Full text data of TCEB2
TCEB2
[Confidence: low (only semi-automatic identification from reviews)]
Transcription elongation factor B polypeptide 2 (Elongin 18 kDa subunit; Elongin-B; EloB; RNA polymerase II transcription factor SIII subunit B; SIII p18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcription elongation factor B polypeptide 2 (Elongin 18 kDa subunit; Elongin-B; EloB; RNA polymerase II transcription factor SIII subunit B; SIII p18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15370
ID ELOB_HUMAN Reviewed; 118 AA.
AC Q15370; B7WPD3;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=Transcription elongation factor B polypeptide 2;
DE AltName: Full=Elongin 18 kDa subunit;
DE AltName: Full=Elongin-B;
DE Short=EloB;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit B;
DE AltName: Full=SIII p18;
GN Name=TCEB2;
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), AND FUNCTION.
RX PubMed=7638163; DOI=10.1073/pnas.92.16.7172;
RA Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S.,
RA Conaway R.C., Conaway J.W.;
RT "Positive regulation of general transcription factor SIII by a tailed
RT ubiquitin homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Bonaldo M.F., Lennon G., Soares M.B.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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=Pancreas, and Placenta;
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 PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH VHL.
RX PubMed=11006129; DOI=10.1006/bbrc.2000.3451;
RA Aso T., Yamazaki K., Aigaki T., Kitajima S.;
RT "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3
RT ubiquitin ligase activity.";
RL Biochem. Biophys. Res. Commun. 276:355-361(2000).
RN [8]
RP INTERACTION WITH HIV VIF.
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
RT Vif-Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [9]
RP INTERACTION WITH SPSB1.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
RN [10]
RP FUNCTION IN EGFR DEGRADATION, AND INTERACTION WITH SOCS5.
RX PubMed=15590694; DOI=10.1074/jbc.M408575200;
RA Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N.,
RA Rechavi G., Yarden Y.;
RT "Suppressors of cytokine signaling 4 and 5 regulate epidermal growth
RT factor receptor signaling.";
RL J. Biol. Chem. 280:7038-7048(2005).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH KLHDC10.
RX PubMed=23102700; DOI=10.1016/j.molcel.2012.09.018;
RA Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T.,
RA Kuranaga E., Miura M., Takeda K., Ichijo H.;
RT "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced
RT ASK1 activation by suppressing PP5.";
RL Mol. Cell 48:692-704(2012).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2.
RX PubMed=22286099; DOI=10.1038/ncb2424;
RA Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C.,
RA Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J.,
RA Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.;
RT "The LIMD1 protein bridges an association between the prolyl
RT hydroxylases and VHL to repress HIF-1 activity.";
RL Nat. Cell Biol. 14:201-208(2012).
RN [15]
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH TCEB1 AND VHL.
RX PubMed=10205047; DOI=10.1126/science.284.5413.455;
RA Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.;
RT "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL
RT tumor suppressor function.";
RL Science 284:455-461(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP HIF1A.
RX PubMed=12050673; DOI=10.1038/nature00767;
RA Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J.,
RA Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.;
RT "Structural basis for the recognition of hydroxyproline in HIF-1 alpha
RT by pVHL.";
RL Nature 417:975-978(2002).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP HIF1A.
RX PubMed=12004076; DOI=10.1126/science.1073440;
RA Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr.,
RA Pavletich N.P.;
RT "Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition
RT in signaling.";
RL Science 296:1886-1889(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH TCEB1 ANS SOX4,
RP AND SUBUNIT.
RX PubMed=17997974; DOI=10.1016/j.str.2007.09.016;
RA Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.;
RT "Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box
RT interface and the molecular basis for SOCS-dependent EGFR
RT degradation.";
RL Structure 15:1493-1504(2007).
CC -!- FUNCTION: SIII, also known as elongin, is a general transcription
CC elongation factor that increases the RNA polymerase II
CC transcription elongation past template-encoded arresting sites.
