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P78347

- GTF2I_HUMAN

UniProt

P78347 - GTF2I_HUMAN

Protein

General transcription factor II-I

Gene

GTF2I

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (13 Dec 2001)
      Previous versions | rss
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    Functioni

    Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. embryo development Source: Ensembl
    2. negative regulation of angiogenesis Source: MGI
    3. negative regulation of cytosolic calcium ion concentration Source: Ensembl
    4. signal transduction Source: ProtInc
    5. transcription from RNA polymerase II promoter Source: ProtInc
    6. transcription initiation from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General transcription factor II-I
    Short name:
    GTFII-I
    Short name:
    TFII-I
    Alternative name(s):
    Bruton tyrosine kinase-associated protein 135
    Short name:
    BAP-135
    Short name:
    BTK-associated protein 135
    SRF-Phox1-interacting protein
    Short name:
    SPIN
    Williams-Beuren syndrome chromosomal region 6 protein
    Gene namesi
    Name:GTF2I
    Synonyms:BAP135, WBSCR6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4659. GTF2I.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
    Note: Colocalizes with BTK in the cytoplasm.

    GO - Cellular componenti

    1. cell projection Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB
    4. neuronal cell body Source: Ensembl
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    GTF2I is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of GTF2I may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi248 – 2481Y → F: Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-398 and F-503. 1 Publication
    Mutagenesisi398 – 3981Y → F: Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-503. 1 Publication
    Mutagenesisi460 – 4601Y → F: No change on BTK-mediated transcriptional activation. 1 Publication
    Mutagenesisi503 – 5031Y → F: Impairs BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-398. 1 Publication

    Keywords - Diseasei

    Williams-Beuren syndrome

    Organism-specific databases

    Orphaneti904. Williams syndrome.
    PharmGKBiPA29045.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 998997General transcription factor II-IPRO_0000083872Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei103 – 1031Phosphoserine4 Publications
    Modified residuei130 – 1301N6-acetyllysineBy similarity
    Modified residuei207 – 2071Phosphoserine2 Publications
    Modified residuei210 – 2101Phosphoserine3 Publications
    Modified residuei248 – 2481Phosphotyrosine; by BTK3 Publications
    Modified residuei318 – 3181Phosphotyrosine; by BTK1 Publication
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei398 – 3981Phosphotyrosine; by BTK2 Publications
    Modified residuei412 – 4121Phosphoserine; by PKG/PRKG12 Publications
    Modified residuei450 – 4501N6-acetyllysineBy similarity
    Modified residuei503 – 5031Phosphotyrosine; by BTK2 Publications
    Modified residuei558 – 5581Phosphothreonine4 Publications
    Modified residuei668 – 6681Phosphoserine2 Publications
    Modified residuei715 – 7151N6-acetyllysineBy similarity
    Modified residuei784 – 7841Phosphoserine; by PKG/PRKG12 Publications
    Modified residuei823 – 8231Phosphoserine2 Publications

    Post-translational modificationi

    Transiently phosphorylated on tyrosine residues by BTK in response to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-398, and perhaps, on Tyr-503 contributes to BTK-mediated transcriptional activation.9 Publications
    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP78347.
    PaxDbiP78347.
    PRIDEiP78347.

    PTM databases

    PhosphoSiteiP78347.

    Expressioni

    Tissue specificityi

    Ubiquitous. Isoform 1 is strongly expressed in fetal brain, weakly in adult brain, muscle, and lymphoblasts and is almost undetectable in other adult tissues, while the other isoforms are equally expressed in all adult tissues.

    Gene expression databases

    ArrayExpressiP78347.
    BgeeiP78347.
    CleanExiHS_GTF2I.
    GenevestigatoriP78347.

    Organism-specific databases

    HPAiCAB004595.
    HPA026638.

    Interactioni

    Subunit structurei

    Homodimer Potential. Interacts with SRF and PHOX1. Binds a pyrimidine-rich initiator (Inr) and a recognition site (E-box) for upstream stimulatory factor 1 (USF1). Associates with the PH domain of Bruton's tyrosine kinase (BTK). May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with BTK and ARID3A. Interacts with isoform beta of PRKG1.4 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383985EBI-359622,EBI-349905
    BTKQ061876EBI-359622,EBI-624835

    Protein-protein interaction databases

    BioGridi109224. 78 interactions.
    DIPiDIP-24252N.
    IntActiP78347. 26 interactions.
    MINTiMINT-1138992.

    Structurei

    Secondary structure

    1
    998
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi106 – 12823
    Helixi138 – 1436
    Beta strandi146 – 1527
    Helixi167 – 1759
    Turni176 – 1794
    Beta strandi181 – 1855
    Helixi361 – 37616
    Helixi387 – 3926
    Turni393 – 3964
    Beta strandi397 – 4015
    Turni411 – 4133
    Helixi416 – 4249
    Turni426 – 4283
    Beta strandi430 – 4345
    Turni437 – 4393
    Helixi466 – 48217
    Helixi492 – 4976
    Turni499 – 5013
    Beta strandi502 – 5065
    Turni516 – 5183
    Helixi521 – 5299
    Turni530 – 5334
    Beta strandi535 – 5395
    Helixi541 – 5444
    Turni856 – 8583
    Helixi861 – 88323
    Helixi894 – 8996
    Beta strandi901 – 9077
    Turni918 – 9203
    Helixi923 – 9319
    Turni932 – 9354
    Beta strandi937 – 9426

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9BNMR-A102-197[»]
    2DN4NMR-A361-446[»]
    2ED2NMR-A466-551[»]
    2EJENMR-A854-954[»]
    ProteinModelPortaliP78347.
    SMRiP78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78347.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati103 – 19795GTF2I-like 1Add
    BLAST
    Repeati352 – 44695GTF2I-like 2Add
    BLAST
    Repeati457 – 55195GTF2I-like 3Add
    BLAST
    Repeati562 – 65695GTF2I-like 4Add
    BLAST
    Repeati724 – 81895GTF2I-like 5Add
    BLAST
    Repeati859 – 95395GTF2I-like 6Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi320 – 3278Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi692 – 6954Poly-Asn

    Sequence similaritiesi

    Belongs to the TFII-I family.PROSITE-ProRule annotation
    Contains 6 GTF2I-like repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG29608.
    HOVERGENiHBG051856.
    InParanoidiP78347.
    KOiK03121.
    OMAiMPPGVAF.
    OrthoDBiEOG7RRF67.
    PhylomeDBiP78347.
    TreeFamiTF352524.

    Family and domain databases

    Gene3Di3.90.1460.10. 6 hits.
    InterProiIPR004212. GTF2I.
    IPR016659. TF_II-I.
    [Graphical view]
    PfamiPF02946. GTF2I. 6 hits.
    [Graphical view]
    PIRSFiPIRSF016441. TF_II-I. 1 hit.
    SUPFAMiSSF117773. SSF117773. 6 hits.
    PROSITEiPS51139. GTF2I. 6 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78347-1) [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

    MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY    50
    ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 100
    RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 150
    QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 200
    VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 250
    YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP 300
    SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN 350
    FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE 400
    GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK 450
    PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN 500
    DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE 550
    VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF 600
    ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI 650
    SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA 700
    VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG 750
    LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK 800
    IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT 850
    IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN 900
    PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN 950
    NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW 998
    Length:998
    Mass (Da):112,416
    Last modified:December 13, 2001 - v2
    Checksum:i4CFA2C19002869B9
    GO
    Isoform 2 (identifier: P78347-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         255-274: Missing.
         294-314: Missing.

    Show »
    Length:957
    Mass (Da):107,970
    Checksum:iE091B620FF633AC8
    GO
    Isoform 3 (identifier: P78347-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         255-274: Missing.

    Show »
    Length:978
    Mass (Da):110,280
    Checksum:i1F006D480F0BE702
    GO
    Isoform 4 (identifier: P78347-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         294-314: Missing.

    Show »
    Length:977
    Mass (Da):110,106
    Checksum:i418D59EC623E6141
    GO
    Isoform 5 (identifier: P78347-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         255-274: Missing.
         294-294: D → G
         295-998: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:274
    Mass (Da):30,409
    Checksum:iC693096D47E9CDC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti174 – 1741L → G in AAB48826. (PubMed:9012831)Curated
    Sequence conflicti178 – 1781A → G in AAB48826. (PubMed:9012831)Curated
    Sequence conflicti481 – 4811A → R in AAB70791. (PubMed:9384587)Curated
    Sequence conflicti634 – 6341R → H in AAB48826. (PubMed:9012831)Curated
    Sequence conflicti960 – 9601E → K in AAB48826. (PubMed:9012831)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti174 – 1741L → V.
    Corresponds to variant rs1057896 [ dbSNP | Ensembl ].
    VAR_051026

