TH1L: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Negative elongation factor C/D''' is a [[protein]] that in humans is encoded by the ''TH1L'' [[gene]].<ref name="pmid11030415">{{cite journal | vauthors = Bonthron DT, Hayward BE, Moran V, Strain L | title = Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13 | journal = Human Genetics | volume = 107 | issue = 2 | pages = 165–75 | date = Aug 2000 | pmid = 11030415 | pmc =  | doi = 10.1007/s004390000344 }}</ref><ref name="pmid11042152">{{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells | journal = Genome Research | volume = 10 | issue = 10 | pages = 1546–60 | date = Oct 2000 | pmid = 11042152 | pmc = 310934 | doi = 10.1101/gr.140200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TH1L TH1-like (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51497| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = TH1-like (Drosophila)
| HGNCid = 15934
| Symbol = TH1L
| AltSymbols =; HSPC130; NELF-C; NELF-D; TH1
| OMIM = 605297
| ECnumber = 
| Homologene = 9496
| MGIid = 1926424
| GeneAtlas_image1 = PBB_GE_TH1L_220607_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51497
    | Hs_Ensembl = ENSG00000101158
    | Hs_RefseqProtein = NP_945327
    | Hs_RefseqmRNA = NM_198976
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 56989706
    | Hs_GenLoc_end = 57003583
    | Hs_Uniprot = Q8IXH7
    | Mm_EntrezGene = 57314
    | Mm_Ensembl = ENSMUSG00000016253
    | Mm_RefseqmRNA = NM_020580
    | Mm_RefseqProtein = NP_065605
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 174058743
    | Mm_GenLoc_end = 174070436
    | Mm_Uniprot = Q3TW27
  }}
}}
'''TH1-like (Drosophila)''', also known as '''TH1L''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TH1L TH1-like (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51497| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The NELF complex of proteins interacts with the DSIF protein complex to repress transcriptional elongation by RNA polymerase II. The protein encoded by this gene is an essential part of the NELF complex. Alternative translation initiation site usage results in the formation of two isoforms with different N-termini.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The NELF complex of proteins interacts with the DSIF protein complex to repress transcriptional elongation by RNA polymerase II. The protein encoded by this gene is an essential part of the NELF complex. Alternative translation initiation site usage results in the formation of two isoforms with different N-termini.<ref name="entrez">{{cite web | title = Entrez Gene: TH1L TH1-like (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51497| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
TH1L has been shown to [[Protein-protein interaction|interact]] with:
* [[ARAF]],<ref name = pmid12620389>{{cite journal | vauthors = Yuryev A, Wennogle LP | title = Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis | journal = Genomics | volume = 81 | issue = 2 | pages = 112–25 | date = Feb 2003 | pmid = 12620389 | doi =  10.1016/s0888-7543(02)00008-3}}</ref><ref name = pmid11952167>{{cite journal | vauthors = Yin XL, Chen S, Gu JX | title = Identification of TH1 as an interaction partner of A-Raf kinase | journal = Molecular and Cellular Biochemistry | volume = 231 | issue = 1-2 | pages = 69–74 | date = Feb 2002 | pmid = 11952167 | doi =  10.1023/A:1014437024129}}</ref>
* [[Cofactor of BRCA1]],<ref name = pmid17353931/><ref name = pmid12612062/> and
* [[RDBP]].<ref name = pmid17353931>{{cite journal | vauthors = 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 | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue =  | pages = 89 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 | year=2007}}</ref><ref name = pmid12612062>{{cite journal | vauthors = Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H | title = Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex | journal = Molecular and Cellular Biology | volume = 23 | issue = 6 | pages = 1863–73 | date = Mar 2003 | pmid = 12612062 | pmc = 149481 | doi =  10.1128/mcb.23.6.1863-1873.2003}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Stevens M, De Clercq E, Balzarini J | title = The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention | journal = Medicinal Research Reviews | volume = 26 | issue = 5 | pages = 595–625 | date = Sep 2006 | pmid = 16838299 | doi = 10.1002/med.20081 }}
| citations =
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595-625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081 }}
* {{cite journal | vauthors = Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H | title = NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation | journal = Cell | volume = 97 | issue = 1 | pages = 41–51 | date = Apr 1999 | pmid = 10199401 | doi = 10.1016/S0092-8674(00)80713-8 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Ping YH, Rana TM | title = DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 12951–8 | date = Apr 2001 | pmid = 11112772 | doi = 10.1074/jbc.M006130200 }}
*{{cite journal | author=Yamaguchi Y, Takagi T, Wada T, ''et al.'' |title=NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. |journal=Cell |volume=97 |issue= 1 |pages= 41-51 |year= 1999 |pmid= 10199401 |doi= }}
* {{cite journal | vauthors = Yin XL, Chen S, Gu JX | title = Identification of TH1 as an interaction partner of A-Raf kinase | journal = Molecular and Cellular Biochemistry | volume = 231 | issue = 1-2 | pages = 69–74 | date = Feb 2002 | pmid = 11952167 | doi = 10.1023/A:1014437024129 }}
*{{cite journal  | author=Bonthron DT, Hayward BE, Moran V, Strain L |title=Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13. |journal=Hum. Genet. |volume=107 |issue= 2 |pages= 165-75 |year= 2000 |pmid= 11030415 |doi=  }}
* {{cite journal | vauthors = Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H | title = Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex | journal = Molecular and Cellular Biology | volume = 23 | issue = 6 | pages = 1863–73 | date = Mar 2003 | pmid = 12612062 | pmc = 149481 | doi = 10.1128/MCB.23.6.1863-1873.2003 }}
*{{cite journal  | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi=  }}
* {{cite journal | vauthors = Yuryev A, Wennogle LP | title = Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis | journal = Genomics | volume = 81 | issue = 2 | pages = 112–25 | date = Feb 2003 | pmid = 12620389 | doi = 10.1016/S0888-7543(02)00008-3 }}
*{{cite journal | author=Ping YH, Rana TM |title=DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12951-8 |year= 2001 |pmid= 11112772 |doi= 10.1074/jbc.M006130200 }}
* {{cite journal | vauthors = Liu W, Shen X, Yang Y, Yin X, Xie J, Yan J, Jiang J, Liu W, Wang H, Sun M, Zheng Y, Gu J | title = Trihydrophobin 1 is a new negative regulator of A-Raf kinase | journal = The Journal of Biological Chemistry | volume = 279 | issue = 11 | pages = 10167–75 | date = Mar 2004 | pmid = 14684750 | doi = 10.1074/jbc.M307994200 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Research | volume = 14 | issue = 7 | pages = 1324–32 | date = Jul 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
*{{cite journal  | author=Yin XL, Chen S, Gu JX |title=Identification of TH1 as an interaction partner of A-Raf kinase. |journal=Mol. Cell. Biochem. |volume=231 |issue= 1-2 |pages= 69-74 |year= 2002 |pmid= 11952167 |doi=  }}
* {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Yang Y, Liu W, Zou W, Wang H, Zong H, Jiang J, Wang Y, Gu J | title = Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP) | journal = Journal of Cellular Biochemistry | volume = 101 | issue = 1 | pages = 167–80 | date = May 2007 | pmid = 17131388 | doi = 10.1002/jcb.21164 }}
*{{cite journal | author=Narita T, Yamaguchi Y, Yano K, ''et al.'' |title=Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex. |journal=Mol. Cell. Biol. |volume=23 |issue= 6 |pages= 1863-73 |year= 2003 |pmid= 12612062 |doi= }}
*{{cite journal | author=Yuryev A, Wennogle LP |title=Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis. |journal=Genomics |volume=81 |issue= 2 |pages= 112-25 |year= 2003 |pmid= 12620389 |doi= }}
*{{cite journal | author=Liu W, Shen X, Yang Y, ''et al.'' |title=Trihydrophobin 1 is a new negative regulator of A-Raf kinase. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 10167-75 |year= 2004 |pmid= 14684750 |doi= 10.1074/jbc.M307994200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Yang Y, Liu W, Zou W, ''et al.'' |title=Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP). |journal=J. Cell. Biochem. |volume=101 |issue= 1 |pages= 167-80 |year= 2007 |pmid= 17131388 |doi= 10.1002/jcb.21164 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
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Latest revision as of 02:12, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Negative elongation factor C/D is a protein that in humans is encoded by the TH1L gene.[1][2][3]

Function

The NELF complex of proteins interacts with the DSIF protein complex to repress transcriptional elongation by RNA polymerase II. The protein encoded by this gene is an essential part of the NELF complex. Alternative translation initiation site usage results in the formation of two isoforms with different N-termini.[3]

Interactions

TH1L has been shown to interact with:

References

  1. ↑ Bonthron DT, Hayward BE, Moran V, Strain L (Aug 2000). "Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13". Human Genetics. 107 (2): 165–75. doi:10.1007/s004390000344. PMID 11030415.
  2. ↑ Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  3. ↑ 3.0 3.1 "Entrez Gene: TH1L TH1-like (Drosophila)".
  4. ↑ Yuryev A, Wennogle LP (Feb 2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis". Genomics. 81 (2): 112–25. doi:10.1016/s0888-7543(02)00008-3. PMID 12620389.
  5. ↑ Yin XL, Chen S, Gu JX (Feb 2002). "Identification of TH1 as an interaction partner of A-Raf kinase". Molecular and Cellular Biochemistry. 231 (1–2): 69–74. doi:10.1023/A:1014437024129. PMID 11952167.
  6. ↑ 6.0 6.1 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". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  7. ↑ 7.0 7.1 Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H (Mar 2003). "Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex". Molecular and Cellular Biology. 23 (6): 1863–73. doi:10.1128/mcb.23.6.1863-1873.2003. PMC 149481. PMID 12612062.

Further reading


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