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O43294

- TGFI1_HUMAN

UniProt

O43294 - TGFI1_HUMAN

Protein

Transforming growth factor beta-1-induced transcript 1 protein

Gene

TGFB1I1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    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.15 Publications

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. I-SMAD binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. Roundabout binding Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. cell adhesion Source: ProtInc
    3. cell fate commitment Source: Ensembl
    4. epithelial cell differentiation Source: Ensembl
    5. morphogenesis of embryonic epithelium Source: Ensembl
    6. negative regulation of cell proliferation Source: ProtInc
    7. negative regulation of fat cell differentiation Source: Ensembl
    8. negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    9. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
    12. response to heat Source: Ensembl
    13. transcription from RNA polymerase II promoter Source: ProtInc
    14. ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCL
    15. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Differentiation, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO43294.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transforming growth factor beta-1-induced transcript 1 protein
    Alternative name(s):
    Androgen receptor coactivator 55 kDa protein
    Androgen receptor-associated protein of 55 kDa
    Hydrogen peroxide-inducible clone 5 protein
    Short name:
    Hic-5
    Gene namesi
    Name:TGFB1I1
    Synonyms:ARA55
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11767. 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. focal adhesion Source: UniProtKB-SubCell
    4. intracellular Source: UniProtKB
    5. nuclear matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601Y → F: Prevents phosphorylation by FAK2 and FYN. Prevents interaction with CSK. 2 Publications
    Mutagenesisi287 – 2871C → A: Abolishes interaction with CBLC and enhancement of CBLC E3 ubiquitin-protein ligase activity. 2 Publications
    Mutagenesisi313 – 3131C → A: No effect on interaction with CBLC. 2 Publications
    Mutagenesisi338 – 3425FLQLF → ALQAA: Loss of interaction with AR; when associated with 456-A--A-460. 1 Publication
    Mutagenesisi369 – 3691C → S: Loss of AR coactivation; when associated with S-372. 2 Publications
    Mutagenesisi372 – 3721C → S: Loss of AR coactivation; when associated with S-369. 2 Publications
    Mutagenesisi428 – 4281H → S: Loss of AR coactivation; when associated with S-431. 2 Publications
    Mutagenesisi431 – 4311C → S: Loss of AR coactivation; when associated with S-428. 2 Publications
    Mutagenesisi456 – 4605FLKLF → ALKAA: Loss of interaction with AR; when associated with 338-A--A-342. 1 Publication

    Organism-specific databases

    PharmGKBiPA36481.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Transforming growth factor beta-1-induced transcript 1 proteinPRO_0000291582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei33 – 331Phosphothreonine1 Publication
    Modified residuei38 – 381PhosphotyrosineBy similarity
    Modified residuei60 – 601Phosphotyrosine; by FAK2 and FYN2 Publications
    Modified residuei68 – 681Phosphoserine1 Publication
    Modified residuei137 – 1371Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by gonadotropin-releasing hormone-activated SRC.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43294.
    PaxDbiO43294.
    PRIDEiO43294.

    PTM databases

    PhosphoSiteiO43294.

    Expressioni

    Tissue specificityi

    Expressed in platelets, smooth muscle and prostate stromal cells (at protein level).9 Publications

    Inductioni

    Up-regulated by TNF and hydrogen peroxide.2 Publications

    Gene expression databases

    ArrayExpressiO43294.
    BgeeiO43294.
    CleanExiHS_TGFB1I1.
    GenevestigatoriO43294.

    Organism-specific databases

    HPAiCAB020844.
    HPA006376.

    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
    ITGA4P136122EBI-1051449,EBI-703044
    PTK2Q053972EBI-1051449,EBI-702142

    Protein-protein interaction databases

    BioGridi112899. 30 interactions.
    DIPiDIP-5931N.
    IntActiO43294. 12 interactions.
    MINTiMINT-243624.
    STRINGi9606.ENSP00000378332.

