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7U5K

Cryo-EM Structure of DPYSL2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006208biological_processpyrimidine nucleobase catabolic process
A0006897biological_processendocytosis
A0007010biological_processcytoskeleton organization
A0007399biological_processnervous system development
A0016020cellular_componentmembrane
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
A0030154biological_processcell differentiation
B0004157molecular_functiondihydropyrimidinase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006208biological_processpyrimidine nucleobase catabolic process
B0006897biological_processendocytosis
B0007010biological_processcytoskeleton organization
B0007399biological_processnervous system development
B0016020cellular_componentmembrane
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
B0030154biological_processcell differentiation
C0004157molecular_functiondihydropyrimidinase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0006208biological_processpyrimidine nucleobase catabolic process
C0006897biological_processendocytosis
C0007010biological_processcytoskeleton organization
C0007399biological_processnervous system development
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
C0030154biological_processcell differentiation
D0004157molecular_functiondihydropyrimidinase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005874cellular_componentmicrotubule
D0006208biological_processpyrimidine nucleobase catabolic process
D0006897biological_processendocytosis
D0007010biological_processcytoskeleton organization
D0007399biological_processnervous system development
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
D0030154biological_processcell differentiation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000250|UniProtKB:Q16555
ChainResidueDetails
ATYR32
BTYR32
CTYR32
DTYR32

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ALYS258
BLYS258
CLYS258
DLYS258

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942
ChainResidueDetails
ASER259
BSER259
CSER259
DSER259

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ATYR431
ATYR499
BTYR431
BTYR499
CTYR431
CTYR499
DTYR431
DTYR499

site_idSWS_FT_FI5
Number of Residues20
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ASER465
BSER542
CSER465
CSER507
CSER537
CSER540
CSER542
DSER465
DSER507
DSER537
DSER540
ASER507
DSER542
ASER537
ASER540
ASER542
BSER465
BSER507
BSER537
BSER540

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P47942
ChainResidueDetails
ACYS504
BCYS504
CCYS504
DCYS504

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16555
ChainResidueDetails
ATHR509
BTHR509
CTHR509
DTHR509

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ATHR512
ATHR521
BTHR512
BTHR521
CTHR512
CTHR521
DTHR512
DTHR521

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by GSK3-beta => ECO:0000250|UniProtKB:Q16555
ChainResidueDetails
ATHR514
BTHR514
CTHR514
DTHR514

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16555
ChainResidueDetails
ASER517
ASER518
BSER517
BSER518
CSER517
CSER518
DSER517
DSER518

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine; by DYRK2 => ECO:0000250|UniProtKB:Q16555
ChainResidueDetails
ASER522
BSER522
CSER522
DSER522

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by ROCK2 => ECO:0000269|PubMed:10818093
ChainResidueDetails
ATHR555
BTHR555
CTHR555
DTHR555

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Asymmetric dimethylarginine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
AARG565
BARG565
CARG565
DARG565

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PDB entries from 2024-07-17

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