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O43294 (TGFI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TGFB1I1
Synonyms:ARA55
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.15 Ref.17 Ref.19 Ref.20 Ref.24 Ref.26 Ref.28 Ref.30 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37

Subunit structure

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32 Ref.33 Ref.35 Ref.36 Ref.41

Subcellular location

Cell junctionfocal adhesion. Nucleus matrix. Cytoplasmcytoskeleton. Note: Associated with the actin cytoskeleton; colocalizes with stress fibers. Ref.9 Ref.12 Ref.13 Ref.20 Ref.23 Ref.26 Ref.30 Ref.37 Ref.41

Tissue specificity

Expressed in platelets, smooth muscle and prostate stromal cells (at protein level). Ref.1 Ref.9 Ref.11 Ref.12 Ref.22 Ref.25 Ref.30 Ref.36 Ref.37

Induction

Up-regulated by TNF and hydrogen peroxide. Ref.14 Ref.16

Domain

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.

Post-translational modification

Phosphorylated by gonadotropin-releasing hormone-activated SRC. Ref.10 Ref.12 Ref.19 Ref.35 Ref.36

Sequence similarities

Belongs to the paxillin family.

Contains 4 LIM zinc-binding domains.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
Wnt signaling pathway
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cell adhesion

Traceable author statement Ref.6. Source: ProtInc

cell fate commitment

Inferred from electronic annotation. Source: Ensembl

epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

morphogenesis of embryonic epithelium

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement PubMed 7929412. Source: ProtInc

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 18762808. Source: BHF-UCL

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 18762808. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 18762808. Source: BHF-UCL

response to heat

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

ubiquitin-dependent SMAD protein catabolic process

Inferred from direct assay PubMed 18762808. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionI-SMAD binding

Inferred from physical interaction PubMed 18762808. Source: BHF-UCL

Roundabout binding

Inferred from physical interaction PubMed 19855388. Source: UniProtKB

androgen receptor binding

Inferred from physical interaction Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43294-1)

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.
Isoform 2 (identifier: O43294-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Transforming growth factor beta-1-induced transcript 1 protein
PRO_0000291582

Regions

Domain226 – 28560LIM zinc-binding 1
Domain286 – 34358LIM zinc-binding 2
Domain344 – 40360LIM zinc-binding 3
Domain404 – 46158LIM zinc-binding 4
Region1 – 240240Interaction with PTK2B/PYK2
Region1 – 200200Transcription activation By similarity
Region83 – 13654Interaction with PTK2/FAK1 By similarity
Motif3 – 1513LD motif 1
Motif92 – 10413LD motif 2
Motif157 – 16812LD motif 3
Motif203 – 21513LD motif 4

Amino acid modifications

Modified residue11N-acetylmethionine Ref.42
Modified residue331Phosphothreonine Ref.38
Modified residue381Phosphotyrosine By similarity
Modified residue601Phosphotyrosine; by FAK2 and FYN Ref.10 Ref.19
Modified residue681Phosphoserine Ref.31
Modified residue1371Phosphoserine Ref.40

Natural variations

Alternative sequence1 – 1717Missing in isoform 2.
VSP_026183
Natural variant1291Q → H. Ref.2
Corresponds to variant rs45475699 [ dbSNP | Ensembl ].
VAR_032831

Experimental info

Mutagenesis601Y → F: Prevents phosphorylation by FAK2 and FYN. Prevents interaction with CSK. Ref.10
Mutagenesis2871C → A: Abolishes interaction with CBLC and enhancement of CBLC E3 ubiquitin-protein ligase activity. Ref.41
Mutagenesis3131C → A: No effect on interaction with CBLC. Ref.41
Mutagenesis338 – 3425FLQLF → ALQAA: Loss of interaction with AR; when associated with 456-A--A-460. Ref.21
Mutagenesis3691C → S: Loss of AR coactivation; when associated with S-372. Ref.32
Mutagenesis3721C → S: Loss of AR coactivation; when associated with S-369. Ref.32
Mutagenesis4281H → S: Loss of AR coactivation; when associated with S-431. Ref.32
Mutagenesis4311C → S: Loss of AR coactivation; when associated with S-428. Ref.32
Mutagenesis456 – 4605FLKLF → ALKAA: Loss of interaction with AR; when associated with 338-A--A-342. Ref.21
Sequence conflict1661S → P in AAD22552. Ref.1
Sequence conflict2001G → A in AAD22552. Ref.1
Sequence conflict3631A → L in AAD22552. Ref.1
Sequence conflict405 – 4062CA → WP in AAD22552. Ref.1
Sequence conflict4301T → A in AAD22552. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: D2C7C32C3FD2C496

