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1A37

14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0042470cellular_componentmelanosome
A0050815molecular_functionphosphoserine residue binding
A0070372biological_processregulation of ERK1 and ERK2 cascade
A0140311molecular_functionprotein sequestering activity
B0005737cellular_componentcytoplasm
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0042470cellular_componentmelanosome
B0050815molecular_functionphosphoserine residue binding
B0070372biological_processregulation of ERK1 and ERK2 cascade
B0140311molecular_functionprotein sequestering activity
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG41-VAL51

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR212-SER230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:18550856, ECO:0000269|PubMed:9632691
ChainResidueDetails
AARG56
AARG127
BARG56
BARG127

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ALYS3
ALYS68
BLYS3
BLYS68

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ASER58
BSER58

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ASER184
ASER212
BSER184
BSER212

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63102
ChainResidueDetails
ASER212
BSER212

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CK1 => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ATHR232
BTHR232

218853

PDB entries from 2024-04-24

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