Annotations for this protein have been verified by the authors of the corresponding papers



DP00490: Growth factor receptor-bound protein 14FASTA viewXML view

General information
DisProt:DP00490
Name:Growth factor receptor-bound protein 14
Synonym(s):GRB14_RAT
GRB14 adapter protein
First appeared in release:Release 3.2 (05/26/2006)
UniProt:O88900
UniGene:Rn.30028
SwissProt: GRB14_RAT
TrEMBL:  
NCBI (GI): 6016156
Source organism:Rattus norvegicus (Rat)
Sequence length:538
Percent disordered:14%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MTTSLQDGQS AAGRAGAQDS PLAVQVCRVA QGKGDAQDPA QVPGLHALSP ASDATRRGAM - 60
DRRKAKDLEV QETPSIPNPF PELCCSPLTS VLSAGLFPRS NSRKKQVIKV YSEDETSRAL - 120
EVPSDVTARD VCQLLILKNH YVDDNSWTLF EHLSHTGVER TVEDHELLTE VLSHWVMEED - 180
NKLYLRKNYA KYEFFKNPMY FFPEHMVSFA TEMNGDRSLT QIPQVFLSSN TYPEIHGFLH - 240
AKEQGKKSWK KAYFFLRRSG LYFSTKGTSK EPRHLQFFSE FSTSNVYMSL AGKKKHGAPT - 300
PYGFCFKPTK AGGPRDLKML CAEEDQSRMC WVTAIRLLKY GMQLYQNYMH PSQARSACSS - 360
QSVSPMRSVS ENSLVAMDFS GQKTRVIDNP TEALSVAVEE GLAWRKKGCL RLGNHGSPTA - 420
PSQSSAVNMA LHRSQPWFHH RISRDEAQQL ITRQGPVDGV FLVRDSQSNP RTFVLSMSHG - 480
QKIKHFQIIP VEDDGEVFHT LDDGHTKFTD LIQLVEFYQL NKGVLPCKLK HYCARMAV



Functional narrative    

Interacts with the cytoplasmic domain of the autophosphorylated insulin receptor which is then inhibited. The interaction is mediated by the SH2 domain. Binds to the ankyrin repeat region of TNKL via its N-terminus.

Region 1: 361-435

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Extended
Name:PIR
Location:361 - 435
Length:75
Region sequence:

QSVSPMRSVSENSLVAMDFSGQKTRVIDNPTEALSVAVEEGLAWRKKGCLRLGNHGSPTA
PSQSSAVNMALHRSQ

Modification type: Fragment
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (300 K; pH: 5; H2O/2H2O (90/10))

  2. Stability at thermal extremes

  3. Small-angle X-ray scattering (SAXS) (NaCl 100 mM; TCEP 1 mM; Tris/HCl (pH 8.0) 50 mM)

  4. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; sodium phosphate (buffer) 10 mM)

References:
  1. Moncoq K, Broutin I, Craescu CT, Vachette P, Ducruix A, Durand D. "SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?" Biophys J. 2004; 87(6): 4056-64. PubMed: 15465854

  2. Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. "The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling." FEBS Lett. 2003; 554(3): 240-6. PubMed: 14623073

Comments:
Residues 399-407 may be transiently structured, and may be important in the binding of Grb14 binding to its partner via a structural transition.




References

  1. Kasus-Jacobi A, Perdereau D, Auzan C, Clauser E, Van Obberghen E, Mauvais-Jarvis F, Girard J, Burnol AF. "Identification of the rat adapter Grb14 as an inhibitor of insulin actions." J Biol Chem. 1998; 273(40): 26026-35. PubMed: 9748281


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