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P32780 (TF2H1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General transcription factor IIH subunit 1
Alternative name(s):
Basic transcription factor 2 62 kDa subunit
Short name=BTF2 p62
General transcription factor IIH polypeptide 1
TFIIH basal transcription factor complex p62 subunit
Gene names
Name:GTF2H1
Synonyms:BTF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.

Subunit structure

One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with PUF60. Ref.8 Ref.9

Subcellular location

Nucleus.

Sequence similarities

Contains 2 BSD domains.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

ATP catabolic process

Inferred from direct assay Ref.8. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8692841. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from direct assay Ref.8. Source: GOC

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement PubMed 7533895. Source: ProtInc

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcore TFIIH complex

Inferred from electronic annotation. Source: InterPro

holo TFIIH complex

Inferred from direct assay Ref.8. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548General transcription factor IIH subunit 1
PRO_0000119245

Regions

Domain99 – 15456BSD 1
Domain180 – 23253BSD 2

Amino acid modifications

Modified residue2401N6-acetyllysine By similarity

Natural variations

Natural variant2341R → W. Ref.3
Corresponds to variant rs4150603 [ dbSNP | Ensembl ].
VAR_014345
Natural variant2851S → F. Ref.3
Corresponds to variant rs4150636 [ dbSNP | Ensembl ].
VAR_014346
Natural variant5171L → V. Ref.3
Corresponds to variant rs4150665 [ dbSNP | Ensembl ].
VAR_014347

Experimental info

Sequence conflict2921S → P in BAB15621. Ref.2
Sequence conflict3851G → A in BAB15621. Ref.2

Secondary structure

................................... 548
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32780 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 8F0FCEBBB1FC9C1D

FASTA54862,032
        10         20         30         40         50         60 
MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI KCQKISPEGK 

        70         80         90        100        110        120 
AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL PKFKRKANKE LEEKNRMLQE 

       130        140        150        160        170        180 
DPVLFQLYKD LVVSQVISAE EFWANRLNVN ATDSSSTSNH KQDVGISAAF LADVRPQTDG 

       190        200        210        220        230        240 
CNGLRYNLTS DIIESIFRTY PAVKMKYAEN VPHNMTEKEF WTRFFQSHYF HRDRLNTGSK 

       250        260        270        280        290        300 
DLFAECAKID EKGLKTMVSL GVKNPLLDLT ALEDKPLDEG YGISSVPSAS NSKSIKENSN 

       310        320        330        340        350        360 
AAIIKRFNHH SAMVLAAGLR KQEAQNEQTS EPSNMDGNSG DADCFQPAVK RAKLQESIEY 

       370        380        390        400        410        420 
EDLGKNNSVK TIALNLKKSD RYYHGPTPIQ SLQYATSQDI INSFQSIRQE MEAYTPKLTQ 

       430        440        450        460        470        480 
VLSSSAASST ITALSPGGAL MQGGTQQAIN QMVPNDIQSE LKHLYVAVGE LLRHFWSCFP 

       490        500        510        520        530        540 
VNTPFLEEKV VKMKSNLERF QVTKLCPFQE KIRRQYLSTN LVSHIEEMLQ TAYNKLHTWQ 


SRRLMKKT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the 62-kilodalton component of basic transcription factor BTF2."
Fischer L., Gerard M., Chalut C., Lutz Y., Humbert S., Kanno M., Chambon P., Egly J.-M.
Science 257:1392-1395(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-234; PHE-285 AND VAL-517.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"An aphidicolin-sensitive fragile site (FRA11C) lies within 100 kb of the putative tumour suppressor gene TSG101 on both human and mouse chromosomes."
Critcher R., Palin A.H., Zhang J., Chin S.F., Gayther S.A., Li L., Cohen S.N., Caldas C., Farr C.J.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 521-548.
[8]"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
[9]"The FBP interacting repressor targets TFIIH to inhibit activated transcription."
Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PUF60.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 103-155.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95809 mRNA. Translation: AAA58399.1.
AK027003 mRNA. Translation: BAB15621.1.
AY163770 Genomic DNA. Translation: AAN46740.1.
CR457368 mRNA. Translation: CAG33649.1.
CH471064 Genomic DNA. Translation: EAW68399.1.
CH471064 Genomic DNA. Translation: EAW68401.1.
BC000365 mRNA. Translation: AAH00365.1.
BC004452 mRNA. Translation: AAH04452.1.
AJ131959 Genomic DNA. Translation: CAC00685.1.
PIRS27958.
RefSeqNP_001135779.1. NM_001142307.1.
NP_005307.1. NM_005316.3.
UniGeneHs.577202.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PFJNMR-A1-108[»]
2DIINMR-A103-150[»]
2RNRNMR-B1-108[»]
ProteinModelPortalP32780.
SMRP32780. Positions 1-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109220. 51 interactions.
DIPDIP-708N.
IntActP32780. 14 interactions.
MINTMINT-192215.
STRING9606.ENSP00000265963.

PTM databases

PhosphoSiteP32780.

Polymorphism databases

DMDM416727.

Proteomic databases

PaxDbP32780.
PeptideAtlasP32780.
PRIDEP32780.

Protocols and materials databases

DNASU2965.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265963; ENSP00000265963; ENSG00000110768.
ENST00000453096; ENSP00000393638; ENSG00000110768.
GeneID2965.
KEGGhsa:2965.
UCSCuc001moh.2. human.

Organism-specific databases

CTD2965.
GeneCardsGC11P018300.
HGNCHGNC:4655. GTF2H1.
HPACAB004637.
HPA046660.
MIM189972. gene.
neXtProtNX_P32780.
PharmGKBPA29041.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315835.
HOGENOMHOG000006589.
HOVERGENHBG060375.
InParanoidP32780.
KOK03141.
OMAEQNGEPS.
OrthoDBEOG7FV3Q4.
PhylomeDBP32780.
TreeFamTF314689.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP32780.
BgeeP32780.
CleanExHS_GTF2H1.
GenevestigatorP32780.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR005607. BSD.
IPR011993. PH_like_dom.
IPR027079. Tfb1/p62.
IPR013876. TFIIH_BTF_p62_N.
[Graphical view]
PANTHERPTHR12856. PTHR12856. 1 hit.
PfamPF03909. BSD. 2 hits.
PF08567. TFIIH_BTF_p62_N. 1 hit.
[Graphical view]
SMARTSM00751. BSD. 2 hits.
[Graphical view]
PROSITEPS50858. BSD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32780.
GeneWikiGTF2H1.
GenomeRNAi2965.
NextBio11752.
PROP32780.
SOURCESearch...

Entry information

Entry nameTF2H1_HUMAN
AccessionPrimary (citable) accession number: P32780
Secondary accession number(s): D3DQY2 expand/collapse secondary AC list , Q6I9Y7, Q9H5K5, Q9NQD9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM