GTF2H1

Protein-coding gene in the species Homo sapiens
GTF2H1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PFJ, 2DII, 2RNR, 2RUK, 2RVB

Identifiers
AliasesGTF2H1, BTF2, P62, TFB1, TFIIH, general transcription factor IIH subunit 1
External IDsOMIM: 189972 MGI: 1277216 HomoloGene: 3885 GeneCards: GTF2H1
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for GTF2H1
Genomic location for GTF2H1
Band11p15.1Start18,322,295 bp[1]
End18,367,045 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for GTF2H1
Genomic location for GTF2H1
Band7|7 B3Start46,445,527 bp[2]
End46,473,224 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • corpus callosum

  • endometrium

  • thymus

  • monocyte

  • islet of Langerhans

  • smooth muscle tissue

  • gallbladder

  • tibial nerve

  • skin of abdomen
Top expressed in
  • spermatocyte

  • spermatid

  • yolk sac

  • lacrimal gland

  • morula

  • seminiferous tubule

  • epithelium of stomach

  • proximal tubule

  • primitive streak

  • oocyte
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein kinase activity
  • ATP-dependent activity, acting on DNA
  • chromatin binding
  • protein binding
  • RNA polymerase II CTD heptapeptide repeat kinase activity
Cellular component
  • nucleoplasm
  • transcription factor TFIIH holo complex
  • nucleus
  • transcription factor TFIIH core complex
Biological process
  • termination of RNA polymerase I transcription
  • regulation of cyclin-dependent protein serine/threonine kinase activity
  • regulation of transcription, DNA-templated
  • transcription initiation from RNA polymerase I promoter
  • transcription elongation from RNA polymerase II promoter
  • 7-methylguanosine mRNA capping
  • transcription by RNA polymerase II
  • transcription, DNA-templated
  • cellular response to DNA damage stimulus
  • global genome nucleotide-excision repair
  • transcription-coupled nucleotide-excision repair
  • transcription initiation from RNA polymerase II promoter
  • nucleotide-excision repair, DNA incision
  • DNA repair
  • positive regulation of transcription by RNA polymerase II
  • nucleotide-excision repair, preincision complex stabilization
  • nucleotide-excision repair
  • nucleotide-excision repair, DNA incision, 5'-to lesion
  • nucleotide-excision repair, preincision complex assembly
  • transcription by RNA polymerase I
  • phosphorylation of RNA polymerase II C-terminal domain
  • nucleotide-excision repair, DNA duplex unwinding
  • nucleotide-excision repair, DNA incision, 3'-to lesion
  • transcription elongation from RNA polymerase I promoter
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2965

14884

Ensembl

ENSG00000110768
ENSG00000288114

ENSMUSG00000006599

UniProt

P32780

Q9DBA9

RefSeq (mRNA)

NM_001142307
NM_005316

NM_001291075
NM_008186
NM_001360075
NM_001360076

RefSeq (protein)

NP_001135779
NP_005307

NP_001278004
NP_032212
NP_001347004
NP_001347005

Location (UCSC)Chr 11: 18.32 – 18.37 MbChr 7: 46.45 – 46.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

General transcription factor IIH subunit 1 is a protein that in humans is encoded by the GTF2H1 gene.[5][6][7]

Interactions

GTF2H1 has been shown to interact with:

See also

References

  1. ^ a b c ENSG00000288114 GRCh38: Ensembl release 89: ENSG00000110768, ENSG00000288114 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006599 – 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. ^ Fischer L, Gerard M, Chalut C, Lutz Y, Humbert S, Kanno M, Chambon P, Egly JM (October 1992). "Cloning of the 62-kilodalton component of basic transcription factor BTF2". Science. 257 (5075): 1392–5. Bibcode:1992Sci...257.1392F. doi:10.1126/science.1529339. PMID 1529339.
  6. ^ Heng HH, Xiao H, Shi XM, Greenblatt J, Tsui LC (May 1994). "Genes encoding general initiation factors for RNA polymerase II transcription are dispersed in the human genome". Hum. Mol. Genet. 3 (1): 61–4. doi:10.1093/hmg/3.1.61. PMID 8162052.
  7. ^ "Entrez Gene: GTF2H1 general transcription factor IIH, polypeptide 1, 62kDa".
  8. ^ a b c Rossignol M, Kolb-Cheynel I, Egly JM (April 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". EMBO J. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.
  9. ^ Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D (March 1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH". Nature. 374 (6519): 283–7. Bibcode:1995Natur.374..283S. doi:10.1038/374283a0. PMID 7533895. S2CID 4282418.
  10. ^ Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y (December 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Res. 55 (24): 6058–62. PMID 8521393.
  11. ^ Vandel L, Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. 18 (15): 4280–91. doi:10.1093/emboj/18.15.4280. PMC 1171504. PMID 10428966.
  12. ^ Drapkin R, Reardon JT, Ansari A, Huang JC, Zawel L, Ahn K, Sancar A, Reinberg D (April 1994). "Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II". Nature. 368 (6473): 769–72. Bibcode:1994Natur.368..769D. doi:10.1038/368769a0. PMID 8152490. S2CID 4363484.
  13. ^ Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S (July 2000). "Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7". Mol. Cell. 6 (1): 127–37. doi:10.1016/s1097-2765(00)00014-9. PMID 10949034.
  14. ^ Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J (October 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. doi:10.1074/jbc.273.42.27593. PMID 9765293.
  15. ^ Pan G, Aso T, Greenblatt J (September 1997). "Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators". J. Biol. Chem. 272 (39): 24563–71. doi:10.1074/jbc.272.39.24563. PMID 9305922.
  16. ^ Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W (July 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nat. Genet. 36 (7): 714–9. doi:10.1038/ng1387. PMID 15220921.
  17. ^ Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (March 1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947.

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447-9. Bibcode:1998CBio....8.R447Y. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670. S2CID 15480646.
  • Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D (1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH". Nature. 374 (6519): 283–7. Bibcode:1995Natur.374..283S. doi:10.1038/374283a0. PMID 7533895. S2CID 4282418.
  • Tong X, Drapkin R, Reinberg D, Kieff E (1995). "The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3259–63. Bibcode:1995PNAS...92.3259T. doi:10.1073/pnas.92.8.3259. PMC 42145. PMID 7724549.
  • Fantes JA, Oghene K, Boyle S, Danes S, Fletcher JM, Bruford EA, Williamson K, Seawright A, Schedl A, Hanson I (1995). "A high-resolution integrated physical, cytogenetic, and genetic map of human chromosome 11: distal p13 to proximal p15.1". Genomics. 25 (2): 447–61. doi:10.1016/0888-7543(95)80045-N. PMID 7789978.
  • Xiao H, Pearson A, Coulombe B, Truant R, Zhang S, Regier JL, Triezenberg SJ, Reinberg D, Flores O, Ingles CJ (1994). "Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53". Mol. Cell. Biol. 14 (10): 7013–24. doi:10.1128/mcb.14.10.7013. PMC 359231. PMID 7935417.
  • Schaeffer L, Moncollin V, Roy R, Staub A, Mezzina M, Sarasin A, Weeda G, Hoeijmakers JH, Egly JM (1994). "The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor". EMBO J. 13 (10): 2388–92. doi:10.1002/j.1460-2075.1994.tb06522.x. PMC 395103. PMID 8194528.
  • Blau J, Xiao H, McCracken S, O'Hare P, Greenblatt J, Bentley D (1996). "Three functional classes of transcriptional activation domain". Mol. Cell. Biol. 16 (5): 2044–55. doi:10.1128/MCB.16.5.2044. PMC 231191. PMID 8628270.
  • Iyer N, Reagan MS, Wu KJ, Canagarajah B, Friedberg EC (1996). "Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein". Biochemistry. 35 (7): 2157–67. doi:10.1021/bi9524124. PMID 8652557.
  • Reardon JT, Ge H, Gibbs E, Sancar A, Hurwitz J, Pan ZQ (1996). "Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6482–7. Bibcode:1996PNAS...93.6482R. doi:10.1073/pnas.93.13.6482. PMC 39049. PMID 8692841.
  • Drapkin R, Le Roy G, Cho H, Akoulitchev S, Reinberg D (1996). "Human cyclin-dependent kinase-activating kinase exists in three distinct complexes". Proc. Natl. Acad. Sci. U.S.A. 93 (13): 6488–93. Bibcode:1996PNAS...93.6488D. doi:10.1073/pnas.93.13.6488. PMC 39050. PMID 8692842.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451. S2CID 13266489.
  • Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature. 384 (6607): 375–8. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526. S2CID 4278432.
  • García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.
  • Marinoni JC, Roy R, Vermeulen W, Miniou P, Lutz Y, Weeda G, Seroz T, Gomez DM, Hoeijmakers JH, Egly JM (1997). "Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH". EMBO J. 16 (5): 1093–102. doi:10.1093/emboj/16.5.1093. PMC 1169708. PMID 9118947.
  • Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. doi:10.1128/mcb.17.4.1817. PMC 232028. PMID 9121429.
  • Rossignol M, Kolb-Cheynel I, Egly JM (1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". EMBO J. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.
  • García-Martínez LF, Mavankal G, Neveu JM, Lane WS, Ivanov D, Gaynor RB (1997). "Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription". EMBO J. 16 (10): 2836–50. doi:10.1093/emboj/16.10.2836. PMC 1169892. PMID 9184228.

External links

  • GTF2H1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Overview of all the structural information available in the PDB for UniProt: P32780 (General transcription factor IIH subunit 1) at the PDBe-KB.
  • v
  • t
  • e
  • 1pfj: Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit
    1pfj: Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit
  • 2dii: Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit
    2dii: Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit
  • v
  • t
  • e
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies

This article incorporates text from the United States National Library of Medicine, which is in the public domain.