ELOC

Protein-coding gene in the species Homo sapiens

ELOC
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1LM8, 1LQB, 1VCB, 2C9W, 2IZV, 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
AliasesELOC, SIII, eloC, TCEB1, transcription elongation factor B subunit 1, elongin C
External IDsOMIM: 600788; MGI: 1915173; HomoloGene: 38083; GeneCards: ELOC; OMA:ELOC - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for ELOC
Genomic location for ELOC
Band8q21.11Start73,939,169 bp[1]
End73,972,307 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for ELOC
Genomic location for ELOC
Band1|1 A3Start16,711,949 bp[2]
End16,727,266 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • oocyte

  • sperm

  • right ventricle

  • gingival epithelium

  • palpebral conjunctiva

  • left testis

  • right testis

  • tendon of biceps brachii

  • biceps brachii

  • amniotic fluid
Top expressed in
  • morula

  • primary oocyte

  • blastocyst

  • primitive streak

  • endothelial cell of lymphatic vessel

  • epithelium of stomach

  • yolk sac

  • facial motor nucleus

  • medial ganglionic eminence

  • atrioventricular valve
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • ubiquitin-protein transferase activity
Cellular component
  • cytosol
  • nucleus
  • elongin complex
  • nucleoplasm
Biological process
  • regulation of transcription by RNA polymerase II
  • transcription elongation from RNA polymerase II promoter
  • regulation of transcription, DNA-templated
  • transcription by RNA polymerase II
  • ubiquitin-dependent protein catabolic process
  • transcription, DNA-templated
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia
  • viral process
  • positive regulation of transcription elongation from RNA polymerase II promoter
  • post-translational protein modification
  • protein ubiquitination
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6921

67923

Ensembl

ENSG00000154582

ENSMUSG00000079658

UniProt

Q15369

P83940

RefSeq (mRNA)
NM_001204857
NM_001204858
NM_001204859
NM_001204860
NM_001204861

NM_001204862
NM_001204863
NM_001204864
NM_005648

NM_001310470
NM_026456

RefSeq (protein)
NP_001191786
NP_001191787
NP_001191788
NP_001191789
NP_001191790

NP_001191791
NP_001191792
NP_001191793
NP_005639

NP_001297399
NP_080732

Location (UCSC)Chr 8: 73.94 – 73.97 MbChr 1: 16.71 – 16.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Elongin C is a protein that in humans is encoded by the ELOC gene.[5][6]

Function

Elongin C 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.[7]

Interactions

TCEB1 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000154582 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079658 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Garrett KP, Haque D, Conaway RC, Conaway JW (Feb 1995). "A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII". Gene. 150 (2): 413–4. doi:10.1016/0378-1119(94)90467-7. PMID 7821821.
  6. ^ Duan DR, Pause A, Burgess WH, Aso T, Chen DY, Garrett KP, Conaway RC, Conaway JW, Linehan WM, Klausner RD (Oct 1995). "Inhibition of transcription elongation by the VHL tumor suppressor protein". Science. 269 (5229): 1402–6. Bibcode:1995Sci...269.1402D. doi:10.1126/science.7660122. PMID 7660122. S2CID 22334719.
  7. ^ "Entrez Gene: TCEB1 transcription elongation factor B (SIII), polypeptide 1 (15kDa, elongin C)".
  8. ^ 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 (Oct 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.
  9. ^ 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.
  10. ^ Krumm A, Groudine M (Sep 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.
  11. ^ a b Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (Feb 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.
  12. ^ 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.
  13. ^ Tsuchiya H, Iseda T, Hino O (Jul 1996). "Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product". Cancer Res. 56 (13): 2881–5. PMID 8674032.
  14. ^ Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (Jun 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.
  15. ^ 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.
  16. ^ Kim BY, Kim H, Cho EJ, Youn HD (Feb 2008). "Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation". Exp. Mol. Med. 40 (1): 71–83. doi:10.3858/emm.2008.40.1.71. PMC 2679322. PMID 18305400.

Further reading

  • 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. Bibcode:1995Sci...269.1439A. doi:10.1126/science.7660129. PMID 7660129. S2CID 37649908.
  • 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. Bibcode:1995Sci...269.1444K. doi:10.1126/science.7660130. PMID 7660130. S2CID 25410108.
  • 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. doi:10.1016/S0021-9258(19)74431-7. PMID 8244996.
  • Pause A, Lee S, Worrell RA, Chen DY, Burgess WH, Linehan WM, Klausner RD (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. Bibcode:1997PNAS...94.2156P. doi:10.1073/pnas.94.6.2156. PMC 20057. PMID 9122164.
  • Lonergan KM, Iliopoulos O, Ohh M, Kamura T, Conaway RC, Conaway JW, Kaelin WG (1998). "Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2". Mol. Cell. Biol. 18 (2): 732–41. doi:10.1128/mcb.18.2.732. PMC 108784. PMID 9447969.
  • Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ, Moritz RL, Cary D, Richardson R, Hausmann G, Kile BJ, Kent SB, Alexander WS, Metcalf D, Hilton DJ, Nicola NA, Baca M (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. Bibcode:1999PNAS...96.2071Z. 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. Bibcode:1999Sci...284..455S. 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. Bibcode:1999PNAS...96.9533P. doi:10.1073/pnas.96.17.9533. PMC 22243. PMID 10449727.
  • Iwai K, Yamanaka K, Kamura T, Minato N, Conaway RC, Conaway JW, Klausner RD, Pause A (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. Bibcode:1999PNAS...9612436I. doi:10.1073/pnas.96.22.12436. PMC 22941. PMID 10535940.
  • Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG (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, Kitajima S, Hatakeyama M (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.
  • Adryan B, Decker HJ, Papas TS, Hsu T (2000). "Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila". Oncogene. 19 (24): 2803–11. doi:10.1038/sj.onc.1203611. PMID 10851083.
  • 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. Bibcode:2000PNAS...9710430K. 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, Branton PE, Shilatifard A, Conaway RC, Conaway JW (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, Kitajima S, Aso T (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.
  • Porkka K, Saramäki O, Tanner M, Visakorpi T (2002). "Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays". Lab. Invest. 82 (5): 629–37. doi:10.1038/labinvest.3780457. PMID 12004003.
  • v
  • t
  • e
  • 1lm8: Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
    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
    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
    1vcb: THE VHL-ELONGINC-ELONGINB STRUCTURE
  • 2c9w: CRYSTAL STRUCTURE OF SOCS-2 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 1.9A RESOLUTION
    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
    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
    2izv: CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 2.55A RESOLUTION