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O43294

- TGFI1_HUMAN

UniProt

O43294 - TGFI1_HUMAN

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Protein

Transforming growth factor beta-1-induced transcript 1 protein

Gene
TGFB1I1, ARA55
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.9 Publications

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi287 – 2871C → A: Abolishes interaction with CBLC and enhancement of CBLC E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi313 – 3131C → A: No effect on interaction with CBLC. 1 Publication
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. 1 Publication
Mutagenesisi372 – 3721C → S: Loss of AR coactivation; when associated with S-369. 1 Publication
Mutagenesisi428 – 4281H → S: Loss of AR coactivation; when associated with S-431. 1 Publication
Mutagenesisi431 – 4311C → S: Loss of AR coactivation; when associated with S-428. 1 Publication
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 – 381Phosphotyrosine By 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.5 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. 29 interactions.
DIPiDIP-5931N.
IntActiO43294. 12 interactions.
MINTiMINT-243624.
STRINGi9606.ENSP00000378332.

Structurei

3D structure databases

ProteinModelPortaliO43294.
SMRiO43294. Positions 228-461.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 240240Interaction with PTK2B/PYK2Add
BLAST
Regioni1 – 200200Transcription activation By similarityAdd
BLAST
Regioni83 – 13654Interaction with PTK2/FAK1 By 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.

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.

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. VSP_026183Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661S → P in AAD22552. 1 Publication
Sequence conflicti200 – 2001G → A in AAD22552. 1 Publication
Sequence conflicti363 – 3631A → L in AAD22552. 1 Publication
Sequence conflicti405 – 4062CA → WP in AAD22552. 1 Publication
Sequence conflicti430 – 4301T → A in AAD22552. 1 Publication

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. 29 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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 108 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

Dasty 3

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