Full text data of TCEB1
TCEB1
[Confidence: low (only semi-automatic identification from reviews)]
Transcription elongation factor B polypeptide 1 (Elongin 15 kDa subunit; Elongin-C; EloC; RNA polymerase II transcription factor SIII subunit C; SIII p15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcription elongation factor B polypeptide 1 (Elongin 15 kDa subunit; Elongin-C; EloC; RNA polymerase II transcription factor SIII subunit C; SIII p15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15369
ID ELOC_HUMAN Reviewed; 112 AA.
AC Q15369; E5RGD9; Q567Q6;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Transcription elongation factor B polypeptide 1;
DE AltName: Full=Elongin 15 kDa subunit;
DE AltName: Full=Elongin-C;
DE Short=EloC;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit C;
DE AltName: Full=SIII p15;
GN Name=TCEB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Peripheral blood;
RX PubMed=7821821; DOI=10.1016/0378-1119(94)90467-7;
RA Garrett K.P., Haque D., Conaway R.C., Conaway J.W.;
RT "A human cDNA encoding the small subunit of RNA polymerase II
RT transcription factor SIII.";
RL Gene 150:413-414(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12004003; DOI=10.1038/labinvest.3780457;
RA Porkka K., Saramaeki O., Tanner M., Visakorpi T.;
RT "Amplification and overexpression of Elongin C gene discovered in
RT prostate cancer by cDNA microarrays.";
RL Lab. Invest. 82:629-637(2002).
RN [7]
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 [8]
RP INTERACTION WITH TMF1.
RX PubMed=15467733; DOI=10.1038/sj.onc.1208149;
RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
RT "TMF/ARA160 is a BC-box-containing protein that mediates the
RT degradation of Stat3.";
RL Oncogene 23:8908-8919(2004).
RN [9]
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 [10]
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 [11]
RP INTERACTION WITH HRSV PROTEIN NS1.
RX PubMed=17251292; DOI=10.1128/JVI.02303-06;
RA Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R.,
RA Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M.,
RA Power U.F., Johnston J.A.;
RT "Respiratory syncytial virus NS1 protein degrades STAT2 by using the
RT Elongin-Cullin E3 ligase.";
RL J. Virol. 81:3428-3436(2007).
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 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-112 IN COMPLEX WITH 1-120
RP OF TCEB2 AND 54-213 OF 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2;
RP 52-113 OF VHL AND 549-582 OF 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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB2; 54-113 OF
RP VHL AND 556-575 OF 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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2
RP ANS SOX4, 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 -!- 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. The elongin BC complex is part of a complex
CC with hydroxylated HIF1A. Substrate adapter protein can be a viral
CC protein such as HIV Vif. Interacts with VHL. Interacts with TMF1.
CC Interacts with human respiratory syncytial virus (HRSV) protein
CC NS1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, TCEB2
CC AND CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may
CC be an E3 ubiquitin ligase complex substrate recognition component.
CC -!- INTERACTION:
CC Q13617:CUL2; NbExp=5; IntAct=EBI-301231, EBI-456179;
CC O41974:GAMMAHV.ORF73 (xeno); NbExp=2; IntAct=EBI-301231, EBI-6933128;
CC Q96G25:MED8; NbExp=3; IntAct=EBI-301231, EBI-394405;
CC O15524:SOCS1; NbExp=2; IntAct=EBI-301231, EBI-968198;
CC O14508:SOCS2; NbExp=2; IntAct=EBI-301231, EBI-617737;
CC Q99619:SPSB2; NbExp=3; IntAct=EBI-301231, EBI-2323209;
CC Q96A44:SPSB4; NbExp=2; IntAct=EBI-301231, EBI-2323233;
CC Q15370:TCEB2; NbExp=5; IntAct=EBI-301231, EBI-301238;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-301231, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15369-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15369-2; Sequence=VSP_045955;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Overexpressed in prostate cancer cell line PC-
CC 3 and breast cancer cell line SK-BR-3.
CC -!- SIMILARITY: Belongs to the SKP1 family.
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DR EMBL; L34587; AAA67650.1; -; mRNA.
