Transcription elongation regulator 1

TCERG1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DK7, 2DOD, 2DOE, 2DOF, 2E71, 2KIQ, 2KIS, 2MW9, 2MWA, 2MWB, 2MWD, 2MWF, 2NNT, 3HFH, 3Q1I, 4FQG, 2N4R, 2N4S, 2N4T, 2N4U, 2N4V, 2N4W
Identifiers
Aliases	TCERG1, CA150, TAF2S, Urn1, transcription elongation regulator 1
External IDs	MGI: 1926421 HomoloGene: 4879 GeneCards: TCERG1
Gene ontology Molecular function • transcription coactivator activity • poly(A) RNA binding • RNA polymerase II transcription corepressor activity • proline-rich region binding • protein binding • RNA polymerase II repressing transcription factor binding Cellular component • nucleolus • nucleus • actin cytoskeleton Biological process • regulation of transcription, DNA-templated • negative regulation of transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • transcription, DNA-templated Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10915	56070
Ensembl	ENSG00000113649	ENSMUSG00000024498
UniProt	O14776	Q8CGF7
RefSeq (mRNA)	NM_001040006 NM_006706	NM_001039474 NM_001289526
RefSeq (protein)	NP_001035095.1 NP_006697.2	NP_001034563.1 NP_001276455.1
Location (UCSC)	Chr 5: 146.45 – 146.51 Mb	Chr 18: 42.51 – 42.58 Mb
PubMed search	[1]	[2]
Wikidata

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Transcription elongation regulator 1, also known as TCERG1, is a protein which in humans is encoded by the TCERG1 gene.^[3][4][5]

Function

This gene encodes a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. The encoded protein interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domains, and with the pre-mRNA splicing factor SF1 via a WW domain. Alternative splicing results in multiple transcripts variants encoding different isoforms.^[3]

Interactions

Transcription elongation regulator 1 has been shown to interact with SF1^[6] and POLR2A.^[7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: TCERG1 transcription elongation regulator 1".
4. Suñé C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA (October 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Molecular and Cellular Biology. 17 (10): 6029–39. PMC 232452. PMID 9315662.
5. Bohne J, Cole SE, Suñe C, Lindman BR, Ko VD, Vogt TF, Garcia-Blanco MA (October 2000). "Expression analysis and mapping of the mouse and human transcriptional regulator CA150". Mammalian Genome : Official Journal of the International Mammalian Genome Society. 11 (10): 930–3. doi:10.1007/s003350010162. PMID 11003711.
6. Goldstrohm, A C; Albrecht T R; Suñé C; Bedford M T; Garcia-Blanco M A (November 2001). "The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1". Mol. Cell. Biol. United States. 21 (22): 7617–28. doi:10.1128/MCB.21.22.7617-7628.2001. ISSN 0270-7306. PMC 99933. PMID 11604498.
7. Carty, S M; Goldstrohm A C; Suñé C; Garcia-Blanco M A; Greenleaf A L (August 2000). "Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 97 (16): 9015–20. doi:10.1073/pnas.160266597. ISSN 0027-8424. PMC 16813. PMID 10908677.

Further reading

• Suñé C, Hayashi T, Liu Y, et al. (1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Mol. Cell. Biol. 17 (10): 6029–39. PMC 232452. PMID 9315662.
• Neubauer G, King A, Rappsilber J, et al. (1998). "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex". Nat. Genet. 20 (1): 46–50. doi:10.1038/1700. PMID 9731529.
• Suñé C, Garcia-Blanco MA (1999). "Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner". Mol. Cell. Biol. 19 (7): 4719–28. PMC 84270. PMID 10373521.
• Carty SM, Goldstrohm AC, Suñé C, et al. (2000). "Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9015–20. doi:10.1073/pnas.160266597. PMC 16813. PMID 10908677.
• Bohne J, Cole SE, Suñe C, et al. (2000). "Expression analysis and mapping of the mouse and human transcriptional regulator CA150". Mamm. Genome. 11 (10): 930–3. doi:10.1007/s003350010162. PMID 11003711.
• Holbert S, Denghien I, Kiechle T, et al. (2001). "The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1811–6. doi:10.1073/pnas.041566798. PMC 29339. PMID 11172033.
• Goldstrohm AC, Albrecht TR, Suñé C, et al. (2001). "The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1". Mol. Cell. Biol. 21 (22): 7617–28. doi:10.1128/MCB.21.22.7617-7628.2001. PMC 99933. PMID 11604498.
• Zhou Z, Licklider LJ, Gygi SP, Reed R (2002). "Comprehensive proteomic analysis of the human spliceosome". Nature. 419 (6903): 182–5. doi:10.1038/nature01031. PMID 12226669.
• Carty SM, Greenleaf AL (2003). "Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing". Mol. Cell Proteomics. 1 (8): 598–610. doi:10.1074/mcp.M200029-MCP200. PMID 12376575.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chattopadhyay B, Ghosh S, Gangopadhyay PK, et al. (2003). "Modulation of age at onset in Huntington's disease and spinocerebellar ataxia type 2 patients originated from eastern India". Neurosci. Lett. 345 (2): 93–6. doi:10.1016/S0304-3940(03)00436-1. PMID 12821179.
• Reuter TY, Medhurst AL, Waisfisz Q, et al. (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
• Palancade B, Marshall NF, Tremeau-Bravard A, et al. (2004). "Dephosphorylation of RNA polymerase II by CTD-phosphatase FCP1 is inhibited by phospho-CTD associating proteins". J. Mol. Biol. 335 (2): 415–24. doi:10.1016/j.jmb.2003.10.036. PMID 14672652.
• Nagel JE, Smith RJ, Shaw L, et al. (2005). "Identification of genes differentially expressed in T cells following stimulation with the chemokines CXCL12 and CXCL10". BMC Immunol. 5: 17. doi:10.1186/1471-2172-5-17. PMC 514893. PMID 15296517.
• Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• Lin KT, Lu RM, Tarn WY (2004). "The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo". Mol. Cell. Biol. 24 (20): 9176–85. doi:10.1128/MCB.24.20.9176-9185.2004. PMC 517884. PMID 15456888.
• Smith MJ, Kulkarni S, Pawson T (2004). "FF domains of CA150 bind transcription and splicing factors through multiple weak interactions". Mol. Cell. Biol. 24 (21): 9274–85. doi:10.1128/MCB.24.21.9274-9285.2004. PMC 522232. PMID 15485897.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• McFie PJ, Wang GL, Timchenko NA, et al. (2006). "Identification of a co-repressor that inhibits the transcriptional and growth-arrest activities of CCAAT/enhancer-binding protein alpha". J. Biol. Chem. 281 (26): 18069–80. doi:10.1074/jbc.M512734200. PMID 16644732.