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei255 – 27420Missing in isoform 2, isoform 3 and isoform 5. 6 PublicationsVSP_003867Add
    BLAST
    Alternative sequencei294 – 31421Missing in isoform 2 and isoform 4. 5 PublicationsVSP_003868Add
    BLAST
    Alternative sequencei294 – 2941D → G in isoform 5. 2 PublicationsVSP_055195
    Alternative sequencei295 – 998704Missing in isoform 5. 2 PublicationsVSP_055196Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015553 mRNA. Translation: AAB70791.1.
    Y14946 mRNA. Translation: CAA75163.1.
    U77948 mRNA. Translation: AAB48826.1.
    AF035737 mRNA. Translation: AAC08312.1.
    AF038967 mRNA. Translation: AAC08313.1.
    AF038968 mRNA. Translation: AAC08314.1.
    AF038969 mRNA. Translation: AAC08315.1.
    BT007450 mRNA. Translation: AAP36118.1.
    AC005231 Genomic DNA. No translation available.
    AC083884 Genomic DNA. Translation: AAS07460.1.
    AC083884 Genomic DNA. Translation: AAS07461.1.
    AC083884 Genomic DNA. Translation: AAS07462.1.
    AC083884 Genomic DNA. Translation: AAS07463.1.
    AC083884 Genomic DNA. Translation: AAS07464.1.
    AC004883 Genomic DNA. Translation: AAL93085.1.
    CH471200 Genomic DNA. Translation: EAW69598.1.
    BC004472 mRNA. Translation: AAH04472.1.
    BC070484 mRNA. Translation: AAH70484.1.
    CCDSiCCDS47614.1. [P78347-2]
    CCDS5573.1. [P78347-1]
    CCDS5574.1. [P78347-3]
    CCDS5575.1. [P78347-4]
    CCDS64680.1. [P78347-5]
    PIRiT03829.
    T09492.
    RefSeqiNP_001157108.1. NM_001163636.2.
    NP_001267729.1. NM_001280800.1.
    NP_001509.3. NM_001518.4. [P78347-2]
    NP_127492.1. NM_032999.3. [P78347-1]
    NP_127493.1. NM_033000.3. [P78347-3]
    NP_127494.1. NM_033001.3. [P78347-4]
    XP_006716005.1. XM_006715942.1. [P78347-1]
    UniGeneiHs.647041.
    Hs.654705.
    Hs.743231.

    Genome annotation databases

    EnsembliENST00000443166; ENSP00000404240; ENSG00000263001. [P78347-5]
    ENST00000573035; ENSP00000460070; ENSG00000263001. [P78347-1]
    GeneIDi2969.
    KEGGihsa:2969.
    UCSCiuc003txo.4. human. [P78347-1]
    uc003uav.3. human. [P78347-4]
    uc003uaw.3. human. [P78347-3]
    uc003uax.3. human. [P78347-2]

    Polymorphism databases

    DMDMi17865459.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF015553 mRNA. Translation: AAB70791.1 .
    Y14946 mRNA. Translation: CAA75163.1 .
    U77948 mRNA. Translation: AAB48826.1 .
    AF035737 mRNA. Translation: AAC08312.1 .
    AF038967 mRNA. Translation: AAC08313.1 .
    AF038968 mRNA. Translation: AAC08314.1 .
    AF038969 mRNA. Translation: AAC08315.1 .
    BT007450 mRNA. Translation: AAP36118.1 .
    AC005231 Genomic DNA. No translation available.
    AC083884 Genomic DNA. Translation: AAS07460.1 .
    AC083884 Genomic DNA. Translation: AAS07461.1 .
    AC083884 Genomic DNA. Translation: AAS07462.1 .
    AC083884 Genomic DNA. Translation: AAS07463.1 .
    AC083884 Genomic DNA. Translation: AAS07464.1 .
    AC004883 Genomic DNA. Translation: AAL93085.1 .
    CH471200 Genomic DNA. Translation: EAW69598.1 .
    BC004472 mRNA. Translation: AAH04472.1 .
    BC070484 mRNA. Translation: AAH70484.1 .
    CCDSi CCDS47614.1. [P78347-2 ]
    CCDS5573.1. [P78347-1 ]
    CCDS5574.1. [P78347-3 ]
    CCDS5575.1. [P78347-4 ]
    CCDS64680.1. [P78347-5 ]
    PIRi T03829.
    T09492.
    RefSeqi NP_001157108.1. NM_001163636.2.
    NP_001267729.1. NM_001280800.1.
    NP_001509.3. NM_001518.4. [P78347-2 ]
    NP_127492.1. NM_032999.3. [P78347-1 ]
    NP_127493.1. NM_033000.3. [P78347-3 ]
    NP_127494.1. NM_033001.3. [P78347-4 ]
    XP_006716005.1. XM_006715942.1. [P78347-1 ]
    UniGenei Hs.647041.
    Hs.654705.
    Hs.743231.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9B NMR - A 102-197 [» ]
    2DN4 NMR - A 361-446 [» ]
    2ED2 NMR - A 466-551 [» ]
    2EJE NMR - A 854-954 [» ]
    ProteinModelPortali P78347.
    SMRi P78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109224. 78 interactions.
    DIPi DIP-24252N.
    IntActi P78347. 26 interactions.
    MINTi MINT-1138992.

