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1LUJ

Crystal Structure of the Beta-catenin/ICAT Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0045296molecular_functioncadherin binding
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001658biological_processbranching involved in ureteric bud morphogenesis
B0002528biological_processregulation of vascular permeability involved in acute inflammatory response
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008013molecular_functionbeta-catenin binding
B0009952biological_processanterior/posterior pattern specification
B0016055biological_processWnt signaling pathway
B0030178biological_processnegative regulation of Wnt signaling pathway
B0030877cellular_componentbeta-catenin destruction complex
B0031333biological_processnegative regulation of protein-containing complex assembly
B0043392biological_processnegative regulation of DNA binding
B0043433biological_processnegative regulation of DNA-binding transcription factor activity
B0045657biological_processpositive regulation of monocyte differentiation
B0045669biological_processpositive regulation of osteoblast differentiation
B0048662biological_processnegative regulation of smooth muscle cell proliferation
B0060633biological_processnegative regulation of transcription initiation by RNA polymerase II
B0070016molecular_functionarmadillo repeat domain binding
B0072201biological_processnegative regulation of mesenchymal cell proliferation
B0090090biological_processnegative regulation of canonical Wnt signaling pathway
B1990711cellular_componentbeta-catenin-ICAT complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
BSER59

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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