TCEB2

Transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B)

PDB rendering based on 1lm8.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1LM8, 1LQB, 1VCB, 2C9W, 2IZV, 2JZ3, 2MA9, 3DCG, 3ZKJ, 3ZNG, 3ZRC, 3ZRF, 3ZTC, 3ZTD, 3ZUN, 4AJY, 4AWJ, 4B95, 4B9K, 4BKS, 4BKT, 4N9F

Identifiers

Symbols

TCEB2 ; ELOB; SIII

External IDs

OMIM: 600787 MGI: 1914923 HomoloGene: 134544 GeneCards: TCEB2 Gene

Gene ontology
Molecular function	• protein binding • ubiquitin protein ligase binding
Cellular component	• nucleoplasm • cytosol • Cul2-RING ubiquitin ligase complex • Cul5-RING ubiquitin ligase complex • extracellular vesicular exosome • elongin complex
Biological process	• transcription from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • protein complex assembly • gene expression • viral process • protein ubiquitination • positive regulation of viral transcription • regulation of transcription from RNA polymerase II promoter in response to hypoxia • cellular response to hypoxia
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
2.77 – 2.78 Mb

Chr 17:
23.82 – 23.83 Mb

PubMed search

Transcription elongation factor B polypeptide 2 is a protein that in humans is encoded by the TCEB2 gene.^[1]

Function

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.^[2]

Interactions

TCEB2 has been shown to interact with:

CUL2,^[3]^[4]
TCEB1,^[5]^[6]^[7]^[8] and
Von Hippel-Lindau tumor suppressor.^[6]^[9]^[10]^[11]^[3]

References

↑ Garrett KP, Aso T, Bradsher JN, Foundling SI, Lane WS, Conaway RC et al. (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 41301. PMID 7638163.
↑ "Entrez Gene: TCEB2 transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B)".
↑ 3.0 3.1 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 2265268. PMID 18173839.
↑ Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E et al. (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.
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (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.
↑ 6.0 6.1 Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B et al. (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 481054. PMID 10587522.
↑ 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.
↑ 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.
↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S et al. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
↑ 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.
↑ 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 2583047. PMID 19030229.

Duan DR, Pause A, Burgess WH, Aso T, Chen DY, Garrett KP et al. (1995). "Inhibition of transcription elongation by the VHL tumor suppressor protein". Science 269 (5229): 1402–6. doi:10.1126/science.7660122. PMID 7660122.
Aso T, Lane WS, Conaway JW, Conaway RC (1995). "Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II". Science 269 (5229): 1439–43. doi:10.1126/science.7660129. PMID 7660129.
Kibel A, Iliopoulos O, DeCaprio JA, Kaelin WG (1995). "Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C". Science 269 (5229): 1444–6. doi:10.1126/science.7660130. PMID 7660130.
Bradsher JN, Jackson KW, Conaway RC, Conaway JW (1994). "RNA polymerase II transcription factor SIII. I. Identification, purification, and properties". J. Biol. Chem. 268 (34): 25587–93. PMID 8244996.
Pause A, Lee S, Worrell RA, Chen DY, Burgess WH, Linehan WM et al. (1997). "The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins". Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2156–61. doi:10.1073/pnas.94.6.2156. PMC 20057. PMID 9122164.
Li XY, Green MR (1998). "The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor". Genes Dev. 12 (19): 2992–6. doi:10.1101/gad.12.19.2992. PMC 317190. PMID 9765201.
Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ et al. (1999). "The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2071–6. doi:10.1073/pnas.96.5.2071. PMC 26738. PMID 10051596.
Stebbins CE, Kaelin WG, Pavletich NP (1999). "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function". Science 284 (5413): 455–61. doi:10.1126/science.284.5413.455. PMID 10205047.
Pause A, Peterson B, Schaffar G, Stearman R, Klausner RD (1999). "Studying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein". Proc. Natl. Acad. Sci. U.S.A. 96 (17): 9533–8. doi:10.1073/pnas.96.17.9533. PMC 22243. PMID 10449727.
Iwai K, Yamanaka K, Kamura T, Minato N, Conaway RC, Conaway JW et al. (1999). "Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12436–41. doi:10.1073/pnas.96.22.12436. PMC 22941. PMID 10535940.
Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B et al. (2000). "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 481054. PMID 10587522.
Aso T, Yamazaki K, Amimoto K, Kuroiwa A, Higashi H, Matsuda Y et al. (2000). "Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testis". J. Biol. Chem. 275 (9): 6546–52. doi:10.1074/jbc.275.9.6546. PMID 10692460.
Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW (2000). "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex". Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10430–5. doi:10.1073/pnas.190332597. PMC 27041. PMID 10973499.
Aso T, Yamazaki K, Aigaki T, Kitajima S (2000). "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity". Biochem. Biophys. Res. Commun. 276 (1): 355–61. doi:10.1006/bbrc.2000.3451. PMID 11006129.
Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E et al. (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.
Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (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.
Yamazaki K, Guo L, Sugahara K, Zhang C, Enzan H, Nakabeppu Y et al. (2002). "Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3". J. Biol. Chem. 277 (29): 26444–51. doi:10.1074/jbc.M202859200. PMID 11994304.
Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076.
Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW et al. (2002). "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL". Nature 417 (6892): 975–8. doi:10.1038/nature00767. PMID 12050673.

PDB gallery

1lm8: Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex

1lqb: Crystal structure of a hydroxylated HIF-1 alpha peptide bound to the pVHL/elongin-C/elongin-B complex

1vcb: THE VHL-ELONGINC-ELONGINB STRUCTURE

2c9w: CRYSTAL STRUCTURE OF SOCS-2 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 1.9A RESOLUTION

2fnj: Crystal structure of a B30.2/SPRY domain-containing protein GUSTAVUS in complex with Elongin B and Elongin C

2izv: CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 2.55A RESOLUTION

TCEB2

Function

Interactions

References

Further reading