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Q15654

- TRIP6_HUMAN

UniProt

Q15654 - TRIP6_HUMAN

Protein

Thyroid receptor-interacting protein 6

Gene

TRIP6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (15 May 2002)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. interleukin-1 receptor binding Source: UniProtKB
    2. kinase binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. thyroid hormone receptor binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. focal adhesion assembly Source: UniProtKB
    2. positive regulation of cell migration Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. release of cytoplasmic sequestered NF-kappaB Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ15654.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:TRIP6
    Synonyms:OIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:12311. TRIP6.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell junctionfocal adhesion 1 Publication. Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Shuttles between nucleus and cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB-SubCell
    3. focal adhesion Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011S → A: Exclusively located in nucleus. 1 Publication
    Mutagenesisi102 – 1021S → A: Exclusively located in nucleus. 1 Publication
    Mutagenesisi474 – 4741T → A: Reduces interaction with MAGI1. 1 Publication

    Organism-specific databases

    PharmGKBiPA36989.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Thyroid receptor-interacting protein 6PRO_0000075908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphotyrosine; by SRC2 Publications
    Modified residuei92 – 921Phosphoserine2 Publications
    Modified residuei142 – 1421Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15654.
    PaxDbiQ15654.
    PeptideAtlasiQ15654.
    PRIDEiQ15654.

    PTM databases

    PhosphoSiteiQ15654.

    Expressioni

    Tissue specificityi

    Abundantly expressed in kidney, liver and lung. Lower levels in heart, placenta and pancreas. Expressed in colonic epithelial cells. Up-regulated in colonic tumors.1 Publication

    Gene expression databases

    ArrayExpressiQ15654.
    BgeeiQ15654.
    CleanExiHS_TRIP6.
    GenevestigatoriQ15654.

    Organism-specific databases

    HPAiCAB046454.
    CAB046460.
    HPA052813.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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.

    Protein-protein interaction databases

    BioGridi113056. 68 interactions.
    IntActiQ15654. 42 interactions.
    MINTiMINT-1366827.
    STRINGi9606.ENSP00000200457.

    Structurei

    Secondary structure

    1
    476
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi280 – 2823
    Beta strandi288 – 2903
    Beta strandi296 – 3005
    Turni302 – 3043
    Beta strandi308 – 3103
    Beta strandi319 – 3246
    Beta strandi326 – 3283
    Helixi329 – 3379

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X61NMR-A279-337[»]
    2DLONMR-A329-396[»]
    ProteinModelPortaliQ15654.
    SMRiQ15654. Positions 251-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15654.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini279 – 31638LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 39860LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini399 – 46769LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni469 – 4768Interaction with MAGI1 and PTPN13

    Domaini

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

    Sequence similaritiesi

    Belongs to the zyxin/ajuba family.Curated
    Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG279196.
    HOVERGENiHBG093602.
    InParanoidiQ15654.
    KOiK12792.
    OrthoDBiEOG7992Q6.
    PhylomeDBiQ15654.
    TreeFamiTF320310.

    Family and domain databases

    Gene3Di2.10.110.10. 3 hits.
    InterProiIPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 3 hits.
    [Graphical view]
    SMARTiSM00132. LIM. 3 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15654-1) [UniParc]FASTAAdd to Basket

    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

    MSGPTWLPPK QPEPARAPQG RAIPRGTPGP PPAHGAALQP HPRVNFCPLP    50
    SEQCYQAPGG PEDRGPAWVG SHGVLQHTQG LPADRGGLRP GSLDAEIDLL 100
    SSTLAELNGG RGHASRRPDR QAYEPPPPPA YRTGSLKPNP ASPLPASPYG 150
    GPTPASYTTA STPAGPAFPV QVKVAQPVRG CGPPRRGASQ ASGPLPGPHF 200
    PLPGRGEVWG PGYRSQREPG PGAKEEAAGV SGPAGRGRGG EHGPQVPLSQ 250
    PPEDELDRLT KKLVHDMNHP PSGEYFGQCG GCGEDVVGDG AGVVALDRVF 300
    HVGCFVCSTC RAQLRGQHFY AVERRAYCEG CYVATLEKCA TCSQPILDRI 350
    LRAMGKAYHP GCFTCVVCHR GLDGIPFTVD ATSQIHCIED FHRKFAPRCS 400
    VCGGAIMPEP GQEETVRIVA LDRSFHIGCY KCEECGLLLS SEGECQGCYP 450
    LDGHILCKAC SAWRIQELSA TVTTDC 476
    Length:476
    Mass (Da):50,288
    Last modified:May 15, 2002 - v3
    Checksum:i2BA7C747DF30A8FD
    GO
    Isoform 2 (identifier: Q15654-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:106
    Mass (Da):10,602
    Checksum:i33931B3C4BFC4DAB
    GO
    Isoform 3 (identifier: Q15654-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:80
    Mass (Da):8,277
    Checksum:iC6244DB637740E54
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 402Missing in AAH02680. (PubMed:15489334)Curated
    Sequence conflicti102 – 1021S → T in AAB62222. (PubMed:10400701)Curated
    Sequence conflicti106 – 1061E → K in AAB62222. (PubMed:10400701)Curated
    Sequence conflicti135 – 1351S → C in CAA05080. (PubMed:9598321)Curated
    Sequence conflicti310 – 3134CRAQ → MPGP in AAC41740. (PubMed:7776974)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111R → Q.1 Publication
    Corresponds to variant rs2437100 [ dbSNP | Ensembl ].
    VAR_062262
    Natural varianti230 – 2301V → I.1 Publication
    Corresponds to variant rs2075756 [ dbSNP | Ensembl ].
    VAR_050171
    Natural varianti296 – 2961L → F.1 Publication
    Corresponds to variant rs17855370 [ dbSNP | Ensembl ].
    VAR_013309

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 10670ALQPH…STLAE → VLPGPRGTGGSGAGVGGVPW STPAHAGAPCRQGGPSPWKP GRRDRLAEQHAGRAEWGSGS CVTATRPTGI in isoform 2. 1 PublicationVSP_047621Add
    BLAST
    Alternative sequencei37 – 8044ALQPH…QHTQG → GAPCRQGGPSPWKPGRRDRL AEQHAGRAEWGSGSCVTATR PTGI in isoform 3. CuratedVSP_047622Add
    BLAST
    Alternative sequencei81 – 476396Missing in isoform 3. CuratedVSP_047623Add
    BLAST
    Alternative sequencei107 – 476370Missing in isoform 2. 1 PublicationVSP_047624Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5708.1. [Q15654-1]
    RefSeqiNP_003293.2. NM_003302.2. [Q15654-1]
    UniGeneiHs.534360.

    Genome annotation databases

    EnsembliENST00000200457; ENSP00000200457; ENSG00000087077. [Q15654-1]
    ENST00000417475; ENSP00000413817; ENSG00000087077. [Q15654-2]
    ENST00000437505; ENSP00000410736; ENSG00000087077. [Q15654-3]
    GeneIDi7205.
    KEGGihsa:7205.
    UCSCiuc003uww.3. human. [Q15654-1]

    Polymorphism databases

    DMDMi20981729.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS5708.1. [Q15654-1 ]
    RefSeqi NP_003293.2. NM_003302.2. [Q15654-1 ]
    UniGenei Hs.534360.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X61 NMR - A 279-337 [» ]
    2DLO NMR - A 329-396 [» ]
    ProteinModelPortali Q15654.
    SMRi Q15654. Positions 251-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113056. 68 interactions.
    IntActi Q15654. 42 interactions.
    MINTi MINT-1366827.
    STRINGi 9606.ENSP00000200457.

    PTM databases

    PhosphoSitei Q15654.

    Polymorphism databases

    DMDMi 20981729.

    Proteomic databases

    MaxQBi Q15654.
    PaxDbi Q15654.
    PeptideAtlasi Q15654.
    PRIDEi Q15654.

    Protocols and materials databases

    DNASUi 7205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000200457 ; ENSP00000200457 ; ENSG00000087077 . [Q15654-1 ]
    ENST00000417475 ; ENSP00000413817 ; ENSG00000087077 . [Q15654-2 ]
    ENST00000437505 ; ENSP00000410736 ; ENSG00000087077 . [Q15654-3 ]
    GeneIDi 7205.
    KEGGi hsa:7205.
    UCSCi uc003uww.3. human. [Q15654-1 ]

    Organism-specific databases

    CTDi 7205.
    GeneCardsi GC07P100464.
    H-InvDB HIX0167828.
    HGNCi HGNC:12311. TRIP6.
    HPAi CAB046454.
    CAB046460.
    HPA052813.
    MIMi 602933. gene.
    neXtProti NX_Q15654.
    PharmGKBi PA36989.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279196.
    HOVERGENi HBG093602.
    InParanoidi Q15654.
    KOi K12792.
    OrthoDBi EOG7992Q6.
    PhylomeDBi Q15654.
    TreeFami TF320310.

    Enzyme and pathway databases

    SignaLinki Q15654.

    Miscellaneous databases

    ChiTaRSi TRIP6. human.
    EvolutionaryTracei Q15654.
    GeneWikii TRIP6.
    GenomeRNAii 7205.
    NextBioi 28238.
    PROi Q15654.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15654.
    Bgeei Q15654.
    CleanExi HS_TRIP6.
    Genevestigatori Q15654.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 3 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiTRIP6_HUMAN
    AccessioniPrimary (citable) accession number: Q15654
    Secondary accession number(s): A4D2E7
    , F2ZC07, F2ZC08, O15170, O15275, Q9BTB2, Q9BUE5, Q9BXP3, Q9UNT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3