SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q15654

- TRIP6_HUMAN

UniProt

Q15654 - TRIP6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Thyroid receptor-interacting protein 6
Gene
TRIP6, OIP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

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
Complete GO annotation...

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 6
PRO_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 PTPN13.2 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.8 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

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.

Miscellaneous databases

EvolutionaryTraceiQ15654.

Family & Domainsi

Domains and Repeats

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

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.

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.
VSP_047621Add
BLAST
Alternative sequencei37 – 8044ALQPH…QHTQG → GAPCRQGGPSPWKPGRRDRL AEQHAGRAEWGSGSCVTATR PTGI in isoform 3.
VSP_047622Add
BLAST
Alternative sequencei81 – 476396Missing in isoform 3.
VSP_047623Add
BLAST
Alternative sequencei107 – 476370Missing in isoform 2.
VSP_047624Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 402Missing in AAH02680. 1 Publication
Sequence conflicti102 – 1021S → T in AAB62222. 1 Publication
Sequence conflicti106 – 1061E → K in AAB62222. 1 Publication
Sequence conflicti135 – 1351S → C in CAA05080. 1 Publication
Sequence conflicti310 – 3134CRAQ → MPGP in AAC41740. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 135 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

Similar proteinsi