FASTA46149,814
        10         20         30         40         50         60 
MEDLDALLSD LETTTSHMPR SGAPKERPAE PLTPPPSYGH QPQTGSGESS GASGDKDHLY 

        70         80         90        100        110        120 
STVCKPRSPK PAAPAAPPFS SSSGVLGTGL CELDRLLQEL NATQFNITDE IMSQFPSSKV 

       130        140        150        160        170        180 
ASGEQKEDQS EDKKRPSLPS SPSPGLPKAS ATSATLELDR LMASLSDFRV QNHLPASGPT 

       190        200        210        220        230        240 
QPPVVSSTNE GSPSPPEPTG KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV 

       250        260        270        280        290        300 
TALGRAWHPE HFVCGGCSTA LGGSSFFEKD GAPFCPECYF ERFSPRCGFC NQPIRHKMVT 

       310        320        330        340        350        360 
ALGTHWHPEH FCCVSCGEPF GDEGFHEREG RPYCRRDFLQ LFAPRCQGCQ GPILDNYISA 

       370        380        390        400        410        420 
LSALWHPDCF VCRECFAPFS GGSFFEHEGR PLCENHFHAR RGSLCATCGL PVTGRCVSAL 

       430        440        450        460 
GRRFHPDHFT CTFCLRPLTK GSFQERAGKP YCQPCFLKLF G 

« Hide

Isoform 2 [UniParc].

Checksum: EC9E92DADE7156B4
Show »

FASTA44447,941

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Potential anti-androgenic activity of roxithromycin in skin."
Inui S., Nakajima T., Fukuzato Y., Fujimoto N., Chang C., Yoshikawa K., Itami S.
J. Dermatol. Sci. 27:147-151(2001) [PubMed] [Europe PMC] [Abstract]
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]"Expression of the LIM proteins paxillin and Hic-5 in human tissues."
Yuminamochi T., Yatomi Y., Osada M., Ohmori T., Ishii Y., Nakazawa K., Hosogaya S., Ozaki Y.
J. Histochem. Cytochem. 51:513-521(2003) [PubMed] [Europe PMC] [Abstract]
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]"Hic-5 regulates an epithelial program mediated by PPARgamma."
Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K., Shivdasani R.A., Spiegelman B.M.
Genes Dev. 19:362-375(2005) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001035919.1. NM_001042454.2.
NP_001158191.1. NM_001164719.1.
NP_057011.2. NM_015927.4.
UniGeneHs.513530.

3D structure databases

ProteinModelPortalO43294.
SMRO43294. Positions 224-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112899. 29 interactions.
DIPDIP-5931N.
IntActO43294. 12 interactions.
MINTMINT-243624.
STRING9606.ENSP00000378332.

PTM databases

PhosphoSiteO43294.

Proteomic databases

PaxDbO43294.
PRIDEO43294.

Protocols and materials databases

DNASU7041.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361773; ENSP00000355117; ENSG00000140682. [O43294-2]
ENST00000394858; ENSP00000378327; ENSG00000140682. [O43294-2]
ENST00000394863; ENSP00000378332; ENSG00000140682. [O43294-1]
ENST00000567607; ENSP00000457586; ENSG00000140682. [O43294-2]
GeneID7041.
KEGGhsa:7041.
UCSCuc002ecd.2. human. [O43294-1]

Organism-specific databases

CTD7041.
GeneCardsGC16P031483.
HGNCHGNC:11767. TGFB1I1.
HPACAB020844.
HPA006376.
MIM602353. gene.
neXtProtNX_O43294.
PharmGKBPA36481.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267887.
HOGENOMHOG000018764.
HOVERGENHBG001512.
InParanoidO43294.
OMATAGEQKE.
PhylomeDBO43294.
TreeFamTF314113.

Enzyme and pathway databases

SignaLinkO43294.

Gene expression databases

ArrayExpressO43294.
BgeeO43294.
CleanExHS_TGFB1I1.
GenevestigatorO43294.

Family and domain databases

Gene3D2.10.110.10. 4 hits.
InterProIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 4 hits.
[Graphical view]
PIRSFPIRSF037881. Leupaxin. 1 hit.
SMARTSM00132. LIM. 4 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTGFB1I1.
GenomeRNAi7041.
NextBio27511.
PROO43294.
SOURCESearch...

Entry information

Entry nameTGFI1_HUMAN
AccessionPrimary (citable) accession number: O43294
Secondary accession number(s): B2R8D5, Q9BPW3, Q9Y2V5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM