMAN Reviewed; 439 AA.
AC P17980; B2R8V1; Q3B757; Q3B865; Q53HU5; Q6GPG8; Q6IBS1; Q96HD3;
read moreDT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 3.
DT 22-JAN-2014, entry version 152.
DE RecName: Full=26S protease regulatory subunit 6A;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
DE AltName: Full=Proteasome 26S subunit ATPase 3;
DE AltName: Full=Proteasome subunit P50;
DE AltName: Full=Tat-binding protein 1;
DE Short=TBP-1;
GN Name=PSMC3; Synonyms=TBP1;
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].
RX PubMed=8419915; DOI=10.1073/pnas.90.1.138;
RA Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R.,
RA Rosen C.A.;
RT "The type 1 human immunodeficiency virus Tat binding protein is a
RT transcriptional activator belonging to an additional family of
RT evolutionarily conserved genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Peripheral nerve;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-439.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, AND INTERACTION WITH HIV-1 TAT.
RX PubMed=2194290; DOI=10.1126/science.2194290;
RA Nelbock P., Dillion P.J., Perkins A., Rosen C.A.;
RT "A cDNA for a protein that interacts with the human immunodeficiency
RT virus Tat transactivator.";
RL Science 248:1650-1653(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
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 [8]
RP PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294;
RP 309-327; 335-344; 351-362; 372-386 AND 398-409, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS
RP SPECTROMETRY.
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 [12]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and
RT inducible SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
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 (By similarity). In case of HIV-1 infection,
CC suppresses Tat-mediated transactivation.
CC -!- SUBUNIT: May form a heterodimer with a related family member.
CC Interacts with PAAF1. Interacts with HIV-1 Tat.
CC -!- INTERACTION:
CC P03255-1:- (xeno); NbExp=2; IntAct=EBI-359720, EBI-6692439;
CC P62333:PSMC6; NbExp=5; IntAct=EBI-359720, EBI-357669;
CC O00233:PSMD9; NbExp=4; IntAct=EBI-359720, EBI-750973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC Cytoplasm, P-body (By similarity). Note=Colocalizes with TRIM5 in
CC the cytoplasmic bodies (By similarity).
CC -!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07805.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
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DR EMBL; AK313518; BAG36298.1; -; mRNA.
DR EMBL; CH471064; EAW67916.1; -; Genomic_DNA.
DR EMBL; BC008713; AAH08713.4; -; mRNA.
DR EMBL; BC073165; AAH73165.3; -; mRNA.
DR EMBL; BC106920; AAI06921.1; -; mRNA.
DR EMBL; BC107804; AAI07805.1; ALT_INIT; mRNA.
DR EMBL; AK222485; BAD96205.1; -; mRNA.
DR EMBL; M34079; AAA36666.1; -; mRNA.
DR EMBL; CR456731; CAG33012.1; -; mRNA.
DR PIR; A34832; A34832.
DR RefSeq; NP_002795.2; NM_002804.4.
DR RefSeq; XP_005253078.1; XM_005253021.1.
DR UniGene; Hs.250758; -.
DR ProteinModelPortal; P17980; -.
DR SMR; P17980; 52-439.
DR DIP; DIP-27555N; -.
DR IntAct; P17980; 25.
DR MINT; MINT-1149785; -.
DR STRING; 9606.ENSP00000298852; -.
DR PhosphoSite; P17980; -.
DR DMDM; 20532406; -.
DR REPRODUCTION-2DPAGE; IPI00018398; -.
DR PaxDb; P17980; -.
DR PeptideAtlas; P17980; -.
DR PRIDE; P17980; -.
DR DNASU; 5702; -.
DR Ensembl; ENST00000298852; ENSP00000298852; ENSG00000165916.
DR GeneID; 5702; -.
DR KEGG; hsa:5702; -.
DR UCSC; uc001nfh.2; human.
DR CTD; 5702; -.
DR GeneCards; GC11M047440; -.
DR HGNC; HGNC:9549; PSMC3.