CC Subunit A is transcriptionally active and its transcription
CC activity is strongly enhanced by binding to the dimeric complex of
CC the SIII regulatory subunits B and C (elongin BC complex).
CC -!- FUNCTION: The elongin BC complex seems to be involved as an
CC adapter protein in the proteasomal degradation of target proteins
CC via different E3 ubiquitin ligase complexes, including the von
CC Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-
CC box motifs it seems to link target recruitment subunits, like VHL
CC and members of the SOCS box family, to Cullin/RBX1 modules that
CC activate E2 ubiquitination enzymes.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterotrimer of an A (A1, A2 or A3), B and C subunit.
CC Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and
CC a substrate adapter protein that can be either SOCS1, SOCS5,
CC TCEB3, VHL or WSB1. Substrate adapter protein can be a viral
CC protein such as HIV Vif. Interacts with VHL. Found in a complex
CC composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with
CC SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase
CC complex substrate recognition component.
CC -!- INTERACTION:
CC Q96G25:MED8; NbExp=5; IntAct=EBI-301238, EBI-394405;
CC Q15369:TCEB1; NbExp=5; IntAct=EBI-301238, EBI-301231;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-301238, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15370-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15370-2; Sequence=VSP_045784;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08452.1; Type=Erroneous gene model prediction;
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DR EMBL; L42856; AAA75522.1; -; mRNA.
DR EMBL; BM700019; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004493; AAC08452.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85472.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85474.1; -; Genomic_DNA.
DR EMBL; BC013306; AAH13306.1; -; mRNA.
DR EMBL; BC065000; AAH65000.1; -; mRNA.
DR PIR; I59405; I59405.
DR RefSeq; NP_009039.1; NM_007108.3.
DR RefSeq; NP_996896.1; NM_207013.2.
DR UniGene; Hs.172772; -.
DR PDB; 1LM8; X-ray; 1.85 A; B=1-118.
DR PDB; 1LQB; X-ray; 2.00 A; A=1-118.
DR PDB; 1VCB; X-ray; 2.70 A; A/D/G/J=1-118.
DR PDB; 2C9W; X-ray; 1.90 A; B=1-118.
DR PDB; 2IZV; X-ray; 2.55 A; B=1-118.
DR PDB; 2JZ3; NMR; -; B=1-118.
DR PDB; 3DCG; X-ray; 2.40 A; A/C=1-118.
DR PDB; 3ZKJ; X-ray; 2.58 A; C/F=1-118.
DR PDB; 3ZRC; X-ray; 2.90 A; A/D/G/J=1-118.
DR PDB; 3ZRF; X-ray; 2.80 A; A/D/G/J=1-118.
DR PDB; 3ZTC; X-ray; 2.65 A; A/D/G/J=1-118.
DR PDB; 3ZTD; X-ray; 2.79 A; A/D/G/J=1-118.
DR PDB; 3ZUN; X-ray; 2.50 A; A/D/G/J=1-118.
DR PDB; 4AJY; X-ray; 1.73 A; B=1-118.
DR PDB; 4AWJ; X-ray; 2.50 A; A/D/G/J=1-104.
DR PDB; 4B95; X-ray; 2.80 A; A/D/G/J=1-118.
DR PDB; 4B9K; X-ray; 2.00 A; A/D/G/J=1-104.
DR PDBsum; 1LM8; -.
DR PDBsum; 1LQB; -.
DR PDBsum; 1VCB; -.
DR PDBsum; 2C9W; -.
DR PDBsum; 2IZV; -.
DR PDBsum; 2JZ3; -.
DR PDBsum; 3DCG; -.
DR PDBsum; 3ZKJ; -.
DR PDBsum; 3ZRC; -.
DR PDBsum; 3ZRF; -.
DR PDBsum; 3ZTC; -.
DR PDBsum; 3ZTD; -.
DR PDBsum; 3ZUN; -.
DR PDBsum; 4AJY; -.
