Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BKN

Human Dihydropyrimidinase-related protein 3 (DPYSL3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006208biological_processpyrimidine nucleobase catabolic process
A0010976biological_processpositive regulation of neuron projection development
A0010977biological_processnegative regulation of neuron projection development
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0017124molecular_functionSH3 domain binding
A0030027cellular_componentlamellipodium
A0030336biological_processnegative regulation of cell migration
A0030426cellular_componentgrowth cone
A0031005molecular_functionfilamin binding
A0031941cellular_componentfilamentous actin
A0035374molecular_functionchondroitin sulfate binding
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0044297cellular_componentcell body
A0045202cellular_componentsynapse
A0048666biological_processneuron development
A0048678biological_processresponse to axon injury
A0051017biological_processactin filament bundle assembly
A0051491biological_processpositive regulation of filopodium assembly
A0051764biological_processactin crosslink formation
A0070382cellular_componentexocytic vesicle
A0071345biological_processcellular response to cytokine stimulus
B0004157molecular_functiondihydropyrimidinase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006208biological_processpyrimidine nucleobase catabolic process
B0010976biological_processpositive regulation of neuron projection development
B0010977biological_processnegative regulation of neuron projection development
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0017124molecular_functionSH3 domain binding
B0030027cellular_componentlamellipodium
B0030336biological_processnegative regulation of cell migration
B0030426cellular_componentgrowth cone
B0031005molecular_functionfilamin binding
B0031941cellular_componentfilamentous actin
B0035374molecular_functionchondroitin sulfate binding
B0042802molecular_functionidentical protein binding
B0042995cellular_componentcell projection
B0044297cellular_componentcell body
B0045202cellular_componentsynapse
B0048666biological_processneuron development
B0048678biological_processresponse to axon injury
B0051017biological_processactin filament bundle assembly
B0051491biological_processpositive regulation of filopodium assembly
B0051764biological_processactin crosslink formation
B0070382cellular_componentexocytic vesicle
B0071345biological_processcellular response to cytokine stimulus
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER259
BSER259

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62188
ChainResidueDetails
ATYR431
ATYR499
BTYR431
BTYR499

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by GSK3 => ECO:0000269|PubMed:16611631, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR509
BTHR509

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by GSK3 => ECO:0000269|PubMed:16611631, ECO:0007744|PubMed:21406692
ChainResidueDetails
ATHR514
BTHR514

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by GSK3 => ECO:0000269|PubMed:16611631
ChainResidueDetails
ASER518
BSER518

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by DYRK2 => ECO:0000269|PubMed:16611631, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER522
BSER522

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q62188
ChainResidueDetails
ASER536
ASER539
ASER541
BSER536
BSER539
BSER541

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q62188
ChainResidueDetails
ATHR543
BTHR543

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon