TCEB2

From Wikipedia, the free encyclopedia
Jump to: navigation, search
ELOB
Protein TCEB2 PDB 1lm8.png
Available structures
PDB Human UniProt search: PDBe RCSB
Identifiers
Aliases ELOB, SIII, TCEB2, transcription elongation factor B subunit 2
External IDs HomoloGene: 134544 GeneCards: ELOB
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_207013
NM_007108

n/a

RefSeq (protein)

NP_009039
NP_996896

n/a

Location (UCSC) Chr 16: 2.77 – 2.78 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human

Transcription elongation factor B polypeptide 2 is a protein that in humans is encoded by the TCEB2 gene.[2]

Function[edit]

This gene encodes the protein elongin B, 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. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[3]

Interactions[edit]

TCEB2 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ Garrett KP, Aso T, Bradsher JN, Foundling SI, Lane WS, Conaway RC, Conaway JW (September 1995). "Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog". Proc Natl Acad Sci U S A. 92 (16): 7172–6. doi:10.1073/pnas.92.16.7172. PMC 41301Freely accessible. PMID 7638163. 
  3. ^ "Entrez Gene: TCEB2 transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B)". 
  4. ^ a b Menon S, Tsuge T, Dohmae N, Takio K, Wei N. "Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome". BMC Biochem. 9: 1. doi:10.1186/1471-2091-9-1. PMC 2265268Freely accessible. PMID 18173839. 
  5. ^ Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E, Branton PE, Shilatifard A, Conaway RC, Conaway JW (August 2001). "Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase". J. Biol. Chem. 276 (32): 29748–53. doi:10.1074/jbc.M103093200. PMID 11384984. 
  6. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  7. ^ a b Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG (Dec 1999). "Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein". J. Clin. Invest. 104 (11): 1583–91. doi:10.1172/JCI8161. PMC 481054Freely accessible. PMID 10587522. 
  8. ^ Krumm A, Groudine M (September 1995). "Tumor suppression and transcription elongation: the dire consequences of changing partners". Science. 269 (5229): 1400–1. doi:10.1126/science.7660121. PMID 7660121. 
  9. ^ Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (February 2002). "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein". J. Biol. Chem. 277 (7): 4656–62. doi:10.1074/jbc.M108269200. PMID 11739384. 
  10. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948Freely accessible. PMID 17353931. 
  11. ^ Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (June 2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science. 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076. 
  12. ^ Hacker KE, Lee CM, Rathmell WK. Zhang B, ed. "VHL type 2B mutations retain VBC complex form and function". PLoS ONE. 3 (11): e3801. doi:10.1371/journal.pone.0003801. PMC 2583047Freely accessible. PMID 19030229. 

Further reading[edit]