DR HPA; HPA006065; -.
DR MIM; 186852; gene.
DR neXtProt; NX_P17980; -.
DR PharmGKB; PA33894; -.
DR eggNOG; COG1222; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P17980; -.
DR KO; K03065; -.
DR OMA; ATELNHE; -.
DR OrthoDB; EOG7TMZRN; -.
DR PhylomeDB; P17980; -.
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; PSMC3; human.
DR GeneWiki; PSMC3; -.
DR GenomeRNAi; 5702; -.
DR NextBio; 22154; -.
DR PMAP-CutDB; P17980; -.
DR PRO; PR:P17980; -.
DR ArrayExpress; P17980; -.
DR Bgee; P17980; -.
DR CleanEx; HS_PSMC3; -.
DR Genevestigator; P17980; -.
DR GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor 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:0001824; P:blastocyst development; IEA:Ensembl.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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; Host-virus interaction; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 439 26S protease regulatory subunit 6A.
FT /FTId=PRO_0000084698.
FT NP_BIND 227 234 ATP (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 9 9 Phosphoserine.
FT MUTAGEN 233 233 K->H: Loss of function.
FT MUTAGEN 289 289 D->A: Loss of function.
FT CONFLICT 356 356 M -> T (in Ref. 5; BAD96205).
FT CONFLICT 409 409 R -> A (in Ref. 6; AAA36666).
SQ SEQUENCE 439 AA; 49204 MW; 0E443465DDDEBB0B CRC64;
MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS EIKIMKSEVL
RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD PNDQEEDGAN IDLDSQRKGK
CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL VGVNKDSYLI LETLPTEYDS RVKAMEVDER
PTEQYSDIGG LDKQIQELVE AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC
AAQTKATFLK LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR KIEFPMPNEE
ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC VEAGMIALRR GATELTHEDY
MEGILEVQAK KKANLQYYA
//
MIM
186852
*RECORD*
*FIELD* NO
186852
*FIELD* TI
*186852 PROTEASOME 26S SUBUNIT, ATPase, 3; PSMC3
;;TAT-BINDING PROTEIN 1; TBP1
*FIELD* TX
read more
CLONING
The human immunodeficiency virus-1 (HIV-1) protein Tat is a potent
activator of virus gene expression and replication. Nelbock et al.
(1990) used biotinylated Tat as a probe to screen a lambda-gt11 fusion
protein library, thereby cloning a cDNA encoding a protein that
interacts with Tat. Expression of this protein, designated Tat-binding
protein-1, was observed in a variety of cell lines, with expression
being highest in human cells. TBP1 was localized predominantly in the
nucleus, which is consistent with the nuclear localization of Tat. In
cotransfection experiments, expression of TBP1 was able to suppress
Tat-mediated transactivation specifically. Nelbock et al. (1990)
recommended their strategy for direct identification and cloning of
genes encoding proteins that associate with other proteins to modulate
their activity in a positive or negative fashion. Ohana et al. (1993)
suggested that TBP1 is involved in Tat-mediated transcriptional
activation.
GENE FUNCTION
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules (see PSMC1; 602706). DeMartino et al. (1996)
identified a protein complex that enhances PA700 activation of the
proteasome. They found that 2 proteins, p42 (PSMC6; 602708) and p50
(PSMC3), are components of both this complex and PA700. By protein
sequence analysis, DeMartino et al. (1996) determined that p50 and TBP1
are identical.
Hoyle et al. (1997) stated that the PSMC3 gene encodes a protein with 1
AAA (ATPases associated with diverse cellular activities) domain (see
PSMC5; 601681) toward the C terminus.
Corn et al. (2003) established that pVHL (608537), the protein that is
mutant in von Hippel-Lindau syndrome (193300), binds to TBP1. TBP1
associates with the beta-domain of pVHL and complexes with pVHL and
hypoxia-inducible transcription factor HIF1A (603348) in vivo.
Overexpression of TBP1 promotes degradation of HIF1A in a pVHL-dependent
manner that requires the ATPase domain of TBP1. Several distinct
mutations in exon 2 of the VHL gene disrupt binding of pVHL to TBP1. A
pVHL mutant containing an exon 2 missense substitution
coimmunoprecipitated with HIF1A, but not TBP1, and did not promote
degradation of HIF1A. Thus, the ability of pVHL to degrade HIF1A depends
in part on its interaction with TBP1 and suggests a new mechanism for
HIF1A stabilization in some pVHL-deficient tumors.
MAPPING
By PCR amplification of a partial PSMC3 sequence, Hoyle et al. (1997)
demonstrated that the PSMC3 gene is located on chromosome 11. By
fluorescence in situ hybridization (FISH), the assignment was
regionalized to 11p13-p12. Tanahashi et al. (1998) mapped the PSMC3 gene
to 11p11.2 by FISH. By interspecific backcross analysis, Sakao et al.
(2000) mapped the mouse Psmc3 gene to chromosome 2.
*FIELD* RF
1. Corn, P. G.; McDonald, E. R., III; Herman, J. G.; El-Deiry, W.
S.: Tat-binding protein-1, a component of the 26S proteasome, contributes
to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nature
Genet. 35: 229-237, 2003.
2. 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.
3. 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.
4. Nelbock, P.; Dillon, P. J.; Perkins, A.; Rosen, C. A.: A cDNA
for a protein that interacts with the human immunodeficiency virus
Tat transactivator. Science 248: 1650-1653, 1990.
5. Ohana, B.; Moore, P. A.; Ruben, S. M.; Southgate, C. D.; Green,
M. R.; Rosen, C. A.: The type 1 human immunodeficiency virus Tat
binding protein is a transcriptional activator belonging to an additional
family of evolutionarily conserved genes. Proc. Nat. Acad. Sci. 90:
138-142, 1993.
6. Sakao, Y.; Kawai, T.; Takeuchi, O.; Copeland, N. G.; Gilbert, D.
J.; Jenkins, N. A.; Takeda, K.; Akira, S.: Mouse proteasomal ATPases
Psmc3 and Psmc4: genomic organization and gene targeting. Genomics 67:
1-7, 2000.
7. 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
Victor A. McKusick - updated: 10/17/2003
Carol A. Bocchini - updated: 2/15/2001
Rebekah S. Rasooly - updated: 6/11/1998
Victor A. McKusick - updated: 2/13/1997
*FIELD* CD
Victor A. McKusick: 8/25/1992
*FIELD* ED
ckniffin: 03/23/2004
alopez: 10/31/2003
alopez: 10/21/2003
terry: 10/17/2003
carol: 2/15/2001
psherman: 6/11/1998
mark: 2/13/1997
terry: 2/11/1997
mark: 5/9/1996
carol: 10/20/1993
carol: 8/25/1992
*RECORD*
*FIELD* NO
186852
*FIELD* TI
*186852 PROTEASOME 26S SUBUNIT, ATPase, 3; PSMC3
;;TAT-BINDING PROTEIN 1; TBP1
*FIELD* TX
read more
CLONING
The human immunodeficiency virus-1 (HIV-1) protein Tat is a potent
activator of virus gene expression and replication. Nelbock et al.
(1990) used biotinylated Tat as a probe to screen a lambda-gt11 fusion
protein library, thereby cloning a cDNA encoding a protein that
interacts with Tat. Expression of this protein, designated Tat-binding
protein-1, was observed in a variety of cell lines, with expression
being highest in human cells. TBP1 was localized predominantly in the
nucleus, which is consistent with the nuclear localization of Tat. In
cotransfection experiments, expression of TBP1 was able to suppress
Tat-mediated transactivation specifically. Nelbock et al. (1990)
recommended their strategy for direct identification and cloning of
genes encoding proteins that associate with other proteins to modulate
their activity in a positive or negative fashion. Ohana et al. (1993)
suggested that TBP1 is involved in Tat-mediated transcriptional
activation.
GENE FUNCTION
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease. The
protease is composed of a 20S catalytic proteasome and 2 PA700
regulatory modules (see PSMC1; 602706). DeMartino et al. (1996)
identified a protein complex that enhances PA700 activation of the
proteasome. They found that 2 proteins, p42 (PSMC6; 602708) and p50
(PSMC3), are components of both this complex and PA700. By protein
sequence analysis, DeMartino et al. (1996) determined that p50 and TBP1
are identical.
Hoyle et al. (1997) stated that the PSMC3 gene encodes a protein with 1
AAA (ATPases associated with diverse cellular activities) domain (see
PSMC5; 601681) toward the C terminus.
Corn et al. (2003) established that pVHL (608537), the protein that is
mutant in von Hippel-Lindau syndrome (193300), binds to TBP1. TBP1
associates with the beta-domain of pVHL and complexes with pVHL and
hypoxia-inducible transcription factor HIF1A (603348) in vivo.
Overexpression of TBP1 promotes degradation of HIF1A in a pVHL-dependent
manner that requires the ATPase domain of TBP1. Several distinct
mutations in exon 2 of the VHL gene disrupt binding of pVHL to TBP1. A
pVHL mutant containing an exon 2 missense substitution
coimmunoprecipitated with HIF1A, but not TBP1, and did not promote
degradation of HIF1A. Thus, the ability of pVHL to degrade HIF1A depends
in part on its interaction with TBP1 and suggests a new mechanism for
HIF1A stabilization in some pVHL-deficient tumors.
MAPPING
By PCR amplification of a partial PSMC3 sequence, Hoyle et al. (1997)
demonstrated that the PSMC3 gene is located on chromosome 11. By
fluorescence in situ hybridization (FISH), the assignment was
regionalized to 11p13-p12. Tanahashi et al. (1998) mapped the PSMC3 gene
to 11p11.2 by FISH. By interspecific backcross analysis, Sakao et al.
(2000) mapped the mouse Psmc3 gene to chromosome 2.
*FIELD* RF
1. Corn, P. G.; McDonald, E. R., III; Herman, J. G.; El-Deiry, W.
S.: Tat-binding protein-1, a component of the 26S proteasome, contributes
to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nature
Genet. 35: 229-237, 2003.
2. 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.
3. 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.
4. Nelbock, P.; Dillon, P. J.; Perkins, A.; Rosen, C. A.: A cDNA
for a protein that interacts with the human immunodeficiency virus
Tat transactivator. Science 248: 1650-1653, 1990.
5. Ohana, B.; Moore, P. A.; Ruben, S. M.; Southgate, C. D.; Green,
M. R.; Rosen, C. A.: The type 1 human immunodeficiency virus Tat
binding protein is a transcriptional activator belonging to an additional
family of evolutionarily conserved genes. Proc. Nat. Acad. Sci. 90:
138-142, 1993.
6. Sakao, Y.; Kawai, T.; Takeuchi, O.; Copeland, N. G.; Gilbert, D.
J.; Jenkins, N. A.; Takeda, K.; Akira, S.: Mouse proteasomal ATPases
Psmc3 and Psmc4: genomic organization and gene targeting. Genomics 67:
1-7, 2000.
7. Tanahashi, N.; Suzuki, M.; Fujiwara, T.; Takahashi, E.; Shimbara,
N.; Chung, C. H.; Tanaka, K.: Chromosomal localization and immunological
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*FIELD* CN
Victor A. McKusick - updated: 10/17/2003
Carol A. Bocchini - updated: 2/15/2001
Rebekah S. Rasooly - updated: 6/11/1998
Victor A. McKusick - updated: 2/13/1997
*FIELD* CD
Victor A. McKusick: 8/25/1992
*FIELD* ED
ckniffin: 03/23/2004
alopez: 10/31/2003
alopez: 10/21/2003
terry: 10/17/2003
carol: 2/15/2001
psherman: 6/11/1998
mark: 2/13/1997
terry: 2/11/1997
mark: 5/9/1996
carol: 10/20/1993
carol: 8/25/1992