Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q62219

- TGFI1_MOUSE

UniProt

Q62219 - TGFI1_MOUSE

Protein

Transforming growth factor beta-1-induced transcript 1 protein

Gene

Tgfb1i1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity.17 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. transcription coactivator activity Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell fate commitment Source: MGI
    2. epithelial cell differentiation Source: MGI
    3. morphogenesis of embryonic epithelium Source: MGI
    4. negative regulation of fat cell differentiation Source: MGI
    5. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    6. positive regulation of epithelial to mesenchymal transition Source: Ensembl
    7. positive regulation of transcription, DNA-templated Source: Ensembl
    8. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    9. response to heat Source: Ensembl
    10. ubiquitin-dependent SMAD protein catabolic process Source: Ensembl
    11. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Differentiation, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transforming growth factor beta-1-induced transcript 1 protein
    Alternative name(s):
    Androgen receptor-associated protein of 55 kDa
    Hydrogen peroxide-inducible clone 5 protein
    Short name:
    Hic-5
    TGF beta-stimulated clone 5
    Short name:
    TSC-5
    Gene namesi
    Name:Tgfb1i1
    Synonyms:Ara55
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:102784. Tgfb1i1.

    Subcellular locationi

    Cell junctionfocal adhesion. Nucleus matrix. Cytoplasmcytoskeleton
    Note: Associated with the actin cytoskeleton, colocalizes with stress fibers.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell
    3. extracellular matrix Source: Ensembl
    4. focal adhesion Source: MGI
    5. nuclear matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-60. 1 Publication
    Mutagenesisi60 – 601Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-38. 1 Publication
    Mutagenesisi64 – 641C → N: Increase in nuclear localization. 1 Publication
    Mutagenesisi91 – 911C → S: Increase in nuclear localization. 1 Publication
    Mutagenesisi161 – 1611L → A: Increase in nuclear localization. 1 Publication
    Mutagenesisi366 – 3661H → G: Loss of interaction with PTPN12; when associated with G-369. 1 Publication
    Mutagenesisi369 – 3691C → A: Loss of localization to focal adhesion; when associated with A-372. 2 Publications
    Mutagenesisi369 – 3691C → G: Loss of interaction with PTPN12; when associated with G-366. 2 Publications
    Mutagenesisi372 – 3721C → A: Loss of localization to focal adhesion; when associated with A-369. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Transforming growth factor beta-1-induced transcript 1 proteinPRO_0000291583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei33 – 331PhosphothreonineBy similarity
    Modified residuei38 – 381Phosphotyrosine2 Publications
    Modified residuei60 – 601Phosphotyrosine2 Publications
    Modified residuei68 – 681PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by gonadotropin-releasing hormone-activated SRC.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ62219.
    PaxDbiQ62219.
    PRIDEiQ62219.

    PTM databases

    PhosphoSiteiQ62219.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Higher expression is detected in lung and spleen. Expression decreases during pregnancy in mammary glands. Expressed in all brain areas, with higher levels in cerebellum, prefrontal cortex and hypothalamus. Expressed in smooth muscle, myoepithelial cells and platelets (at protein level). Preferentially expressed in mesenchymal versus epithelial cells (at protein level).6 Publications

    Developmental stagei

    First detected in the developing heart tube at E8.0 and then in cardiac, skeletal and smooth muscle during early stages of development. Highly expressed in differentiating gut epithelial cells.3 Publications

    Inductioni

    Up-regulated during epithelial to mesenchymal transformation. Up-regulated by TGFB1 and hydrogen peroxide.2 Publications

    Gene expression databases

    ArrayExpressiQ62219.
    BgeeiQ62219.
    GenevestigatoriQ62219.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with CRIP2, HSPB1, ILK, LIMS1, LIMS2, NCK2, NUDT16L1, PAK, PPARG, PTPN12, TCF3, TCF7L2 and VCL. Forms a complex with GIT1 and ARHGEF7. Interacts with AR/androgen receptor in a ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG, PTK2/FAK1, PTK2B/PYK2, SLC6A3, SLC6A4, SMAD3, SRC and talin. Interacts (via LIM zinc-binding domain 2) with CBLC (via RING-type zinc finger); the interaction is direct and enhances CBLC E3 ubiquitin-protein ligase activity.20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Plekhh2Q8C1153EBI-642844,EBI-6512409
    PTK2Q053973EBI-642844,EBI-702142From a different organism.

