Transcription elongation factor A protein 1 (TCEA1)

The protein contains 301 amino acids for an estimated molecular weight of 33970 Da.

 

Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 48%
Model score: 18

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The reference OMIM entry for this protein is 601425

Transcription elongation factor a, 1; tcea1
Tcea
Tfiis; tf2s
Sii

CLONING

Transcription elongation factors help RNA polymerase II (see 180660) to transcribe past blockages due to specific DNA sequences, DNA-binding proteins, and transcription-arresting drugs. Transcription elongation factors in humans fall into 2 classes: the SIII (see 600788)/TF2F (see 189968) class, members of which increase the average rate of RNA chain elongation (Aso et al., 1995); and the SII class, which releases RNA polymerase II from transcriptional arrest (Reines, 1994). Park et al. (1994) cloned and characterized a human gene encoding an SII-type elongation factor that they called TFIIS. The TFIIS gene produces a 2.5-kb transcript.

GENE FUNCTION

Thomas et al. (1998) addressed whether the intrinsic 3-prime to 5-prime nuclease activity of human RNA polymerase II (pol II) can proofread during transcription in vitro. In the presence of SII, a protein that stimulates the nuclease activity, pol II quantitatively removed misincorporated nucleotides from the nascent transcript during rapid chain extension. The basis of discrimination between the correct and incorrect base was the slow addition of the next nucleotide to the mismatched terminus. Incorporation of inosine monophosphate inhibited the next nucleotide addition by a similar magnitude as a mismatched base. Thomas et al. (1998) demonstrated that addition of SII to a transcription reaction dramatically altered the RNA base content, reflecting the stable incorporation of more 'correct' (GMP) and fewer 'incorrect' (IMP) nucleotides. In vivo transcription by RNA polymerase II takes place in the context of chromatin. Guermah et al. (2006) found that a purified, reconstituted RNA polymerase II system that sufficed for activator-dependent transcription on DNA templates was incapable of transcribing chromatin templates, even in the presence of factors that effected transcription in less-purified assay systems. Using a complementation and HeLa cell nuclear extract fractionation scheme, Guermah et al. (2006) identified and purified an activity, designated CTEA (chromatin transcription-enabling activity), that allowed for transcription through chromatin templates in a manner that was both activator and p300 (EP300; 602700)/acetyl-CoA dependent. CTEA acted primarily at the elongation step and enabled RNA polymerase II machinery to transcribe efficiently through several contiguously positioned nucleosomes. Guermah et al. (2006) identified the major functional component of CTEA as transcription elongation factor SII. SII was essential for productive transcription elongation, and its function at this step was dependent on p300-dependent acetylation. These synergistic transcriptional elongation activities were potentiated by HMGB2 (163906). Astrom et al. (1999) showed that activation of PLAG1 (603026) in salivary gland tumors (181030) is not confined to adenomas with 8q12 abnormalities but is also found in tumors with a normal karyotype. They showed further that PLAG1 may be activated by cryptic rearrangements in cases with normal karyotypes, leading to fusions between PLAG1 and CTNNB1 (116806) or the TCEA1 gene.

GENE STRUCTURE

Park et al. (1994) determined that the TCEA1 gene is 2.8 kb long and intronless.

MAPPING

DiMarco et al. (1996) designed PCR primers for the TCEA1 gene and mapped it to human chromosome 3 by analysis of human-rodent hybrid mapping panel. Further regionalization to chromosome 3p22-p21.3 was accomplished by fluorescence in sit ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601425 was added.

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed