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Q62219 (TGFI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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-associated protein of 55 kDa
Hydrogen peroxide-inducible clone 5 protein
Short name=Hic-5
TGF beta-stimulated clone 5
Short name=TSC-5
Gene names
Name:Tgfb1i1
Synonyms:Ara55
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.8 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32 Ref.33 Ref.34

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.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32

Subcellular location

Cell junctionfocal adhesion. Nucleus matrix. Cytoplasmcytoskeleton. Note: Associated with the actin cytoskeleton, colocalizes with stress fibers. Ref.11 Ref.12 Ref.14 Ref.23 Ref.25 Ref.27 Ref.31

Tissue specificity

Ubiquitously expressed. Higher expression is detected in lung and spleen. Expression decreases during pregnancy in mammary glands. Expressed in all brain areas, with higher levels in cerebellum, prefrontal cortex and hypothalamus. Expressed in smooth muscle, myoepithelial cells and platelets (at protein level). Preferentially expressed in mesenchymal versus epithelial cells (at protein level). Ref.1 Ref.3 Ref.22 Ref.27 Ref.28 Ref.32

Developmental stage

First detected in the developing heart tube at E8.0 and then in cardiac, skeletal and smooth muscle during early stages of development. Highly expressed in differentiating gut epithelial cells. Ref.15 Ref.18 Ref.26

Induction

Up-regulated during epithelial to mesenchymal transformation. Up-regulated by TGFB1 and hydrogen peroxide. Ref.1 Ref.28

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 By similarity. Ref.25 Ref.32

Sequence similarities

Belongs to the paxillin family.

Contains 4 LIM zinc-binding domains.

Sequence caution

The sequence AAH02049.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAZ82195.1 differs from that shown. Reason: Frameshift at position 28.

The sequence AAZ82200.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAE33707.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAE34493.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
   Biological processDifferentiation
Wnt signaling pathway
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   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

cell fate commitment

Inferred from genetic interaction Ref.26. Source: MGI

epithelial cell differentiation

Inferred from genetic interaction Ref.26. Source: MGI

morphogenesis of embryonic epithelium

Inferred from mutant phenotype Ref.26. Source: MGI

negative regulation of fat cell differentiation

Inferred from genetic interaction Ref.26. Source: MGI

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

ubiquitin-dependent SMAD protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from direct assay PubMed 11784865. Source: MGI

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 22832517Ref.7. Source: IntAct

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Plekhh2Q8C1153EBI-642844,EBI-6512409
PTK2Q053973EBI-642844,EBI-702142From a different organism.

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62219-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Transcripts of the alpha group are more abundantly expressed.
Isoform 2 (identifier: Q62219-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
Isoform 3 (identifier: Q62219-3)

Also known as: Alpha-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MEDLDALLSD...PPPPYGHQPQ → MSPCSPFIAP...SASAPPWRTW
Note: Transcripts of the alpha group are more abundantly expressed.
Isoform 4 (identifier: Q62219-4)

Also known as: Alpha-E;

The sequence of this isoform differs from the canonical sequence as follows:
     62-107: Missing.
Note: Transcripts of the alpha group are more abundantly expressed.
Isoform 5 (identifier: Q62219-5)

Also known as: Beta-G;

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.
     60-82: YSTVCKPRSPKPVAPVAPPFSSS → MATSHRQGLENLQEPLGTRIIYT
Isoform 6 (identifier: Q62219-6)

Also known as: Alpha-C;

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: S → R
     62-461: Missing.
Note: Transcripts of the alpha group are more abundantly expressed. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 7 (identifier: Q62219-7)

Also known as: Beta-B; Beta-D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.
Isoform 8 (identifier: Q62219-8)

Also known as: Beta-C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
     61-61: S → R
     62-461: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 9 (identifier: Q62219-9)

Also known as: Beta-E; Beta-F;

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.
     63-138: VCKPRSPKPV...QSEDKSSPTV → MPPSSTLQMK...SEVIHGVLHN
Isoform 10 (identifier: Q62219-10)

Also known as: Alpha-D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
     111-148: IMSQFPSSKM...PPSPFPAPSK → MPPSSTLQMK...NLKTRAHPLS
Note: Transcripts of the alpha group are more abundantly expressed.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Transforming growth factor beta-1-induced transcript 1 protein
PRO_0000291583

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 By similarity
Region1 – 200200Transcription activation
Region83 – 13654Interaction with PTK2/FAK1
Motif3 – 1513LD motif 1
Motif92 – 10413LD motif 2
Motif157 – 16812LD motif 3
Motif203 – 21513LD motif 4

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue331Phosphothreonine By similarity
Modified residue381Phosphotyrosine Ref.25
Modified residue601Phosphotyrosine Ref.25
Modified residue681Phosphoserine By similarity