DR PDBsum; 4AWJ; -.
DR PDBsum; 4B95; -.
DR PDBsum; 4B9K; -.
DR ProteinModelPortal; Q15370; -.
DR SMR; Q15370; 1-118.
DR DIP; DIP-29570N; -.
DR IntAct; Q15370; 30.
DR MINT; MINT-1323839; -.
DR STRING; 9606.ENSP00000262306; -.
DR PhosphoSite; Q15370; -.
DR DMDM; 32699512; -.
DR PaxDb; Q15370; -.
DR PeptideAtlas; Q15370; -.
DR PRIDE; Q15370; -.
DR DNASU; 6923; -.
DR Ensembl; ENST00000262306; ENSP00000262306; ENSG00000103363.
DR Ensembl; ENST00000409906; ENSP00000386652; ENSG00000103363.
DR GeneID; 6923; -.
DR KEGG; hsa:6923; -.
DR UCSC; uc002crm.3; human.
DR CTD; 6923; -.
DR GeneCards; GC16M002824; -.
DR HGNC; HGNC:11619; TCEB2.
DR MIM; 600787; gene.
DR neXtProt; NX_Q15370; -.
DR PharmGKB; PA36378; -.
DR eggNOG; NOG316144; -.
DR HOGENOM; HOG000293425; -.
DR HOVERGEN; HBG008581; -.
DR KO; K03873; -.
DR OMA; TLGDCGF; -.
DR OrthoDB; EOG7GQXX6; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q15370; -.
DR GeneWiki; TCEB2; -.
DR GenomeRNAi; 6923; -.
DR NextBio; 27083; -.
DR PRO; PR:Q15370; -.
DR ArrayExpress; Q15370; -.
DR Bgee; Q15370; -.
DR CleanEx; HS_TCEB2; -.
DR Genevestigator; Q15370; -.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1 118 Transcription elongation factor B
FT polypeptide 2.
FT /FTId=PRO_0000114914.
FT DOMAIN 1 66 Ubiquitin-like.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 118 118 Q -> HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPT
FT QVHPRWGL (in isoform 2).
FT /FTId=VSP_045784.
FT STRAND 2 10
FT STRAND 12 19
FT HELIX 24 35
FT HELIX 39 41
FT STRAND 42 46
FT STRAND 49 51
FT TURN 57 61
FT HELIX 64 66
FT STRAND 73 79
FT STRAND 82 84
FT STRAND 96 98
FT HELIX 101 103
FT STRAND 110 112
SQ SEQUENCE 118 AA; 13133 MW; C045F58FBED0EC47 CRC64;
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC
GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ
//
ID ELOB_HUMAN Reviewed; 118 AA.
AC Q15370; B7WPD3;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=Transcription elongation factor B polypeptide 2;
DE AltName: Full=Elongin 18 kDa subunit;
DE AltName: Full=Elongin-B;
DE Short=EloB;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit B;
DE AltName: Full=SIII p18;
GN Name=TCEB2;
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), AND FUNCTION.
RX PubMed=7638163; DOI=10.1073/pnas.92.16.7172;
RA Garrett K.P., Aso T., Bradsher J.N., Foundling S.I., Lane W.S.,
RA Conaway R.C., Conaway J.W.;
RT "Positive regulation of general transcription factor SIII by a tailed
RT ubiquitin homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7172-7176(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Bonaldo M.F., Lennon G., Soares M.B.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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=Pancreas, and Placenta;
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 PROTEIN SEQUENCE OF 1-8 AND 44-80, ACETYLATION AT MET-1, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP INTERACTION WITH VHL.
RX PubMed=11006129; DOI=10.1006/bbrc.2000.3451;
RA Aso T., Yamazaki K., Aigaki T., Kitajima S.;
RT "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3
RT ubiquitin ligase activity.";
RL Biochem. Biophys. Res. Commun. 276:355-361(2000).
RN [8]
RP INTERACTION WITH HIV VIF.
