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1T08

Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0045296molecular_functioncadherin binding
B0008013molecular_functionbeta-catenin binding
B0030178biological_processnegative regulation of Wnt signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17009320, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER191

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17009320
ChainResidueDetails
ASER246

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PTK6 => ECO:0000269|PubMed:20026641
ChainResidueDetails
ATYR331

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC and PTK6 => ECO:0000269|PubMed:22056988, ECO:0000305|PubMed:20026641
ChainResidueDetails
ATYR333

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER552

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336
ChainResidueDetails
ATHR556

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q02248
ChainResidueDetails
ACYS619

218853

PDB entries from 2024-04-24

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