    Structurei

    3D structure databases

    ProteinModelPortaliO43294.
    SMRiO43294. 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/PYK2Add
    BLAST
    Regioni1 – 200200Transcription activationBy similarityAdd
    BLAST
    Regioni83 – 13654Interaction with PTK2/FAK1By similarityAdd
    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.
    HOGENOMiHOG000018764.
    HOVERGENiHBG001512.
    InParanoidiO43294.
    OMAiTAGEQKE.
    PhylomeDBiO43294.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43294-1) [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

    MEDLDALLSD LETTTSHMPR SGAPKERPAE PLTPPPSYGH QPQTGSGESS    50
    GASGDKDHLY STVCKPRSPK PAAPAAPPFS SSSGVLGTGL CELDRLLQEL 100
    NATQFNITDE IMSQFPSSKV ASGEQKEDQS EDKKRPSLPS SPSPGLPKAS 150
    ATSATLELDR LMASLSDFRV QNHLPASGPT QPPVVSSTNE GSPSPPEPTG 200
    KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV TALGRAWHPE 250
    HFVCGGCSTA LGGSSFFEKD GAPFCPECYF ERFSPRCGFC NQPIRHKMVT 300
    ALGTHWHPEH FCCVSCGEPF GDEGFHEREG RPYCRRDFLQ LFAPRCQGCQ 350
    GPILDNYISA LSALWHPDCF VCRECFAPFS GGSFFEHEGR PLCENHFHAR 400
    RGSLCATCGL PVTGRCVSAL GRRFHPDHFT CTFCLRPLTK GSFQERAGKP 450
    YCQPCFLKLF G 461
    Length:461
    Mass (Da):49,814
    Last modified:June 26, 2007 - v2
    Checksum:iD2C7C32C3FD2C496
    GO
    Isoform 2 (identifier: O43294-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:444
    Mass (Da):47,941
    Checksum:iEC9E92DADE7156B4
    GO

    Sequence cautioni

    The sequence AAH32545.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661S → P in AAD22552. (PubMed:10075738)Curated
    Sequence conflicti200 – 2001G → A in AAD22552. (PubMed:10075738)Curated
    Sequence conflicti363 – 3631A → L in AAD22552. (PubMed:10075738)Curated
    Sequence conflicti405 – 4062CA → WP in AAD22552. (PubMed:10075738)Curated
    Sequence conflicti430 – 4301T → A in AAD22552. (PubMed:10075738)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291Q → H.1 Publication
    Corresponds to variant rs45475699 [ dbSNP | Ensembl ].
    VAR_032831

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717Missing in isoform 2. 3 PublicationsVSP_026183Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116343 mRNA. Translation: AAD22552.1.
    DQ309025 Genomic DNA. Translation: ABB96286.1.
    AK313327 mRNA. Translation: BAG36132.1.
    CH471192 Genomic DNA. Translation: EAW52126.1.
    BC001507 mRNA. Translation: AAH01507.2.
    BC001830 mRNA. Translation: AAH01830.1.
    BC017288 mRNA. Translation: AAH17288.1.
    BC032545 mRNA. Translation: AAH32545.1. Different initiation.
    AB007836 mRNA. Translation: BAA24799.1.
    CCDSiCCDS10713.1. [O43294-2]
    CCDS42156.1. [O43294-1]
    RefSeqiNP_001035919.1. NM_001042454.2. [O43294-1]
    NP_001158191.1. NM_001164719.1. [O43294-2]
    NP_057011.2. NM_015927.4. [O43294-2]
    UniGeneiHs.513530.

    Genome annotation databases

    EnsembliENST00000361773; ENSP00000355117; ENSG00000140682. [O43294-2]
    ENST00000394858; ENSP00000378327; ENSG00000140682. [O43294-2]
    ENST00000394863; ENSP00000378332; ENSG00000140682. [O43294-1]
    ENST00000567607; ENSP00000457586; ENSG00000140682. [O43294-2]
    GeneIDi7041.
    KEGGihsa:7041.
    UCSCiuc002ecd.2. human. [O43294-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116343 mRNA. Translation: AAD22552.1 .
    DQ309025 Genomic DNA. Translation: ABB96286.1 .
    AK313327 mRNA. Translation: BAG36132.1 .
    CH471192 Genomic DNA. Translation: EAW52126.1 .
    BC001507 mRNA. Translation: AAH01507.2 .
    BC001830 mRNA. Translation: AAH01830.1 .
    BC017288 mRNA. Translation: AAH17288.1 .
    BC032545 mRNA. Translation: AAH32545.1 . Different initiation.
    AB007836 mRNA. Translation: BAA24799.1 .
    CCDSi CCDS10713.1. [O43294-2 ]
    CCDS42156.1. [O43294-1 ]
    RefSeqi NP_001035919.1. NM_001042454.2. [O43294-1 ]
    NP_001158191.1. NM_001164719.1. [O43294-2 ]
    NP_057011.2. NM_015927.4. [O43294-2 ]
    UniGenei Hs.513530.