    Protein-protein interaction databases

    BioGridi204158. 5 interactions.
    IntActiQ62219. 5 interactions.
    MINTiMINT-1666684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62219.
    SMRiQ62219. Positions 228-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini226 – 28560LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 34358LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini344 – 40360LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 46158LIM zinc-binding 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 240240Interaction with PTK2B/PYK2By similarityAdd
    BLAST
    Regioni1 – 200200Transcription activationAdd
    BLAST
    Regioni83 – 13654Interaction with PTK2/FAK1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3 – 1513LD motif 1Add
    BLAST
    Motifi92 – 10413LD motif 2Add
    BLAST
    Motifi157 – 16812LD motif 3Add
    BLAST
    Motifi203 – 21513LD motif 4Add
    BLAST

    Domaini

    The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12.
    The LD (leucine and aspartate-rich) motif 3 mediates interaction with GIT1 and functions as a nuclear export signal.

    Sequence similaritiesi

    Belongs to the paxillin family.Curated
    Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG267887.
    GeneTreeiENSGT00740000114891.
    HOVERGENiHBG001512.
    InParanoidiQ62219.
    OMAiTAGEQKE.
    OrthoDBiEOG70ZZQN.
    PhylomeDBiQ62219.
    TreeFamiTF314113.

    Family and domain databases

    Gene3Di2.10.110.10. 4 hits.
    InterProiIPR017305. Tgfb1i1/Leupaxin.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 4 hits.
    [Graphical view]
    PIRSFiPIRSF037881. Leupaxin. 1 hit.
    SMARTiSM00132. LIM. 4 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q62219-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MEDLDALLSD LETTTSHMSR LGAPKERPPE TLTPPPPYGH QPQTGSGESS    50
    GTTGDKDHLY STVCKPRSPK PVAPVAPPFS SSSGVLGNGL CELDRLLQEL 100
    NATQFNITDE IMSQFPSSKM AEGEEKEDQS EDKSSPTVPP SPFPAPSKPS 150
    ATSATQELDR LMASLSDFRV QNHLPASGPP QPPAASPTRE GCPSPPGQTS 200
    KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV TALGRAWHPE 250
    HFLCSGCSTT LGGSSFFEKD GAPFCPECYF ERFSPRCGFC NQPIRHKMVT 300
    ALGTHWHPEH FCCVSCGEPF GEEGFHEREG RPYCRRDFLQ LFAPRCQGCQ 350
    GPILDNYISA LSALWHPDCF VCRECLAPFS GGSFFEHEGR PLCENHFHAQ 400
    RGSLCATCGL PVTGRCVSAL GRRFHPDHFT CTFCLRPLTK GSFQERASKP 450
    YCQPCFLKLF G 461

    Note: Transcripts of the alpha group are more abundantly expressed.

    Length:461
    Mass (Da):50,101
    Last modified:June 26, 2007 - v2
    Checksum:i6AB15FFF466FEE73
    GO
    Isoform 2 (identifier: Q62219-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.

    Show »
    Length:444
    Mass (Da):48,228
    Checksum:i54E80E09A7CC7C51
    GO
    Isoform 3 (identifier: Q62219-3) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: MEDLDALLSD...PPPPYGHQPQ → MSPCSPFIAP...SASAPPWRTW

    Note: Transcripts of the alpha group are more abundantly expressed.

    Show »
    Length:483
    Mass (Da):51,988
    Checksum:iFE6D462670C2BFFE
    GO
    Isoform 4 (identifier: Q62219-4) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-E

    The sequence of this isoform differs from the canonical sequence as follows:
         62-107: Missing.

    Note: Transcripts of the alpha group are more abundantly expressed.

