Reviewed, UniProtKB/Swiss-Prot Q62219 (TGFI1_MOUSE)

Names and origin

Protein names

Recommended name:
    Transforming growth factor beta-1-induced transcript 1 protein
Alternative name(s):
    Hydrogen peroxide-inducible clone 5 protein
      Short name=Hic-5
    Androgen receptor-associated protein of 55 kDa
    TGF beta-stimulated clone 5
      Short name=TSC-5

Gene names

Name:	Tgfb1i1
Synonyms:	Ara55

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 AR/androgen receptor in a ligand-dependent manner. Interacts with LYN, PTK2B, SLC6A4, SMAD3, SRC and talin By similarity. Forms a complex with GIT1 and ARHGEF7. Interacts with CRIP2, CSK, HSPB1, ILK, LIMS1, LIMS2, MAPK15, NCK2, NR3C1, NUDT16L1, PAK, PARVA, PPARG, PTK2, PTPN12, SLC6A3, TCF3, TCF7L2 and VCL.
Subcellular location	Cell junction › focal adhesion. Nucleus matrix. Cytoplasm › cytoskeleton. Note: Associated with the actin cytoskeleton, colocalizes with stress fibers. Ref.12 Ref.14 Ref.25 Ref.27 Ref.31 Ref.11 Ref.23
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.27 Ref.32 Ref.3 Ref.22 Ref.28
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.18 Ref.26 Ref.15
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.
Sequence similarities	Belongs to the paxillin family. Contains 4 LIM zinc-binding domains.
Sequence caution	The sequence AAZ82195.1 differs from that shown. Reason: Frameshift at position 28.

Ontologies

Keywords
Biological process	Differentiation Wnt signaling pathway
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell fate commitment Ref.26 Inferred from genetic interaction. Source: MGI epithelial cell differentiation Ref.26 Inferred from genetic interaction. Source: MGI morphogenesis of embryonic epithelium Ref.26 Inferred from mutant phenotype. Source: MGI negative regulation of fat cell differentiation Ref.26 Inferred from genetic interaction. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: MGI nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.7 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTK2	Q05397	2	EBI-642844,EBI-702142	From 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:
     1-85: Missing.
     86-107: LGNGLCELDRLLQELNATQFNI → MATSHRQGLENLQEPLGTRIIY

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

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:
     1-106: Missing.
     107-113: ITDEIMS → MPPSSTL

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Transforming growth factor beta-1-induced transcript 1 protein		PRO_0000291583
Regions
	Domain	226 – 285	60	LIM zinc-binding 1
	Domain	286 – 343	58	LIM zinc-binding 2
	Domain	344 – 403	60	LIM zinc-binding 3
	Domain	404 – 461	58	LIM zinc-binding 4
	Region	1 – 240	240	Interaction with PTK2B By similarity
	Region	1 – 200	200	Transcription activation
	Region	83 – 136	54	Interaction with PTK2
	Motif	3 – 15	13	LD motif 1
	Motif	92 – 104	13	LD motif 2
	Motif	157 – 168	12	LD motif 3
	Motif	203 – 215	13	LD motif 4
Amino acid modifications
	Modified residue	33	1	Phosphothreonine By similarity
	Modified residue	38	1	Phosphotyrosine Ref.25
	Modified residue	60	1	Phosphotyrosine Ref.25
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	194	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 111	111	Missing in isoform 7.		VSP_026184
	Alternative sequence	1 – 110	110	Missing in isoform 10.		VSP_026185
	Alternative sequence	1 – 106	106	Missing in isoform 8.		VSP_026186
	Alternative sequence	1 – 85	85	Missing in isoform 6.		VSP_026187
	Alternative sequence	1 – 62	62	Missing in isoform 9.		VSP_026188
	Alternative sequence	1 – 59	59	Missing in isoform 5.		VSP_026189
	Alternative sequence	1 – 43	43	MEDLD…GHQPQ → MSPCSPFIAPPPPTVSQRVP ASIHGHGPASNSLTSPPSPS SAPTGHGPRPTLPKLSASAP PWRTW in isoform 3.		VSP_026190
	Alternative sequence	1 – 17	17	Missing in isoform 2.		VSP_026191
	Alternative sequence	60 – 82	23	YSTVC…PFSSS → MATSHRQGLENLQEPLGTRI IYT in isoform 5.		VSP_026192
	Alternative sequence	62 – 107	46	Missing in isoform 4.		VSP_026193
	Alternative sequence	63 – 138	76	VCKPR…SSPTV → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLCEF GRVGRAGKRMMGPACLTYQR GVRLAGSEVIHGVLHN in isoform 9.		VSP_026194
	Alternative sequence	86 – 107	22	LGNGL…TQFNI → MATSHRQGLENLQEPLGTRI IY in isoform 6.		VSP_026195
	Alternative sequence	107 – 113	7	ITDEIMS → MPPSSTL in isoform 8.		VSP_026196
	Alternative sequence	111 – 148	38	IMSQF…PAPSK → MPPSSTLQMKSCLSSHLVKW LKGKRRRTNLKTRAHPLS in isoform 10.		VSP_026197
Experimental info
	Mutagenesis	38	1	Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-60. Ref.25
	Mutagenesis	60	1	Y → F: Reduced phosphorylation. Loss of phosphorylation; when associated with F-38. Ref.25
	Mutagenesis	64	1	C → N: Increase in nuclear localization. Ref.23
	Mutagenesis	91	1	C → S: Increase in nuclear localization. Ref.23
	Mutagenesis	161	1	L → A: Increase in nuclear localization. Ref.23
	Mutagenesis	366	1	H → G: Loss of interaction with PTPN12; when associated with G-369. Ref.9
	Mutagenesis	369	1	C → A: Loss of localization to focal adhesion; when associated with A-372. Ref.25 Ref.9
	Mutagenesis	369	1	C → G: Loss of interaction with PTPN12; when associated with G-366. Ref.25 Ref.9
	Mutagenesis	372	1	C → A: Loss of localization to focal adhesion; when associated with A-369. Ref.25

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 6AB15FFF466FEE73	FASTA	461	50,101
	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
	Isoform 2 (Beta). Checksum: 54E80E09A7CC7C51	FASTA	444	48,228
	10 20 30 40 50 60 MSRLGAPKER PPETLTPPPP YGHQPQTGSG ESSGTTGDKD HLYSTVCKPR SPKPVAPVAP 70 80 90 100 110 120 PFSSSSGVLG NGLCELDRLL QELNATQFNI TDEIMSQFPS SKMAEGEEKE DQSEDKSSPT 130 140 150 160 170 180 VPPSPFPAPS KPSATSATQE LDRLMASLSD FRVQNHLPAS GPPQPPAASP TREGCPSPPG 190 200 210 220 230 240 QTSKGSLDTM LGLLQSDLSR RGVPTQAKGL CGSCNKPIAG QVVTALGRAW HPEHFLCSGC 250 260 270 280 290 300 STTLGGSSFF EKDGAPFCPE CYFERFSPRC GFCNQPIRHK MVTALGTHWH PEHFCCVSCG 310 320 330 340 350 360 EPFGEEGFHE REGRPYCRRD FLQLFAPRCQ GCQGPILDNY ISALSALWHP DCFVCRECLA 370 380 390 400 410 420 PFSGGSFFEH EGRPLCENHF HAQRGSLCAT CGLPVTGRCV SALGRRFHPD HFTCTFCLRP 430 440 LTKGSFQERA SKPYCQPCFL KLFG
	Isoform 3 (Alpha-B). Checksum: FE6D462670C2BFFE	FASTA	483	51,988
	10 20 30 40 50 60 MSPCSPFIAP PPPTVSQRVP ASIHGHGPAS NSLTSPPSPS SAPTGHGPRP TLPKLSASAP 70 80 90 100 110 120 PWRTWTGSGE SSGTTGDKDH LYSTVCKPRS PKPVAPVAPP FSSSSGVLGN GLCELDRLLQ 130 140 150 160 170 180 ELNATQFNIT DEIMSQFPSS KMAEGEEKED QSEDKSSPTV PPSPFPAPSK PSATSATQEL 190 200 210 220 230 240 DRLMASLSDF RVQNHLPASG PPQPPAASPT REGCPSPPGQ TSKGSLDTML GLLQSDLSRR 250 260 270 280 290 300 GVPTQAKGLC GSCNKPIAGQ VVTALGRAWH PEHFLCSGCS TTLGGSSFFE KDGAPFCPEC 310 320 330 340 350 360 YFERFSPRCG FCNQPIRHKM VTALGTHWHP EHFCCVSCGE PFGEEGFHER EGRPYCRRDF 370 380 390 400 410 420 LQLFAPRCQG CQGPILDNYI SALSALWHPD CFVCRECLAP FSGGSFFEHE GRPLCENHFH 430 440 450 460 470 480 AQRGSLCATC GLPVTGRCVS ALGRRFHPDH FTCTFCLRPL TKGSFQERAS KPYCQPCFLK LFG
	Isoform 4 (Alpha-E). Checksum: F6065EA4A754FEF5	FASTA	415	45,266
	10 20 30 40 50 60 MEDLDALLSD LETTTSHMSR LGAPKERPPE TLTPPPPYGH QPQTGSGESS GTTGDKDHLY 70 80 90 100 110 120 STDEIMSQFP SSKMAEGEEK EDQSEDKSSP TVPPSPFPAP SKPSATSATQ ELDRLMASLS 130 140 150 160 170 180 DFRVQNHLPA SGPPQPPAAS PTREGCPSPP GQTSKGSLDT MLGLLQSDLS RRGVPTQAKG 190 200 210 220 230 240 LCGSCNKPIA GQVVTALGRA WHPEHFLCSG CSTTLGGSSF FEKDGAPFCP ECYFERFSPR 250 260 270 280 290 300 CGFCNQPIRH KMVTALGTHW HPEHFCCVSC GEPFGEEGFH EREGRPYCRR DFLQLFAPRC 310 320 330 340 350 360 QGCQGPILDN YISALSALWH PDCFVCRECL APFSGGSFFE HEGRPLCENH FHAQRGSLCA 370 380 390 400 410 TCGLPVTGRC VSALGRRFHP DHFTCTFCLR PLTKGSFQER ASKPYCQPCF LKLFG
	Isoform 5 (Beta-G). Checksum: AF3A2DD21C47869E	FASTA	402	44,059
	10 20 30 40 50 60 MATSHRQGLE NLQEPLGTRI IYTSGVLGNG LCELDRLLQE LNATQFNITD EIMSQFPSSK 70 80 90 100 110 120 MAEGEEKEDQ SEDKSSPTVP PSPFPAPSKP SATSATQELD RLMASLSDFR VQNHLPASGP 130 140 150 160 170 180 PQPPAASPTR EGCPSPPGQT SKGSLDTMLG LLQSDLSRRG VPTQAKGLCG SCNKPIAGQV 190 200 210 220 230 240 VTALGRAWHP EHFLCSGCST TLGGSSFFEK DGAPFCPECY FERFSPRCGF CNQPIRHKMV 250 260 270 280 290 300 TALGTHWHPE HFCCVSCGEP FGEEGFHERE GRPYCRRDFL QLFAPRCQGC QGPILDNYIS 310 320 330 340 350 360 ALSALWHPDC FVCRECLAPF SGGSFFEHEG RPLCENHFHA QRGSLCATCG LPVTGRCVSA 370 380 390 400 LGRRFHPDHF TCTFCLRPLT KGSFQERASK PYCQPCFLKL FG
	Isoform 6 (Alpha-C). Checksum: 3BB7B052BAB657BA	FASTA	376	41,258
	10 20 30 40 50 60 MATSHRQGLE NLQEPLGTRI IYTDEIMSQF PSSKMAEGEE KEDQSEDKSS PTVPPSPFPA 70 80 90 100 110 120 PSKPSATSAT QELDRLMASL SDFRVQNHLP ASGPPQPPAA SPTREGCPSP PGQTSKGSLD 130 140 150 160 170 180 TMLGLLQSDL SRRGVPTQAK GLCGSCNKPI AGQVVTALGR AWHPEHFLCS GCSTTLGGSS 190 200 210 220 230 240 FFEKDGAPFC PECYFERFSP RCGFCNQPIR HKMVTALGTH WHPEHFCCVS CGEPFGEEGF 250 260 270 280 290 300 HEREGRPYCR RDFLQLFAPR CQGCQGPILD NYISALSALW HPDCFVCREC LAPFSGGSFF 310 320 330 340 350 360 EHEGRPLCEN HFHAQRGSLC ATCGLPVTGR CVSALGRRFH PDHFTCTFCL RPLTKGSFQE 370 RASKPYCQPC FLKLFG
	Isoform 7 (Beta-B) (Beta-D). Checksum: 3AFEE18DB06963F9	FASTA	350	38,289
	10 20 30 40 50 60 MSQFPSSKMA EGEEKEDQSE DKSSPTVPPS PFPAPSKPSA TSATQELDRL MASLSDFRVQ 70 80 90 100 110 120 NHLPASGPPQ PPAASPTREG CPSPPGQTSK GSLDTMLGLL QSDLSRRGVP TQAKGLCGSC 130 140 150 160 170 180 NKPIAGQVVT ALGRAWHPEH FLCSGCSTTL GGSSFFEKDG APFCPECYFE RFSPRCGFCN 190 200 210 220 230 240 QPIRHKMVTA LGTHWHPEHF CCVSCGEPFG EEGFHEREGR PYCRRDFLQL FAPRCQGCQG 250 260 270 280 290 300 PILDNYISAL SALWHPDCFV CRECLAPFSG GSFFEHEGRP LCENHFHAQR GSLCATCGLP 310 320 330 340 350 VTGRCVSALG RRFHPDHFTC TFCLRPLTKG SFQERASKPY CQPCFLKLFG
	Isoform 8 (Beta-C). Checksum: 85E1D9C34B0A643C	FASTA	355	38,785
	10 20 30 40 50 60 MPPSSTLQFP SSKMAEGEEK EDQSEDKSSP TVPPSPFPAP SKPSATSATQ ELDRLMASLS 70 80 90 100 110 120 DFRVQNHLPA SGPPQPPAAS PTREGCPSPP GQTSKGSLDT MLGLLQSDLS RRGVPTQAKG 130 140 150 160 170 180 LCGSCNKPIA GQVVTALGRA WHPEHFLCSG CSTTLGGSSF FEKDGAPFCP ECYFERFSPR 190 200 210 220 230 240 CGFCNQPIRH KMVTALGTHW HPEHFCCVSC GEPFGEEGFH EREGRPYCRR DFLQLFAPRC 250 260 270 280 290 300 QGCQGPILDN YISALSALWH PDCFVCRECL APFSGGSFFE HEGRPLCENH FHAQRGSLCA 310 320 330 340 350 TCGLPVTGRC VSALGRRFHP DHFTCTFCLR PLTKGSFQER ASKPYCQPCF LKLFG
	Isoform 9 (Beta-E) (Beta-F). Checksum: DD062C34B5C62F81	FASTA	399	43,798
	10 20 30 40 50 60 MPPSSTLQMK SCLSSHLVKW LKGKRRRTNL KTRAHPLCEF GRVGRAGKRM MGPACLTYQR 70 80 90 100 110 120 GVRLAGSEVI HGVLHNPPSP FPAPSKPSAT SATQELDRLM ASLSDFRVQN HLPASGPPQP 130 140 150 160 170 180 PAASPTREGC PSPPGQTSKG SLDTMLGLLQ SDLSRRGVPT QAKGLCGSCN KPIAGQVVTA 190 200 210 220 230 240 LGRAWHPEHF LCSGCSTTLG GSSFFEKDGA PFCPECYFER FSPRCGFCNQ PIRHKMVTAL 250 260 270 280 290 300 GTHWHPEHFC CVSCGEPFGE EGFHEREGRP YCRRDFLQLF APRCQGCQGP ILDNYISALS 310 320 330 340 350 360 ALWHPDCFVC RECLAPFSGG SFFEHEGRPL CENHFHAQRG SLCATCGLPV TGRCVSALGR 370 380 390 RFHPDHFTCT FCLRPLTKGS FQERASKPYC QPCFLKLFG
	Isoform 10 (Alpha-D). Checksum: 79F2BFB888438DDC	FASTA	351	38,669
	10 20 30 40 50 60 MPPSSTLQMK SCLSSHLVKW LKGKRRRTNL KTRAHPLSPS ATSATQELDR LMASLSDFRV 70 80 90 100 110 120 QNHLPASGPP QPPAASPTRE GCPSPPGQTS KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS 130 140 150 160 170 180 CNKPIAGQVV TALGRAWHPE HFLCSGCSTT LGGSSFFEKD GAPFCPECYF ERFSPRCGFC 190 200 210 220 230 240 NQPIRHKMVT ALGTHWHPEH FCCVSCGEPF GEEGFHEREG RPYCRRDFLQ LFAPRCQGCQ 250 260 270 280 290 300 GPILDNYISA LSALWHPDCF VCRECLAPFS GGSFFEHEGR PLCENHFHAQ RGSLCATCGL 310 320 330 340 350 PVTGRCVSAL GRRFHPDHFT CTFCLRPLTK GSFQERASKP YCQPCFLKLF G

References

	« Hide 'large scale' referencesShow '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: 7929412] [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: 10831843] [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: 16219310] [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: 16141072] [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: 15489334] [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: 9422762] [Abstract] Cited for: INTERACTION WITH PTK2 AND PTK2B.
[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: 9756887] [Abstract] Cited for: INTERACTION WITH PTK2.
[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: 9722648] [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: 10092676] [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: 10330411] [Abstract] Cited for: INTERACTION WITH ARHGEF7; GIT2; NCK2; PTK2 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: 9858471] [Abstract] Cited for: INTERACTION WITH CSK; PTK2 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: 10649439] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2.
[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: 11134073] [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: 10848625] [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: 11437454] [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: 11546764] [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: 11463817] [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: 11937715] [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: 12153727] [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: 11779876] [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: 11805099] [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: 12177201] [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: 12631731] [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: 14755691] [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: 16183059] [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: 15687259] [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: 15713747] [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: 16219691] [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: 16291758] [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: 16624805] [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: 16737959] [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: 17233630] [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: 17299801] [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: 17166536] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. 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. BC002049 mRNA. Translation: AAH02049.1. Different initiation. BC056362 mRNA. Translation: AAH56362.1.
IPI	IPI00123274. IPI00652166. IPI00653891. IPI00654035. IPI00828289. IPI00848883. IPI00849982. IPI00850187. IPI00850542. IPI00850722.
PIR	A55071.
RefSeq	NP_033391.1.
UniGene	Mm.3248
3D structure databases
HSSP	HSSP built from PDB template 1NYP based on UniProtKB P48059.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62219. 2 interactions.
PTM databases
PhosphoSite	Q62219.
Genome annotation databases
Ensembl	ENSMUSG00000030782. Mus musculus. [Contig view]
GeneID	21804.
KEGG	mmu:21804.
Organism-specific databases
MGI	MGI:102784. Tgfb1i1.
Phylogenomic databases
HOVERGEN	Q62219.
OMA	Q62219. LETTTSH.
Gene expression databases
ArrayExpress	Q62219.
Bgee	Q62219.
Family and domain databases
InterPro	IPR017305. Leupaxin. IPR001781. Znf_LIM. [Graphical view]
Gene3D	G3DSA:2.10.110.10. Znf_LIM. 3 hits.
Pfam	PF00412. LIM. 4 hits. [Graphical view]
PIRSF	PIRSF037881. Leupaxin. 1 hit.
ProDom	PD000094. LIM. 4 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00132. LIM. 4 hits. [Graphical view]
PROSITE	PS00478. LIM_DOMAIN_1. 4 hits. PS50023. LIM_DOMAIN_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	301180.
SOURCE	Search...

Entry information

Entry name

TGFI1_MOUSE

Accession

Primary (citable) accession number: Q62219
Secondary accession number(s): Q3YBY7 , 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:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)