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6Y1J

14-3-3 sigma in complex with IkappaBalpha pS63 peptide

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
A0030216biological_processkeratinocyte differentiation
A0030307biological_processpositive regulation of cell growth
A0031424biological_processkeratinization
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AGLU35
AGLU110
AGLU188
AHOH552
AHOH602
AHOH638

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 302
ChainResidue
ALYS9
AHOH660
AHOH688

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 303
ChainResidue
AGLU75
AGLU161
AHOH485
AHOH572
AHOH622
AHOH635

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 304
ChainResidue
ALYS124
ATYR128
ASER146
AHOH454
AHOH461

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 305
ChainResidue
AGLY-4
AGLU76
AGLY78
APRO79
AARG82
AHOH484

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 306
ChainResidue
ATYR48
AVAL95
ATHR98
AHOH532
AHOH651

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 307
ChainResidue
ATYR19
AASN50
AHOH440
AHOH563
PTRP66
PLYS67

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 308
ChainResidue
AASP97
ALEU100
ATYR128
AHOH402
AHOH416
AHOH535

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL A 309
ChainResidue
AARG148
AASP211
AASP215
AHOH430
AHOH566

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL A 310
ChainResidue
AGLU110
AMET202
ALEU205
ATYR213
AHOH403
AHOH428
AHOH441

site_idAD2
Number of Residues4
Detailsbinding site for residue CA A 311
ChainResidue
ATYR19
AGLU20
AHOH587
AHOH624

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. YKDSTLIMQLLRDNLTLWTA
ChainResidueDetails
ATYR213-ALA232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with phosphoserine on interacting protein
ChainResidueDetails
AARG56
AARG129

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER5

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER74

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER248

221051

PDB entries from 2024-06-12

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