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1A4O

14-3-3 PROTEIN ZETA ISOFORM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
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
B0008104biological_processprotein localization
B0042470cellular_componentmelanosome
B0050815molecular_functionphosphoserine residue binding
B0070372biological_processregulation of ERK1 and ERK2 cascade
B0140311molecular_functionprotein sequestering activity
C0005737cellular_componentcytoplasm
C0006468biological_processprotein phosphorylation
C0007165biological_processsignal transduction
C0008104biological_processprotein localization
C0042470cellular_componentmelanosome
C0050815molecular_functionphosphoserine residue binding
C0070372biological_processregulation of ERK1 and ERK2 cascade
C0140311molecular_functionprotein sequestering activity
D0005737cellular_componentcytoplasm
D0006468biological_processprotein phosphorylation
D0007165biological_processsignal transduction
D0008104biological_processprotein localization
D0042470cellular_componentmelanosome
D0050815molecular_functionphosphoserine residue binding
D0070372biological_processregulation of ERK1 and ERK2 cascade
D0140311molecular_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
ATYR211-SER230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:18550856, ECO:0000269|PubMed:9632691
ChainResidueDetails
AARG56
AARG127
BARG56
BARG127
CARG56
CARG127
DARG56
DARG127

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ALYS3
ALYS68
BLYS3
BLYS68
CLYS3
CLYS68
DLYS3
DLYS68

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ASER58
BSER58
CSER58
DSER58

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ASER184
ASER207
BSER184
BSER207
CSER184
CSER207
DSER184
DSER207

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63102
ChainResidueDetails
ASER210
BSER210
CSER210
DSER210

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by CK1 => ECO:0000250|UniProtKB:P63104
ChainResidueDetails
ATHR232
BTHR232
CTHR232
DTHR232

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PDB entries from 2024-09-18

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