Q15654 · TRIP6_HUMAN
- ProteinThyroid receptor-interacting protein 6
- GeneTRIP6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids476 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | stress fiber | |
Molecular Function | interleukin-1 receptor binding | |
Molecular Function | kinase binding | |
Molecular Function | metal ion binding | |
Molecular Function | nuclear thyroid hormone receptor binding | |
Molecular Function | RNA binding | |
Biological Process | chordate embryonic development | |
Biological Process | focal adhesion assembly | |
Biological Process | positive regulation of cell migration | |
Biological Process | positive regulation of non-canonical NF-kappaB signal transduction | |
Biological Process | signal transduction |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThyroid receptor-interacting protein 6
- Short namesTR-interacting protein 6; TRIP-6
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15654
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 101 | Exclusively located in nucleus. | ||||
Sequence: S → A | ||||||
Mutagenesis | 102 | Exclusively located in nucleus. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_062262 | 111 | in dbSNP:rs2437100 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_050171 | 230 | in dbSNP:rs2075756 | |||
Sequence: V → I | ||||||
Natural variant | VAR_013309 | 296 | in dbSNP:rs17855370 | |||
Sequence: L → F | ||||||
Mutagenesis | 474 | Reduces interaction with MAGI1. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 617 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000075908 | 1-476 | UniProt | Thyroid receptor-interacting protein 6 | |||
Sequence: MSGPTWLPPKQPEPARAPQGRAIPRGTPGPPPAHGAALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGLRPGSLDAEIDLLSSTLAELNGGRGHASRRPDRQAYEPPPPPAYRTGSLKPNPASPLPASPYGGPTPASYTTASTPAGPAFPVQVKVAQPVRGCGPPRRGASQASGPLPGPHFPLPGRGEVWGPGYRSQREPGPGAKEEAAGVSGPAGRGRGGEHGPQVPLSQPPEDELDRLTKKLVHDMNHPPSGEYFGQCGGCGEDVVGDGAGVVALDRVFHVGCFVCSTCRAQLRGQHFYAVERRAYCEGCYVATLEKCATCSQPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC | |||||||
Modified residue | 25 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 25 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 55 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 92 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 111 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 123 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 142 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 179 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 186 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 189 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 205 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 236 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 238 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 249 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 424 | PRIDE | Phosphoserine | ||||
Sequence: S |
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (PubMed:14688263).
Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain) (PubMed:10400701, PubMed:10826496, PubMed:17591779, PubMed:19017743).
Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain) (PubMed:10826496).
Found in a complex with PTPN13 and PDLIM4 (By similarity).
Interacts with SVIL isoform 2 (PubMed:16880273).
Interacts with LPAR2 but not other LPA receptors (PubMed:14688263).
Interacts with PRKAA2 (PubMed:16624523).
Interacts with MAGI1 (PubMed:19017743).
Interacts with SCRIB (PubMed:16137684).
In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609).
Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain) (PubMed:10400701, PubMed:10826496, PubMed:17591779, PubMed:19017743).
Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain) (PubMed:10826496).
Found in a complex with PTPN13 and PDLIM4 (By similarity).
Interacts with SVIL isoform 2 (PubMed:16880273).
Interacts with LPAR2 but not other LPA receptors (PubMed:14688263).
Interacts with PRKAA2 (PubMed:16624523).
Interacts with MAGI1 (PubMed:19017743).
Interacts with SCRIB (PubMed:16137684).
