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Q15654 (TRIP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Thyroid receptor-interacting protein 6

Short name=TR-interacting protein 6
Short name=TRIP-6
Alternative name(s):
Opa-interacting protein 1
Short name=OIP-1
Zyxin-related protein 1
Short name=ZRP-1
Gene names
Name:TRIP6
Synonyms:OIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor. Ref.11 Ref.12 Ref.16 Ref.21

Subunit structure

Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. Interacts with PTPN13. Interacts with SVIL isoform 2. Interacts with LPAR2 but not other LPA receptors. Interacts with PRKAA2. Interacts with MAGI1. Interacts with SCRIB By similarity. Binds to S.typhimurium protein sseI. Ref.2 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Subcellular location

Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytoplasm. Ref.16

Tissue specificity

Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors. Ref.21

Domain

The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI.

Post-translational modification

Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13. Ref.14 Ref.19

Sequence similarities

Belongs to the zyxin/ajuba family.

Contains 3 LIM zinc-binding domains.

Sequence caution

The sequence AAC41740.1 differs from that shown. Reason: Frameshift at position 461.

Ontologies

Keywords
   Biological processCell adhesion
Transcription
Transcription regulation
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfocal adhesion assembly

Non-traceable author statement Ref.12. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.12. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

release of cytoplasmic sequestered NF-kappaB

Inferred from direct assay PubMed 15657077. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from direct assay Ref.12. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functioninterleukin-1 receptor binding

Inferred from direct assay PubMed 15657077. Source: UniProtKB

kinase binding

Inferred from physical interaction PubMed 15657077. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

thyroid hormone receptor binding

Non-traceable author statement Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATN1P542592EBI-742327,EBI-945980
Hoxa1P090223EBI-742327,EBI-3957603From a different organism.
HOXA9P312694EBI-742327,EBI-742314
PPP1R16AQ96I343EBI-742327,EBI-710402
SVILO463855EBI-742327,EBI-6995105From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15654-1)

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: Q15654-2)

The sequence of this isoform differs from the canonical sequence as follows:
     37-106: ALQPHPRVNF...IDLLSSTLAE → VLPGPRGTGG...CVTATRPTGI
     107-476: Missing.
Isoform 3 (identifier: Q15654-3)

The sequence of this isoform differs from the canonical sequence as follows:
     37-80: ALQPHPRVNF...SHGVLQHTQG → GAPCRQGGPS...CVTATRPTGI
     81-476: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Thyroid receptor-interacting protein 6
PRO_0000075908

Regions

Domain279 – 31638LIM zinc-binding 1
Domain339 – 39860LIM zinc-binding 2
Domain399 – 46769LIM zinc-binding 3
Region469 – 4768Interaction with MAGI1 and PTPN13

Amino acid modifications

Modified residue551Phosphotyrosine; by SRC Ref.14 Ref.19
Modified residue921Phosphoserine Ref.15 Ref.22
Modified residue1421Phosphoserine Ref.20

Natural variations

Alternative sequence37 – 10670ALQPH…STLAE → VLPGPRGTGGSGAGVGGVPW STPAHAGAPCRQGGPSPWKP GRRDRLAEQHAGRAEWGSGS CVTATRPTGI in isoform 2.
VSP_047621
Alternative sequence37 – 8044ALQPH…QHTQG → GAPCRQGGPSPWKPGRRDRL AEQHAGRAEWGSGSCVTATR PTGI in isoform 3.
VSP_047622
Alternative sequence81 – 476396Missing in isoform 3.
VSP_047623
Alternative sequence107 – 476370Missing in isoform 2.
VSP_047624
Natural variant1111R → Q. Ref.9
Corresponds to variant rs2437100 [ dbSNP | Ensembl ].
VAR_062262
Natural variant2301V → I. Ref.9
Corresponds to variant rs2075756 [ dbSNP | Ensembl ].
VAR_050171
Natural variant2961L → F. Ref.9
Corresponds to variant rs17855370 [ dbSNP | Ensembl ].
VAR_013309

Experimental info

Mutagenesis1011S → A: Exclusively located in nucleus. Ref.16
Mutagenesis1021S → A: Exclusively located in nucleus. Ref.16
Mutagenesis4741T → A: Reduces interaction with MAGI1. Ref.21
Sequence conflict39 – 402Missing in AAH02680. Ref.9
Sequence conflict1021S → T in AAB62222. Ref.2
Sequence conflict1061E → K in AAB62222. Ref.2
Sequence conflict1351S → C in CAA05080. Ref.1
Sequence conflict310 – 3134CRAQ → MPGP in AAC41740. Ref.10

Secondary structure

................ 476
Helix Strand Turn

Details...

Sequences

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

Last modified May 15, 2002. Version 3.
Checksum: 2BA7C747DF30A8FD

FASTA47650,288
        10         20         30         40         50         60 
MSGPTWLPPK QPEPARAPQG RAIPRGTPGP PPAHGAALQP HPRVNFCPLP SEQCYQAPGG 

        70         80         90        100        110        120 
PEDRGPAWVG SHGVLQHTQG LPADRGGLRP GSLDAEIDLL SSTLAELNGG RGHASRRPDR 

       130        140        150        160        170        180 
QAYEPPPPPA YRTGSLKPNP ASPLPASPYG GPTPASYTTA STPAGPAFPV QVKVAQPVRG 

       190        200        210        220        230        240 
CGPPRRGASQ ASGPLPGPHF PLPGRGEVWG PGYRSQREPG PGAKEEAAGV SGPAGRGRGG 

       250        260        270        280        290        300 
EHGPQVPLSQ PPEDELDRLT KKLVHDMNHP PSGEYFGQCG GCGEDVVGDG AGVVALDRVF 

       310        320        330        340        350        360 
HVGCFVCSTC RAQLRGQHFY AVERRAYCEG CYVATLEKCA TCSQPILDRI LRAMGKAYHP 

       370        380        390        400        410        420 
GCFTCVVCHR GLDGIPFTVD ATSQIHCIED FHRKFAPRCS VCGGAIMPEP GQEETVRIVA 

       430        440        450        460        470 
LDRSFHIGCY KCEECGLLLS SEGECQGCYP LDGHILCKAC SAWRIQELSA TVTTDC 

« Hide

Isoform 2 [UniParc].

Checksum: 33931B3C4BFC4DAB
Show »

FASTA10610,602
Isoform 3 [UniParc].

Checksum: C6244DB637740E54
Show »

FASTA808,277

References

« Hide 'large scale' references
[1]"The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis."
Yi J., Beckerle M.C.
Genomics 49:314-316(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E."
Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.
J. Biol. Chem. 274:20679-20687(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INTERACTION WITH PTPN13.
[3]"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Identification and characterization of novel isoforms of human TRIP6."
Kojima H., Masuhiro Y., Hanazawa S.
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLN-111; ILE-230 AND PHE-296.
Tissue: Cervix, Kidney and Pancreas.
[10]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 310-476 (ISOFORM 1).
[11]"A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters."
Kassel O., Schneider S., Heilbock C., Litfin M., Goettlicher M., Herrlich P.
Genes Dev. 18:2518-2528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"TRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptor."
Xu J., Lai Y.-J., Lin W.-C., Lin F.-T.
J. Biol. Chem. 279:10459-10468(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPAR2, FUNCTION.
[13]"The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins."
Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N., Van de Ven W.J.M.
FEBS Lett. 579:5061-5068(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCRIB.
[14]"c-Src-mediated phosphorylation of TRIP6 regulates its function in lysophosphatidic acid-induced cell migration."
Lai Y.-J., Chen C.-S., Lin W.-C., Lin F.-T.
Mol. Cell. Biol. 25:5859-5868(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-55.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase."
Solaz-Fuster M.C., Gimeno-Alcaniz J.V., Casado M., Sanz P.
Cell. Signal. 18:1702-1712(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKAA2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-101 AND SER-102, FUNCTION.
[17]"Supervillin modulation of focal adhesions involving TRIP6/ZRP-1."
Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J., Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J.
J. Cell Biol. 174:447-458(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SVIL.
[18]"Salmonella typhimurium disseminates within its host by manipulating the motility of infected cells."
Worley M.J., Nieman G.S., Geddes K., Heffron F.
Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SALMONELLA TYPHIMURIUM SSEI.
[19]"PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration."
Lai Y.-J., Lin W.-C., Lin F.-T.
J. Biol. Chem. 282:24381-24387(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN13, PHOSPHORYLATION AT TYR-55.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"TRIP6, a novel molecular partner of the MAGI-1 scaffolding molecule, promotes invasiveness."
Chastre E., Abdessamad M., Kruglov A., Bruyneel E., Bracke M., Di Gioia Y., Beckerle M.C., van Roy F., Kotelevets L.
FASEB J. 23:916-928(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGI1 AND PTPN13, MUTAGENESIS OF THR-474, TISSUE SPECIFICITY, FUNCTION.
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Solution structure of the first and second LIM domain of thyroid receptor interacting protein 6 (TRIP6)."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 279-396.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001902 mRNA. Translation: CAA05080.1.
AF000974 mRNA. Translation: AAB62222.1.
AF093836, AF093834, AF093835 Genomic DNA. Translation: AAD03037.1.
AF312032 Genomic DNA. Translation: AAK21007.1.
AB628086 mRNA. Translation: BAK20497.1.
AB628087 mRNA. Translation: BAK20498.1.
AK291906 mRNA. Translation: BAF84595.1.
AC011895 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23817.1.
CH471091 Genomic DNA. Translation: EAW76472.1.
BC002680 mRNA. Translation: AAH02680.1.
BC004249 mRNA. Translation: AAH04249.1.
BC004999 mRNA. Translation: AAH04999.1.
BC021540 mRNA. Translation: AAH21540.1.
BC028985 mRNA. Translation: AAH28985.1.
L40374 mRNA. Translation: AAC41740.1. Frameshift.
RefSeqNP_003293.2. NM_003302.2.
UniGeneHs.534360.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X61NMR-A279-337[»]
2DLONMR-A329-396[»]
ProteinModelPortalQ15654.
SMRQ15654. Positions 277-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113056. 68 interactions.
IntActQ15654. 42 interactions.
MINTMINT-1366827.
STRING9606.ENSP00000200457.

PTM databases

PhosphoSiteQ15654.

Polymorphism databases

DMDM20981729.

Proteomic databases

PaxDbQ15654.
PeptideAtlasQ15654.
PRIDEQ15654.

Protocols and materials databases

DNASU7205.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000200457; ENSP00000200457; ENSG00000087077. [Q15654-1]
ENST00000417475; ENSP00000413817; ENSG00000087077. [Q15654-2]
ENST00000437505; ENSP00000410736; ENSG00000087077. [Q15654-3]
GeneID7205.
KEGGhsa:7205.
UCSCuc003uww.3. human. [Q15654-1]

Organism-specific databases

CTD7205.
GeneCardsGC07P100464.
H-InvDBHIX0167828.
HGNCHGNC:12311. TRIP6.
HPACAB046454.
CAB046460.
HPA052813.
MIM602933. gene.
neXtProtNX_Q15654.
PharmGKBPA36989.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279196.
HOVERGENHBG093602.
InParanoidQ15654.
KOK12792.
OrthoDBEOG7992Q6.
PhylomeDBQ15654.
TreeFamTF320310.

Enzyme and pathway databases

SignaLinkQ15654.

Gene expression databases

ArrayExpressQ15654.
BgeeQ15654.
CleanExHS_TRIP6.
GenevestigatorQ15654.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 3 hits.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIP6. human.
EvolutionaryTraceQ15654.
GeneWikiTRIP6.
GenomeRNAi7205.
NextBio28238.
PROQ15654.
SOURCESearch...

Entry information

Entry nameTRIP6_HUMAN
AccessionPrimary (citable) accession number: Q15654
Secondary accession number(s): A4D2E7 expand/collapse secondary AC list , F2ZC07, F2ZC08, O15170, O15275, Q9BTB2, Q9BUE5, Q9BXP3, Q9UNT4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 15, 2002
Last modified: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM