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1F8A

STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS

Functional Information from GO Data
ChainGOidnamespacecontents
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001666biological_processresponse to hypoxia
B0001932biological_processregulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0003774molecular_functioncytoskeletal motor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0007088biological_processregulation of mitotic nuclear division
B0008013molecular_functionbeta-catenin binding
B0010468biological_processregulation of gene expression
B0016607cellular_componentnuclear speck
B0016859molecular_functioncis-trans isomerase activity
B0030182biological_processneuron differentiation
B0030496cellular_componentmidbody
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0031434molecular_functionmitogen-activated protein kinase kinase binding
B0031647biological_processregulation of protein stability
B0032091biological_processnegative regulation of protein binding
B0032092biological_processpositive regulation of protein binding
B0032465biological_processregulation of cytokinesis
B0032794molecular_functionGTPase activating protein binding
B0035307biological_processpositive regulation of protein dephosphorylation
B0036064cellular_componentciliary basal body
B0042177biological_processnegative regulation of protein catabolic process
B0043547biological_processpositive regulation of GTPase activity
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046785biological_processmicrotubule polymerization
B0048156molecular_functiontau protein binding
B0050808biological_processsynapse organization
B0050815molecular_functionphosphoserine residue binding
B0050816molecular_functionphosphothreonine residue binding
B0050821biological_processprotein stabilization
B0051219molecular_functionphosphoprotein binding
B0060255biological_processregulation of macromolecule metabolic process
B0060392biological_processnegative regulation of SMAD protein signal transduction
B0070373biological_processnegative regulation of ERK1 and ERK2 cascade
B0080090biological_processregulation of primary metabolic process
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
B0098978cellular_componentglutamatergic synapse
B0099524cellular_componentpostsynaptic cytosol
B1900180biological_processregulation of protein localization to nucleus
B1902430biological_processnegative regulation of amyloid-beta formation
B1990757molecular_functionubiquitin ligase activator activity
B2000146biological_processnegative regulation of cell motility
Functional Information from PROSITE/UniProt
site_idPS00115
Number of Residues7
DetailsRNA_POL_II_REPEAT Eukaryotic RNA polymerase II heptapeptide repeat. YSPTSPS
ChainResidueDetails
CTYR170-SER176

site_idPS01096
Number of Residues21
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG
ChainResidueDetails
BPHE107-GLY127

site_idPS01159
Number of Residues27
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. WekrmsrssgrvYYfnhitnaSQWERP
ChainResidueDetails
BTRP15-PRO41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER47

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS50

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by DAPK1 => ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:29686383
ChainResidueDetails
BSER75

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
BSER112

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1nmw
ChainResidueDetails
BCYS117
BHIS161
BHIS63

site_idMCSA1
Number of Residues5
DetailsM-CSA 511
ChainResidueDetails
BHIS63proton shuttle (general acid/base)
BCYS117covalently attached, electrostatic stabiliser
BGLN135electrostatic stabiliser
BSER158electrostatic stabiliser
BHIS161electrostatic stabiliser

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PDB entries from 2024-09-18

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