In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Pro residues | ||||
Sequence: MSGPTWLPPKQPEPA | ||||||
Region | 1-93 | Disordered | ||||
Sequence: MSGPTWLPPKQPEPARAPQGRAIPRGTPGPPPAHGAALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGLRPGSL | ||||||
Region | 108-253 | Disordered | ||||
Sequence: NGGRGHASRRPDRQAYEPPPPPAYRTGSLKPNPASPLPASPYGGPTPASYTTASTPAGPAFPVQVKVAQPVRGCGPPRRGASQASGPLPGPHFPLPGRGEVWGPGYRSQREPGPGAKEEAAGVSGPAGRGRGGEHGPQVPLSQPPE | ||||||
Domain | 279-316 | LIM zinc-binding 1 | ||||
Sequence: CGGCGEDVVGDGAGVVALDRVFHVGCFVCSTCRAQLRG | ||||||
Domain | 339-398 | LIM zinc-binding 2 | ||||
Sequence: CATCSQPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPR | ||||||
Domain | 399-467 | LIM zinc-binding 3 | ||||
Sequence: CSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQE | ||||||
Region | 469-476 | Interaction with MAGI1 and PTPN13 | ||||
Sequence: SATVTTDC |
Domain
The LIM zinc-binding domains mediate interaction with LPAR2 and with S.typhimurium protein sseI.
Sequence similarities
Belongs to the zyxin/ajuba family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
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.
- Name1
- Length476
- Mass (Da)50,288
- Last updated2002-05-15 v3
- Checksum2BA7C747DF30A8FD
Q15654-2
- Name2
Q15654-3
- Name3
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7BZE2 | H7BZE2_HUMAN | TRIP6 | 215 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Pro residues | ||||
Sequence: MSGPTWLPPKQPEPA | ||||||
Alternative sequence | VSP_047622 | 37-80 | in isoform 3 | |||
Sequence: ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQG → GAPCRQGGPSPWKPGRRDRLAEQHAGRAEWGSGSCVTATRPTGI | ||||||
Alternative sequence | VSP_047621 | 37-106 | in isoform 2 | |||
Sequence: ALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGLRPGSLDAEIDLLSSTLAE → VLPGPRGTGGSGAGVGGVPWSTPAHAGAPCRQGGPSPWKPGRRDRLAEQHAGRAEWGSGSCVTATRPTGI | ||||||
Sequence conflict | 39-40 | in Ref. 9; AAH02680 | ||||
Sequence: Missing | ||||||
Alternative sequence | VSP_047623 | 81-476 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 102 | in Ref. 2; AAB62222 | ||||
Sequence: S → T | ||||||
Sequence conflict | 106 | in Ref. 2; AAB62222 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_047624 | 107-476 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 135 | in Ref. 1; CAA05080 | ||||
Sequence: S → C | ||||||
Sequence conflict | 310-313 | in Ref. 10; AAC41740 | ||||
Sequence: CRAQ → MPGP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ001902 EMBL· GenBank· DDBJ | CAA05080.1 EMBL· GenBank· DDBJ | mRNA | ||
AF000974 EMBL· GenBank· DDBJ | AAB62222.1 EMBL· GenBank· DDBJ | mRNA | ||
AF093836 EMBL· GenBank· DDBJ | AAD03037.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF093834 EMBL· GenBank· DDBJ | AAD03037.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF093835 EMBL· GenBank· DDBJ | AAD03037.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF312032 EMBL· GenBank· DDBJ | AAK21007.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB628086 EMBL· GenBank· DDBJ | BAK20497.1 EMBL· GenBank· DDBJ | mRNA | ||
AB628087 EMBL· GenBank· DDBJ | BAK20498.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291906 EMBL· GenBank· DDBJ | BAF84595.1 EMBL· GenBank· DDBJ | mRNA | ||
AC011895 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236956 EMBL· GenBank· DDBJ | EAL23817.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76472.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002680 EMBL· GenBank· DDBJ | AAH02680.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004249 EMBL· GenBank· DDBJ | AAH04249.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004999 EMBL· GenBank· DDBJ | AAH04999.1 EMBL· GenBank· DDBJ | mRNA | ||
BC021540 EMBL· GenBank· DDBJ | AAH21540.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028985 EMBL· GenBank· DDBJ | AAH28985.1 EMBL· GenBank· DDBJ | mRNA | ||
L40374 EMBL· GenBank· DDBJ | AAC41740.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |