Reviewed, UniProtKB/Swiss-Prot O43294 (TGFI1_HUMAN)

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

Gene names

Name:	TGFB1I1
Synonyms:	ARA55

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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.5 Ref.13 Ref.15 Ref.17 Ref.18 Ref.22 Ref.24 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.34 Ref.36
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 By similarity. Interacts with AR/androgen receptor in a ligand-dependent manner. Interacts with CSK, LYN, MAPK15, NR3C1, PPARG, PTK2, PTK2B, SLC6A3, SLC6A4, SMAD3, SRC and talin.
Subcellular location	Cell junction › focal adhesion. Nucleus matrix. Cytoplasm › cytoskeleton. Note: Associated with the actin cytoskeleton; colocalizes with stress fibers. Ref.18 Ref.24 Ref.28 Ref.36 Ref.7 Ref.10 Ref.11 Ref.21
Tissue specificity	Expressed in platelets, smooth muscle and prostate stromal cells (at protein level). Ref.1 Ref.28 Ref.34 Ref.36 Ref.7 Ref.10 Ref.9 Ref.20 Ref.23
Induction	Up-regulated by TNF-alpha and hydrogen peroxide. Ref.12 Ref.14
Domain	The LIM zinc-binding domains mediate glucocorticoid receptor coactivation and interaction with AR, CRIP2, ILK, LIMS1, NR3C1, PPARG, TCF3, TCF7L2, SLC6A3 and SMAD3. The LIM zinc-binding 2 and LIM zinc-binding 3 domains mediate targeting to focal adhesions and actin stress fibers. The LIM zinc-binding 3 and LIM zinc-binding 4 domains mediate interaction with TRAF4 and MAPK15. The LIM zinc-binding 4 domain mediates interaction with HSPB1, homooligomerization and targeting to the nuclear matrix. The LIM zinc-binding 3 domain mediates interaction with PTPN12. The LD (leucine and aspartate-rich) motif 3 mediates interaction with GIT1 and functions as a nuclear export signal.
Post-translational modification	Phosphorylated by gonadotropin-releasing hormone-activated SRC. Ref.17 Ref.34 Ref.10 Ref.8 Ref.29 Ref.33 Ref.35 Ref.37
Sequence similarities	Belongs to the paxillin family. Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
Biological process	Differentiation Wnt signaling pathway
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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 androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB cell adhesion Ref.4 Traceable author statement. Source: ProtInc cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Traceable author statement. Source: ProtInc negative regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of epithelial to mesenchymal transition Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB positive regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: UniProtKB transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc ubiquitin-dependent SMAD protein catabolic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from direct assay. Source: HPA focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	I-SMAD binding Inferred from physical interaction. Source: UniProtKB androgen receptor binding Ref.1 Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Ref.1 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNA1	P78396	1	EBI-1051449,EBI-375065
PTK2	Q05397	1	EBI-1051449,EBI-702142
VHL	P40337	1	EBI-1051449,EBI-301246

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43294-1)

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

Isoform 2 (identifier: O43294-2)

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

Sequence annotation (Features)