DR EMBL; BX649138; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013809; AAH13809.1; -; mRNA.
DR EMBL; BC093065; AAH93065.1; -; mRNA.
DR EMBL; BC100028; AAI00029.1; -; mRNA.
DR EMBL; BC100283; AAI00284.1; -; mRNA.
DR RefSeq; NP_001191786.1; NM_001204857.1.
DR RefSeq; NP_001191787.1; NM_001204858.1.
DR RefSeq; NP_001191788.1; NM_001204859.1.
DR RefSeq; NP_001191789.1; NM_001204860.1.
DR RefSeq; NP_001191790.1; NM_001204861.1.
DR RefSeq; NP_001191791.1; NM_001204862.1.
DR RefSeq; NP_001191792.1; NM_001204863.1.
DR RefSeq; NP_001191793.1; NM_001204864.1.
DR RefSeq; NP_005639.1; NM_005648.3.
DR RefSeq; XP_005251347.1; XM_005251290.1.
DR UniGene; Hs.533437; -.
DR UniGene; Hs.554594; -.
DR UniGene; Hs.731928; -.
DR PDB; 1LM8; X-ray; 1.85 A; C=17-112.
DR PDB; 1LQB; X-ray; 2.00 A; B=17-112.
DR PDB; 1VCB; X-ray; 2.70 A; B/E/H/K=1-112.
DR PDB; 2C9W; X-ray; 1.90 A; C=17-112.
DR PDB; 2IZV; X-ray; 2.55 A; C=17-112.
DR PDB; 3DCG; X-ray; 2.40 A; B/D=17-112.
DR PDB; 3ZKJ; X-ray; 2.58 A; B/E=17-112.
DR PDB; 3ZRC; X-ray; 2.90 A; B/E/H/K=17-112.
DR PDB; 3ZRF; X-ray; 2.80 A; B/E/H/K=17-112.
DR PDB; 3ZTC; X-ray; 2.65 A; B/E/H/K=17-112.
DR PDB; 3ZTD; X-ray; 2.79 A; B/E/H/K=17-112.
DR PDB; 3ZUN; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4AJY; X-ray; 1.73 A; C=17-112.
DR PDB; 4AWJ; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4B95; X-ray; 2.80 A; B/E/H/K=17-112.
DR PDB; 4B9K; X-ray; 2.00 A; B/E/H/K=17-112.
DR PDBsum; 1LM8; -.
DR PDBsum; 1LQB; -.
DR PDBsum; 1VCB; -.
DR PDBsum; 2C9W; -.
DR PDBsum; 2IZV; -.
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; Q15369; -.
DR SMR; Q15369; 17-112.
DR DIP; DIP-29571N; -.
DR IntAct; Q15369; 49.
DR MINT; MINT-1323870; -.
DR STRING; 9606.ENSP00000284811; -.
DR PhosphoSite; Q15369; -.
DR DMDM; 32699511; -.
DR PaxDb; Q15369; -.
DR PRIDE; Q15369; -.
DR DNASU; 6921; -.
DR Ensembl; ENST00000284811; ENSP00000284811; ENSG00000154582.
DR Ensembl; ENST00000518127; ENSP00000428334; ENSG00000154582.
DR Ensembl; ENST00000519487; ENSP00000429596; ENSG00000154582.
DR Ensembl; ENST00000520210; ENSP00000430224; ENSG00000154582.
DR Ensembl; ENST00000520242; ENSP00000428171; ENSG00000154582.
DR Ensembl; ENST00000522337; ENSP00000429906; ENSG00000154582.
DR Ensembl; ENST00000523815; ENSP00000428074; ENSG00000154582.
DR GeneID; 6921; -.
DR KEGG; hsa:6921; -.
DR UCSC; uc003xzx.2; human.
DR CTD; 6921; -.
DR GeneCards; GC08M074858; -.
DR HGNC; HGNC:11617; TCEB1.
DR MIM; 600788; gene.
DR neXtProt; NX_Q15369; -.
DR PharmGKB; PA36376; -.
DR eggNOG; NOG298860; -.
DR HOGENOM; HOG000216525; -.
DR HOVERGEN; HBG007440; -.
DR InParanoid; Q15369; -.
DR KO; K03872; -.
DR OMA; YFHYWYR; -.
DR OrthoDB; EOG77M8QN; -.
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 ChiTaRS; TCEB1; human.
DR EvolutionaryTrace; Q15369; -.
DR GeneWiki; TCEB1; -.
DR GenomeRNAi; 6921; -.
DR NextBio; 27077; -.
DR PRO; PR:Q15369; -.
DR ArrayExpress; Q15369; -.
DR Bgee; Q15369; -.
DR CleanEx; HS_TCEB1; -.
DR Genevestigator; Q15369; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030891; C:VCB complex; IEA:Ensembl.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR001232; Skp1_comp.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR Pfam; PF03931; Skp1_POZ; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Host-virus interaction; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1 112 Transcription elongation factor B
FT polypeptide 1.
FT /FTId=PRO_0000187258.
FT VAR_SEQ 1 16 Missing (in isoform 2).
FT /FTId=VSP_045955.
FT STRAND 18 22
FT STRAND 24 26
FT STRAND 28 32
FT HELIX 33 36
FT HELIX 40 46
FT STRAND 59 61
FT HELIX 67 83
FT HELIX 97 99
FT HELIX 100 110
SQ SEQUENCE 112 AA; 12473 MW; 98D88696E883538B CRC64;
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV
NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC
//
ID ELOC_HUMAN Reviewed; 112 AA.
AC Q15369; E5RGD9; Q567Q6;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Transcription elongation factor B polypeptide 1;
DE AltName: Full=Elongin 15 kDa subunit;
DE AltName: Full=Elongin-C;
DE Short=EloC;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit C;
DE AltName: Full=SIII p15;
GN Name=TCEB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Peripheral blood;
RX PubMed=7821821; DOI=10.1016/0378-1119(94)90467-7;
RA Garrett K.P., Haque D., Conaway R.C., Conaway J.W.;
RT "A human cDNA encoding the small subunit of RNA polymerase II
RT transcription factor SIII.";
RL Gene 150:413-414(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [5]
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12004003; DOI=10.1038/labinvest.3780457;
RA Porkka K., Saramaeki O., Tanner M., Visakorpi T.;
RT "Amplification and overexpression of Elongin C gene discovered in
RT prostate cancer by cDNA microarrays.";
RL Lab. Invest. 82:629-637(2002).
RN [7]
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 [8]
RP INTERACTION WITH TMF1.
RX PubMed=15467733; DOI=10.1038/sj.onc.1208149;
RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
RT "TMF/ARA160 is a BC-box-containing protein that mediates the
RT degradation of Stat3.";
RL Oncogene 23:8908-8919(2004).
RN [9]
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 [10]
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 [11]
RP INTERACTION WITH HRSV PROTEIN NS1.
RX PubMed=17251292; DOI=10.1128/JVI.02303-06;
RA Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R.,
RA Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M.,
RA Power U.F., Johnston J.A.;
RT "Respiratory syncytial virus NS1 protein degrades STAT2 by using the
RT Elongin-Cullin E3 ligase.";
RL J. Virol. 81:3428-3436(2007).
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 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-112 IN COMPLEX WITH 1-120
RP OF TCEB2 AND 54-213 OF 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2;
RP 52-113 OF VHL AND 549-582 OF 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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) COMPLEX WITH TCEB2; 54-113 OF
RP VHL AND 556-575 OF 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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 17-112 IN COMPLEX WITH TCEB2
RP ANS SOX4, 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 -!- 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. The elongin BC complex is part of a complex
CC with hydroxylated HIF1A. Substrate adapter protein can be a viral
CC protein such as HIV Vif. Interacts with VHL. Interacts with TMF1.
CC Interacts with human respiratory syncytial virus (HRSV) protein
CC NS1. Interacts with SPSB1. posed of LIMD1, VHL, EGLN1/PHD2, TCEB2
CC AND CUL2. Interacts with SPSB1. Interacts with KLHDC10; which may
CC be an E3 ubiquitin ligase complex substrate recognition component.
