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0  structures 852  species 0  interactions 1087  sequences 13  architectures

Family: EAF (PF09816)

Summary: RNA polymerase II transcription elongation factor

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EAF family Edit Wikipedia article

EAF
Identifiers
Symbol EAF
Pfam PF09816
InterPro IPR019194

In molecular biology, the EAF family of proteins act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors .[1][2][3][3] EAF proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. ELL and EAF1 are components of Cajal bodies, which have a role in leukemogenesis.[2] EAF1 also has the capacity to interact with ELL1 and ELL2. The N terminus of approx 120 of EAF1 has a region of high serine, aspartic acid, and glutamic acid residues.[1][4]

References

  1. ^ a b Simone F, Polak PE, Kaberlein JJ, Luo RT, Levitan DA, Thirman MJ (July 2001). "EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein". Blood. 98 (1): 201–9. doi:10.1182/blood.V98.1.201. PMID 11418481. 
  2. ^ a b Polak PE, Simone F, Kaberlein JJ, Luo RT, Thirman MJ (April 2003). "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia". Mol. Biol. Cell. 14 (4): 1517–28. doi:10.1091/mbc.E02-07-0394. PMC 153119Freely accessible. PMID 12686606. 
  3. ^ a b Kong SE, Banks CA, Shilatifard A, Conaway JW, Conaway RC (July 2005). "ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL". Proc. Natl. Acad. Sci. U.S.A. 102 (29): 10094–8. doi:10.1073/pnas.0503017102. PMC 1177379Freely accessible. PMID 16006523. 
  4. ^ Banks CA, Kong SE, Spahr H, Florens L, Martin-Brown S, Washburn MP, Conaway JW, Mushegian A, Conaway RC (February 2007). "Identification and Characterization of a Schizosaccharomyces pombe RNA Polymerase II Elongation Factor with Similarity to the Metazoan Transcription Factor ELL". J. Biol. Chem. 282 (8): 5761–9. doi:10.1074/jbc.M610393200. PMID 17150956. 

This article incorporates text from the public domain Pfam and InterPro IPR019194

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

RNA polymerase II transcription elongation factor Provide feedback

Members of this family act as transcriptional transactivators of ELL and ELL2 elongation activities [1]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. The N-terminus of approx 120 residues is globular and highly conserved [5].

Literature references

  1. Simone F, Polak PE, Kaberlein JJ, Luo RT, Levitan DA, Thirman MJ; , Blood. 2001;98:201-209.: EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein. PUBMED:11418481 EPMC:11418481

  2. Polak PE, Simone F, Kaberlein JJ, Luo RT, Thirman MJ; , Mol Biol Cell. 2003;14:1517-1528.: ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. PUBMED:12686606 EPMC:12686606

  3. Kong SE, Banks CA, Shilatifard A, Conaway JW, Conaway RC; , Proc Natl Acad Sci U S A. 2005;102:10094-10098.: ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL. PUBMED:16006523 EPMC:16006523

  4. Kong SE, Banks CA, Shilatifard A, Conaway JW, Conaway RC; , Proc Natl Acad Sci U S A. 2005;102:10094-10098.: ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL. PUBMED:16006523 EPMC:16006523

  5. Banks CA, Kong SE, Spahr H, Florens L, Martin-Brown S, Washburn MP, Conaway JW, Mushegian A, Conaway RC; , J Biol Chem. 2007;282:5761-5769.: Identification and Characterization of a Schizosaccharomyces pombe RNA Polymerase II Elongation Factor with Similarity to the Metazoan Transcription Factor ELL. PUBMED:17150956 EPMC:17150956


This tab holds annotation information from the InterPro database.

InterPro entry IPR019194

This entry represents the N-terminal domain of ELL-associated factor (Eaf) proteins, which act as transcriptional transactivators of ELL and ELL2 RNA Polymerase II (Pol II) transcriptional elongation factors [PUBMED:11418481, PUBMED:12686606, PUBMED:16006523, PUBMED:16006523]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. ELL and EAF1 are components of Cajal bodies, which have a role in leukemogenesis [PUBMED:12686606]. EAF1 also has the capacity to interact with ELL1 and ELL2. The N terminus of approx 120 of EAF1 has a region of high serine, aspartic acid, and glutamic acid residues [PUBMED:11418481, PUBMED:17150956].

Domain organisation

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Alignments

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  Seed
(106)
Full
(1087)
Representative proteomes UniProt
(1493)
NCBI
(1935)
Meta
(0)
RP15
(256)
RP35
(562)
RP55
(862)
RP75
(1053)
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  Seed
(106)
Full
(1087)
Representative proteomes UniProt
(1493)
NCBI
(1935)
Meta
(0)
RP15
(256)
RP35
(562)
RP55
(862)
RP75
(1053)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(106)
Full
(1087)
Representative proteomes UniProt
(1493)
NCBI
(1935)
Meta
(0)
RP15
(256)
RP35
(562)
RP55
(862)
RP75
(1053)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Curation and family details

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Curation View help on the curation process

Seed source: KOGs (KOG4795)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: KOGs, Finn RD , Sammut SJ
Number in seed: 106
Number in full: 1087
Average length of the domain: 101.90 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 28.45 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 21.0 20.5
Noise cut-off 20.4 20.4
Model length: 100
Family (HMM) version: 9
Download: download the raw HMM for this family

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