    Show »
    Length:415
    Mass (Da):45,266
    Checksum:iF6065EA4A754FEF5
    GO
    Isoform 5 (identifier: Q62219-5) [UniParc]FASTAAdd to Basket

    Also known as: Beta-G

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.
         60-82: YSTVCKPRSPKPVAPVAPPFSSS → MATSHRQGLENLQEPLGTRIIYT

    Show »
    Length:402
    Mass (Da):44,059
    Checksum:iAF3A2DD21C47869E
    GO
    Isoform 6 (identifier: Q62219-6) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-C

    The sequence of this isoform differs from the canonical sequence as follows:
         61-61: S → R
         62-461: Missing.

    Note: Transcripts of the alpha group are more abundantly expressed. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:61
    Mass (Da):6,605
    Checksum:iE45E004C4EFCFAC7
    GO
    Isoform 7 (identifier: Q62219-7) [UniParc]FASTAAdd to Basket

    Also known as: Beta-B, Beta-D

    The sequence of this isoform differs from the canonical sequence as follows:
         1-111: Missing.

    Show »
    Length:350
    Mass (Da):38,289
    Checksum:i3AFEE18DB06963F9
    GO
    Isoform 8 (identifier: Q62219-8) [UniParc]FASTAAdd to Basket

    Also known as: Beta-C

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.
         61-61: S → R
         62-461: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:44
    Mass (Da):4,732
    Checksum:iFDEBBC62BE006A91
    GO
    Isoform 9 (identifier: Q62219-9) [UniParc]FASTAAdd to Basket

    Also known as: Beta-E, Beta-F

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: Missing.
         63-138: VCKPRSPKPV...QSEDKSSPTV → MPPSSTLQMK...SEVIHGVLHN

    Show »
    Length:399
    Mass (Da):43,798
    Checksum:iDD062C34B5C62F81
    GO
    Isoform 10 (identifier: Q62219-10) [UniParc]FASTAAdd to Basket

    Also known as: Alpha-D

    The sequence of this isoform differs from the canonical sequence as follows:
         1-110: Missing.
         111-148: IMSQFPSSKM...PPSPFPAPSK → MPPSSTLQMK...NLKTRAHPLS

    Note: Transcripts of the alpha group are more abundantly expressed.

    Show »
    Length:351
    Mass (Da):38,669
    Checksum:i79F2BFB888438DDC
    GO

    Sequence cautioni

    The sequence AAZ82195.1 differs from that shown. Reason: Frameshift at position 28.
    The sequence AAH02049.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE33707.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 111111Missing in isoform 7. 1 PublicationVSP_026184Add
    BLAST
    Alternative sequencei1 – 110110Missing in isoform 10. 1 PublicationVSP_026185Add
    BLAST
    Alternative sequencei1 – 6262Missing in isoform 9. 1 PublicationVSP_026188Add
    BLAST
    Alternative sequencei1 – 5959Missing in isoform 5. 1 PublicationVSP_026189Add
    BLAST
    Alternative sequencei1 – 4343MEDLD…GHQPQ → MSPCSPFIAPPPPTVSQRVP ASIHGHGPASNSLTSPPSPS SAPTGHGPRPTLPKLSASAP PWRTW in isoform 3. 1 PublicationVSP_026190Add
    BLAST
    Alternative sequencei1 – 1717Missing in isoform 2 and isoform 8. 3 PublicationsVSP_026191Add
    BLAST
    Alternative sequencei60 – 8223YSTVC…PFSSS → MATSHRQGLENLQEPLGTRI IYT in isoform 5. 1 PublicationVSP_026192Add
    BLAST
    Alternative sequencei61 – 611S → R in isoform 6 and isoform 8. 2 PublicationsVSP_039813
    Alternative sequencei62 – 461400Missing in isoform 6 and isoform 8. 2 PublicationsVSP_039814Add
    BLAST
    Alternative sequencei62 – 10746Missing in isoform 4. 1 PublicationVSP_026193Add
    BLAST
    Alternative sequencei63 – 13876VCKPR…SSPTV → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLCEF GRVGRAGKRMMGPACLTYQR GVRLAGSEVIHGVLHN in isoform 9. 1 PublicationVSP_026194Add
    BLAST
    Alternative sequencei111 – 14838IMSQF…PAPSK → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLS in isoform 10. 1 PublicationVSP_026197Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22482 mRNA. Translation: AAA62226.1.
    AF083064 Genomic DNA. Translation: AAD51090.1.
    DQ143891 mRNA. Translation: AAZ82195.1. Frameshift.
    DQ143892 mRNA. Translation: AAZ82196.1.
    DQ143893 mRNA. Translation: AAZ82197.1.
    DQ143894 mRNA. Translation: AAZ82198.1.
    DQ143895 mRNA. Translation: AAZ82199.1.
    DQ143896 mRNA. Translation: AAZ82200.1. Sequence problems.
    DQ143897 mRNA. Translation: AAZ82201.1.
    DQ143898 mRNA. Translation: AAZ82202.1.
    DQ143899 mRNA. Translation: AAZ82203.1.
    DQ143900 mRNA. Translation: AAZ82204.1.
    AK156423 mRNA. Translation: BAE33707.1. Different initiation.
    AK158409 mRNA. Translation: BAE34493.1. Sequence problems.
    BC002049 mRNA. Translation: AAH02049.1. Different initiation.
    BC056362 mRNA. Translation: AAH56362.1.
    CCDSiCCDS21893.2. [Q62219-1]
    PIRiA55071.
    RefSeqiNP_001276479.1. NM_001289550.1. [Q62219-1]
    NP_001276481.1. NM_001289552.1.
    NP_001276482.1. NM_001289553.1. [Q62219-7]
    XP_006507630.1. XM_006507567.1. [Q62219-3]
    UniGeneiMm.3248.

    Genome annotation databases

    EnsembliENSMUST00000070656; ENSMUSP00000068529; ENSMUSG00000030782. [Q62219-2]
    ENSMUST00000163609; ENSMUSP00000133134; ENSMUSG00000030782. [Q62219-7]
    ENSMUST00000164710; ENSMUSP00000130964; ENSMUSG00000030782. [Q62219-3]
    ENSMUST00000167965; ENSMUSP00000132100; ENSMUSG00000030782. [Q62219-1]
    ENSMUST00000169919; ENSMUSP00000131705; ENSMUSG00000030782. [Q62219-6]
    GeneIDi21804.
    KEGGimmu:21804.
    UCSCiuc009jyl.1. mouse. [Q62219-1]
    uc009jyo.1. mouse. [Q62219-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22482 mRNA. Translation: AAA62226.1 .
    AF083064 Genomic DNA. Translation: AAD51090.1 .
    DQ143891 mRNA. Translation: AAZ82195.1 . Frameshift.
    DQ143892 mRNA. Translation: AAZ82196.1 .
    DQ143893 mRNA. Translation: AAZ82197.1 .
    DQ143894 mRNA. Translation: AAZ82198.1 .
    DQ143895 mRNA. Translation: AAZ82199.1 .
    DQ143896 mRNA. Translation: AAZ82200.1 . Sequence problems.
    DQ143897 mRNA. Translation: AAZ82201.1 .
    DQ143898 mRNA. Translation: AAZ82202.1 .
    DQ143899 mRNA. Translation: AAZ82203.1 .
    DQ143900 mRNA. Translation: AAZ82204.1 .
    AK156423 mRNA. Translation: BAE33707.1 . Different initiation.
    AK158409 mRNA. Translation: BAE34493.1 . Sequence problems.
    BC002049 mRNA. Translation: AAH02049.1 . Different initiation.
    BC056362 mRNA. Translation: AAH56362.1 .
    CCDSi CCDS21893.2. [Q62219-1 ]
    PIRi A55071.
    RefSeqi NP_001276479.1. NM_001289550.1. [Q62219-1 ]
    NP_001276481.1. NM_001289552.1.
    NP_001276482.1. NM_001289553.1. [Q62219-7 ]
    XP_006507630.1. XM_006507567.1. [Q62219-3 ]
    UniGenei Mm.3248.

    3D structure databases

    ProteinModelPortali Q62219.
    SMRi Q62219. Positions 228-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204158. 5 interactions.
    IntActi Q62219. 5 interactions.
    MINTi MINT-1666684.

    PTM databases

    PhosphoSitei Q62219.

    Proteomic databases

    MaxQBi Q62219.
    PaxDbi Q62219.
    PRIDEi Q62219.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070656 ; ENSMUSP00000068529 ; ENSMUSG00000030782 . [Q62219-2 ]
    ENSMUST00000163609 ; ENSMUSP00000133134 ; ENSMUSG00000030782 . [Q62219-7 ]
    ENSMUST00000164710 ; ENSMUSP00000130964 ; ENSMUSG00000030782 . [Q62219-3 ]
    ENSMUST00000167965 ; ENSMUSP00000132100 ; ENSMUSG00000030782 . [Q62219-1 ]
    ENSMUST00000169919 ; ENSMUSP00000131705 ; ENSMUSG00000030782 . [Q62219-6 ]
    GeneIDi 21804.
    KEGGi mmu:21804.
    UCSCi uc009jyl.1. mouse. [Q62219-1 ]
    uc009jyo.1. mouse. [Q62219-4 ]

    Organism-specific databases

    CTDi 7041.
    MGIi MGI:102784. Tgfb1i1.

    Phylogenomic databases

    eggNOGi NOG267887.
    GeneTreei ENSGT00740000114891.
    HOVERGENi HBG001512.
    InParanoidi Q62219.
    OMAi TAGEQKE.
    OrthoDBi EOG70ZZQN.
    PhylomeDBi Q62219.
    TreeFami TF314113.

    Miscellaneous databases

    NextBioi 301180.
    PROi Q62219.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62219.
    Bgeei Q62219.
    Genevestigatori Q62219.

    Family and domain databases

    Gene3Di 2.10.110.10. 4 hits.
    InterProi IPR017305. Tgfb1i1/Leupaxin.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF037881. Leupaxin. 1 hit.
    SMARTi SM00132. LIM. 4 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
    PS50023. LIM_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence."
      Shibanuma M., Mashimo J.I., Kuroki T., Nose K.
      J. Biol. Chem. 269:26767-26774(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION BY TGFB1 AND HYDROGEN PEROXIDE, TISSUE SPECIFICITY.
      Tissue: Calvaria.
    2. "Genomic structure and chromosomal mapping of the mouse hic-5 gene that encodes a focal adhesion protein."
      Mashimo J.I., Shibanuma M., Satoh H., Chida K., Nose K.
      Gene 249:99-103(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Identification and analysis of Hic-5/ARA55 isoforms: implications for integrin signaling and steroid hormone action."
      Gao Z., Schwartz L.M.
      FEBS Lett. 579:5651-5657(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8; 9 AND 10), TISSUE SPECIFICITY.
      Strain: BALB/c.
    4. "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] (ISOFORMS 1 AND 6).
      Strain: NOD.
      Tissue: Inner ear and Spleen.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6.
      Tissue: Brain and Mammary tumor.
    6. "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions."
      Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T.
      J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2.
    7. "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."
      Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.
      J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1.
    8. "The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro."
      Nishiya N., Sabe H., Nose K., Shibanuma M.
      Nucleic Acids Res. 26:4267-4273(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain."
      Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L., Nose K.
      J. Biol. Chem. 274:9847-9853(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN12, MUTAGENESIS OF HIS-366 AND CYS-369.
    10. "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling."
      Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N., McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.
      J. Cell Biol. 145:851-863(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF7; GIT2; NCK2; PTK2/FAK1 AND PAK.
    11. "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin."
      Thomas S.M., Hagel M., Turner C.E.
      J. Cell Sci. 112:181-190(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSK; PTK2/FAK1 AND VCL, SUBCELLULAR LOCATION.
    12. "Specific decrease in the level of Hic-5, a focal adhesion protein, during immortalization of mouse embryonic fibroblasts, and its association with focal adhesion kinase."
      Ishino K., Kim Kaneyama J.-R., Shibanuma M., Nose K.
      J. Cell. Biochem. 76:411-419(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1.
    13. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
      Nikolopoulos S.N., Turner C.E.
      J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARVA.
    14. "Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix."
      Yang L., Guerrero J., Hong H., DeFranco D.B., Stallcup M.R.
      Mol. Biol. Cell 11:2007-2018(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
    15. "Novel cell lines promote the discovery of genes involved in early heart development."
      Brunskill E.W., Witte D.P., Yutzey K.E., Potter S.S.
      Dev. Biol. 235:507-520(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    16. "Identification and characterization of hic-5/ARA55 as an hsp27 binding protein."
      Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.
      J. Biol. Chem. 276:39911-39918(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPB1.
    17. "Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase."
      Nishiya N., Tachibana K., Shibanuma M., Mashimo J.I., Nose K.
      Mol. Cell. Biol. 21:5332-5345(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Possible involvement of hic-5, a focal adhesion protein, in the differentiation of C2C12 myoblasts."
      Shibanuma M., Iwabuchi Y., Nose K.
      Cell Struct. Funct. 27:21-27(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    19. "Hic-5 interacts with GIT1 with a different binding mode from paxillin."
      Nishiya N., Shirai T., Suzuki W., Nose K.
      J. Biochem. 132:279-289(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GIT1 AND ARHGEF7.
    20. "The FXXLF motif mediates androgen receptor-specific interactions with coregulators."
      He B., Minges J.T., Lee L.W., Wilson E.M.
      J. Biol. Chem. 277:10226-10235(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR.
    21. "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5."
      Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S., French B., Neveu W., Goetinck P.F.
      J. Biol. Chem. 277:12270-12274(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUDT16L1.
    22. "The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter."
      Carneiro A.M.D., Ingram S.L., Beaulieu J.-M., Sweeney A., Amara S.G., Thomas S.M., Caron M.G., Torres G.E.
      J. Neurosci. 22:7045-7054(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC6A3, TISSUE SPECIFICITY.
    23. "Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal."
      Shibanuma M., Kim-Kaneyama J.-R., Ishino K., Sakamoto N., Hishiki T., Yamaguchi K., Mori K., Mashimo J.I., Nose K.
      Mol. Biol. Cell 14:1158-1171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-64; CYS-91 AND LEU-161.
    24. "A LIM protein, Hic-5, functions as a potential coactivator for Sp1."
      Shibanuma M., Kim-Kaneyama J.-R., Sato S., Nose K.
      J. Cell. Biochem. 91:633-645(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD3.
    25. "Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation."
      Hetey S.E., Lalonde D.P., Turner C.E.
      Exp. Cell Res. 311:147-156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-38; TYR-60; CYS-369 AND CYS-372, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-38 AND TYR-60.
    26. Cited for: FUNCTION, INTERACTION WITH PPARG, DEVELOPMENTAL STAGE.
    27. "Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo."
      Kim-Kaneyama J.-R., Suzuki W., Ichikawa K., Ohki T., Kohno Y., Sata M., Nose K., Shibanuma M.
      J. Cell Sci. 118:937-949(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CRIP2.
    28. "Regulation of paxillin family members during epithelial-mesenchymal transformation: a putative role for paxillin delta."
      Tumbarello D.A., Brown M.C., Hetey S.E., Turner C.E.
      J. Cell Sci. 118:4849-4863(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, TISSUE SPECIFICITY.
    29. "HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription."
      Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.
      J. Biol. Chem. 281:1755-1764(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TCF3 AND TCF7L2.
    30. "ERK8 down-regulates transactivation of the glucocorticoid receptor through Hic-5."
      Saelzler M.P., Spackman C.C., Liu Y., Martinez L.C., Harris J.P., Abe M.K.
      J. Biol. Chem. 281:16821-16832(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPK15.
    31. "Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex."
      Mori K., Asakawa M., Hayashi M., Imura M., Ohki T., Hirao E., Kim-Kaneyama J.-R., Nose K., Shibanuma M.
      J. Biol. Chem. 281:22048-22061(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ILK; LIMS1 AND LIMS2.
    32. "Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets."
      Rathore V.B., Okada M., Newman P.J., Newman D.K.
      Biochem. J. 403:275-281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH CSK.
    33. "Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway."
      Tumbarello D.A., Turner C.E.
      J. Cell. Physiol. 211:736-747(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    34. "Hic-5/ARA55 a prostate stroma-specific AR coactivator."
      Heitzer M.D., DeFranco D.B.
      Steroids 72:218-220(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTGFI1_MOUSE
    AccessioniPrimary (citable) accession number: Q62219
    Secondary accession number(s): Q3YBY7
    , Q3YBY8, Q3YBZ0, Q3YBZ1, Q3YBZ3, Q3YBZ4, Q3YBZ5, Q3YBZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 116 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