    3D structure databases

    ProteinModelPortali O43294.
    SMRi O43294. Positions 228-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112899. 30 interactions.
    DIPi DIP-5931N.
    IntActi O43294. 12 interactions.
    MINTi MINT-243624.
    STRINGi 9606.ENSP00000378332.

    PTM databases

    PhosphoSitei O43294.

    Proteomic databases

    MaxQBi O43294.
    PaxDbi O43294.
    PRIDEi O43294.

    Protocols and materials databases

    DNASUi 7041.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361773 ; ENSP00000355117 ; ENSG00000140682 . [O43294-2 ]
    ENST00000394858 ; ENSP00000378327 ; ENSG00000140682 . [O43294-2 ]
    ENST00000394863 ; ENSP00000378332 ; ENSG00000140682 . [O43294-1 ]
    ENST00000567607 ; ENSP00000457586 ; ENSG00000140682 . [O43294-2 ]
    GeneIDi 7041.
    KEGGi hsa:7041.
    UCSCi uc002ecd.2. human. [O43294-1 ]

    Organism-specific databases

    CTDi 7041.
    GeneCardsi GC16P031483.
    HGNCi HGNC:11767. TGFB1I1.
    HPAi CAB020844.
    HPA006376.
    MIMi 602353. gene.
    neXtProti NX_O43294.
    PharmGKBi PA36481.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267887.
    HOGENOMi HOG000018764.
    HOVERGENi HBG001512.
    InParanoidi O43294.
    OMAi TAGEQKE.
    PhylomeDBi O43294.
    TreeFami TF314113.

    Enzyme and pathway databases

    SignaLinki O43294.

    Miscellaneous databases

    GeneWikii TGFB1I1.
    GenomeRNAii 7041.
    NextBioi 27511.
    PROi O43294.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43294.
    Bgeei O43294.
    CleanExi HS_TGFB1I1.
    Genevestigatori O43294.

