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Q9DBA9

- TF2H1_MOUSE

UniProt

Q9DBA9 - TF2H1_MOUSE

Protein

General transcription factor IIH subunit 1

Gene

Gtf2h1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    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.

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. nucleotide-excision repair Source: InterPro
    3. protein phosphorylation Source: GOC
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription from RNA polymerase II promoter Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Gtf2h1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1277216. Gtf2h1.

    Subcellular locationi

    GO - Cellular componenti

    1. core TFIIH complex Source: InterPro
    2. holo TFIIH complex Source: UniProtKB
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 547547General transcription factor IIH subunit 1PRO_0000119246Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9DBA9.
    PRIDEiQ9DBA9.

    PTM databases

    PhosphoSiteiQ9DBA9.

    Expressioni

    Gene expression databases

    CleanExiMM_GTF2H1.
    GenevestigatoriQ9DBA9.

    Interactioni

    Subunit structurei

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200111. 3 interactions.
    IntActiQ9DBA9. 1 interaction.
    STRINGi10090.ENSMUSP00000103271.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBA9.
    SMRiQ9DBA9. Positions 1-155.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 15456BSD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini179 – 23153BSD 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 BSD domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315835.
    HOGENOMiHOG000006589.
    HOVERGENiHBG060375.
    InParanoidiQ9DBA9.
    KOiK03141.
    PhylomeDBiQ9DBA9.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR005607. BSD.
    IPR011993. PH_like_dom.
    IPR027079. Tfb1/p62.
    IPR013876. TFIIH_BTF_p62_N.
    [Graphical view]
    PANTHERiPTHR12856. PTHR12856. 1 hit.
    PfamiPF03909. BSD. 2 hits.
    PF08567. TFIIH_BTF_p62_N. 1 hit.
    [Graphical view]
    SMARTiSM00751. BSD. 2 hits.
    [Graphical view]
    PROSITEiPS50858. BSD. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBA9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI    50
    KCQKISPEGK AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL 100
    PKFKRKANKE LEEKNRMLQE DPVLFQLYKD LVVSQVISAE EFWANRLNVN 150
    ATDSSTSSHK QDVGISAAFL ADVRPQTDGC NGLRYNLTSD IIESIFRTYP 200
    AVKMKYAETV PHNMTEKEFW TRFFQSHYFH RDRLNTGSKD LFAECAKIDE 250
    KGLKTMVSLG VKNPMLDLTS LEDKPLDEGY SISSVPSTSN SKSIKENSNA 300
    AIIKRFNHHS AMVLAAGLRK QQAQNGQNGE PSSVDGNSGD TDCFQPAVKR 350
    AKLQESIEYE DLGNNNSVKT IALNLKKSDR YYHGPTPIQS LQYATSQDII 400
    NSFQSIRQEM EAYTPKLTQV LSSSAASSTI TALSPGGALM QGGTQQAVNQ 450
    MVPNDIQSEL KHLYVAVGEL LRHFWSCFPV NTPFLEEKVV KMKSNLERFQ 500
    VTKLCPFQEK IRRQYLSTNL VSHIEEMLQT AYNKLHTWQS RRLMKKT 547
    Length:547
    Mass (Da):61,851
    Last modified:October 18, 2001 - v2
    Checksum:i0167316D11F87969
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371I → F in BAB23789. (PubMed:16141072)Curated
    Sequence conflicti208 – 2081E → G in BAB23789. (PubMed:16141072)Curated
    Sequence conflicti281 – 2811S → G in BAB23789. (PubMed:16141072)Curated
    Sequence conflicti537 – 5371T → A in BAB23789. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002366 mRNA. Translation: CAA05340.1.
    AK005065 mRNA. Translation: BAB23789.1.
    CCDSiCCDS21287.1.
    RefSeqiNP_001278004.1. NM_001291075.1.
    NP_032212.3. NM_008186.4.
    UniGeneiMm.22700.

    Genome annotation databases

    GeneIDi14884.
    KEGGimmu:14884.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002366 mRNA. Translation: CAA05340.1 .
    AK005065 mRNA. Translation: BAB23789.1 .
    CCDSi CCDS21287.1.
    RefSeqi NP_001278004.1. NM_001291075.1.
    NP_032212.3. NM_008186.4.
    UniGenei Mm.22700.

    3D structure databases

    ProteinModelPortali Q9DBA9.
    SMRi Q9DBA9. Positions 1-155.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200111. 3 interactions.
    IntActi Q9DBA9. 1 interaction.
    STRINGi 10090.ENSMUSP00000103271.

    PTM databases

    PhosphoSitei Q9DBA9.

    Proteomic databases

    PaxDbi Q9DBA9.
    PRIDEi Q9DBA9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 14884.
    KEGGi mmu:14884.

    Organism-specific databases

    CTDi 2965.
    MGIi MGI:1277216. Gtf2h1.

    Phylogenomic databases

    eggNOGi NOG315835.
    HOGENOMi HOG000006589.
    HOVERGENi HBG060375.
    InParanoidi Q9DBA9.
    KOi K03141.
    PhylomeDBi Q9DBA9.

    Miscellaneous databases

    ChiTaRSi GTF2H1. mouse.
    NextBioi 287163.
    PROi Q9DBA9.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_GTF2H1.
    Genevestigatori Q9DBA9.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR005607. BSD.
    IPR011993. PH_like_dom.
    IPR027079. Tfb1/p62.
    IPR013876. TFIIH_BTF_p62_N.
    [Graphical view ]
    PANTHERi PTHR12856. PTHR12856. 1 hit.
    Pfami PF03909. BSD. 2 hits.
    PF08567. TFIIH_BTF_p62_N. 1 hit.
    [Graphical view ]
    SMARTi SM00751. BSD. 2 hits.
    [Graphical view ]
    PROSITEi PS50858. BSD. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization and promoter characterization of the mouse and human genes encoding p62 subunit of the transcription/DNA repair factor TFIIH."
      Perez C., Auriol J., Seroz T., Egly J.-M.
      Gene 213:73-82(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Teratocarcinoma.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTF2H1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBA9
    Secondary accession number(s): O35637
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3