ELOB

ELOB
Available structures
PDB	Human UniProt 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, 4W9C, 4W9D, 4W9E, 4W9F, 4W9G, 4W9H, 4W9I, 4W9J, 4W9K, 4W9L, 4WQO, 5BO4
Identifiers
Aliases	ELOB, SIII, TCEB2, transcription elongation factor B subunit 2, elongin B
External IDs	OMIM: 600787; HomoloGene: 134544; GeneCards: ELOB; OMA:ELOB - orthologs
Gene location (Human)
Chr.	Chromosome 16 (human)
End	2,777,289 bp
RNA expression pattern
	Top expressed in
	left testis; ; right testis; ; apex of heart; ; muscle of thigh; ; stromal cell of endometrium; ; anterior pituitary; ; nucleus accumbens; ; olfactory zone of nasal mucosa; ; prefrontal cortex; ; ganglionic eminence;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding; ubiquitin protein ligase binding;
Cellular component	Cul2-RING ubiquitin ligase complex; cytosol; Cul5-RING ubiquitin ligase complex; VCB complex; nucleus; elongin complex; nucleoplasm;
Biological process	transcription elongation from RNA polymerase II promoter; regulation of transcription, DNA-templated; transcription by RNA polymerase II; transcription, DNA-templated; regulation of transcription from RNA polymerase II promoter in response to hypoxia; protein ubiquitination; post-translational protein modification; protein-containing complex assembly;
	Sources:Amigo / QuickGO
Orthologs
	6923
	n/a
	ENSG00000103363
	n/a
	Q15370
	n/a
	NM_207013; NM_007108
	n/a
	NP_009039; NP_996896
	n/a
	Wikidata
View/Edit Human

Elongin B is a protein that in humans is encoded by the ELOB gene.^[3]

Function

Elongin B 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.^[4]

Interactions

TCEB2 has been shown to interact with:

CUL2,^[5]^[6]
TCEB1,^[7]^[8]^[9]^[10] and
Von Hippel-Lindau tumor suppressor.^[5]^[8]^[11]^[12]^[13]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000103363 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1995PNAS...92.7172G. doi:10.1073/pnas.92.16.7172. PMC 41301. PMID 7638163.
^ "ELOB elongin B [ Homo sapiens (human) ]".
^ ^a ^b Menon S, Tsuge T, Dohmae N, Takio K, Wei N (2008). "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, 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.
^ 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
^ ^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 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. Bibcode:1995Sci...269.1400K. doi:10.1126/science.7660121. PMID 7660121. S2CID 39758696.
^ 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, 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 (2007). "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. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440. PMID 12004076. S2CID 19641938.
^ Hacker KE, Lee CM, Rathmell WK (2008). Zhang B (ed.). "VHL type 2B mutations retain VBC complex form and function". PLOS ONE. 3 (11): e3801. Bibcode:2008PLoSO...3.3801H. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229.

External links

PDBe-KB provides an overview of all the structure information available in the PDB for Human Elongin-B

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000103363 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7638163-3] 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. Bibcode:1995PNAS...92.7172G. doi:10.1073/pnas.92.16.7172. PMC 41301. PMID 7638163.

[entrez-4] "ELOB elongin B [ Homo sapiens (human) ]".

[pmid18173839-5] Menon S, Tsuge T, Dohmae N, Takio K, Wei N (2008). "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.

[pmid11384984-6] 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.

[pmid16189514-7] 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

[pmid10587522-8] 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 481054. PMID 10587522.

[pmid7660129-9] Krumm A, Groudine M (September 1995). "Tumor suppression and transcription elongation: the dire consequences of changing partners". Science. 269 (5229): 1400–1. Bibcode:1995Sci...269.1400K. doi:10.1126/science.7660121. PMID 7660121. S2CID 39758696.

[pmid11739384-10] 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.

[pmid17353931-11] 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

[pmid12004076-12] 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. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440. PMID 12004076. S2CID 19641938.

[pmid19030229-13] Hacker KE, Lee CM, Rathmell WK (2008). Zhang B (ed.). "VHL type 2B mutations retain VBC complex form and function". PLOS ONE. 3 (11): e3801. Bibcode:2008PLoSO...3.3801H. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229.

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[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

Function

Interactions

References

Further reading

External links