ID   STYX_PONAB              Reviewed;         223 AA.
AC   Q5RDP3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Serine/threonine/tyrosine-interacting protein {ECO:0000305};
DE   AltName: Full=Inactive tyrosine-protein phosphatase STYX {ECO:0000305};
DE   AltName: Full=Phosphoserine/threonine/tyrosine interaction protein {ECO:0000250|UniProtKB:Q60969};
GN   Name=STYX;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytically inactive phosphatase. Acts as a nuclear anchor
CC       for MAPK1/MAPK3 (ERK1/ERK2). Modulates cell-fate decisions and cell
CC       migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2). By
CC       binding to the F-box of FBXW7, prevents the assembly of FBXW7 into the
CC       SCF E3 ubiquitin-protein ligase complex, and thereby inhibits
CC       degradation of its substrates (By similarity). Plays a role in
CC       spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q60969,
CC       ECO:0000250|UniProtKB:Q8WUJ0}.
CC   -!- SUBUNIT: Interacts with MAPK1; independently of MAPK1 phosphorylation
CC       status (By similarity). Interacts with CARHSP1/Crhsp-24 (By
CC       similarity). Interacts (via FQQ motif) with FBXW7 (via F-box domain);
CC       the interaction is direct and prevents FBXW7 interaction with SKP1, a
CC       component of the SCF(FBXW7) complex. {ECO:0000250|UniProtKB:Q60969,
CC       ECO:0000250|UniProtKB:Q8WUJ0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WUJ0}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WUJ0}. Note=Predominantly
CC       localizes to the nucleus. {ECO:0000250|UniProtKB:Q8WUJ0}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
CC   -!- CAUTION: Contains a Gly residue instead of a conserved Cys residue at
CC       position 120 in the dsPTPase catalytic loop which renders it
CC       catalytically inactive as a phosphatase (By similarity). The binding
CC       pocket is however sufficiently preserved to bind phosphorylated
CC       substrates, and may protect them from phosphatases (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WUJ0}.
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DR   EMBL; CR857861; CAH90114.1; -; mRNA.
DR   RefSeq; NP_001153320.1; NM_001159848.1.
DR   AlphaFoldDB; Q5RDP3; -.
DR   SMR; Q5RDP3; -.
DR   STRING; 9601.ENSPPYP00000006613; -.
DR   GeneID; 100294693; -.
DR   KEGG; pon:100294693; -.
DR   CTD; 6815; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   InParanoid; Q5RDP3; -.
DR   OrthoDB; 1576308at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0045204; P:MAPK export from nucleus; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..223
FT                   /note="Serine/threonine/tyrosine-interacting protein"
FT                   /id="PRO_0000351653"
FT   DOMAIN          28..176
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          197..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           76..78
FT                   /note="Interaction with FBXW7"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUJ0"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUJ0"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUJ0"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUJ0"
SQ   SEQUENCE   223 AA;  25506 MW;  9069175A678538F2 CRC64;
     MEDVKLEFPS LPQCKEDAEE WTYPMRREMQ EILPGLFLGP YSSAMKSKLP ILQKHGITHI
     ICIRQNIEAN FIKPNFQQLF RYLVLDIADN PVENIIRFFP MTKEFIDGSL QMGGKVLVHG
     NAGISRSAAF VIAYIMETFG MKYRDAFAYV QERRFCINPN AGFVHQLQEY EAIYLAKLTI
     QMMSPLQIER SLSVHSGTTG SLKRTHEEED DFGTMQVATA QNG