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
RT Vif-Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [9]
RP INTERACTION WITH SPSB1.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
RN [10]
RP FUNCTION IN EGFR DEGRADATION, AND INTERACTION WITH SOCS5.
RX PubMed=15590694; DOI=10.1074/jbc.M408575200;
RA Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N.,
RA Rechavi G., Yarden Y.;
RT "Suppressors of cytokine signaling 4 and 5 regulate epidermal growth
RT factor receptor signaling.";
RL J. Biol. Chem. 280:7038-7048(2005).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH KLHDC10.
RX PubMed=23102700; DOI=10.1016/j.molcel.2012.09.018;
RA Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T.,
RA Kuranaga E., Miura M., Takeda K., Ichijo H.;
RT "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced
RT ASK1 activation by suppressing PP5.";
RL Mol. Cell 48:692-704(2012).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND CUL2.
RX PubMed=22286099; DOI=10.1038/ncb2424;
RA Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C.,
RA Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J.,
RA Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V.;
RT "The LIMD1 protein bridges an association between the prolyl
RT hydroxylases and VHL to repress HIF-1 activity.";
RL Nat. Cell Biol. 14:201-208(2012).
RN [15]
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH TCEB1 AND VHL.
RX PubMed=10205047; DOI=10.1126/science.284.5413.455;
RA Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.;
RT "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL
RT tumor suppressor function.";
RL Science 284:455-461(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP HIF1A.
RX PubMed=12050673; DOI=10.1038/nature00767;
RA Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J.,
RA Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.;
RT "Structural basis for the recognition of hydroxyproline in HIF-1 alpha
RT by pVHL.";
RL Nature 417:975-978(2002).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB1; VHL AND
RP HIF1A.
RX PubMed=12004076; DOI=10.1126/science.1073440;
RA Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr.,
RA Pavletich N.P.;
RT "Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition
RT in signaling.";
RL Science 296:1886-1889(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH TCEB1 ANS SOX4,
RP AND SUBUNIT.
RX PubMed=17997974; DOI=10.1016/j.str.2007.09.016;
RA Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.;
RT "Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box
RT interface and the molecular basis for SOCS-dependent EGFR
RT degradation.";
RL Structure 15:1493-1504(2007).
CC -!- FUNCTION: SIII, also known as elongin, is a general transcription
CC elongation factor that increases the RNA polymerase II
CC transcription elongation past template-encoded arresting sites.
CC Subunit A is transcriptionally active and its transcription
CC activity is strongly enhanced by binding to the dimeric complex of
CC the SIII regulatory subunits B and C (elongin BC complex).
CC -!- FUNCTION: The elongin BC complex seems to be involved as an
CC adapter protein in the proteasomal degradation of target proteins
CC via different E3 ubiquitin ligase complexes, including the von
CC Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-
CC box motifs it seems to link target recruitment subunits, like VHL
CC and members of the SOCS box family, to Cullin/RBX1 modules that
CC activate E2 ubiquitination enzymes.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterotrimer of an A (A1, A2 or A3), B and C subunit.
CC Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and
CC a substrate adapter protein that can be either SOCS1, SOCS5,
CC TCEB3, VHL or WSB1. Substrate adapter protein can be a viral
CC protein such as HIV Vif. Interacts with VHL. Found in a complex
CC composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Interacts with
CC SPSB1. Interacts with KLHDC10; which may be an E3 ubiquitin ligase
CC complex substrate recognition component.
CC -!- INTERACTION:
CC Q96G25:MED8; NbExp=5; IntAct=EBI-301238, EBI-394405;
CC Q15369:TCEB1; NbExp=5; IntAct=EBI-301238, EBI-301231;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-301238, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15370-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15370-2; Sequence=VSP_045784;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08452.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
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DR EMBL; L42856; AAA75522.1; -; mRNA.
DR EMBL; BM700019; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC004493; AAC08452.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85472.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85474.1; -; Genomic_DNA.