    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. "Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate."
      Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A., Chang C.
      J. Biol. Chem. 274:8316-8321(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH AR, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-129.
    3. "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] (ISOFORM 2).
      Tissue: Testis.
    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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-461 (ISOFORM 1).
      Tissue: Muscle, Ovary and Uterus.
    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: NUCLEOTIDE SEQUENCE [MRNA] OF 2-461 (ISOFORM 1), INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2.
      Tissue: Hippocampus.
    7. "Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts."
      Shibanuma M., Mochizuki E., Maniwa R., Mashimo J.I., Nishiya N., Imai S., Takano T., Oshimura M., Nose K.
      Mol. Cell. Biol. 17:1224-1235(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "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.
    9. "Recruitment of the LIM protein hic-5 to focal contacts of human platelets."
      Hagmann J., Grob M., Welman A., van Willigen G., Burger M.M.
      J. Cell Sci. 111:2181-2188(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1 AND TALIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    10. "Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."
      Ishino M., Aoto H., Sasaski H., Suzuki R., Sasaki T.
      FEBS Lett. 474:179-183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-60, PHOSPHORYLATION AT TYR-60, INTERACTION WITH CSK AND PTK2B/PYK2.
    11. "Molecular cloning of human Hic-5, a potential regulator involved in signal transduction and cellular senescence."
      Zhang J., Zhang L.-X., Meltzer P.S., Barrett J.C., Trent J.M.
      Mol. Carcinog. 27:177-183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Involvement of Hic-5 in platelet activation: integrin alphaIIbbeta3-dependent tyrosine phosphorylation and association with proline-rich tyrosine kinase 2."
      Osada M., Ohmori T., Yatomi Y., Satoh K., Hosogaya S., Ozaki Y.
      Biochem. J. 355:691-697(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH PTK2B/PYK2, SUBCELLULAR LOCATION.
    13. "CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk."
      Oda A., Ochs H.D., Lasky L.A., Spencer S., Ozaki K., Fujihara M., Handa M., Ikebuchi K., Ikeda H.
      Blood 97:2633-2639(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. Cited for: INDUCTION BY HYDROGEN PEROXIDE.
    15. "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.
    16. "Different expression of androgen receptor coactivators in human prostate."
      Fujimoto N., Mizokami A., Harada S., Matsumoto T.
      Urology 58:289-294(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY TNF.
    17. "Transcriptional activation of the c-fos gene by a LIM protein, Hic-5."
      Kim-Kaneyama J.-R., Shibanuma M., Nose K.
      Biochem. Biophys. Res. Commun. 299:360-365(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "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: INTERACTION WITH GIT1.
    19. "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator."
      Wang X., Yang Y., Guo X., Sampson E.R., Hsu C.-L., Tsai M.-Y., Yeh S., Wu G., Guo Y., Chang C.
      J. Biol. Chem. 277:15426-15431(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTK2B/PYK2, PHOSPHORYLATION AT TYR-60 BY FAK2.
    20. "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: FUNCTION, INTERACTION WITH SLC6A3, SUBCELLULAR LOCATION.
    21. "The use of phage display technique for the isolation of androgen receptor interacting peptides with (F/W)XXL(F/W) and FXXLY new signature motifs."
      Hsu C.-L., Chen Y.-L., Yeh S., Ting H.-J., Hu Y.-C., Lin H., Wang X., Chang C.
      J. Biol. Chem. 278:23691-23698(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR, MUTAGENESIS OF 338-PHE--PHE-342 AND 456-PHE--PHE-460.
    22. Cited for: 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.
    24. "Inactivation of androgen receptor coregulator ARA55 inhibits androgen receptor activity and agonist effect of antiandrogens in prostate cancer cells."
      Rahman M.M., Miyamoto H., Lardy H., Chang C.
      Proc. Natl. Acad. Sci. U.S.A. 100:5124-5129(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    25. "Expression of androgen receptor coactivators in normal and cancer prostate tissues and cultured cell lines."
      Mestayer C., Blanchere M., Jaubert F., Dufour B., Mowszowicz I.
      Prostate 56:192-200(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    26. "Distinct LIM domains of Hic-5/ARA55 are required for nuclear matrix targeting and glucocorticoid receptor binding and coactivation."
      Guerrero-Santoro J., Yang L., Stallcup M.R., DeFranco D.B.
      J. Cell. Biochem. 92:810-819(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
    27. Cited for: INTERACTION WITH PPARG.
    28. "Novel function of androgen receptor-associated protein 55/Hic-5 as a negative regulator of Smad3 signaling."
      Wang H., Song K., Sponseller T.L., Danielpour D.
      J. Biol. Chem. 280:5154-5162(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD3.
    29. "Subcellular targeting of oxidants during endothelial cell migration."
      Wu R.F., Xu Y.C., Ma Z., Nwariaku F.E., Sarosi G.A. Jr., Terada L.S.
      J. Cell Biol. 171:893-904(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF4.
    30. "Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells."
      Heitzer M.D., DeFranco D.B.
      Cancer Res. 66:7326-7333(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    31. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "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: FUNCTION, INTERACTION WITH MAPK15, MUTAGENESIS OF CYS-369; CYS-372; HIS-428 AND CYS-431.
    33. "Serotonin-, protein kinase C-, and Hic-5-associated redistribution of the platelet serotonin transporter."
      Carneiro A.M.D., Blakely R.D.
      J. Biol. Chem. 281:24769-24780(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLC6A4.
    34. "Mechanism of action of Hic-5/androgen receptor activator 55, a LIM domain-containing nuclear receptor coactivator."
      Heitzer M.D., DeFranco D.B.
      Mol. Endocrinol. 20:56-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5."
      Maudsley S., Davidson L., Pawson A.J., Freestone S.H., Lopez de Maturana R., Thomson A.A., Millar R.P.
      Neuroendocrinology 84:285-300(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR; PTK2B/PYK2 AND SRC, PHOSPHORYLATION.
    36. "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 AND LYN.
    37. "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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    38. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "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-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Cbl-c ubiquitin ligase activity is increased via the interaction of its RING finger domain with a LIM domain of the paxillin homolog, Hic 5."
      Ryan P.E., Kales S.C., Yadavalli R., Nau M.M., Zhang H., Lipkowitz S.
      PLoS ONE 7:E49428-E49428(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBLC, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-287 AND CYS-313.
    42. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTGFI1_HUMAN
    AccessioniPrimary (citable) accession number: O43294
    Secondary accession number(s): B2R8D5, Q9BPW3, Q9Y2V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 109 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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