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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	OMIM: 605409; MGI: 1926421; HomoloGene: 4879; GeneCards: TCERG1; OMA:TCERG1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q32 Start 146,447,311 bp End 146,511,961 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 B3 Start 42,644,552 bp End 42,708,858 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum right uterine tube sural nerve ventricular zone Achilles tendon ganglionic eminence left ovary right ovary anterior pituitary skin of abdomen Top expressed in tail of embryo genital tubercle zygote ventricular zone neural layer of retina yolk sac secondary oocyte embryo embryo dentate gyrus of hippocampal formation granule cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transcription coactivator activity transcription corepressor activity proline-rich region binding protein binding RNA binding identical protein binding RNA polymerase binding Cellular component nucleus nucleoplasm Biological process regulation of transcription, DNA-templated negative regulation of transcription by RNA polymerase II transcription by RNA polymerase II transcription, DNA-templated positive regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10915 56070 Ensembl ENSG00000113649 ENSMUSG00000024498 UniProt O14776 Q8CGF7 RefSeq (mRNA) NM_001040006 NM_006706 NM_001382548 NM_001039474 NM_001289526 NM_001360881 NM_019512 RefSeq (protein) NP_001035095 NP_006697 NP_001369477 NP_001034563 NP_001276455 NP_001347810 Location (UCSC) Chr 5: 146.45 – 146.51 Mb Chr 18: 42.64 – 42.71 Mb PubMed search
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.

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.

Interactions

Transcription elongation regulator 1 has been shown to interact with SF1 and POLR2A.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000113649 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000024498 – 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. ^ "Entrez Gene: TCERG1 transcription elongation regulator 1".
6. 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. doi:10.1128/MCB.17.10.6029. PMC 232452. PMID 9315662.
7. 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. 11 (10): 930–3. doi:10.1007/s003350010162. PMID 11003711. S2CID 2396234.
8. 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. 21 (22): 7617–28. doi:10.1128/MCB.21.22.7617-7628.2001. ISSN 0270-7306. PMC 99933. PMID 11604498.
9. 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. 97 (16): 9015–20. Bibcode:2000PNAS...97.9015C. 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. doi:10.1128/MCB.17.10.6029. 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. S2CID 585778.
• 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. doi:10.1128/MCB.19.7.4719. 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. Bibcode:2000PNAS...97.9015C. 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. S2CID 2396234.
• 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. Bibcode:2002Natur.419..182Z. doi:10.1038/nature01031. PMID 12226669. S2CID 4372405.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 33727221.
• 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. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• 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.

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