Natural variations

Alternative sequence1 – 111111Missing in isoform 7.
VSP_026184
Alternative sequence1 – 110110Missing in isoform 10.
VSP_026185
Alternative sequence1 – 6262Missing in isoform 9.
VSP_026188
Alternative sequence1 – 5959Missing in isoform 5.
VSP_026189
Alternative sequence1 – 4343MEDLD…GHQPQ → MSPCSPFIAPPPPTVSQRVP ASIHGHGPASNSLTSPPSPS SAPTGHGPRPTLPKLSASAP PWRTW in isoform 3.
VSP_026190
Alternative sequence1 – 1717Missing in isoform 2 and isoform 8.
VSP_026191
Alternative sequence60 – 8223YSTVC…PFSSS → MATSHRQGLENLQEPLGTRI IYT in isoform 5.
VSP_026192
Alternative sequence611S → R in isoform 6 and isoform 8.
VSP_039813
Alternative sequence62 – 461400Missing in isoform 6 and isoform 8.
VSP_039814
Alternative sequence62 – 10746Missing in isoform 4.
VSP_026193
Alternative sequence63 – 13876VCKPR…SSPTV → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLCEF GRVGRAGKRMMGPACLTYQR GVRLAGSEVIHGVLHN in isoform 9.
VSP_026194
Alternative sequence111 – 14838IMSQF…PAPSK → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLS in isoform 10.
VSP_026197

Experimental info

Mutagenesis381Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-60. Ref.25
Mutagenesis601Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-38. Ref.25
Mutagenesis641C → N: Increase in nuclear localization. Ref.23
Mutagenesis911C → S: Increase in nuclear localization. Ref.23
Mutagenesis1611L → A: Increase in nuclear localization. Ref.23
Mutagenesis3661H → G: Loss of interaction with PTPN12; when associated with G-369. Ref.9
Mutagenesis3691C → A: Loss of localization to focal adhesion; when associated with A-372. Ref.9 Ref.25
Mutagenesis3691C → G: Loss of interaction with PTPN12; when associated with G-366. Ref.9 Ref.25
Mutagenesis3721C → A: Loss of localization to focal adhesion; when associated with A-369. Ref.25

Sequences

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

Last modified June 26, 2007. Version 2.
Checksum: 6AB15FFF466FEE73

FASTA46150,101
        10         20         30         40         50         60 
MEDLDALLSD LETTTSHMSR LGAPKERPPE TLTPPPPYGH QPQTGSGESS GTTGDKDHLY 

        70         80         90        100        110        120 
STVCKPRSPK PVAPVAPPFS SSSGVLGNGL CELDRLLQEL NATQFNITDE IMSQFPSSKM 

       130        140        150        160        170        180 
AEGEEKEDQS EDKSSPTVPP SPFPAPSKPS ATSATQELDR LMASLSDFRV QNHLPASGPP 

       190        200        210        220        230        240 
QPPAASPTRE GCPSPPGQTS KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV 

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

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

       370        380        390        400        410        420 
LSALWHPDCF VCRECLAPFS GGSFFEHEGR PLCENHFHAQ RGSLCATCGL PVTGRCVSAL 

       430        440        450        460 
GRRFHPDHFT CTFCLRPLTK GSFQERASKP YCQPCFLKLF G 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 54E80E09A7CC7C51
Show »

FASTA44448,228
Isoform 3 (Alpha-B) [UniParc].

Checksum: FE6D462670C2BFFE
Show »

FASTA48351,988
Isoform 4 (Alpha-E) [UniParc].

Checksum: F6065EA4A754FEF5
Show »

FASTA41545,266
Isoform 5 (Beta-G) [UniParc].

Checksum: AF3A2DD21C47869E
Show »

FASTA40244,059
Isoform 6 (Alpha-C) [UniParc].

Checksum: E45E004C4EFCFAC7
Show »

FASTA616,605
Isoform 7 (Beta-B) (Beta-D) [UniParc].

Checksum: 3AFEE18DB06963F9
Show »

FASTA35038,289
Isoform 8 (Beta-C) [UniParc].

Checksum: FDEBBC62BE006A91
Show »

FASTA444,732
Isoform 9 (Beta-E) (Beta-F) [UniParc].

Checksum: DD062C34B5C62F81
Show »

FASTA39943,798
Isoform 10 (Alpha-D) [UniParc].