DR EMBL; BC013306; AAH13306.1; -; mRNA.
DR EMBL; BC065000; AAH65000.1; -; mRNA.
DR PIR; I59405; I59405.
DR RefSeq; NP_009039.1; NM_007108.3.
DR RefSeq; NP_996896.1; NM_207013.2.
DR UniGene; Hs.172772; -.
DR PDB; 1LM8; X-ray; 1.85 A; B=1-118.
DR PDB; 1LQB; X-ray; 2.00 A; A=1-118.
DR PDB; 1VCB; X-ray; 2.70 A; A/D/G/J=1-118.
DR PDB; 2C9W; X-ray; 1.90 A; B=1-118.
DR PDB; 2IZV; X-ray; 2.55 A; B=1-118.
DR PDB; 2JZ3; NMR; -; B=1-118.
DR PDB; 3DCG; X-ray; 2.40 A; A/C=1-118.
DR PDB; 3ZKJ; X-ray; 2.58 A; C/F=1-118.
DR PDB; 3ZRC; X-ray; 2.90 A; A/D/G/J=1-118.
DR PDB; 3ZRF; X-ray; 2.80 A; A/D/G/J=1-118.
DR PDB; 3ZTC; X-ray; 2.65 A; A/D/G/J=1-118.
DR PDB; 3ZTD; X-ray; 2.79 A; A/D/G/J=1-118.
DR PDB; 3ZUN; X-ray; 2.50 A; A/D/G/J=1-118.
DR PDB; 4AJY; X-ray; 1.73 A; B=1-118.
DR PDB; 4AWJ; X-ray; 2.50 A; A/D/G/J=1-104.
DR PDB; 4B95; X-ray; 2.80 A; A/D/G/J=1-118.
DR PDB; 4B9K; X-ray; 2.00 A; A/D/G/J=1-104.
DR PDBsum; 1LM8; -.
DR PDBsum; 1LQB; -.
DR PDBsum; 1VCB; -.
DR PDBsum; 2C9W; -.
DR PDBsum; 2IZV; -.
DR PDBsum; 2JZ3; -.
DR PDBsum; 3DCG; -.
DR PDBsum; 3ZKJ; -.
DR PDBsum; 3ZRC; -.
DR PDBsum; 3ZRF; -.
DR PDBsum; 3ZTC; -.
DR PDBsum; 3ZTD; -.
DR PDBsum; 3ZUN; -.
DR PDBsum; 4AJY; -.
DR PDBsum; 4AWJ; -.
DR PDBsum; 4B95; -.
DR PDBsum; 4B9K; -.
DR ProteinModelPortal; Q15370; -.
DR SMR; Q15370; 1-118.
DR DIP; DIP-29570N; -.
DR IntAct; Q15370; 30.
DR MINT; MINT-1323839; -.
DR STRING; 9606.ENSP00000262306; -.
DR PhosphoSite; Q15370; -.
DR DMDM; 32699512; -.
DR PaxDb; Q15370; -.
DR PeptideAtlas; Q15370; -.
DR PRIDE; Q15370; -.
DR DNASU; 6923; -.
DR Ensembl; ENST00000262306; ENSP00000262306; ENSG00000103363.
DR Ensembl; ENST00000409906; ENSP00000386652; ENSG00000103363.
DR GeneID; 6923; -.
DR KEGG; hsa:6923; -.
DR UCSC; uc002crm.3; human.
DR CTD; 6923; -.
DR GeneCards; GC16M002824; -.
DR HGNC; HGNC:11619; TCEB2.
DR MIM; 600787; gene.
DR neXtProt; NX_Q15370; -.
DR PharmGKB; PA36378; -.
DR eggNOG; NOG316144; -.
DR HOGENOM; HOG000293425; -.
DR HOVERGEN; HBG008581; -.
DR KO; K03873; -.
DR OMA; TLGDCGF; -.
DR OrthoDB; EOG7GQXX6; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q15370; -.
