NP_001191786.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
39.5 kDa
NCBI Official Full Name
transcription elongation factor B polypeptide 1 isoform a
NCBI Official Synonym Full Names
transcription elongation factor B (SIII), polypeptide 1 (15kDa, elongin C)
NCBI Official Synonym Symbols
NCBI Protein Information
transcription elongation factor B polypeptide 1
UniProt Protein Name
Transcription elongation factor B polypeptide 1
UniProt Synonym Protein Names
Elongin 15 kDa subunit; Elongin-C; EloC; RNA polymerase II transcription factor SIII subunit C; SIII p15
UniProt Synonym Gene Names
UniProt Entry Name
ELOC_HUMAN
NCBI Summary for TCEB1
This gene encodes the protein elongin C, which is a subunit of the transcription factor B (SIII) complex. The SIII complex is composed of elongins A/A2, B and C. It activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin A functions as the transcriptionally active component of the SIII complex, whereas elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and capable of forming a stable complex with elongins B and C. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation. Multiple alternatively spliced transcript variants encoding two distinct isoforms have been identified. [provided by RefSeq, Mar 2011]
UniProt Comments for TCEB1
TCEB1: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). Belongs to the SKP1 family.
Protein type: Transcription initiation complex
Chromosomal Location of Human Ortholog: 8q21.11
Cellular Component: cytosol; nucleoplasm
Molecular Function: protein binding; ubiquitin-protein ligase activity
Biological Process: gene expression; positive regulation of RNA elongation from RNA polymerase II promoter; positive regulation of viral transcription; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of transcription from RNA polymerase II promoter; RNA elongation from RNA polymerase II promoter; transcription from RNA polymerase II promoter; viral reproduction
Product References and Citations for TCEB1 recombinant protein
A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII.Garrett K.P., Haque D., Conaway R.C., Conaway J.W.Gene 150:413-414(1994)
The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007)
DNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006)
Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity.Aso T., Yamazaki K., Aigaki T., Kitajima S.Biochem. Biophys. Res. Commun. 276:355-361(2000)
Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays.Porkka K., Saramaeki O., Tanner M., Visakorpi T.Lab. Invest. 82:629-637(2002)
Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation.Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.Genes Dev. 18:2861-2866(2004)
TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3.Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.Oncogene 23:8908-8919(2004)
Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.J. Biol. Chem. 280:7038-7048(2005)
Structural basis for protein recognition by B30.2/SPRY domains.Woo J.S., Suh H.Y., Park S.Y., Oh B.H.Mol. Cell 24:967-976(2006)
Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase.Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A.J. Virol. 81:3428-3436(2007)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5.Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.Mol. Cell 48:692-704(2012)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Structure of the VHL-ElonginC-ElonginB complex
implications for VHL tumor suppressor function.Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P.Science 284:455-461(1999)
Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.Hon W.-C., Wilson M.I., Harlos K., Claridge T.D.W., Schofield C.J., Pugh C.W., Maxwell P.H., Ratcliffe P.J., Stuart D.I., Jones E.Y.Nature 417:975-978(2002)
Structure of an HIF-1alpha-pVHL complex
hydroxyproline recognition in signaling.Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G. Jr., Pavletich N.P.Science 296:1886-1889(2002)
Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation.Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S.Structure 15:1493-1504(2007)
Research Articles on TCEB1
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Organs/Tissues associated with TCEB1 recombinant protein
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