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8XI3

Structure of mouse SCMC-14-3-3gama complex

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ALAGftDgTVRIWDL
ChainResidueDetails
BALA402-LEU416

site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
FARG42-VAL52

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
FTYR216-SER235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000255
ChainResidueDetails
BSEP139
BSER187
BSEP209
DARG132

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H808
ChainResidueDetails
BSER519
DMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed => ECO:0000250|UniProtKB:P61981
ChainResidueDetails
FVAL2
DVAL2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
FSER71
DSER71

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
FTYR133
DTYR133

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P61981
ChainResidueDetails
FTHR145
FTHR234
DTHR145
DTHR234

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61983
ChainResidueDetails
FSER215
DSER215

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61981
ChainResidueDetails
FSER235
DSER235

225681

PDB entries from 2024-10-02

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