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Q13888

- TF2H2_HUMAN

UniProt

Q13888 - TF2H2_HUMAN

Protein

General transcription factor IIH subunit 2

Gene

GTF2H2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri291 – 30818C4-typeAdd
    BLAST

    GO - Molecular functioni

    1. nucleic acid binding Source: ProtInc
    2. protein binding Source: UniProtKB
    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
    6. zinc ion binding Source: InterPro

    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. G-protein coupled receptor internalization Source: UniProtKB
    6. nucleotide-excision repair Source: Reactome
    7. nucleotide-excision repair, DNA damage removal Source: Reactome
    8. positive regulation of viral transcription Source: Reactome
    9. protein phosphorylation Source: GOC
    10. response to UV Source: ProtInc
    11. termination of RNA polymerase I transcription Source: Reactome
    12. transcription-coupled nucleotide-excision repair Source: Reactome
    13. transcription elongation from RNA polymerase II promoter Source: Reactome
    14. transcription elongation from RNA polymerase I promoter Source: Reactome
    15. transcription from RNA polymerase II promoter Source: UniProtKB
    16. transcription from RNA polymerase I promoter Source: Reactome
    17. transcription initiation from RNA polymerase II promoter Source: Reactome
    18. transcription initiation from RNA polymerase I promoter Source: Reactome
    19. translation Source: GOC
    20. 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 2
    Alternative name(s):
    Basic transcription factor 2 44 kDa subunit
    Short name:
    BTF2 p44
    General transcription factor IIH polypeptide 2
    TFIIH basal transcription factor complex p44 subunit
    Gene namesi
    Name:GTF2H2
    Synonyms:BTF2P44
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4656. GTF2H2.

    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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi291 – 2911C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication
    Mutagenesisi308 – 3081C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication
    Mutagenesisi345 – 3451C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi360 – 3601C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi363 – 3631C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi376 – 3761H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi380 – 3801H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi382 – 3821C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA29042.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395General transcription factor IIH subunit 2PRO_0000119248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei95 – 951PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13888.
    PaxDbiQ13888.
    PRIDEiQ13888.

    PTM databases

    PhosphoSiteiQ13888.

    Expressioni

    Tissue specificityi

    Widely expressed, with higher expression in skeletal muscle.

    Gene expression databases

    BgeeiQ13888.
    CleanExiHS_GTF2H2.
    GenevestigatoriQ13888.

    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 XPB, XPD, GTF2H1 and GTF2H3. Interacts with varicella-zoster virus IE63 protein.2 Publications

    Protein-protein interaction databases

    BioGridi109221. 15 interactions.
    DIPiDIP-786N.
    IntActiQ13888. 4 interactions.
    MINTiMINT-3028823.
    STRINGi9606.ENSP00000274400.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi333 – 3353
    Helixi336 – 3394
    Turni346 – 3494
    Beta strandi355 – 3584
    Turni361 – 3644
    Helixi369 – 3735
    Turni374 – 3785
    Beta strandi381 – 3833

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z60NMR-A328-386[»]
    ProteinModelPortaliQ13888.
    SMRiQ13888. Positions 328-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13888.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini60 – 236177VWFAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GTF2H2 family.Curated
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri291 – 30818C4-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5151.
    HOGENOMiHOG000159415.
    HOVERGENiHBG059468.
    InParanoidiQ13888.
    KOiK03142.
    OMAiECKVCGL.
    PhylomeDBiQ13888.
    TreeFamiTF314037.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR007198. Ssl1-like.
    IPR004595. TFIIH_C1-like_dom.
    IPR012170. TFIIH_SSL1/p44.
    IPR002035. VWF_A.
    IPR007087. Znf_C2H2.
    [Graphical view]
    PANTHERiPTHR12695. PTHR12695. 1 hit.
    PfamiPF07975. C1_4. 1 hit.
    PF04056. Ssl1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015919. TFIIH_SSL1. 1 hit.
    SMARTiSM01047. C1_4. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    TIGRFAMsiTIGR00622. ssl1. 1 hit.
    PROSITEiPS50234. VWFA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms may be produced. The isoforms may be also produced by incomplete gene duplication.

    Isoform 1 (identifier: Q13888-1) [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

    MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH    50
    GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP 100
    ISQIGIIVTK SKRAEKLTEL SGNPRKHITS LKKAVDMTCH GEPSLYNSLS 150
    IAMQTLKHMP GHTSREVLII FSSLTTCDPS NIYDLIKTLK AAKIRVSVIG 200
    LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP ASSSSECSLI 250
    RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE 300
    LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG 350
    ELKDQHVYVC AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV 395
    Length:395
    Mass (Da):44,419
    Last modified:November 1, 1996 - v1
    Checksum:i56D1BD8841288739
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291T → S(PubMed:7552146)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511I → M.1 Publication
    VAR_011664
    Natural varianti236 – 2361V → L.1 Publication
    VAR_011665

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z30094 mRNA. Translation: CAA82910.1.
    AF078847 mRNA. Translation: AAD44479.1.
    U21911 mRNA. Translation: AAA64502.1.
    U21910 mRNA. Translation: AAA64503.1.
    BC005345 mRNA. Translation: AAH05345.1.
    U80017 Genomic DNA. Translation: AAC52046.1.
    CCDSiCCDS34183.1. [Q13888-1]
    PIRiS44454.
    RefSeqiNP_001506.1. NM_001515.3. [Q13888-1]
    XP_005248541.1. XM_005248484.1. [Q13888-1]
    XP_005276841.1. XM_005276784.1. [Q13888-1]
    XP_005276843.1. XM_005276786.2. [Q13888-1]
    XP_006714657.1. XM_006714594.1. [Q13888-1]
    XP_006725511.1. XM_006725448.1. [Q13888-1]
    XP_006725512.1. XM_006725449.1. [Q13888-1]
    XP_006726280.1. XM_006726217.1. [Q13888-1]
    UniGeneiHs.191356.
    Hs.422901.
    Hs.607501.

    Genome annotation databases

    EnsembliENST00000274400; ENSP00000274400; ENSG00000145736. [Q13888-1]
    ENST00000330280; ENSP00000328901; ENSG00000145736. [Q13888-1]
    GeneIDi2966.
    728340.
    KEGGihsa:2966.
    hsa:728340.
    UCSCiuc003kau.4. human. [Q13888-1]

    Polymorphism databases

    DMDMi17380326.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z30094 mRNA. Translation: CAA82910.1 .
    AF078847 mRNA. Translation: AAD44479.1 .
    U21911 mRNA. Translation: AAA64502.1 .
    U21910 mRNA. Translation: AAA64503.1 .
    BC005345 mRNA. Translation: AAH05345.1 .
    U80017 Genomic DNA. Translation: AAC52046.1 .
    CCDSi CCDS34183.1. [Q13888-1 ]
    PIRi S44454.
    RefSeqi NP_001506.1. NM_001515.3. [Q13888-1 ]
    XP_005248541.1. XM_005248484.1. [Q13888-1 ]
    XP_005276841.1. XM_005276784.1. [Q13888-1 ]
    XP_005276843.1. XM_005276786.2. [Q13888-1 ]
    XP_006714657.1. XM_006714594.1. [Q13888-1 ]
    XP_006725511.1. XM_006725448.1. [Q13888-1 ]
    XP_006725512.1. XM_006725449.1. [Q13888-1 ]
    XP_006726280.1. XM_006726217.1. [Q13888-1 ]
    UniGenei Hs.191356.
    Hs.422901.
    Hs.607501.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z60 NMR - A 328-386 [» ]
    ProteinModelPortali Q13888.
    SMRi Q13888. Positions 328-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109221. 15 interactions.
    DIPi DIP-786N.
    IntActi Q13888. 4 interactions.
    MINTi MINT-3028823.
    STRINGi 9606.ENSP00000274400.

