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IID00449
UniprotP31948
ProteinStress-induced-phosphoprotein 1
GeneSTIP1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
543
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-118 Hetero dimer :
 Evidence X-RAY 1elw A Reference
       Region 1elw A 1-1 disorder
       Region 1elw A 2-118 order
Seq 1-118 Hetero dimer :
 Evidence X-RAY 1elw B Reference
       Region 1elw B 1-115 order
       Region 1elw B 116-118 disorder
Seq 220-350 Monomer :
 Evidence NMR 2nc9 A Reference
       Region 2nc9 A 220-350 order
Seq 223-349 Hetero tetramer : IID00536Complex
 Evidence X-RAY 3fwv B Reference
       Region 3fwv B 223-349 order
 Evidence X-RAY 3fwv A Reference
       Region 3fwv A 223-349 order
Seq 223-350 Hetero dimer : IID00440Complex
 Evidence X-RAY 3esk A Reference
       Region 3esk A 223-349 order
       Region 3esk A 350-350 disorder
Seq 223-352 Hetero dimer : Q9H2A1
 Evidence X-RAY 1elr A Reference
       Region 1elr A 223-349 order
       Region 1elr A 350-352 disorder
Seq 356-477 Monomer :
 Evidence NMR 2lni A Reference
       Region 2lni A 356-477 order
Seqphosphorylation
    481-481 Phosphoserine
    354-354 Phosphotyrosine
    332-332 Phosphothreonine
    198-198 Phosphothreonine
    16-16 Phosphoserine
Seqacetylation
    1-1 N-acetylmethionine
    446-446 N6-acetyllysine
    8-8 N6-acetyllysine
    344-344 N6-acetyllysine
    312-312 N6-acetyllysine
    325-325 N6-acetyllysine
    301-301 N6-acetyllysine
 
Prediction
NeProc
Disorder 191-219
Order 1-190,220-543
ProS 191-194,211-219
AlphaFold
Disorder 121-125,188-217,543-543
Order 1-120,126-187,218-542
Pfam Hmmer
PF00515 4-37 7.7e-07
PF07719 225-258 2.8e-05
PF00515 300-333 6e-07
PF00515 360-393 1.8e-07
PF00515 394-427 1.9e-08
PF00515 428-461 9.8e-07
SEG 192-216
Function
Function in SwissProt
Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity).