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Reviewed, UniProtKB/Swiss-Prot O75962 (TRIO_HUMAN)

Last modified November 25, 2008. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Triple functional domain protein
    EC=2.7.11.1
Alternative name(s):
    PTPRF-interacting protein
Gene names
Name: TRIO
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3038 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Promotes the exchange of GDP by GTP. Together with leukocyte antigen-related (LAR) protein, it could play a role in coordinating cell-matrix and cytoskeletal rearrangements necessary for cell migration and cell growth.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts to form a complex with leukocyte antigen related protein.

Subcellular location

CytoplasmBy similarity.

Tissue specificity

Highly expressed in heart, skeletal muscle, brain, pancreas, placenta, liver, kidney and lung.

Domain

The N-terminal DBL/GEF domain specifically catalyzes nucleotide exchange for RAC1, leading to the activation of Jun kinase and the production of membrane ruffles. The second DBL/GEF domain is an exchange factor for rhoa and induces the formation of stress fibers.

Post-translational modification

Phosphorylated on serine residue(s).

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 1 CRAL-TRIO domain.

Contains 2 DH (DBL-homology) domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 2 PH domains.

Contains 1 protein kinase domain.

Contains 2 SH3 domains.

Contains 4 spectrin repeats.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75962-1)

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: O75962-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2309-2309: G → E
     2310-3038: Missing.
Notes: Ref.1 (AAC43042) sequence differs from that shown due to a frameshift in position 2241.
Isoform 3 (identifier: O75962-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2442: Missing.
     2443-2485: FPGDSDSLQR...QSVQSTQSNG → MLPSQAQGLL...LARNTFLKAC
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 30383038Triple functional domain protein
PRO_0000080978

Regions

Domain6 – 151146CRAL-TRIO
Repeat252 – 359108Spectrin 1
Repeat479 – 585107Spectrin 2
Repeat819 – 925107Spectrin 3
Repeat1050 – 1157108Spectrin 4
Domain1233 – 1408176DH 1
Domain1421 – 1532112PH 1
Domain1597 – 165357SH3 1
Domain1910 – 2086177DH 2
Domain2098 – 2212115PH 2
Domain2492 – 255766SH3 2
Domain2626 – 271691Ig-like C2-type
Domain2737 – 2993257Protein kinase
Nucleotide binding2743 – 27519ATP By similarity
Compositional bias656 – 6594Poly-Gln
Compositional bias1786 – 17916Poly-Ser
Compositional bias2233 – 225321Poly-Gly
Compositional bias2486 – 24927Poly-Ser

Sites

Active site28561 By similarity
Binding site27661ATP By similarity

Amino acid modifications

Modified residue14861Phosphothreonine
Modified residue18441Phosphothreonine
Disulfide bond2637 ↔ 2700 Potential

Natural variations

Alternative sequence1 – 24422442Missing in isoform 3.
VSP_023306
Alternative sequence23091G → E in isoform 2.
VSP_004467
Alternative sequence2310 – 3038729Missing in isoform 2.
VSP_004468
Alternative sequence2443 – 248543FPGDS…TQSNG → MLPSQAQGLLWWVFPLFPAS SLSYPPVSYRADGLARNTFL KAC in isoform 3.
VSP_023307
Natural variant2321S → T
VAR_041899
Natural variant15851T → M
VAR_041900
Natural variant16311H → R
VAR_041901
Natural variant19191V → M in a metastatic melanoma sample; somatic mutation.
VAR_041902
Natural variant21831T → M
VAR_041903

Experimental info

Mutagenesis12401E → A: 50% decrease in nucleotide exchange activity
Mutagenesis12441T → A: 40% decrease in nucleotide exchange activity
Mutagenesis13301N → A: No change in nucleotide exchange activity
Mutagenesis13671V → A: 90% decrease in nucleotide exchange activity
Mutagenesis13681Q → A: 80% decrease in nucleotide exchange activity
Mutagenesis13691R → A: 80% decrease in nucleotide exchange activity
Mutagenesis13711T → A: 80% decrease in nucleotide exchange activity
Mutagenesis13721K → A: Loss of nucleotide exchange activity
Mutagenesis13751L → A: 40% decrease in nucleotide exchange activity
Mutagenesis13781K → A: No change in nucleotide exchange activity
Mutagenesis13791E → A: 30% decrease in nucleotide exchange activity
Sequence conflict491 – 4944HVRT → QLEN in AAH35585. Ref.4
Sequence conflict491 – 4944HVRT → QLEN in BAD92991. Ref.5
Sequence conflict5151E → D in AAH35585. Ref.4
Sequence conflict5151E → D in BAD92991. Ref.5
Sequence conflict728 – 7292HV → QL in AAH35585. Ref.4
Sequence conflict728 – 7292HV → QL in BAD92991. Ref.5
Sequence conflict2486 – 250419SESSS…THDYT → VSASGGPRPPAPLPLSRQL in BAD92991. Ref.5

Secondary structure

................................................. 3038
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1998. Version 1.
Checksum: 28620F3B513EB74B

FASTA3,038341,617
        10         20         30         40         50         60 
MKAMDVLPIL KEKVAYLSGG RDKRGGPILT FPARSNHDRI RQEDLRRLIS YLACIPSEEV 

        70         80         90        100        110        120 
CKRGFTVIVD MRGSKWDSIK PLLKILQESF PCCIHVALII KPDNFWQKQR TNFGSSKFEF 

       130        140        150        160        170        180 
ETNMVSLEGL TKVVDPSQLT PEFDGCLEYN HEEWIEIRVA FEDYISNATH MLSRLEE