STYX_MOUSE
ID STYX_MOUSE Reviewed; 223 AA.
AC Q60969; Q3TMA3; Q60970; Q9DCF8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
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:0000303|PubMed:7592916};
GN Name=Styx {ECO:0000303|PubMed:7592916, ECO:0000312|MGI:MGI:1891150};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, LACK OF CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-120.
RC TISSUE=Skeletal muscle;
RX PubMed=7592916; DOI=10.1074/jbc.270.45.26782;
RA Wishart M.J., Denu J.M., Williams J.A., Dixon J.E.;
RT "A single mutation converts a novel phosphotyrosine binding domain into a
RT dual-specificity phosphatase.";
RL J. Biol. Chem. 270:26782-26785(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, Lung, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INTERACTION WITH CARHSP1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11842224; DOI=10.1073/pnas.251686198;
RA Wishart M.J., Dixon J.E.;
RT "The archetype STYX/dead-phosphatase complexes with a spermatid mRNA-
RT binding protein and is essential for normal sperm production.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2112-2117(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalytically inactive phosphatase (PubMed:7592916). Acts as
CC a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2) (By similarity). Modulates
CC cell-fate decisions and cell migration by spatiotemporal regulation of
CC MAPK1/MAPK3 (ERK1/ERK2) (By similarity). By binding to the F-box of
CC FBXW7, prevents the assembly of FBXW7 into the SCF E3 ubiquitin-protein
CC ligase complex, and thereby inhibits degradation of its substrates (By
CC similarity). Plays a role in spermatogenesis (PubMed:11842224).
CC {ECO:0000250|UniProtKB:Q8WUJ0, ECO:0000269|PubMed:11842224,
CC ECO:0000269|PubMed:7592916}.
CC -!- SUBUNIT: Interacts with MAPK1; independently of MAPK1 phosphorylation
CC status (By similarity). Interacts with CARHSP1/Crhsp-24
CC (PubMed:11842224). Interacts (via FQQ motif) with FBXW7 (via F-box
CC domain); the interaction is direct and prevents FBXW7 interaction with
CC SKP1, a component of the SCF(FBXW7) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUJ0, ECO:0000269|PubMed:11842224}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60969-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60969-2; Sequence=VSP_005174;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in muscle,
CC testis and brain (PubMed:7592916). In testis, expression starts 13-14
CC days after birth and is limited to the seminiferous tubule and to round
CC and elongating spermatids (PubMed:11842224). Expression is low in
CC condensing spermatids and pachytene spermatocytes, and absent in
CC spermatogonia, spermatozoa and somatic Sertoli cells (PubMed:11842224).
CC {ECO:0000269|PubMed:11842224, ECO:0000269|PubMed:7592916}.
CC -!- DISRUPTION PHENOTYPE: Males are infertile due to a disrupted spermatid
CC development, resulting in a >1000-fold decrease in spermatozoa
CC production. {ECO:0000269|PubMed:11842224}.
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. The binding pocket is however
CC sufficiently preserved to bind phosphorylated substrates, and may
CC protect them from phosphatases. {ECO:0000269|PubMed:7592916}.
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DR EMBL; U34973; AAA87036.1; -; mRNA.
DR EMBL; U34973; AAA87037.1; -; mRNA.
DR EMBL; AK002822; BAB22384.1; -; mRNA.
DR EMBL; AK030122; BAC26793.1; -; mRNA.
DR EMBL; AK046970; BAC32931.1; -; mRNA.
DR EMBL; AK166043; BAE38539.1; -; mRNA.
DR EMBL; BC038608; AAH38608.1; -; mRNA.
DR CCDS; CCDS26975.1; -. [Q60969-1]
DR PIR; I49364; I49364.
DR PIR; I49365; I49365.
DR RefSeq; NP_062611.2; NM_019637.3. [Q60969-1]
DR AlphaFoldDB; Q60969; -.
DR SMR; Q60969; -.
DR BioGRID; 207879; 1.
DR STRING; 10090.ENSMUSP00000094153; -.
DR iPTMnet; Q60969; -.
DR PhosphoSitePlus; Q60969; -.
DR MaxQB; Q60969; -.
DR PaxDb; Q60969; -.
DR PRIDE; Q60969; -.
DR ProteomicsDB; 257099; -. [Q60969-1]
DR ProteomicsDB; 257100; -. [Q60969-2]
DR DNASU; 56291; -.
DR Ensembl; ENSMUST00000096420; ENSMUSP00000094153; ENSMUSG00000071748. [Q60969-1]
DR Ensembl; ENSMUST00000226873; ENSMUSP00000153854; ENSMUSG00000053205. [Q60969-1]
DR Ensembl; ENSMUST00000228311; ENSMUSP00000154148; ENSMUSG00000053205. [Q60969-1]
DR GeneID; 56291; -.
DR KEGG; mmu:56291; -.
DR UCSC; uc007tgo.1; mouse. [Q60969-1]
DR CTD; 6815; -.
DR MGI; MGI:1891150; Styx.
DR VEuPathDB; HostDB:ENSMUSG00000053205; -.
DR VEuPathDB; HostDB:ENSMUSG00000071748; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000154859; -.
DR HOGENOM; CLU_027074_7_1_1; -.
DR InParanoid; Q60969; -.
DR OMA; EWRYEMR; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q60969; -.
DR TreeFam; TF350439; -.
DR BioGRID-ORCS; 56291; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q60969; -.
DR Proteomes; UP000000589; Chromosome 14.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q60969; protein.
DR Bgee; ENSMUSG00000053205; Expressed in spermatocyte and 99 other tissues.
DR ExpressionAtlas; Q60969; baseline and differential.
DR Genevisible; Q60969; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990444; F:F-box domain binding; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0001691; F:pseudophosphatase activity; ISO:MGI.
DR GO; GO:0045204; P:MAPK export from nucleus; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0062026; P:negative regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..223
FT /note="Serine/threonine/tyrosine-interacting protein"
FT /id="PRO_0000094951"
FT DOMAIN 28..176
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 199..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 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUJ0"
FT VAR_SEQ 169..223
FT /note="EYEAIYLAKLTIQMMSPLQIERSLAVHSGTTGSVKRTHEEDDDFGNMQVATA
FT QNG -> LWLSWNSARSAPLPLKQRQVYHCAFKTSKNKQTNNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7592916"
FT /id="VSP_005174"
FT MUTAGEN 120
FT /note="G->C: Confers phosphatase activity."
FT /evidence="ECO:0000269|PubMed:7592916"
FT CONFLICT 11
FT /note="L -> V (in Ref. 1; AAA87036/AAA87037)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="R -> T (in Ref. 2; BAC32931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 25430 MW; 7D13AFEF2B66B723 CRC64;
MEDVKLEFPS LPQCKDDAEE WTYPMRREMQ EVLPGLFLGP YSSAMKSKLP ILQKHGITHI
ICIRQNIEAN FIKPNFQQLF RYLVLDIADN PVENIIRFFP MTKEFIDGSL QNGGKVLVHG
NAGISRSAAF VIAYIMETFG MKYRDAFAYV QERRFCINPN AGFVHQLQEY EAIYLAKLTI
QMMSPLQIER SLAVHSGTTG SVKRTHEEDD DFGNMQVATA QNG
