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4Y32

Crystal structure of C-terminal modified Tau peptide-hybrid 109B with 14-3-3sigma

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001836biological_processrelease of cytochrome c from mitochondria
A0003334biological_processkeratinocyte development
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006469biological_processnegative regulation of protein kinase activity
A0006611biological_processprotein export from nucleus
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
A0008426molecular_functionprotein kinase C inhibitor activity
A0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
A0010482biological_processregulation of epidermal cell division
A0010737biological_processprotein kinase A signaling
A0010839biological_processnegative regulation of keratinocyte proliferation
A0019901molecular_functionprotein kinase binding
A0022407biological_processregulation of cell-cell adhesion
A0030216biological_processkeratinocyte differentiation
A0030307biological_processpositive regulation of cell growth
A0031424biological_processkeratinization
A0032880biological_processregulation of protein localization
A0042802molecular_functionidentical protein binding
A0043588biological_processskin development
A0043616biological_processkeratinocyte proliferation
A0045296molecular_functioncadherin binding
A0045606biological_processpositive regulation of epidermal cell differentiation
A0045785biological_processpositive regulation of cell adhesion
A0045824biological_processnegative regulation of innate immune response
A0046827biological_processpositive regulation of protein export from nucleus
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0051726biological_processregulation of cell cycle
A0061436biological_processestablishment of skin barrier
A0070062cellular_componentextracellular exosome
A0072089biological_processstem cell proliferation
A0140311molecular_functionprotein sequestering activity
A1903077biological_processnegative regulation of protein localization to plasma membrane
A1903829biological_processpositive regulation of protein localization
A2000647biological_processnegative regulation of stem cell proliferation
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001836biological_processrelease of cytochrome c from mitochondria
B0003334biological_processkeratinocyte development
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006469biological_processnegative regulation of protein kinase activity
B0006611biological_processprotein export from nucleus
B0007165biological_processsignal transduction
B0008104biological_processprotein localization
B0008426molecular_functionprotein kinase C inhibitor activity
B0008630biological_processintrinsic apoptotic signaling pathway in response to DNA damage
B0010482biological_processregulation of epidermal cell division
B0010737biological_processprotein kinase A signaling
B0010839biological_processnegative regulation of keratinocyte proliferation
B0019901molecular_functionprotein kinase binding
B0022407biological_processregulation of cell-cell adhesion
B0030216biological_processkeratinocyte differentiation
B0030307biological_processpositive regulation of cell growth
B0031424biological_processkeratinization
B0032880biological_processregulation of protein localization
B0042802molecular_functionidentical protein binding
B0043588biological_processskin development
B0043616biological_processkeratinocyte proliferation
B0045296molecular_functioncadherin binding
B0045606biological_processpositive regulation of epidermal cell differentiation
B0045785biological_processpositive regulation of cell adhesion
B0045824biological_processnegative regulation of innate immune response
B0046827biological_processpositive regulation of protein export from nucleus
B0050815molecular_functionphosphoserine residue binding
B0051219molecular_functionphosphoprotein binding
B0051726biological_processregulation of cell cycle
B0061436biological_processestablishment of skin barrier
B0070062cellular_componentextracellular exosome
B0072089biological_processstem cell proliferation
B0140311molecular_functionprotein sequestering activity
B1903077biological_processnegative regulation of protein localization to plasma membrane
B1903829biological_processpositive regulation of protein localization
B2000647biological_processnegative regulation of stem cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue 49F C 301
ChainResidue
AASN42
ASER45
APHE119
AILE168
AHOH407
AHOH540
CTHR217
CHOH410

site_idAC2
Number of Residues17
Detailsbinding site for Di-peptide PRO C 213 and SEP C 214
ChainResidue
AARG56
AARG129
ATYR130
AASN175
AVAL178
AASN226
CARG211
CTHR212
CLEU215
CPRO216
CHOH401
CHOH403
CHOH404
CHOH406
CHOH407
CHOH408
ALYS49

site_idAC3
Number of Residues16
Detailsbinding site for Di-peptide SEP C 214 and LEU C 215
ChainResidue
ALYS49
AARG56
AARG129
ATYR130
ALEU174
AASN175
CTHR212
CPRO213
CPRO216
CTHR217
CHOH401
CHOH403
CHOH404
CHOH406
CHOH407
CHOH408

site_idAC4
Number of Residues19
Detailsbinding site for Di-peptide PRO D 213 and SEP D 214
ChainResidue
BLYS49
BARG56
BARG129
BTYR130
BASN175
BVAL178
BASN226
BHOH386
DTHR212
DLEU215
DPRO216
DHOH301
DHOH302
DHOH303
DHOH304
DHOH306
DHOH307
DHOH308
DHOH312

site_idAC5
Number of Residues16
Detailsbinding site for Di-peptide SEP D 214 and LEU D 215
ChainResidue
BLYS49
BARG56
BARG129
BTYR130
BLEU174
BASN175
DTHR212
DPRO213
DPRO216
DHOH301
DHOH303
DHOH304
DHOH306
DHOH307
DHOH308
DHOH312

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG41-VAL51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:9614189
ChainResidueDetails
CTHR212
DTHR212
BARG56
BARG129

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails
CSEP214
DSEP214

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179
ChainResidueDetails
CTHR217
DTHR217

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PDB entries from 2024-07-24

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