DR GeneWiki; TCEB2; -.
DR GenomeRNAi; 6923; -.
DR NextBio; 27083; -.
DR PRO; PR:Q15370; -.
DR ArrayExpress; Q15370; -.
DR Bgee; Q15370; -.
DR CleanEx; HS_TCEB2; -.
DR Genevestigator; Q15370; -.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1 118 Transcription elongation factor B
FT polypeptide 2.
FT /FTId=PRO_0000114914.
FT DOMAIN 1 66 Ubiquitin-like.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 118 118 Q -> HLHVHSQTMAKSRNTSWSQCPGLTACSTREPQDGPT
FT QVHPRWGL (in isoform 2).
FT /FTId=VSP_045784.
FT STRAND 2 10
FT STRAND 12 19
FT HELIX 24 35
FT HELIX 39 41
FT STRAND 42 46
FT STRAND 49 51
FT TURN 57 61
FT HELIX 64 66
FT STRAND 73 79
FT STRAND 82 84
FT STRAND 96 98
FT HELIX 101 103
FT STRAND 110 112
SQ SEQUENCE 118 AA; 13133 MW; C045F58FBED0EC47 CRC64;
MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC
GFTSQTARPQ APATVGLAFR ADDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ
//
MIM
600787
*RECORD*
*FIELD* NO
600787
*FIELD* TI
*600787 TRANSCRIPTION ELONGATION FACTOR B, POLYPEPTIDE 2; TCEB2
;;ELONGIN B; ELOB;;
read moreELONGIN, 18-KD SUBUNIT
*FIELD* TX
The elongin (SIII) complex is a heterotrimer composed of A, B, and C
subunits of 110, 18, and 15 kD, respectively. Aso et al. (1995)
demonstrated that elongin A (TCEB3; 600786) functions as the
transcriptionally active component of the SIII complex, whereas elongins
B and C (TCEB1; 600788) are regulatory subunits.
Duan et al. (1995) and Kibel et al. (1995) reported results suggesting
that the tumor suppression activity of the von Hippel-Lindau (VHL;
608537) tumor suppressor gene product is a function of its ability to
bind to elongins B and C and thereby inhibit transcription elongation. A
preponderance of the tumor-disposing inherited missense mutations
detected in von Hippel-Lindau disease are within the elongin-binding
domain of VHL. Schoenfeld et al. (2000) reported that VHL proteins
harboring mutations that disrupt elongin binding were unstable and
rapidly degraded by the proteasome. In contrast, wildtype VHL proteins
were directly stabilized by associating with both elongins B and C. In
addition, elongins B and C were stabilized through their interactions
with each other and VHL. Thus, the entire VHL/elongin complex is
resistant to proteasomal degradation. Because the elongin-binding domain
of VHL is frequently mutated in cancers, these results suggest that loss
of elongin binding causes tumorigenesis by compromising VHL protein
stability and/or potential VHL ubiquitination functions.
*FIELD* RF
1. Aso, T.; Lane, W. S.; Conaway, J. W.; Conaway, R. C.: Elongin
(SIII): a multisubunit regulator of elongation by RNA polymerase II. Science 269:
1439-1443, 1995.
2. Duan, D. R.; Pause, A.; Burgess, W. H.; Aso, T.; Chen, D. Y. T.;
Garrett, K. P.; Conaway, R. C.; Conaway, J. W.; Linehan, W. M.; Klausner,
R. D.: Inhibition of transcription elongation by the VHL tumor suppressor
protein. Science 269: 1402-1406, 1995.
3. Kibel, A.; Iliopoulos, O.; DeCaprio, J. A.; Kaelin, W. G., Jr.
: Binding of the von Hippel-Lindau tumor suppressor protein to elongin
B and C. Science 269: 1444-1446, 1995.
4. Schoenfeld, A. R.; Davidowitz, E. J.; Burk, R. D.: Elongin BC
complex prevents degradation of von Hippel-Lindau tumor suppressor
gene products. Proc. Nat. Acad. Sci. 97: 8507-8512, 2000.
*FIELD* CN
Victor A. McKusick - updated: 8/23/2000
*FIELD* CD
Victor A. McKusick: 11/6/1995
*FIELD* ED
mgross: 02/02/2012
mgross: 8/8/2005
ckniffin: 3/23/2004
mcapotos: 8/30/2000
mcapotos: 8/29/2000
terry: 8/23/2000
kayiaros: 7/13/1999
alopez: 5/21/1999
alopez: 5/5/1999
terry: 9/17/1996
mark: 11/6/1995
*RECORD*
*FIELD* NO
600787
*FIELD* TI
*600787 TRANSCRIPTION ELONGATION FACTOR B, POLYPEPTIDE 2; TCEB2
;;ELONGIN B; ELOB;;
read moreELONGIN, 18-KD SUBUNIT
*FIELD* TX
The elongin (SIII) complex is a heterotrimer composed of A, B, and C
subunits of 110, 18, and 15 kD, respectively. Aso et al. (1995)
demonstrated that elongin A (TCEB3; 600786) functions as the
transcriptionally active component of the SIII complex, whereas elongins
B and C (TCEB1; 600788) are regulatory subunits.
Duan et al. (1995) and Kibel et al. (1995) reported results suggesting
that the tumor suppression activity of the von Hippel-Lindau (VHL;
608537) tumor suppressor gene product is a function of its ability to
bind to elongins B and C and thereby inhibit transcription elongation. A
preponderance of the tumor-disposing inherited missense mutations
detected in von Hippel-Lindau disease are within the elongin-binding
domain of VHL. Schoenfeld et al. (2000) reported that VHL proteins
harboring mutations that disrupt elongin binding were unstable and
rapidly degraded by the proteasome. In contrast, wildtype VHL proteins
were directly stabilized by associating with both elongins B and C. In
addition, elongins B and C were stabilized through their interactions
with each other and VHL. Thus, the entire VHL/elongin complex is
resistant to proteasomal degradation. Because the elongin-binding domain
of VHL is frequently mutated in cancers, these results suggest that loss
of elongin binding causes tumorigenesis by compromising VHL protein
stability and/or potential VHL ubiquitination functions.
*FIELD* RF
1. Aso, T.; Lane, W. S.; Conaway, J. W.; Conaway, R. C.: Elongin
(SIII): a multisubunit regulator of elongation by RNA polymerase II. Science 269:
1439-1443, 1995.
2. Duan, D. R.; Pause, A.; Burgess, W. H.; Aso, T.; Chen, D. Y. T.;
Garrett, K. P.; Conaway, R. C.; Conaway, J. W.; Linehan, W. M.; Klausner,
R. D.: Inhibition of transcription elongation by the VHL tumor suppressor
protein. Science 269: 1402-1406, 1995.
3. Kibel, A.; Iliopoulos, O.; DeCaprio, J. A.; Kaelin, W. G., Jr.
: Binding of the von Hippel-Lindau tumor suppressor protein to elongin
B and C. Science 269: 1444-1446, 1995.
4. Schoenfeld, A. R.; Davidowitz, E. J.; Burk, R. D.: Elongin BC
complex prevents degradation of von Hippel-Lindau tumor suppressor
gene products. Proc. Nat. Acad. Sci. 97: 8507-8512, 2000.
*FIELD* CN
Victor A. McKusick - updated: 8/23/2000
*FIELD* CD
Victor A. McKusick: 11/6/1995
*FIELD* ED
mgross: 02/02/2012
mgross: 8/8/2005
ckniffin: 3/23/2004
mcapotos: 8/30/2000
mcapotos: 8/29/2000
terry: 8/23/2000
kayiaros: 7/13/1999
alopez: 5/21/1999
alopez: 5/5/1999
terry: 9/17/1996
mark: 11/6/1995