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Q62219

- TGFI1_MOUSE

UniProt

Q62219 - TGFI1_MOUSE

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Protein
Transforming growth factor beta-1-induced transcript 1 protein
Gene
Tgfb1i1, Ara55
Organism
Mus musculus (Mouse)
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.17 Publications

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:102784. Tgfb1i1.

Subcellular locationi

Cell junctionfocal adhesion. Nucleus matrix. Cytoplasmcytoskeleton
Note: Associated with the actin cytoskeleton, colocalizes with stress fibers.7 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Transforming growth factor beta-1-induced transcript 1 protein
PRO_0000291583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei33 – 331Phosphothreonine By similarity
Modified residuei38 – 381Phosphotyrosine1 Publication
Modified residuei60 – 601Phosphotyrosine1 Publication
Modified residuei68 – 681Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by gonadotropin-releasing hormone-activated SRC By similarity.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ62219.
PaxDbiQ62219.
PRIDEiQ62219.

PTM databases

PhosphoSiteiQ62219.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Inductioni

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

Gene expression databases

ArrayExpressiQ62219.
BgeeiQ62219.
GenevestigatoriQ62219.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ62219.
SMRiQ62219. Positions 228-461.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 240240Interaction with PTK2B/PYK2 By similarity
Add
BLAST
Regioni1 – 200200Transcription activation
Add
BLAST
Regioni83 – 13654Interaction with PTK2/FAK1
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 1513LD motif 1
Add
BLAST
Motifi92 – 10413LD motif 2
Add
BLAST
Motifi157 – 16812LD motif 3
Add
BLAST
Motifi203 – 21513LD motif 4
Add
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.
GeneTreeiENSGT00740000114891.
HOVERGENiHBG001512.
InParanoidiQ62219.
OMAiTAGEQKE.
OrthoDBiEOG70ZZQN.
PhylomeDBiQ62219.
TreeFamiTF314113.

Family and domain databases

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

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. Align

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

Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

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

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

Also known as: Beta

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

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

Also known as: Alpha-B

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

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

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

Also known as: Alpha-E

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

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

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

Also known as: Beta-G

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

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

Also known as: Alpha-C

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

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

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

Also known as: Beta-B, Beta-D

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

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

Also known as: Beta-C

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

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

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

Also known as: Beta-E, Beta-F

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

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

Also known as: Alpha-D

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

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

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

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111Missing in isoform 7.
VSP_026184Add
BLAST
Alternative sequencei1 – 110110Missing in isoform 10.
VSP_026185Add
BLAST
Alternative sequencei1 – 6262Missing in isoform 9.
VSP_026188Add
BLAST
Alternative sequencei1 – 5959Missing in isoform 5.
VSP_026189Add
BLAST
Alternative sequencei1 – 4343MEDLD…GHQPQ → MSPCSPFIAPPPPTVSQRVP ASIHGHGPASNSLTSPPSPS SAPTGHGPRPTLPKLSASAP PWRTW in isoform 3.
VSP_026190Add
BLAST
Alternative sequencei1 – 1717Missing in isoform 2 and isoform 8.
VSP_026191Add
BLAST
Alternative sequencei60 – 8223YSTVC…PFSSS → MATSHRQGLENLQEPLGTRI IYT in isoform 5.
VSP_026192Add
BLAST
Alternative sequencei61 – 611S → R in isoform 6 and isoform 8.
VSP_039813
Alternative sequencei62 – 461400Missing in isoform 6 and isoform 8.
VSP_039814Add
BLAST
Alternative sequencei62 – 10746Missing in isoform 4.
VSP_026193Add
BLAST
Alternative sequencei63 – 13876VCKPR…SSPTV → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLCEF GRVGRAGKRMMGPACLTYQR GVRLAGSEVIHGVLHN in isoform 9.
VSP_026194Add
BLAST
Alternative sequencei111 – 14838IMSQF…PAPSK → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLS in isoform 10.
VSP_026197Add
BLAST

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei Q62219.

Proteomic databases

MaxQBi Q62219.
PaxDbi Q62219.
PRIDEi Q62219.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 7041.
MGIi MGI:102784. Tgfb1i1.

Phylogenomic databases

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

Miscellaneous databases

NextBioi 301180.
PROi Q62219.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q62219.
Bgeei Q62219.
Genevestigatori Q62219.

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiTGFI1_MOUSE
AccessioniPrimary (citable) accession number: Q62219
Secondary accession number(s): Q3YBY7
, Q3YBY8, Q3YBZ0, Q3YBZ1, Q3YBZ3, Q3YBZ4, Q3YBZ5, Q3YBZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: September 3, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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