    PTM databases

    PhosphoSitei Q13888.

    Polymorphism databases

    DMDMi 17380326.

    Proteomic databases

    MaxQBi Q13888.
    PaxDbi Q13888.
    PRIDEi Q13888.

    Protocols and materials databases

    DNASUi 2966.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274400 ; ENSP00000274400 ; ENSG00000145736 . [Q13888-1 ]
    ENST00000330280 ; ENSP00000328901 ; ENSG00000145736 . [Q13888-1 ]
    GeneIDi 2966.
    728340.
    KEGGi hsa:2966.
    hsa:728340.
    UCSCi uc003kau.4. human. [Q13888-1 ]

    Organism-specific databases

    CTDi 2966.
    728340.
    GeneCardsi GC05M070366.
    HGNCi HGNC:4656. GTF2H2.
    MIMi 601748. gene.
    neXtProti NX_Q13888.
    PharmGKBi PA29042.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5151.
    HOGENOMi HOG000159415.
    HOVERGENi HBG059468.
    InParanoidi Q13888.
    KOi K03142.
    OMAi ECKVCGL.
    PhylomeDBi Q13888.
    TreeFami TF314037.

    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

    EvolutionaryTracei Q13888.
    GeneWikii GTF2H2.
    NextBioi 11756.
    PROi Q13888.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13888.
    CleanExi HS_GTF2H2.
    Genevestigatori Q13888.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR007198. Ssl1-like.
    IPR004595. TFIIH_C1-like_dom.
    IPR012170. TFIIH_SSL1/p44.
    IPR002035. VWF_A.
    IPR007087. Znf_C2H2.
    [Graphical view ]
    PANTHERi PTHR12695. PTHR12695. 1 hit.
    Pfami PF07975. C1_4. 1 hit.
    PF04056. Ssl1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015919. TFIIH_SSL1. 1 hit.
    SMARTi SM01047. C1_4. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    TIGRFAMsi TIGR00622. ssl1. 1 hit.
    PROSITEi PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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], PROTEIN SEQUENCE OF 35-40; 46-54; 60-68; 117-125 AND 214-229.
    2. Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y., Zhou J., Chen Z., Chen J.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pituitary tumor.
    3. "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: Skin.
    4. "A provisional transcript map of the spinal muscular atrophy (SMA) critical region."
      van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M.
      Eur. J. Hum. Genet. 3:87-95(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-130 AND 327-395.
      Tissue: Pre-B cell.
    5. "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular atrophy candidate genes SMN and NAIP."
      Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., MacKenzie A.E.
      Genomics 48:121-127(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-395.
      Tissue: Brain.
    6. "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.
    7. "A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH."
      Tremeau-Bravard A., Perez C., Egly J.-M.
      J. Biol. Chem. 276:27693-27697(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-291; CYS-308; CYS-345; CYS-360; CYS-363; HIS-376; HIS-380 AND CYS-382.
    8. "Varicella-zoster virus IE63 protein represses the basal transcription machinery by disorganizing the pre-initiation complex."
      Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N., Vanderplasschen A., Sadzot-Delvaux C., Piette J.
      Biol. Chem. 386:255-267(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A multicopy transcription-repair gene, BTF2p44, maps to the SMA region and demonstrates SMA associated deletions."
      Carter T.A., Bonnemann C.G., Wang C.H., Obici S., Parano E., Bonaldo M.F., Ross B.M., Penchaszadeh G.K., Mackenzie A.E., Soares M.B., Kunkel L.M., Gilliam T.C.
      Hum. Mol. Genet. 6:229-236(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MET-151 AND LEU-236.

    Entry informationi

    Entry nameiTF2H2_HUMAN
    AccessioniPrimary (citable) accession number: Q13888
    Secondary accession number(s): Q15570, Q15571, Q9BS41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3