DP00154: SHC-transforming protein 1FASTA viewXML view

General information
DisProt:DP00154
Name:SHC-transforming protein 1
Synonym(s):SHC1_HUMAN
Src homology 2 domain-containing-transforming protein C1
SH2 domain protein C1
First appeared in release:Release 2.2 (04/14/2005)
UniProt:P29353
UniGene:Hs.433795
SwissProt: SHC1_HUMAN
TrEMBL:  
NCBI (GI): 182676455
Source organism:Homo sapiens (Human)
Sequence length:583
Percent disordered:9%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MDLLPPKPKY NPLRNESLSS LEEGASGSTP PEELPSPSAS SLGPILPPLP GDDSPTTLCS - 60
FFPRMSNLRL ANPAGGRPGS KGEPGRAADD GEGIDGAAMP ESGPLPLLQD MNKLSGGGGR - 120
RTRVEGGQLG GEEWTRHGSF VNKPTRGWLH PNDKVMGPGV SYLVRYMGCV EVLQSMRALD - 180
FNTRTQVTRE AISLVCEAVP GAKGATRRRK PCSRPLSSIL GRSNLKFAGM PITLTVSTSS - 240
LNLMAADCKQ IIANHHMQSI SFASGGDPDT AEYVAYVAKD PVNQRACHIL ECPEGLAQDV - 300
ISTIGQAFEL RFKQYLRNPP KLVTPHDRMA GFDGSAWDEE EEEPPDHQYY NDFPGKEPPL - 360
GGVVDMRLRE GAAPGAARPT APNAQTPSHL GATLPVGQPV GGDPEVRKQM PPPPPCPGRE - 420
LFDDPSYVNV QNLDKARQAV GGAGPPNPAI NGSAPRDLFD MKPFEDALRV PPPPQSVSMA - 480
EQLRGEPWFH GKLSRREAEA LLQLNGDFLV RESTTTPGQY VLTGLQSGQP KHLLLVDPEG - 540
VVRTKDHRFE SVSHLISYHM DNHLPIISAG SELCLQQPVE RKL



Functional narrative    

SHC transforming protein 1 is involved in the beginning of the Ras cascade and alters growth factor and tyrosine kinases as a part of this signaling network. SHC transforming protein 1 is found in the beginning of the signal transduction pathway and can be located in the cytoplasm. SHC transforming protein 1 interacts and/or adapts tyrosine kinases and the GRB2/SOS complex directly, in order to indirectly activate Ras. In the presence of large amounts of interacting partners (e.g., when they are over expressed), SHC transforming protein 1 can cause tumors and become highly cancerous. SHC transforming protein 1 belongs to the Src homology 2 domain containing transforming protein 1 family. The two disordered regions of this isoform, (1-41) and (192-207) both have the capability to bind to a ligand that induces the structural change requisite for subsequent peptide-peptide interactions, thus, initiating the signaling process.

Region 2: 128-152 Region 1: 128-166 Region 3: 303-318 Region 4: 311-318

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: 
Location:128 - 166
Length:39
Region sequence:

QLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRY

Modification type: Complex
Engineered
Fragment
Isoform
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (308 K; pH: 6.5; )
References:
  1. Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. "Coupling of folding and binding in the PTB domain of the signaling protein Shc." Structure. 2003; 11(8): 905-13. PubMed: 12906822
Comments:
This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide.

The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence.


Region 2
Type:Disordered - Extended
Name: 
Location:128 - 152
Length:25
Region sequence:

QLGGEEWTRHGSFVNKPTRGWLHPN

Modification type: Engineered
Fragment
Isoform
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Substrate/ligand binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (308 K; pH: 6.5; )
References:
  1. Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. "Coupling of folding and binding in the PTB domain of the signaling protein Shc." Structure. 2003; 11(8): 905-13. PubMed: 12906822
Comments:
This entry is from the characterization of a fragment containing residues 17-207 in solution.

The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence.


Region 3
Type:Disordered
Name: 
Location:303 - 318
Length:16
Region sequence:

TIGQAFELRFKQYLRN

Modification type: Engineered
Fragment
Isoform
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (308 K; pH: 6.5; )
References:
  1. Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. "Coupling of folding and binding in the PTB domain of the signaling protein Shc." Structure. 2003; 11(8): 905-13. PubMed: 12906822
Comments:
This entry is from the characterization of a fragment containing residues 17-207 in solution.

The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence.


Region 4
Type:Disordered
Name: 
Location:311 - 318
Length:8
Region sequence:

RFKQYLRN

Modification type: Complex
Engineered
Fragment
Isoform
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (308 K; pH: 6.5; )
References:
  1. Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. "Coupling of folding and binding in the PTB domain of the signaling protein Shc." Structure. 2003; 11(8): 905-13. PubMed: 12906822
Comments:
This entry is from the characterization of the experimental fragment in complex with a 12 residue tyrosine-phosphated peptide.

The experimental fragment consisted of residues 128 - 318 of the Swiss-Prot sequence.

If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


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