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IID00007
 UniprotO15169
ProteinAxin-1
GeneAXIN1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
862
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 74-220 Homo dimer :
 Evidence X-RAY 1dk8 A Reference
       Region 1dk8 A 74-220 order
Seq 80-211 Hetero dimer : IID00035Complex
 Evidence X-RAY 1emu A Reference
       Region 1emu A 80-211 order
Seq 375-394 Hetero dimer : IID00120Complex
 Evidence X-RAY 5wzz H Reference
       Region 5wzz H 375-376 disorder
       Region 5wzz H 377-387 order
       Region 5wzz H 388-394 disorder
 Evidence X-RAY 5wzz E Reference
       Region 5wzz E 375-376 disorder
       Region 5wzz E 377-387 order
       Region 5wzz E 388-394 disorder
 Evidence X-RAY 5wzz F Reference
       Region 5wzz F 375-378 disorder
       Region 5wzz F 379-387 order
       Region 5wzz F 388-394 disorder
 Evidence X-RAY 5wzz G Reference
       Region 5wzz G 375-377 disorder
       Region 5wzz G 378-387 order
       Region 5wzz G 388-394 disorder
Seq 383-400 Hetero tetramer : IID00052Complex
 Evidence X-RAY 1o9u B Reference
       Region 1o9u B 383-400 order
Seq 383-402 Hetero trimer : IID00052Complex
 Evidence X-RAY 4nm5 B Reference
       Region 4nm5 B 383-401 order
       Region 4nm5 B 402-402 disorder
Seq 383-402 Hetero dimer : IID00052Complex
 Evidence X-RAY 3zdi B Reference
       Region 3zdi B 383-383 disorder
       Region 3zdi B 384-400 order
 Evidence X-RAY 4nm3 B Reference
       Region 4nm3 B 383-401 order
       Region 4nm3 B 402-402 disorder
 Evidence X-RAY 4nm0 B Reference
       Region 4nm0 B 383-401 order
       Region 4nm0 B 402-402 disorder
 Evidence X-RAY 4b7t B Reference
       Region 4b7t B 383-400 order
Seq 383-402 Hetero trimer : IID00052Complex
 Evidence X-RAY 4nm7 B Reference
       Region 4nm7 B 383-401 order
       Region 4nm7 B 402-402 disorder
Seq 383-402 Hetero dimer : IID50236Complex
 Evidence X-RAY 4nu1 B Reference
       Region 4nu1 B 383-401 order
       Region 4nu1 B 402-402 disorder
SeqProS possible 383-400 This region binds to GSK3 beta. The binding site of this fragment in GSK3 beta is also the binding site for a fragment of FRAT. The axin fragment and the FRAT fragment share no sequence similarity. The binding sites to GSK3 beta are close, but the modes of binding are different. Hetero tetramer : IID00052Complex
       Region 1o9u B 383-400 order
SeqProS possible 383-401 This region binds to GSK3 beta. The binding site of this fragment in GSK3 beta is also the binding site for a fragment of FRAT. The axin fragment and the FRAT fragment share no sequence similarity. The binding sites to GSK3 beta are close, but the modes of binding are different. Hetero dimer : IID50236Complex
       Region 4nu1 B 383-401 order
SeqProS possible 383-401 This region binds to GSK3 beta. The binding site of this fragment in GSK3 beta is also the binding site for a fragment of FRAT. The axin fragment and the FRAT fragment share no sequence similarity. The binding sites to GSK3 beta are close, but the modes of binding are different. Hetero trimer : IID00052Complex
       Region 4nm5 B 383-401 order
SeqProS possible 383-401 This region binds to GSK3 beta. The binding site of this fragment in GSK3 beta is also the binding site for a fragment of FRAT. The axin fragment and the FRAT fragment share no sequence similarity. The binding sites to GSK3 beta are close, but the modes of binding are different. Hetero trimer : IID00052Complex
       Region 4nm7 B 383-401 order
SeqProS possible 383-401 This region binds to GSK3 beta. The binding site of this fragment in GSK3 beta is also the binding site for a fragment of FRAT. The axin fragment and the FRAT fragment share no sequence similarity. The binding sites to GSK3 beta are close, but the modes of binding are different. Hetero dimer : IID00052Complex
       Region 4nm3 B 383-401 order
       Region 4nm0 B 383-401 order
       Region 3zdi B 384-400 order
       Region 4b7t B 383-400 order
Seqphosphorylation
    75-75 Phosphoserine; by CK1
    581-581 Phosphoserine
    511-511 Phosphoserine
    493-493 Phosphoserine
    486-486 Phosphoserine
    481-481 Phosphothreonine; by GSK3-beta
    217-217 Phosphoserine; by CK1
    469-469 Phosphoserine; by CK1
    77-77 Phosphoserine; by CK1
 
Prediction
NeProc
Disorder 1-80,215-388,427-780
Order 81-214,389-426,781-862
ProS 4-38,60-74,239-250,265-332,338-343,353-388,454-457,463-484,492-497,521-528,543-580,625-644,671-695,702-713
AlphaFold
Disorder 1-77,214-241,243-243,245-348,363-382,420-465,481-624,642-693,721-780
Order 78-213,242-242,244-244,349-362,383-419,466-480,625-641,694-720,781-862
Pfam Hmmer
PF00615 88-211 1.6e-06
PF00778 780-862 1.1e-46
SEG 225-236 ,325-339 ,401-434 ,530-541 ,708-724
Function
Function in SwissProt
Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (PubMed:16601693). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development (PubMed:17210684). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (PubMed:17210684).
Biological Process
Diagram with PDB data
AXIN1/GSK3BCrystal structure of GSK-3/Axin complex bound to phosphorylated N-terminal auto-inhibitory pS9 peptide
See also
Diagram with PDB data
APC/CTNNB1Beta-catenin in complex with a phosphorylated APC 20aa repeat fragment