CC -!- INTERACTION:
CC Q13617:CUL2; NbExp=5; IntAct=EBI-301231, EBI-456179;
CC O41974:GAMMAHV.ORF73 (xeno); NbExp=2; IntAct=EBI-301231, EBI-6933128;
CC Q96G25:MED8; NbExp=3; IntAct=EBI-301231, EBI-394405;
CC O15524:SOCS1; NbExp=2; IntAct=EBI-301231, EBI-968198;
CC O14508:SOCS2; NbExp=2; IntAct=EBI-301231, EBI-617737;
CC Q99619:SPSB2; NbExp=3; IntAct=EBI-301231, EBI-2323209;
CC Q96A44:SPSB4; NbExp=2; IntAct=EBI-301231, EBI-2323233;
CC Q15370:TCEB2; NbExp=5; IntAct=EBI-301231, EBI-301238;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-301231, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15369-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15369-2; Sequence=VSP_045955;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Overexpressed in prostate cancer cell line PC-
CC 3 and breast cancer cell line SK-BR-3.
CC -!- SIMILARITY: Belongs to the SKP1 family.
CC -----------------------------------------------------------------------
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DR EMBL; L34587; AAA67650.1; -; mRNA.
DR EMBL; BX649138; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013809; AAH13809.1; -; mRNA.
DR EMBL; BC093065; AAH93065.1; -; mRNA.
DR EMBL; BC100028; AAI00029.1; -; mRNA.
DR EMBL; BC100283; AAI00284.1; -; mRNA.
DR RefSeq; NP_001191786.1; NM_001204857.1.
DR RefSeq; NP_001191787.1; NM_001204858.1.
DR RefSeq; NP_001191788.1; NM_001204859.1.
DR RefSeq; NP_001191789.1; NM_001204860.1.
DR RefSeq; NP_001191790.1; NM_001204861.1.
DR RefSeq; NP_001191791.1; NM_001204862.1.
DR RefSeq; NP_001191792.1; NM_001204863.1.
DR RefSeq; NP_001191793.1; NM_001204864.1.
DR RefSeq; NP_005639.1; NM_005648.3.
DR RefSeq; XP_005251347.1; XM_005251290.1.
DR UniGene; Hs.533437; -.
DR UniGene; Hs.554594; -.
DR UniGene; Hs.731928; -.
DR PDB; 1LM8; X-ray; 1.85 A; C=17-112.
DR PDB; 1LQB; X-ray; 2.00 A; B=17-112.
DR PDB; 1VCB; X-ray; 2.70 A; B/E/H/K=1-112.
DR PDB; 2C9W; X-ray; 1.90 A; C=17-112.
DR PDB; 2IZV; X-ray; 2.55 A; C=17-112.
DR PDB; 3DCG; X-ray; 2.40 A; B/D=17-112.
DR PDB; 3ZKJ; X-ray; 2.58 A; B/E=17-112.
DR PDB; 3ZRC; X-ray; 2.90 A; B/E/H/K=17-112.
DR PDB; 3ZRF; X-ray; 2.80 A; B/E/H/K=17-112.
DR PDB; 3ZTC; X-ray; 2.65 A; B/E/H/K=17-112.
DR PDB; 3ZTD; X-ray; 2.79 A; B/E/H/K=17-112.
DR PDB; 3ZUN; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4AJY; X-ray; 1.73 A; C=17-112.
DR PDB; 4AWJ; X-ray; 2.50 A; B/E/H/K=17-112.
DR PDB; 4B95; X-ray; 2.80 A; B/E/H/K=17-112.
DR PDB; 4B9K; X-ray; 2.00 A; B/E/H/K=17-112.
DR PDBsum; 1LM8; -.
DR PDBsum; 1LQB; -.
DR PDBsum; 1VCB; -.
DR PDBsum; 2C9W; -.
DR PDBsum; 2IZV; -.
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; Q15369; -.
DR SMR; Q15369; 17-112.
DR DIP; DIP-29571N; -.
DR IntAct; Q15369; 49.
DR MINT; MINT-1323870; -.
DR STRING; 9606.ENSP00000284811; -.
DR PhosphoSite; Q15369; -.
DR DMDM; 32699511; -.
DR PaxDb; Q15369; -.
DR PRIDE; Q15369; -.
DR DNASU; 6921; -.
DR Ensembl; ENST00000284811; ENSP00000284811; ENSG00000154582.
DR Ensembl; ENST00000518127; ENSP00000428334; ENSG00000154582.
DR Ensembl; ENST00000519487; ENSP00000429596; ENSG00000154582.
DR Ensembl; ENST00000520210; ENSP00000430224; ENSG00000154582.
DR Ensembl; ENST00000520242; ENSP00000428171; ENSG00000154582.
DR Ensembl; ENST00000522337; ENSP00000429906; ENSG00000154582.
DR Ensembl; ENST00000523815; ENSP00000428074; ENSG00000154582.
DR GeneID; 6921; -.
DR KEGG; hsa:6921; -.
DR UCSC; uc003xzx.2; human.
DR CTD; 6921; -.
DR GeneCards; GC08M074858; -.
DR HGNC; HGNC:11617; TCEB1.
DR MIM; 600788; gene.
DR neXtProt; NX_Q15369; -.
DR PharmGKB; PA36376; -.
DR eggNOG; NOG298860; -.
DR HOGENOM; HOG000216525; -.
DR HOVERGEN; HBG007440; -.
DR InParanoid; Q15369; -.
DR KO; K03872; -.
DR OMA; YFHYWYR; -.
DR OrthoDB; EOG77M8QN; -.
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 ChiTaRS; TCEB1; human.
DR EvolutionaryTrace; Q15369; -.
DR GeneWiki; TCEB1; -.
DR GenomeRNAi; 6921; -.
DR NextBio; 27077; -.
DR PRO; PR:Q15369; -.
DR ArrayExpress; Q15369; -.
DR Bgee; Q15369; -.
DR CleanEx; HS_TCEB1; -.
DR Genevestigator; Q15369; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030891; C:VCB complex; IEA:Ensembl.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR001232; Skp1_comp.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR Pfam; PF03931; Skp1_POZ; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Host-virus interaction; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1 112 Transcription elongation factor B
FT polypeptide 1.
FT /FTId=PRO_0000187258.
FT VAR_SEQ 1 16 Missing (in isoform 2).
FT /FTId=VSP_045955.
FT STRAND 18 22
FT STRAND 24 26
FT STRAND 28 32
FT HELIX 33 36
FT HELIX 40 46
FT STRAND 59 61
FT HELIX 67 83
FT HELIX 97 99
FT HELIX 100 110
SQ SEQUENCE 112 AA; 12473 MW; 98D88696E883538B CRC64;
MDGEEKTYGG CEGPDAMYVK LISSDGHEFI VKREHALTSG TIKAMLSGPG QFAENETNEV
NFREIPSHVL SKVCMYFTYK VRYTNSSTEI PEFPIAPEIA LELLMAANFL DC
//
MIM
600788
*RECORD*
*FIELD* NO
600788
*FIELD* TI
*600788 TRANSCRIPTION ELONGATION FACTOR B, POLYPEPTIDE 1; TCEB1
;;ELONGIN C; ELOC;;
read moreELONGIN, 15-KD SUBUNIT
*FIELD* TX
CLONING
The elongin (SIII) complex is a heterotrimer composed of 3 subunits,
called A, B, and C, of 110, 18, and 15 kD, respectively. Aso et al.
(1995) demonstrated that the 110-kD polypeptide designated elongin A
(600786) functions as the transcriptionally active component of the SIII
complex, whereas elongins B (600787) and C (TCEB1) are regulatory
subunits. Garrett et al. (1994) isolated and sequenced the human TCEB1
gene (which they had referred to as p15).
GENE FUNCTION
Duan et al. (1995) and Kibel et al. (1995) reported results suggesting
that the tumor suppression activity of the von Hippel-Lindau tumor
suppressor gene product (608537) is a function of its ability to bind to
elongin B (TCEB2) and C (TCEB1) and thereby inhibit transcription
elongation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TCEB1
gene to chromosome 8 (TMAP stSG4816).
