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IID00511
UniprotP29353
ProteinSHC-transforming protein 1
GeneSHC1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
583
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 111-317 Monomer :
 Evidence X-RAY 4xwx A Reference
       Region 4xwx A 147-205 order
       Region 4xwx A 206-212 disorder
       Region 4xwx A 213-311 order
 Evidence NMR 1oy2 A Reference
       Region 1oy2 A 111-126 disorder
       Region 1oy2 A 127-189 order
       Region 1oy2 A 190-221 disorder
       Region 1oy2 A 222-285 order
       Region 1oy2 A 286-292 disorder
       Region 1oy2 A 293-317 order
 Evidence NMR 1n3h A Reference
       Region 1n3h A 111-189 order
       Region 1n3h A 190-221 disorder
       Region 1n3h A 222-285 order
       Region 1n3h A 286-292 disorder
       Region 1n3h A 293-317 order
Seq 127-317 Hetero dimer : IID00535Complex
 Evidence NMR 1shc A Reference
       Region 1shc A 127-317 order
Seq 127-317 Hetero dimer : P05106
 Evidence NMR 2l1c A Reference
       Region 2l1c A 127-317 order
       Region 2l1c A 127-142 high_rmsd
Seq 344-356 Hetero dimer :
 Evidence X-RAY 4jmh B This region binds to Grb2 fusioned with FN3. Reference
       Region 4jmh B 344-346 disorder
       Region 4jmh B 347-354 order
       Region 4jmh B 355-356 disorder
Seq 345-353 Hetero dimer : IID00262Complex
 Evidence X-RAY 5czi B Reference
       Region 5czi B 345-345 disorder
       Region 5czi B 346-352 order
       Region 5czi B 353-353 disorder
Seq 423-435 Hetero dimer : IID00459Complex
 Evidence NMR 1qg1 I Reference
       Region 1qg1 I 423-435 order
Seq 480-583 Hetero dimer : IID00544Complex
 Evidence NMR 1tce A Reference
       Region 1tce A 480-583 order
Seq 482-583 Monomer :
 Evidence X-RAY 1mil A Reference
       Region 1mil A 482-583 order
SeqProS verified 190-221,286-292 Hetero dimer : IID00535Complex
       Region 1shc A 127-317 order
       Region 1n3h A 190-221 disorder
       Region 1n3h A 286-292 disorder
SeqProS predicted 423-435 The unbound state of this region is deduced to be disordered based on the results of prediction tools (DICHOT, Mobi, d2p2 etc). Hetero dimer : IID00459Complex
       Region 1qg1 I 423-435 order
Seqphosphorylation
    350-350 Phosphotyrosine
    139-139 Phosphoserine
    36-36 Phosphoserine
    349-349 Phosphotyrosine
    427-427 Phosphotyrosine
    453-453 Phosphoserine
Seqacetylation
    154-154 N6-acetyllysine
    1-1 N-acetylmethionine
    1-1 N-acetylmethionine
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-145,204-214,317-481
Order 146-203,215-316,482-583
ProS 1-25,55-70,136-145,204-214,326-340,347-354,360-370,375-438,454-469
AlphaFold
Disorder 1-146,203-215,318-350,353-478,539-539,583-583
Order 147-202,216-317,351-352,479-538,540-582
Pfam Hmmer
PF00640 162-318 3.9e-67
PF00017 488-559 2.9e-27
SEG 16-55 ,116-127 ,372-384 ,439-455
Function
Function in SwissProt
Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis.