Full text data of PSMC4
PSMC4
(MIP224, TBP7)
[Confidence: high (present in two of the MS resources)]
26S protease regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3; MB67-interacting protein; MIP224; Proteasome 26S subunit ATPase 4; Tat-binding protein 7; TBP-7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S protease regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3; MB67-interacting protein; MIP224; Proteasome 26S subunit ATPase 4; Tat-binding protein 7; TBP-7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00020042
IPI00020042 Splice Isoform 1 Of 26S protease regulatory subunit 6B 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 LQQELEFLEVQEEYIK found at its expected molecular weight found at molecular weight
IPI00020042 Splice Isoform 1 Of 26S protease regulatory subunit 6B 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 LQQELEFLEVQEEYIK found at its expected molecular weight found at molecular weight
UniProt
P43686
ID PRS6B_HUMAN Reviewed; 418 AA.
AC P43686; Q96FV5; Q9UBM3; Q9UEX3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=26S protease regulatory subunit 6B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE AltName: Full=MB67-interacting protein;
DE AltName: Full=MIP224;
DE AltName: Full=Proteasome 26S subunit ATPase 4;
DE AltName: Full=Tat-binding protein 7;
DE Short=TBP-7;
GN Name=PSMC4; Synonyms=MIP224, TBP7;
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).
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] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH NR1I3.
RX PubMed=8603043; DOI=10.1016/0960-0760(95)00220-0;
RA Choi H.S., Seol W., Moore D.D.;
RT "A component of the 26S proteasome binds on orphan member of the
RT nuclear hormone receptor superfamily.";
RL J. Steroid Biochem. Mol. Biol. 56:23-30(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bi A., Yu L., Zheng L.;
RT "Cloning and expression analysis of a novel human gene homologous to
RT mouse proteasomal ATPase (Tat-binding protein 7).";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Pancreas, and Skin;
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 PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT
RP MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8060531;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Tat-binding protein 7 is a subunit of the 26S protease.";
RL Biol. Chem. Hoppe-Seyler 375:237-240(1994).
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-28, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-401, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP 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 [18]
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 [19]
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 [20]
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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE
RP PSMD10.
RX PubMed=17292836; DOI=10.1016/j.str.2006.11.015;
RA Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y.,
RA Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S.;
RT "Structure of the oncoprotein gankyrin in complex with S6 ATPase of
RT the 26S proteasome.";
RL Structure 15:179-189(2007).
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 with NR1I3. Interacts with PAAF1. Interacts
CC with TRIM5.
CC -!- INTERACTION:
CC P62195:PSMC5; NbExp=11; IntAct=EBI-743997, EBI-357745;
CC P62333:PSMC6; NbExp=3; IntAct=EBI-743997, EBI-357669;
CC O75832:PSMD10; NbExp=8; IntAct=EBI-743997, EBI-752185;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43686-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43686-2; Sequence=VSP_000022;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF038965; AAC26843.1; -; mRNA.
DR EMBL; U27515; AAC99817.1; -; mRNA.
DR EMBL; AF020736; AAC32612.1; -; mRNA.
DR EMBL; BT007232; AAP35896.1; -; mRNA.
DR EMBL; AC007842; AAD39267.1; -; Genomic_DNA.
DR EMBL; BC000343; AAH00343.1; -; mRNA.
DR EMBL; BC010396; AAH10396.1; -; mRNA.
DR EMBL; BC014488; AAH14488.1; -; mRNA.
DR RefSeq; NP_006494.1; NM_006503.3.
DR RefSeq; NP_694546.1; NM_153001.2.
DR UniGene; Hs.211594; -.
DR PDB; 2DVW; X-ray; 2.30 A; B=337-418.
DR PDBsum; 2DVW; -.
DR ProteinModelPortal; P43686; -.
DR SMR; P43686; 41-418.
DR DIP; DIP-29274N; -.
DR IntAct; P43686; 20.
DR MINT; MINT-5004247; -.
DR STRING; 9606.ENSP00000157812; -.
DR PhosphoSite; P43686; -.
DR DMDM; 20532409; -.
DR OGP; P43686; -.
DR PaxDb; P43686; -.
DR PRIDE; P43686; -.
DR DNASU; 5704; -.
DR Ensembl; ENST00000157812; ENSP00000157812; ENSG00000013275.
DR Ensembl; ENST00000455878; ENSP00000413869; ENSG00000013275.
DR GeneID; 5704; -.
DR KEGG; hsa:5704; -.
DR UCSC; uc002omq.4; human.
DR CTD; 5704; -.
DR GeneCards; GC19P040477; -.
DR HGNC; HGNC:9551; PSMC4.
DR HPA; HPA002044; -.
DR HPA; HPA005471; -.
DR MIM; 602707; gene.
DR neXtProt; NX_P43686; -.
DR PharmGKB; PA33896; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P43686; -.
DR KO; K03063; -.
DR OMA; FIRINGS; -.
DR OrthoDB; EOG7F24ST; -.
DR PhylomeDB; P43686; -.
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; PSMC4; human.
DR EvolutionaryTrace; P43686; -.
DR GeneWiki; PSMC4; -.
DR GenomeRNAi; 5704; -.
DR NextBio; 22160; -.
DR PRO; PR:P43686; -.
DR ArrayExpress; P43686; -.
DR Bgee; P43686; -.
DR CleanEx; HS_PSMC4; -.
DR Genevestigator; P43686; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
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; 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: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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT CHAIN 1 418 26S protease regulatory subunit 6B.
FT /FTId=PRO_0000084686.
FT NP_BIND 206 213 ATP (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 397 397 N6-acetyllysine.
FT MOD_RES 401 401 N6-acetyllysine.
FT VAR_SEQ 46 76 Missing (in isoform 2).
FT /FTId=VSP_000022.
FT CONFLICT 73 73 L -> F (in Ref. 4; AAC32612).
FT CONFLICT 110 110 N -> S (in Ref. 4; AAC32612).
FT CONFLICT 118 118 T -> A (in Ref. 1; no nucleotide entry).
FT CONFLICT 157 157 D -> G (in Ref. 4; AAC32612).
FT CONFLICT 185 185 L -> V (in Ref. 4; AAC32612).
FT HELIX 338 348
FT TURN 349 351
FT HELIX 361 364
FT HELIX 372 388
FT STRAND 392 394
FT HELIX 396 406
SQ SEQUENCE 418 AA; 47366 MW; 80F9523C61B88F0C CRC64;
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
//
ID PRS6B_HUMAN Reviewed; 418 AA.
AC P43686; Q96FV5; Q9UBM3; Q9UEX3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=26S protease regulatory subunit 6B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE AltName: Full=MB67-interacting protein;
DE AltName: Full=MIP224;
DE AltName: Full=Proteasome 26S subunit ATPase 4;
DE AltName: Full=Tat-binding protein 7;
DE Short=TBP-7;
GN Name=PSMC4; Synonyms=MIP224, TBP7;
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).
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] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH NR1I3.
RX PubMed=8603043; DOI=10.1016/0960-0760(95)00220-0;
RA Choi H.S., Seol W., Moore D.D.;
RT "A component of the 26S proteasome binds on orphan member of the
RT nuclear hormone receptor superfamily.";
RL J. Steroid Biochem. Mol. Biol. 56:23-30(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bi A., Yu L., Zheng L.;
RT "Cloning and expression analysis of a novel human gene homologous to
RT mouse proteasomal ATPase (Tat-binding protein 7).";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Pancreas, and Skin;
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 PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT
RP MET-1, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8060531;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Tat-binding protein 7 is a subunit of the 26S protease.";
RL Biol. Chem. Hoppe-Seyler 375:237-240(1994).
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-28, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-28, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-401, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP 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 [18]
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 [19]
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 [20]
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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE
RP PSMD10.
RX PubMed=17292836; DOI=10.1016/j.str.2006.11.015;
RA Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y.,
RA Tanaka A., Horikoshi M., Padmanabhan B., Yokoyama S.;
RT "Structure of the oncoprotein gankyrin in complex with S6 ATPase of
RT the 26S proteasome.";
RL Structure 15:179-189(2007).
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 with NR1I3. Interacts with PAAF1. Interacts
CC with TRIM5.
CC -!- INTERACTION:
CC P62195:PSMC5; NbExp=11; IntAct=EBI-743997, EBI-357745;
CC P62333:PSMC6; NbExp=3; IntAct=EBI-743997, EBI-357669;
CC O75832:PSMD10; NbExp=8; IntAct=EBI-743997, EBI-752185;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43686-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43686-2; Sequence=VSP_000022;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF038965; AAC26843.1; -; mRNA.
DR EMBL; U27515; AAC99817.1; -; mRNA.
DR EMBL; AF020736; AAC32612.1; -; mRNA.
DR EMBL; BT007232; AAP35896.1; -; mRNA.
DR EMBL; AC007842; AAD39267.1; -; Genomic_DNA.
DR EMBL; BC000343; AAH00343.1; -; mRNA.
DR EMBL; BC010396; AAH10396.1; -; mRNA.
DR EMBL; BC014488; AAH14488.1; -; mRNA.
DR RefSeq; NP_006494.1; NM_006503.3.
DR RefSeq; NP_694546.1; NM_153001.2.
DR UniGene; Hs.211594; -.
DR PDB; 2DVW; X-ray; 2.30 A; B=337-418.
DR PDBsum; 2DVW; -.
DR ProteinModelPortal; P43686; -.
DR SMR; P43686; 41-418.
DR DIP; DIP-29274N; -.
DR IntAct; P43686; 20.
DR MINT; MINT-5004247; -.
DR STRING; 9606.ENSP00000157812; -.
DR PhosphoSite; P43686; -.
DR DMDM; 20532409; -.
DR OGP; P43686; -.
DR PaxDb; P43686; -.
DR PRIDE; P43686; -.
DR DNASU; 5704; -.
DR Ensembl; ENST00000157812; ENSP00000157812; ENSG00000013275.
DR Ensembl; ENST00000455878; ENSP00000413869; ENSG00000013275.
DR GeneID; 5704; -.
DR KEGG; hsa:5704; -.
DR UCSC; uc002omq.4; human.
DR CTD; 5704; -.
DR GeneCards; GC19P040477; -.
DR HGNC; HGNC:9551; PSMC4.
DR HPA; HPA002044; -.
DR HPA; HPA005471; -.
DR MIM; 602707; gene.
DR neXtProt; NX_P43686; -.
DR PharmGKB; PA33896; -.
DR eggNOG; COG1222; -.
DR HOGENOM; HOG000225143; -.
DR HOVERGEN; HBG000109; -.
DR InParanoid; P43686; -.
DR KO; K03063; -.
DR OMA; FIRINGS; -.
DR OrthoDB; EOG7F24ST; -.
DR PhylomeDB; P43686; -.
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; PSMC4; human.
DR EvolutionaryTrace; P43686; -.
DR GeneWiki; PSMC4; -.
DR GenomeRNAi; 5704; -.
DR NextBio; 22160; -.
DR PRO; PR:P43686; -.
DR ArrayExpress; P43686; -.
DR Bgee; P43686; -.
DR CleanEx; HS_PSMC4; -.
DR Genevestigator; P43686; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
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; 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: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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT CHAIN 1 418 26S protease regulatory subunit 6B.
FT /FTId=PRO_0000084686.
FT NP_BIND 206 213 ATP (Potential).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 397 397 N6-acetyllysine.
FT MOD_RES 401 401 N6-acetyllysine.
FT VAR_SEQ 46 76 Missing (in isoform 2).
FT /FTId=VSP_000022.
FT CONFLICT 73 73 L -> F (in Ref. 4; AAC32612).
FT CONFLICT 110 110 N -> S (in Ref. 4; AAC32612).
FT CONFLICT 118 118 T -> A (in Ref. 1; no nucleotide entry).
FT CONFLICT 157 157 D -> G (in Ref. 4; AAC32612).
FT CONFLICT 185 185 L -> V (in Ref. 4; AAC32612).
FT HELIX 338 348
FT TURN 349 351
FT HELIX 361 364
FT HELIX 372 388
FT STRAND 392 394
FT HELIX 396 406
SQ SEQUENCE 418 AA; 47366 MW; 80F9523C61B88F0C CRC64;
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
//
MIM
602707
*RECORD*
*FIELD* NO
602707
*FIELD* TI
*602707 PROTEASOME 26S SUBUNIT, ATPase, 4; PSMC4
;;TAT-BINDING PROTEIN 7; TBP7;;
PROTEASE 26S, SUBUNIT 6; S6
read more*FIELD* TX
CLONING
Ohana et al. (1993) identified a cDNA encoding Tat-binding protein-7
(TBP7). The predicted 458-amino acid TBP7 protein is 57% identical to
TBP1 (PSMC3; 186852) over a 210-amino acid stretch. Using the yeast
2-hybrid system, Ohana et al. (1993) found that TBP1 and TBP7 can form
heterodimers. They suggested that the dimerization was mediated by the
N-terminal leucine zipper domains of these proteins. By
immunofluorescence, Ohana et al. (1993) showed that TBP7 is located
primarily in the nucleus.
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease that
consists of more than 30 subunits (see PSMC1; 602706). By protein
sequence analysis, Dubiel et al. (1994) found that subunit 6 (S6), an
approximately 50-kD polypeptide, is encoded by the TBP7 gene. Dubiel et
al. (1994) noted differences between the C-terminal regions of S6 and
the predicted TBP7 protein described by Ohana et al. (1993) and
attributed them to a hypothetical frameshift in TBP7 resulting from a
sequencing error. The predicted 418-amino acid S6 protein contains an
ATPase domain similar to those of PSMC1 and PSMC2 (154365).
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the PSMC4 gene to 19q13.11-q13.13. By interspecific backcross analysis,
Sakao et al. (2000) mapped the mouse Psmc4 gene to chromosome 7.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Rechsteiner, M.: Tat-binding protein
7 is a subunit of the 26S protease. Biol. Chem. Hoppe Seyler 375:
237-240, 1994.
2. 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.
3. 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.
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
Carol A. Bocchini - updated: 2/15/2001
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
carol: 06/11/2012
terry: 9/17/2010
carol: 2/15/2001
psherman: 6/13/1998
psherman: 6/11/1998
*RECORD*
*FIELD* NO
602707
*FIELD* TI
*602707 PROTEASOME 26S SUBUNIT, ATPase, 4; PSMC4
;;TAT-BINDING PROTEIN 7; TBP7;;
PROTEASE 26S, SUBUNIT 6; S6
read more*FIELD* TX
CLONING
Ohana et al. (1993) identified a cDNA encoding Tat-binding protein-7
(TBP7). The predicted 458-amino acid TBP7 protein is 57% identical to
TBP1 (PSMC3; 186852) over a 210-amino acid stretch. Using the yeast
2-hybrid system, Ohana et al. (1993) found that TBP1 and TBP7 can form
heterodimers. They suggested that the dimerization was mediated by the
N-terminal leucine zipper domains of these proteins. By
immunofluorescence, Ohana et al. (1993) showed that TBP7 is located
primarily in the nucleus.
Ubiquitinated proteins are degraded by a 26S ATP-dependent protease that
consists of more than 30 subunits (see PSMC1; 602706). By protein
sequence analysis, Dubiel et al. (1994) found that subunit 6 (S6), an
approximately 50-kD polypeptide, is encoded by the TBP7 gene. Dubiel et
al. (1994) noted differences between the C-terminal regions of S6 and
the predicted TBP7 protein described by Ohana et al. (1993) and
attributed them to a hypothetical frameshift in TBP7 resulting from a
sequencing error. The predicted 418-amino acid S6 protein contains an
ATPase domain similar to those of PSMC1 and PSMC2 (154365).
MAPPING
By fluorescence in situ hybridization, Tanahashi et al. (1998) mapped
the PSMC4 gene to 19q13.11-q13.13. By interspecific backcross analysis,
Sakao et al. (2000) mapped the mouse Psmc4 gene to chromosome 7.
*FIELD* RF
1. Dubiel, W.; Ferrell, K.; Rechsteiner, M.: Tat-binding protein
7 is a subunit of the 26S protease. Biol. Chem. Hoppe Seyler 375:
237-240, 1994.
2. 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.
3. 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.
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
Carol A. Bocchini - updated: 2/15/2001
*FIELD* CD
Rebekah S. Rasooly: 6/10/1998
*FIELD* ED
carol: 06/11/2012
terry: 9/17/2010
carol: 2/15/2001
psherman: 6/13/1998
psherman: 6/11/1998