    PTM databases

    PhosphoSitei P78347.

    Polymorphism databases

    DMDMi 17865459.

    Proteomic databases

    MaxQBi P78347.
    PaxDbi P78347.
    PRIDEi P78347.

    Protocols and materials databases

    DNASUi 2969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000443166 ; ENSP00000404240 ; ENSG00000263001 . [P78347-5 ]
    ENST00000573035 ; ENSP00000460070 ; ENSG00000263001 . [P78347-1 ]
    GeneIDi 2969.
    KEGGi hsa:2969.
    UCSCi uc003txo.4. human. [P78347-1 ]
    uc003uav.3. human. [P78347-4 ]
    uc003uaw.3. human. [P78347-3 ]
    uc003uax.3. human. [P78347-2 ]

    Organism-specific databases

    CTDi 2969.
    GeneCardsi GC07P074071.
    H-InvDB HIX0023260.
    HGNCi HGNC:4659. GTF2I.
    HPAi CAB004595.
    HPA026638.
    MIMi 601679. gene.
    neXtProti NX_P78347.
    Orphaneti 904. Williams syndrome.
    PharmGKBi PA29045.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29608.
    HOVERGENi HBG051856.
    InParanoidi P78347.
    KOi K03121.
    OMAi MPPGVAF.
    OrthoDBi EOG7RRF67.
    PhylomeDBi P78347.
    TreeFami TF352524.

    Miscellaneous databases

    ChiTaRSi GTF2I. human.
    EvolutionaryTracei P78347.
    GeneWikii GTF2I.
    GenomeRNAii 2969.
    NextBioi 11768.
    PROi P78347.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78347.
    Bgeei P78347.
    CleanExi HS_GTF2I.
    Genevestigatori P78347.

    Family and domain databases

    Gene3Di 3.90.1460.10. 6 hits.
    InterProi IPR004212. GTF2I.
    IPR016659. TF_II-I.
    [Graphical view ]
    Pfami PF02946. GTF2I. 6 hits.
    [Graphical view ]
    PIRSFi PIRSF016441. TF_II-I. 1 hit.
    SUPFAMi SSF117773. SSF117773. 6 hits.
    PROSITEi PS51139. GTF2I. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1."
      Roy A.L., Du H., Gregor P.D., Novina C.D., Martinez E., Roeder R.G.
      EMBO J. 16:7091-7104(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 162-171; 366-372; 646-658 AND 940-956.
    2. "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I."
      Grueneberg D.A., Henry R.W., Brauer A., Novina C.D., Cheriyath V., Roy A.L., Gilman M.
      Genes Dev. 11:2482-2493(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 291-294 AND 316-333.
      Tissue: Cervix carcinoma.
    3. "BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement."
      Yang W., Desiderio S.
      Proc. Natl. Acad. Sci. U.S.A. 94:604-609(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 144-154; 495-514 AND 681-702.
    4. "A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK."
      Perez Jurado L.A., Wang Y.-K., Peoples R., Coloma A., Cruces J., Francke U.
      Hum. Mol. Genet. 7:325-334(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Lymph and Ovary.
    9. Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-20; 131-140; 178-185; 364-371; 444-456; 495-514; 540-555; 574-594; 620-628; 870-878; 917-927 AND 929-937, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon adenocarcinoma.
    10. "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase."
      Novina C.D., Kumar S., Bajpai U., Cheriyath V., Zhang K., Pillai S., Wortis H.H., Roy A.L.
      Mol. Cell. Biol. 19:5014-5024(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BTK, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    11. "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I."
      Egloff A.M., Desiderio S.
      J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
    12. "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I."
      Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B.
      J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-412 AND SER-784 BY PRKG1, INTERACTION WITH PRKG1.
    13. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I."
      Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.
      Mol. Cell. Biol. 26:4758-4768(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARID3A AND BTK, PHOSPHORYLATION AT TYR-248, FUNCTION.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-207; SER-210 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; THR-558 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Solution structure of RSGI RUH-052, a GTF2I domain in human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 102-197 AND 361-554.

    Entry informationi

    Entry nameiGTF2I_HUMAN
    AccessioniPrimary (citable) accession number: P78347
    Secondary accession number(s): O14743
    , O15359, O43546, O43588, O43589, Q75M85, Q75M86, Q75M87, Q75M88, Q86U51, Q9BSZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: December 13, 2001
    Last modified: October 1, 2014
    This is version 150 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

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

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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