1433G_PONAB
ID 1433G_PONAB Reviewed; 247 AA.
AC Q5RC20;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=14-3-3 protein gamma;
DE Contains:
DE RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN Name=YWHAG;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner.
CC -!- SUBUNIT: Homodimer. Interacts with MDM4 (phosphorylated); negatively
CC regulates MDM4 activity toward TP53. Interacts with RAF1, SSH1 and
CC CRTC2/TORC2. Interacts with ABL1 (phosphorylated form); the interaction
CC retains it in the cytoplasm. Interacts with GAB2 and SAMSN1. Interacts
CC with PKA-phosphorylated AANAT and SIRT2 (By similarity). Interacts with
CC the 'Thr-369' phosphorylated form of DAPK2 (By similarity). Interacts
CC with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with
CC SLITRK1 (By similarity). Interacts with LRRK2; this interaction is
CC dependent on LRRK2 phosphorylation (By similarity). Interacts with
CC MARK2 and MARK3 (By similarity). Interacts with MEFV (By similarity).
CC Interacts with ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens
CC its interaction with TSC2 and PIK3C3 (By similarity). Interacts with TH
CC (phosphorylated form); one YWHAG dimer bounds to one TH tetramer, this
CC interaction may influence the phosphorylation and dephosphorylation of
CC TH (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61981,
CC ECO:0000250|UniProtKB:P61982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by various PKC isozymes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; CR858462; CAH90690.1; -; mRNA.
DR RefSeq; NP_001127322.1; NM_001133850.1.
DR AlphaFoldDB; Q5RC20; -.
DR SMR; Q5RC20; -.
DR STRING; 9601.ENSPPYP00000019583; -.
DR GeneID; 100174383; -.
DR KEGG; pon:100174383; -.
DR CTD; 7532; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; Q5RC20; -.
DR OMA; MANTERD; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102003; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..247
FT /note="14-3-3 protein gamma"
FT /id="PRO_0000058608"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT CHAIN 2..247
FT /note="14-3-3 protein gamma, N-terminally processed"
FT /id="PRO_0000367909"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 2
FT /note="N-acetylvaline; in 14-3-3 protein gamma, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61983"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61981"
SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64;
MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK
VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
DGGEGNN