Checksum: 79F2BFB888438DDC
Show »

FASTA35138,669

References

« Hide 'large scale' references
[1]"Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence."
Shibanuma M., Mashimo J.I., Kuroki T., Nose K.
J. Biol. Chem. 269:26767-26774(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION BY TGFB1 AND HYDROGEN PEROXIDE, TISSUE SPECIFICITY.
Tissue: Calvaria.
[2]"Genomic structure and chromosomal mapping of the mouse hic-5 gene that encodes a focal adhesion protein."
Mashimo J.I., Shibanuma M., Satoh H., Chida K., Nose K.
Gene 249:99-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Identification and analysis of Hic-5/ARA55 isoforms: implications for integrin signaling and steroid hormone action."
Gao Z., Schwartz L.M.
FEBS Lett. 579:5651-5657(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8; 9 AND 10), TISSUE SPECIFICITY.
Strain: BALB/c.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
Strain: NOD.
Tissue: Inner ear and Spleen.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
Tissue: Brain and Mammary tumor.
[6]"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions."
Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T.
J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1 AND PTK2B/PYK2.
[7]"Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."
Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.
J. Biol. Chem. 273:26516-26521(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1.
[8]"The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro."
Nishiya N., Sabe H., Nose K., Shibanuma M.
Nucleic Acids Res. 26:4267-4273(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain."
Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L., Nose K.
J. Biol. Chem. 274:9847-9853(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN12, MUTAGENESIS OF HIS-366 AND CYS-369.
[10]"Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling."
Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N., McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.
J. Cell Biol. 145:851-863(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF7; GIT2; NCK2; PTK2/FAK1 AND PAK.
[11]"Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin."
Thomas S.M., Hagel M., Turner C.E.
J. Cell Sci. 112:181-190(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSK; PTK2/FAK1 AND VCL, SUBCELLULAR LOCATION.
[12]"Specific decrease in the level of Hic-5, a focal adhesion protein, during immortalization of mouse embryonic fibroblasts, and its association with focal adhesion kinase."
Ishino K., Kim Kaneyama J.-R., Shibanuma M., Nose K.
J. Cell. Biochem. 76:411-419(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK1.
[13]"Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
Nikolopoulos S.N., Turner C.E.
J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARVA.
[14]"Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix."
Yang L., Guerrero J., Hong H., DeFranco D.B., Stallcup M.R.
Mol. Biol. Cell 11:2007-2018(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
[15]"Novel cell lines promote the discovery of genes involved in early heart development."
Brunskill E.W., Witte D.P., Yutzey K.E., Potter S.S.
Dev. Biol. 235:507-520(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[16]"Identification and characterization of hic-5/ARA55 as an hsp27 binding protein."
Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.
J. Biol. Chem. 276:39911-39918(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSPB1.
[17]"Hic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinase."
Nishiya N., Tachibana K., Shibanuma M., Mashimo J.I., Nose K.
Mol. Cell. Biol. 21:5332-5345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Possible involvement of hic-5, a focal adhesion protein, in the differentiation of C2C12 myoblasts."
Shibanuma M., Iwabuchi Y., Nose K.
Cell Struct. Funct. 27:21-27(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[19]"Hic-5 interacts with GIT1 with a different binding mode from paxillin."
Nishiya N., Shirai T., Suzuki W., Nose K.
J. Biochem. 132:279-289(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GIT1 AND ARHGEF7.
[20]"The FXXLF motif mediates androgen receptor-specific interactions with coregulators."
He B., Minges J.T., Lee L.W., Wilson E.M.
J. Biol. Chem. 277:10226-10235(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AR.
[21]"Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5."
Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S., French B., Neveu W., Goetinck P.F.
J. Biol. Chem. 277:12270-12274(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUDT16L1.
[22]"The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter."
Carneiro A.M.D., Ingram S.L., Beaulieu J.-M., Sweeney A., Amara S.G., Thomas S.M., Caron M.G., Torres G.E.
J. Neurosci. 22:7045-7054(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC6A3, TISSUE SPECIFICITY.
[23]"Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal."
Shibanuma M., Kim-Kaneyama J.-R., Ishino K., Sakamoto N., Hishiki T., Yamaguchi K., Mori K., Mashimo J.I., Nose K.
Mol. Biol. Cell 14:1158-1171(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-64; CYS-91 AND LEU-161.
[24]"A LIM protein, Hic-5, functions as a potential coactivator for Sp1."
Shibanuma M., Kim-Kaneyama J.-R., Sato S., Nose K.
J. Cell. Biochem. 91:633-645(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMAD3.
[25]"Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation."
Hetey S.E., Lalonde D.P., Turner C.E.
Exp. Cell Res. 311:147-156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-38; TYR-60; CYS-369 AND CYS-372, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-38 AND TYR-60.
[26]"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: FUNCTION, INTERACTION WITH PPARG, DEVELOPMENTAL STAGE.
[27]"Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo."
Kim-Kaneyama J.-R., Suzuki W., Ichikawa K., Ohki T., Kohno Y., Sata M., Nose K., Shibanuma M.
J. Cell Sci. 118:937-949(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CRIP2.
[28]"Regulation of paxillin family members during epithelial-mesenchymal transformation: a putative role for paxillin delta."
Tumbarello D.A., Brown M.C., Hetey S.E., Turner C.E.
J. Cell Sci. 118:4849-4863(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY.
[29]"HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription."
Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., Gradl D.
J. Biol. Chem. 281:1755-1764(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TCF3 AND TCF7L2.
[30]"ERK8 down-regulates transactivation of the glucocorticoid receptor through Hic-5."
Saelzler M.P., Spackman C.C., Liu Y., Martinez L.C., Harris J.P., Abe M.K.
J. Biol. Chem. 281:16821-16832(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK15.
[31]"Oligomerizing potential of a focal adhesion LIM protein Hic-5 organizing a nuclear-cytoplasmic shuttling complex."
Mori K., Asakawa M., Hayashi M., Imura M., Ohki T., Hirao E., Kim-Kaneyama J.-R., Nose K., Shibanuma M.
J. Biol. Chem. 281:22048-22061(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ILK; LIMS1 AND LIMS2.
[32]"Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets."
Rathore V.B., Okada M., Newman P.J., Newman D.K.
Biochem. J. 403:275-281(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH CSK.
[33]"Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway."
Tumbarello D.A., Turner C.E.
J. Cell. Physiol. 211:736-747(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[34]"Hic-5/ARA55 a prostate stroma-specific AR coactivator."
Heitzer M.D., DeFranco D.B.
Steroids 72:218-220(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22482 mRNA. Translation: AAA62226.1.
AF083064 Genomic DNA. Translation: AAD51090.1.
DQ143891 mRNA. Translation: AAZ82195.1. Frameshift.
DQ143892 mRNA. Translation: AAZ82196.1.
DQ143893 mRNA. Translation: AAZ82197.1.
DQ143894 mRNA. Translation: AAZ82198.1.
DQ143895 mRNA. Translation: AAZ82199.1.
DQ143896 mRNA. Translation: AAZ82200.1. Sequence problems.
DQ143897 mRNA. Translation: AAZ82201.1.
DQ143898 mRNA. Translation: AAZ82202.1.
DQ143899 mRNA. Translation: AAZ82203.1.
DQ143900 mRNA. Translation: AAZ82204.1.
AK156423 mRNA. Translation: BAE33707.1. Different initiation.
AK158409 mRNA. Translation: BAE34493.1. Sequence problems.
BC002049 mRNA. Translation: AAH02049.1. Different initiation.
BC056362 mRNA. Translation: AAH56362.1.
PIRA55071.
RefSeqNP_001276479.1. NM_001289550.1. [Q62219-1]
NP_001276481.1. NM_001289552.1.
NP_001276482.1. NM_001289553.1. [Q62219-7]
XP_006507630.1. XM_006507567.1. [Q62219-3]
UniGeneMm.3248.

3D structure databases

ProteinModelPortalQ62219.
SMRQ62219. Positions 228-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204158. 5 interactions.
IntActQ62219. 5 interactions.
MINTMINT-1666684.

PTM databases

PhosphoSiteQ62219.

Proteomic databases

MaxQBQ62219.
PaxDbQ62219.
PRIDEQ62219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070656; ENSMUSP00000068529; ENSMUSG00000030782. [Q62219-2]
ENSMUST00000163609; ENSMUSP00000133134; ENSMUSG00000030782. [Q62219-7]
ENSMUST00000164710; ENSMUSP00000130964; ENSMUSG00000030782. [Q62219-3]
ENSMUST00000167965; ENSMUSP00000132100; ENSMUSG00000030782. [Q62219-1]
ENSMUST00000169919; ENSMUSP00000131705; ENSMUSG00000030782. [Q62219-6]
GeneID21804.
KEGGmmu:21804.
UCSCuc009jyl.1. mouse. [Q62219-1]
uc009jyo.1. mouse. [Q62219-4]

Organism-specific databases

CTD7041.
MGIMGI:102784. Tgfb1i1.

Phylogenomic databases

eggNOGNOG267887.
GeneTreeENSGT00740000114891.
HOVERGENHBG001512.
InParanoidQ62219.
OMATAGEQKE.
OrthoDBEOG70ZZQN.
PhylomeDBQ62219.
TreeFamTF314113.

Gene expression databases

ArrayExpressQ62219.
BgeeQ62219.
GenevestigatorQ62219.

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

NextBio301180.
PROQ62219.
SOURCESearch...

Entry information

Entry nameTGFI1_MOUSE
AccessionPrimary (citable) accession number: Q62219
Secondary accession number(s): Q3YBY7 expand/collapse secondary AC list , Q3YBY8, Q3YBZ0, Q3YBZ1, Q3YBZ3, Q3YBZ4, Q3YBZ5, Q3YBZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot