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IID00304
UniprotP46937
ProteinTranscriptional coactivator YAP1
GeneYAP1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
504
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 50-171 Hetero dimer : IID00547Complex
 Evidence X-RAY 4re1 C Reference
       Region 4re1 C 50-99 order
       Region 4re1 C 100-171 disorder
 Evidence X-RAY 4re1 D Reference
       Region 4re1 D 50-52 disorder
       Region 4re1 D 53-99 order
       Region 4re1 D 100-171 disorder
 Evidence X-RAY 3kys D Reference
       Region 3kys D 50-51 disorder
       Region 3kys D 52-100 order
       Region 3kys D 101-171 disorder
 Evidence X-RAY 3kys B Reference
       Region 3kys B 50-100 order
       Region 3kys B 101-171 disorder
Seq 60-100 Hetero dimer : Q15561
 Evidence X-RAY 5oaq L Reference
       Region 5oaq L 60-99 order
       Region 5oaq L 100-100 disorder
Seq 124-133 Hetero dimer : IID00301Complex
 Evidence X-RAY 3mhr P Reference
       Region 3mhr P 124-133 order
Seq 165-204 Hetero dimer :
 Evidence NMR 1k9q A Reference
       Region 1k9q A 165-204 order
       Region 1k9q A 165-170 high_rmsd
Seq 165-204 Hetero dimer :
 Evidence NMR 1k9r A Reference
       Region 1k9r A 165-204 order
       Region 1k9r A 165-170 high_rmsd
       Region 1k9r A 204-204 high_rmsd
Seq 165-209 Monomer :
 Evidence X-RAY 4rex A Reference
       Region 4rex A 165-208 order
       Region 4rex A 209-209 disorder
Seq 165-210 Hetero dimer : Q96G27
 Evidence NMR 1k5r A Reference
       Region 1k5r A 165-204 order
       Region 1k5r A 165-171 high_rmsd
       Region 1k5r A 203-204 high_rmsd
 Evidence NMR 1jmq A Reference
       Region 1jmq A 165-210 order
       Region 1jmq A 165-165 high_rmsd
       Region 1jmq A 208-210 high_rmsd
Seq 170-205 Hetero dimer : IID00174Complex
 Evidence NMR 2lay A Reference
       Region 2lay A 170-205 order
 Evidence NMR 2lax A Reference
       Region 2lax A 170-205 order
Seq 170-205 Hetero dimer : IID00135Complex
 Evidence NMR 2ltw A Reference
       Region 2ltw A 170-205 order
Seq 230-263 Hetero dimer : IID00174Complex
 Evidence NMR 2law A Reference
       Region 2law A 230-263 order
Seq 230-265 Hetero dimer : IID00135Complex
 Evidence NMR 2ltv A Reference
       Region 2ltv A 230-265 order
SeqProS verified 124-133 Hetero dimer : IID00301Complex
       Region 3mhr P 124-133 order
       Region 3kys D 101-171 disorder
Seqphosphorylation
    382-382 Phosphoserine
    388-388 Phosphoserine
    371-371 Phosphoserine
    397-397 Phosphoserine; by LATS1 and LATS2
    381-381 Phosphoserine
    289-289 Phosphoserine
    367-367 Phosphoserine; by MAPK8 and MAPK9
    164-164 Phosphoserine; by LATS1 and LATS2
    274-274 Phosphoserine
    154-154 Phosphothreonine; by MAPK8 and MAPK9
    138-138 Phosphoserine; by MAPK8 and MAPK9
    128-128 Phosphoserine
    131-131 Phosphoserine
    127-127 Phosphoserine; by LATS1 and LATS2
    110-110 Phosphothreonine
    119-119 Phosphothreonine; by MAPK8 and MAPK9
    105-105 Phosphoserine
    109-109 Phosphoserine; by LATS1 and LATS2
    63-63 Phosphothreonine
    61-61 Phosphoserine; by LATS1 and LATS2
    400-400 Phosphoserine; by CK1
    407-407 Phosphotyrosine; by ABL1
    412-412 Phosphothreonine; by MAPK8 and MAPK9
    403-403 Phosphoserine; by CK1
 
Prediction
NeProc
Disorder 1-298,329-386,393-412,459-469,489-499
Order 299-328,387-392,413-458,470-488,500-504
ProS 1-4,55-99,104-118,174-205,231-251,264-271,278-285,329-334,340-355,364-375,382-386,393-412,489-499
AlphaFold
Disorder 1-56,58-58,60-61,75-82,101-170,208-229,265-300,330-504
Order 57-57,59-59,62-74,83-100,171-207,230-264,301-329
Pfam Hmmer
PF00397 173-202 7.2e-13
PF00397 232-261 1e-12
SEG 3-51 ,302-328
Function
Function in SwissProt
Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). Plays a key role in controlling cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration (PubMed:18158288). The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction (PubMed:18579750). Suppresses ciliogenesis via acting as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity).
Isoform 2
Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3).
Isoform 3
Activates the C-terminal fragment (CTF) of ERBB4 (isoform 3).
Biological Process
Diagram with PDB data
YAP1/SFN14-3-3 sigma in complex with YAP pS127-peptide
See also
Diagram with PDB data
SMAD1/YAP1Structure of the first WW domain of human YAP in complex with a phosphorylated human Smad1 derived peptide