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4E2E

Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide (YWHAG) from Homo sapiens at 2.25 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0002181biological_processcytoplasmic translation
A0002841biological_processnegative regulation of T cell mediated immune response to tumor cell
A0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
A0003723molecular_functionRNA binding
A0005080molecular_functionprotein kinase C binding
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006469biological_processnegative regulation of protein kinase activity
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
A0008426molecular_functionprotein kinase C inhibitor activity
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0022409biological_processpositive regulation of cell-cell adhesion
A0030971molecular_functionreceptor tyrosine kinase binding
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031669biological_processcellular response to nutrient levels
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0032880biological_processregulation of protein localization
A0034198biological_processcellular response to amino acid starvation
A0038202biological_processTORC1 signaling
A0042149biological_processcellular response to glucose starvation
A0042802molecular_functionidentical protein binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045202cellular_componentsynapse
A0045664biological_processregulation of neuron differentiation
A0045947biological_processnegative regulation of translational initiation
A0045948biological_processpositive regulation of translational initiation
A0048167biological_processregulation of synaptic plasticity
A0050821biological_processprotein stabilization
A0050868biological_processnegative regulation of T cell activation
A0050870biological_processpositive regulation of T cell activation
A0061462biological_processprotein localization to lysosome
A0070062cellular_componentextracellular exosome
A0085020biological_processprotein K6-linked ubiquitination
A0098793cellular_componentpresynapse
A0140031molecular_functionphosphorylation-dependent protein binding
A0140311molecular_functionprotein sequestering activity
A1904262biological_processnegative regulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
ALEU225
AASN229

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG42-VAL52

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR216-SER235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
ChainResidueDetails
AARG57
AARG132

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial => ECO:0000269|Ref.7
ChainResidueDetails
AMSE1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330
ChainResidueDetails
AVAL2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER71

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
ATYR133

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|Ref.7
ChainResidueDetails
ATHR145

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
ASER215

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR234

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER235

237735

PDB entries from 2025-06-18

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