	Feature 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_0000291582
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
	Region	1 – 200	200	Transcription activation By similarity
	Region	83 – 136	54	Interaction with PTK2 By similarity
	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 Ref.37
	Modified residue	38	1	Phosphotyrosine By similarity
	Modified residue	60	1	Phosphotyrosine; by FAK2 and FYN Ref.17 Ref.8
	Modified residue	68	1	Phosphoserine Ref.29
	Modified residue	122	1	Phosphoserine Ref.35
	Modified residue	192	1	Phosphoserine Ref.37
	Modified residue	194	1	Phosphoserine Ref.37
Natural variations
	Alternative sequence	1 – 17	17	Missing in isoform 2.		VSP_026183
	Natural variant	129	1	Q → H: dbSNP rs45475699. Ref.2		VAR_032831
Experimental info
	Mutagenesis	60	1	Y → F: Prevents phosphorylation by FAK2 and FYN. Prevents interaction with CSK. Ref.8
	Mutagenesis	338 – 342	5	FLQLF → ALQAA: Loss of interaction with AR; when associated with 456-A--A-460. Ref.19
	Mutagenesis	369	1	C → S: Loss of AR coactivation; when associated with S-372. Ref.30
	Mutagenesis	372	1	C → S: Loss of AR coactivation; when associated with S-369. Ref.30
	Mutagenesis	428	1	H → S: Loss of AR coactivation; when associated with S-431. Ref.30
	Mutagenesis	431	1	C → S: Loss of AR coactivation; when associated with S-428. Ref.30
	Mutagenesis	456 – 460	5	FLKLF → ALKAA: Loss of interaction with AR; when associated with 338-A--A-342. Ref.19
	Sequence conflict	166	1	S → P in AAD22552. Ref.1
	Sequence conflict	200	1	G → A in AAD22552. Ref.1
	Sequence conflict	363	1	A → L in AAD22552. Ref.1
	Sequence conflict	405 – 406	2	CA → WP in AAD22552. Ref.1
	Sequence conflict	430	1	T → A in AAD22552. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: D2C7C32C3FD2C496	FASTA	461	49,814
	10 20 30 40 50 60 MEDLDALLSD LETTTSHMPR SGAPKERPAE PLTPPPSYGH QPQTGSGESS GASGDKDHLY 70 80 90 100 110 120 STVCKPRSPK PAAPAAPPFS SSSGVLGTGL CELDRLLQEL NATQFNITDE IMSQFPSSKV 130 140 150 160 170 180 ASGEQKEDQS EDKKRPSLPS SPSPGLPKAS ATSATLELDR LMASLSDFRV QNHLPASGPT 190 200 210 220 230 240 QPPVVSSTNE GSPSPPEPTG KGSLDTMLGL LQSDLSRRGV PTQAKGLCGS CNKPIAGQVV 250 260 270 280 290 300 TALGRAWHPE HFVCGGCSTA LGGSSFFEKD GAPFCPECYF ERFSPRCGFC NQPIRHKMVT 310 320 330 340 350 360 ALGTHWHPEH FCCVSCGEPF GDEGFHEREG RPYCRRDFLQ LFAPRCQGCQ GPILDNYISA 370 380 390 400 410 420 LSALWHPDCF VCRECFAPFS GGSFFEHEGR PLCENHFHAR RGSLCATCGL PVTGRCVSAL 430 440 450 460 GRRFHPDHFT CTFCLRPLTK GSFQERAGKP YCQPCFLKLF G
	Isoform 2. Checksum: EC9E92DADE7156B4	FASTA	444	47,941
	10 20 30 40 50 60 MPRSGAPKER PAEPLTPPPS YGHQPQTGSG ESSGASGDKD HLYSTVCKPR SPKPAAPAAP 70 80 90 100 110 120 PFSSSSGVLG TGLCELDRLL QELNATQFNI TDEIMSQFPS SKVASGEQKE DQSEDKKRPS 130 140 150 160 170 180 LPSSPSPGLP KASATSATLE LDRLMASLSD FRVQNHLPAS GPTQPPVVSS TNEGSPSPPE 190 200 210 220 230 240 PTGKGSLDTM LGLLQSDLSR RGVPTQAKGL CGSCNKPIAG QVVTALGRAW HPEHFVCGGC 250 260 270 280 290 300 STALGGSSFF EKDGAPFCPE CYFERFSPRC GFCNQPIRHK MVTALGTHWH PEHFCCVSCG 310 320 330 340 350 360 EPFGDEGFHE REGRPYCRRD FLQLFAPRCQ GCQGPILDNY ISALSALWHP DCFVCRECFA 370 380 390 400 410 420 PFSGGSFFEH EGRPLCENHF HARRGSLCAT CGLPVTGRCV SALGRRFHPD HFTCTFCLRP 430 440 LTKGSFQERA GKPYCQPCFL KLFG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate." Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A., Chang C. J. Biol. Chem. 274:8316-8321(1999) [PubMed: 10075738] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH AR, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[2]	NIEHS SNPs program Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-129.
[3]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-461 (ISOFORM 1). Tissue: Muscle, Ovary and Uterus.
[4]	"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: NUCLEOTIDE SEQUENCE [MRNA] OF 2-461 (ISOFORM 1), INTERACTION WITH PTK2 AND PTK2B. Tissue: Hippocampus.
[5]	"Induction of senescence-like phenotypes by forced expression of hic-5, which encodes a novel LIM motif protein, in immortalized human fibroblasts." Shibanuma M., Mochizuki E., Maniwa R., Mashimo J.I., Nishiya N., Imai S., Takano T., Oshimura M., Nose K. Mol. Cell. Biol. 17:1224-1235(1997) [PubMed: 9032249] [Abstract] Cited for: FUNCTION.
[6]	"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.
[7]	"Recruitment of the LIM protein hic-5 to focal contacts of human platelets." Hagmann J., Grob M., Welman A., van Willigen G., Burger M.M. J. Cell Sci. 111:2181-2188(1998) [PubMed: 9664039] [Abstract] Cited for: INTERACTION WITH PTK2 AND TALIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]	"Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn." Ishino M., Aoto H., Sasaski H., Suzuki R., Sasaki T. FEBS Lett. 474:179-183(2000) [PubMed: 10838081] [Abstract] Cited for: MUTAGENESIS OF TYR-60, PHOSPHORYLATION AT TYR-60, INTERACTION WITH CSK AND PTK2B.
[9]	"Molecular cloning of human Hic-5, a potential regulator involved in signal transduction and cellular senescence." Zhang J., Zhang L.-X., Meltzer P.S., Barrett J.C., Trent J.M. Mol. Carcinog. 27:177-183(2000) [PubMed: 10708479] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Involvement of Hic-5 in platelet activation: integrin alphaIIbbeta3-dependent tyrosine phosphorylation and association with proline-rich tyrosine kinase 2." Osada M., Ohmori T., Yatomi Y., Satoh K., Hosogaya S., Ozaki Y. Biochem. J. 355:691-697(2001) [PubMed: 11311131] [Abstract] Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH PTK2B, SUBCELLULAR LOCATION.
[11]	"CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk." Oda A., Ochs H.D., Lasky L.A., Spencer S., Ozaki K., Fujihara M., Handa M., Ikebuchi K., Ikeda H. Blood 97:2633-2639(2001) [PubMed: 11313252] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Potential anti-androgenic activity of roxithromycin in skin." Inui S., Nakajima T., Fukuzato Y., Fujimoto N., Chang C., Yoshikawa K., Itami S. J. Dermatol. Sci. 27:147-151(2001) [PubMed: 11532379] [Abstract] Cited for: INDUCTION BY HYDROGEN PEROXIDE.
[13]	"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.
[14]	"Different expression of androgen receptor coactivators in human prostate." Fujimoto N., Mizokami A., Harada S., Matsumoto T. Urology 58:289-294(2001) [PubMed: 11489729] [Abstract] Cited for: INDUCTION BY TNF-ALPHA.
[15]	"Transcriptional activation of the c-fos gene by a LIM protein, Hic-5." Kim-Kaneyama J.-R., Shibanuma M., Nose K. Biochem. Biophys. Res. Commun. 299:360-365(2002) [PubMed: 12445807] [Abstract] Cited for: FUNCTION.
[16]	"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: INTERACTION WITH GIT1.
[17]	"Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator." Wang X., Yang Y., Guo X., Sampson E.R., Hsu C.-L., Tsai M.-Y., Yeh S., Wu G., Guo Y., Chang C. J. Biol. Chem. 277:15426-15431(2002) [PubMed: 11856738] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTK2B, PHOSPHORYLATION AT TYR-60 BY FAK2.
[18]	"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: FUNCTION, INTERACTION WITH SLC6A3, SUBCELLULAR LOCATION.
[19]	"The use of phage display technique for the isolation of androgen receptor interacting peptides with (F/W)XXL(F/W) and FXXLY new signature motifs." Hsu C.-L., Chen Y.-L., Yeh S., Ting H.-J., Hu Y.-C., Lin H., Wang X., Chang C. J. Biol. Chem. 278:23691-23698(2003) [PubMed: 12714604] [Abstract] Cited for: INTERACTION WITH AR, MUTAGENESIS OF 338-PHE--PHE-342 AND 456-PHE--PHE-460.
[20]	"Expression of the LIM proteins paxillin and Hic-5 in human tissues." Yuminamochi T., Yatomi Y., Osada M., Ohmori T., Ishii Y., Nakazawa K., Hosogaya S., Ozaki Y. J. Histochem. Cytochem. 51:513-521(2003) [PubMed: 12642630] [Abstract] Cited for: TISSUE SPECIFICITY.
[21]	"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.
[22]	"Inactivation of androgen receptor coregulator ARA55 inhibits androgen receptor activity and agonist effect of antiandrogens in prostate cancer cells." Rahman M.M., Miyamoto H., Lardy H., Chang C. Proc. Natl. Acad. Sci. U.S.A. 100:5124-5129(2003) [PubMed: 12700349] [Abstract] Cited for: FUNCTION, SUBUNIT.
[23]	"Expression of androgen receptor coactivators in normal and cancer prostate tissues and cultured cell lines." Mestayer C., Blanchere M., Jaubert F., Dufour B., Mowszowicz I. Prostate 56:192-200(2003) [PubMed: 12772188] [Abstract] Cited for: TISSUE SPECIFICITY.
[24]	"Distinct LIM domains of Hic-5/ARA55 are required for nuclear matrix targeting and glucocorticoid receptor binding and coactivation." Guerrero-Santoro J., Yang L., Stallcup M.R., DeFranco D.B. J. Cell. Biochem. 92:810-819(2004) [PubMed: 15211577] [Abstract] Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
[25]	"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: INTERACTION WITH PPARG.
[26]	"Novel function of androgen receptor-associated protein 55/Hic-5 as a negative regulator of Smad3 signaling." Wang H., Song K., Sponseller T.L., Danielpour D. J. Biol. Chem. 280:5154-5162(2005) [PubMed: 15561701] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD3.
[27]	"Subcellular targeting of oxidants during endothelial cell migration." Wu R.F., Xu Y.C., Ma Z., Nwariaku F.E., Sarosi G.A. Jr., Terada L.S. J. Cell Biol. 171:893-904(2005) [PubMed: 16330715] [Abstract] Cited for: INTERACTION WITH TRAF4.
[28]	"Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells." Heitzer M.D., DeFranco D.B. Cancer Res. 66:7326-7333(2006) [PubMed: 16849583] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[29]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, MASS SPECTROMETRY.
[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: FUNCTION, INTERACTION WITH MAPK15, MUTAGENESIS OF CYS-369; CYS-372; HIS-428 AND CYS-431.
[31]	"Serotonin-, protein kinase C-, and Hic-5-associated redistribution of the platelet serotonin transporter." Carneiro A.M.D., Blakely R.D. J. Biol. Chem. 281:24769-24780(2006) [PubMed: 16803896] [Abstract] Cited for: FUNCTION, INTERACTION WITH SLC6A4.
[32]	"Mechanism of action of Hic-5/androgen receptor activator 55, a LIM domain-containing nuclear receptor coactivator." Heitzer M.D., DeFranco D.B. Mol. Endocrinol. 20:56-64(2006) [PubMed: 16141357] [Abstract] Cited for: FUNCTION.
[33]	"Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5." Maudsley S., Davidson L., Pawson A.J., Freestone S.H., Lopez de Maturana R., Thomson A.A., Millar R.P. Neuroendocrinology 84:285-300(2006) [PubMed: 17202804] [Abstract] Cited for: INTERACTION WITH AR; PTK2B AND SRC, PHOSPHORYLATION.
[34]	"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 AND LYN.
[35]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY.
[36]	"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, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[37]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-192 AND SER-194, MASS SPECTROMETRY.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF116343 mRNA. Translation: AAD22552.1. DQ309025 Genomic DNA. Translation: ABB96286.1. BC001507 mRNA. Translation: AAH01507.2. BC001830 mRNA. Translation: AAH01830.1. BC017288 mRNA. Translation: AAH17288.1. BC032545 mRNA. Translation: AAH32545.1. Different initiation. AB007836 mRNA. Translation: BAA24799.1.
IPI	IPI00396399. IPI00761017.
RefSeq	NP_001035919.1. NP_057011.2.
UniGene	Hs.513530
3D structure databases
HSSP	HSSP built from PDB template 1NYP based on UniProtKB P48059.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43294. 4 interactions.
PTM databases
PhosphoSite	O43294.
Proteomic databases
PRIDE	O43294.
Genome annotation databases
Ensembl	ENSG00000140682. Homo sapiens. [Contig view]
GeneID	7041.
KEGG	hsa:7041.
Organism-specific databases
GeneCards	GC16P031390.
H-InvDB	HIX0012992.
HGNC	HGNC:11767. TGFB1I1.
HPA	HPA006376.
MIM	602353. gene.
PharmGKB	PA36481.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O43294.
HOVERGEN	O43294.
OMA	O43294. LETTTSH.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_pathway. Coregulation of Androgen receptor activity.
Gene expression databases
ArrayExpress	O43294.
Bgee	O43294.
CleanEx	HS_TGFB1I1.
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	27511.
SOURCE	Search...

Entry information

Entry name

TGFI1_HUMAN

Accession

Primary (citable) accession number: O43294
Secondary accession number(s): Q9BPW3, Q9Y2V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	June 16, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)