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Q13889

- TF2H3_HUMAN

UniProt

Q13889 - TF2H3_HUMAN

Protein

General transcription factor IIH subunit 3

Gene

GTF2H3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      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. Anchors XPB.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri268 – 28518C4-typeAdd
    BLAST

    GO - Molecular functioni

    1. damaged DNA binding Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. protein N-terminus binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. translation factor activity, nucleic acid binding Source: ProtInc

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. ATP catabolic process Source: GOC
    3. DNA repair Source: Reactome
    4. gene expression Source: Reactome
    5. nucleotide-excision repair Source: Reactome
    6. nucleotide-excision repair, DNA damage removal Source: Reactome
    7. positive regulation of viral transcription Source: Reactome
    8. protein phosphorylation Source: GOC
    9. termination of RNA polymerase I transcription Source: Reactome
    10. transcription-coupled nucleotide-excision repair Source: Reactome
    11. transcription elongation from RNA polymerase II promoter Source: Reactome
    12. transcription elongation from RNA polymerase I promoter Source: Reactome
    13. transcription from RNA polymerase II promoter Source: UniProtKB
    14. transcription from RNA polymerase I promoter Source: Reactome
    15. transcription initiation from RNA polymerase II promoter Source: Reactome
    16. transcription initiation from RNA polymerase I promoter Source: Reactome
    17. translation Source: GOC
    18. viral process Source: Reactome

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General transcription factor IIH subunit 3
    Alternative name(s):
    Basic transcription factor 2 34 kDa subunit
    Short name:
    BTF2 p34
    General transcription factor IIH polypeptide 3
    TFIIH basal transcription factor complex p34 subunit
    Gene namesi
    Name:GTF2H3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4657. GTF2H3.

    Subcellular locationi

    GO - Cellular componenti

    1. core TFIIH complex Source: InterPro
    2. holo TFIIH complex Source: UniProtKB
    3. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29043.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 308308General transcription factor IIH subunit 3PRO_0000119251Add
    BLAST

    Proteomic databases

    MaxQBiQ13889.
    PaxDbiQ13889.
    PRIDEiQ13889.

    PTM databases

    PhosphoSiteiQ13889.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13889.
    BgeeiQ13889.
    CleanExiHS_GTF2H3.
    GenevestigatoriQ13889.

    Organism-specific databases

    HPAiHPA004844.
    HPA053562.

    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 RARA; the interaction requires prior phosphorylation of RARA on 'Ser-369' which then enhances interaction of RARA with CDK7 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi109222. 14 interactions.
    DIPiDIP-787N.
    IntActiQ13889. 1 interaction.
    MINTiMINT-3028878.
    STRINGi9606.ENSP00000228955.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13889.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TFB4 family.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri268 – 28518C4-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5242.
    HOGENOMiHOG000175900.
    HOVERGENiHBG054271.
    InParanoidiQ13889.
    KOiK03143.
    OMAiICSTCET.
    PhylomeDBiQ13889.
    TreeFamiTF314336.

    Family and domain databases

    InterProiIPR004600. TFIIH_Tfb4/p34.
    [Graphical view]
    PANTHERiPTHR12831. PTHR12831. 1 hit.
    PfamiPF03850. Tfb4. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00627. tfb4. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13889-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVSDEDELNL LVIVVDANPI WWGKQALKES QFTLSKCIDA VMVLGNSHLF    50
    MNRSNKLAVI ASHIQESRFL YPGKNGRLGD FFGDPGNPPE FNPSGSKDGK 100
    YELLTSANEV IVEEIKDLMT KSDIKGQHTE TLLAGSLAKA LCYIHRMNKE 150
    VKDNQEMKSR ILVIKAAEDS ALQYMNFMNV IFAAQKQNIL IDACVLDSDS 200
    GLLQQACDIT GGLYLKVPQM PSLLQYLLWV FLPDQDQRSQ LILPPPVHVD 250
    YRAACFCHRN LIEIGYVCSV CLSIFCNFSP ICTTCETAFK ISLPPVLKAK 300
    KKKLKVSA 308
    Length:308
    Mass (Da):34,378
    Last modified:July 19, 2004 - v2
    Checksum:iE739E2176CD6BAA5
    GO
    Isoform 2 (identifier: Q13889-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:267
    Mass (Da):29,777
    Checksum:i9415C0930FAADD34
    GO

    Sequence cautioni

    The sequence CAA82909.1 differs from that shown. Reason: Frameshift at position 302.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform 2. 1 PublicationVSP_055153Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298128 mRNA. Translation: BAG60408.1.
    AK313200 mRNA. Translation: BAG36016.1.
    AF548661 Genomic DNA. Translation: AAN40702.1.
    AC117503 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98426.1.
    BC039726 mRNA. Translation: AAH39726.1.
    BC047868 mRNA. Translation: AAH47868.2.
    BC065250 mRNA. Translation: AAH65250.1.
    Z30093 mRNA. Translation: CAA82909.1. Frameshift.
    CCDSiCCDS61275.1. [Q13889-2]
    CCDS9252.1. [Q13889-1]
    PIRiS44455.
    RefSeqiNP_001258795.1. NM_001271866.1.
    NP_001258796.1. NM_001271867.1.
    NP_001258797.1. NM_001271868.1.
    NP_001507.2. NM_001516.4.
    UniGeneiHs.355348.

    Genome annotation databases

    EnsembliENST00000228955; ENSP00000228955; ENSG00000111358. [Q13889-2]
    ENST00000543341; ENSP00000445162; ENSG00000111358. [Q13889-1]
    GeneIDi2967.
    KEGGihsa:2967.
    UCSCiuc001ufo.2. human. [Q13889-1]

    Polymorphism databases

    DMDMi50403772.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298128 mRNA. Translation: BAG60408.1 .
    AK313200 mRNA. Translation: BAG36016.1 .
    AF548661 Genomic DNA. Translation: AAN40702.1 .
    AC117503 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98426.1 .
    BC039726 mRNA. Translation: AAH39726.1 .
    BC047868 mRNA. Translation: AAH47868.2 .
    BC065250 mRNA. Translation: AAH65250.1 .
    Z30093 mRNA. Translation: CAA82909.1 . Frameshift.
    CCDSi CCDS61275.1. [Q13889-2 ]
    CCDS9252.1. [Q13889-1 ]
    PIRi S44455.
    RefSeqi NP_001258795.1. NM_001271866.1.
    NP_001258796.1. NM_001271867.1.
    NP_001258797.1. NM_001271868.1.
    NP_001507.2. NM_001516.4.
    UniGenei Hs.355348.

    3D structure databases

    ProteinModelPortali Q13889.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109222. 14 interactions.
    DIPi DIP-787N.
    IntActi Q13889. 1 interaction.
    MINTi MINT-3028878.
    STRINGi 9606.ENSP00000228955.

    PTM databases

    PhosphoSitei Q13889.

    Polymorphism databases

    DMDMi 50403772.

    Proteomic databases

    MaxQBi Q13889.
    PaxDbi Q13889.
    PRIDEi Q13889.

    Protocols and materials databases

    DNASUi 2967.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228955 ; ENSP00000228955 ; ENSG00000111358 . [Q13889-2 ]
    ENST00000543341 ; ENSP00000445162 ; ENSG00000111358 . [Q13889-1 ]
    GeneIDi 2967.
    KEGGi hsa:2967.
    UCSCi uc001ufo.2. human. [Q13889-1 ]

    Organism-specific databases

    CTDi 2967.
    GeneCardsi GC12P124118.
    H-InvDB HIX0026378.
    HGNCi HGNC:4657. GTF2H3.
    HPAi HPA004844.
    HPA053562.
    MIMi 601750. gene.
    neXtProti NX_Q13889.
    PharmGKBi PA29043.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5242.
    HOGENOMi HOG000175900.
    HOVERGENi HBG054271.
    InParanoidi Q13889.
    KOi K03143.
    OMAi ICSTCET.
    PhylomeDBi Q13889.
    TreeFami TF314336.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    GenomeRNAii 2967.
    NextBioi 11760.
    PROi Q13889.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13889.
    Bgeei Q13889.
    CleanExi HS_GTF2H3.
    Genevestigatori Q13889.

    Family and domain databases

    InterProi IPR004600. TFIIH_Tfb4/p34.
    [Graphical view ]
    PANTHERi PTHR12831. PTHR12831. 1 hit.
    Pfami PF03850. Tfb4. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00627. tfb4. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
      , 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] (ISOFORMS 1 AND 2).
    2. NIEHS SNPs program
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Brain, Eye and Testis.
    6. "p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair."
      Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M., Moncollin V.
      EMBO J. 13:2393-2398(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-305 (ISOFORM 1), PROTEIN SEQUENCE OF 57-68; 78-97; 107-112; 127-132 AND 239-251 (ISOFORMS 1/2).
    7. "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.

    Entry informationi

    Entry nameiTF2H3_HUMAN
    AccessioniPrimary (citable) accession number: Q13889
    Secondary accession number(s): B2R819
    , B4DNZ6, Q7L0G0, Q96AT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3