- Pseudogene
A gene designated TCEB1L because of its high sequence similarity to
TCEB1 was later found to be the same as OCP2 (SKP1A; 601434), which maps
to chromosome 5. Demetrick et al. (1996) mapped the SKP1A gene to 7q11.2
by fluorescence in situ hybridization, but this was later determined to
be a pseudogene of TCEB1 (TCEB1P).
*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. Demetrick, D. J.; Zhang, H.; Beach, D. H.: Chromosomal mapping
of the genes for the human CDK2/cyclin A-associated proteins p19 (SKP1A
and SKP1B) and p45 (SKP2). Cytogenet. Cell Genet. 73: 104-107, 1996.
3. 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.
4. Garrett, K. P.; Haque, D.; Conaway, R. C.; Conaway, J. W.: A human
cDNA encoding the small subunit of RNA polymerase II transcription
factor SIII. Gene 150: 413-414, 1994.
5. 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.
*FIELD* CN
Carol A. Bocchini - updated: 2/11/2003
*FIELD* CD
Victor A. McKusick: 10/6/1995
*FIELD* ED
mgross: 02/02/2012
mgross: 8/8/2005
ckniffin: 3/23/2004
carol: 2/11/2003
kayiaros: 7/13/1999
alopez: 5/21/1999
alopez: 5/5/1999
terry: 9/17/1996
mark: 11/6/1995
terry: 10/6/1995
*RECORD*
*FIELD* NO
600788
*FIELD* TI
*600788 TRANSCRIPTION ELONGATION FACTOR B, POLYPEPTIDE 1; TCEB1
;;ELONGIN C; ELOC;;
read moreELONGIN, 15-KD SUBUNIT
*FIELD* TX
CLONING
The elongin (SIII) complex is a heterotrimer composed of 3 subunits,
called A, B, and C, of 110, 18, and 15 kD, respectively. Aso et al.
(1995) demonstrated that the 110-kD polypeptide designated elongin A
(600786) functions as the transcriptionally active component of the SIII
complex, whereas elongins B (600787) and C (TCEB1) are regulatory
subunits. Garrett et al. (1994) isolated and sequenced the human TCEB1
gene (which they had referred to as p15).
GENE FUNCTION
Duan et al. (1995) and Kibel et al. (1995) reported results suggesting
that the tumor suppression activity of the von Hippel-Lindau tumor
suppressor gene product (608537) is a function of its ability to bind to
elongin B (TCEB2) and C (TCEB1) and thereby inhibit transcription
elongation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TCEB1
gene to chromosome 8 (TMAP stSG4816).
- Pseudogene
A gene designated TCEB1L because of its high sequence similarity to
TCEB1 was later found to be the same as OCP2 (SKP1A; 601434), which maps
to chromosome 5. Demetrick et al. (1996) mapped the SKP1A gene to 7q11.2
by fluorescence in situ hybridization, but this was later determined to
be a pseudogene of TCEB1 (TCEB1P).
*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. Demetrick, D. J.; Zhang, H.; Beach, D. H.: Chromosomal mapping
of the genes for the human CDK2/cyclin A-associated proteins p19 (SKP1A
and SKP1B) and p45 (SKP2). Cytogenet. Cell Genet. 73: 104-107, 1996.
3. 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.
4. Garrett, K. P.; Haque, D.; Conaway, R. C.; Conaway, J. W.: A human
cDNA encoding the small subunit of RNA polymerase II transcription
factor SIII. Gene 150: 413-414, 1994.
5. 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.
*FIELD* CN
Carol A. Bocchini - updated: 2/11/2003
*FIELD* CD
Victor A. McKusick: 10/6/1995
*FIELD* ED
mgross: 02/02/2012
mgross: 8/8/2005
ckniffin: 3/23/2004
carol: 2/11/2003
kayiaros: 7/13/1999
alopez: 5/21/1999
alopez: 5/5/1999
terry: 9/17/1996
mark: 11/6/1995
terry: 10/6/1995