ID STYL1_HUMAN Reviewed; 313 AA.
AC Q9Y6J8; Q9UBP1; Q9UK06; Q9UK07; Q9UKG2; Q9UKG3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 181.
DE RecName: Full=Serine/threonine/tyrosine-interacting-like protein 1;
DE AltName: Full=Dual specificity phosphatase inhibitor MK-STYX;
DE AltName: Full=Dual specificity protein phosphatase 24;
DE AltName: Full=Inactive dual specificity protein phosphatase MK-STYX {ECO:0000305};
DE AltName: Full=Map kinase phosphatase-like protein MK-STYX;
GN Name=STYXL1; Synonyms=DUSP24, MKSTYX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9757831; DOI=10.1016/s0968-0004(98)01241-9;
RA Wishart M.J., Dixon J.E.;
RT "Gathering STYX: phosphatase-like form predicts functions for unique
RT protein-interaction domains.";
RL Trends Biochem. Sci. 23:301-306(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 46-313 (ISOFORMS 3; 4 AND 5).
RA Walker L.C., Morris C.M.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-313 (ISOFORMS 2 AND 3).
RA Dayton M.A., Blanchard K.L.;
RT "Differential expression of PTPase RNAs resulting from K562 differentiation
RT induced by PMA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, LACK OF CATALYTIC ACTIVITY, INTERACTION WITH G3BP1, AND
RP MUTAGENESIS OF 245-PHE-SER-246.
RX PubMed=20180778; DOI=10.1042/bj20091383;
RA Hinton S.D., Myers M.P., Roggero V.R., Allison L.A., Tonks N.K.;
RT "The pseudophosphatase MK-STYX interacts with G3BP and decreases stress
RT granule formation.";
RL Biochem. J. 427:349-357(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21262771; DOI=10.1128/mcb.00788-10;
RA Niemi N.M., Lanning N.J., Klomp J.A., Tait S.W., Xu Y., Dykema K.J.,
RA Murphy L.O., Gaither L.A., Xu H.E., Furge K.A., Green D.R., MacKeigan J.P.;
RT "MK-STYX, a catalytically inactive phosphatase regulating mitochondrially
RT dependent apoptosis.";
RL Mol. Cell. Biol. 31:1357-1368(2011).
RN [8]
RP FUNCTION, LACK OF CATALYTIC ACTIVITY, AND MUTAGENESIS OF 245-PHE-SER-246.
RX PubMed=23163895; DOI=10.1111/febs.12068;
RA Barr J.E., Munyikwa M.R., Frazier E.A., Hinton S.D.;
RT "The pseudophosphatase MK-STYX inhibits stress granule assembly
RT independently of Ser149 phosphorylation of G3BP-1.";
RL FEBS J. 280:273-284(2013).
RN [9]
RP FUNCTION, AND INTERACTION WITH PTPMT1.
RX PubMed=24709986; DOI=10.1371/journal.pone.0093896;
RA Niemi N.M., Sacoman J.L., Westrate L.M., Gaither L.A., Lanning N.J.,
RA Martin K.R., MacKeigan J.P.;
RT "The pseudophosphatase MK-STYX physically and genetically interacts with
RT the mitochondrial phosphatase PTPMT1.";
RL PLoS ONE 9:E93896-E93896(2014).
RN [10]
RP FUNCTION.
RX PubMed=29250526; DOI=10.3389/fmolb.2017.00076;
RA Banks D.A., Dahal A., McFarland A.G., Flowers B.M., Stephens C.A.,
RA Swack B., Gugssa A., Anderson W.A., Hinton S.D.;
RT "MK-STYX Alters the Morphology of Primary Neurons, and Outgrowths in MK-
RT STYX Overexpressing PC-12 Cells Develop a Neuronal Phenotype.";
RL Front. Mol. Biosci. 4:76-76(2017).
CC -!- FUNCTION: Catalytically inactive phosphatase (PubMed:20180778,
CC PubMed:23163895). By binding to G3BP1, inhibits the formation of G3BP1-
CC induced stress granules (PubMed:20180778, PubMed:23163895). Does not
CC act by protecting the dephosphorylation of G3BP1 at 'Ser-149'
CC (PubMed:23163895). Inhibits PTPMT1 phosphatase activity
CC (PubMed:24709986). By inhibiting PTPMT1, positively regulates intrinsic
CC apoptosis (PubMed:21262771). May play a role in the formation of
CC neurites during neuronal development (PubMed:29250526).
CC {ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:21262771,
CC ECO:0000269|PubMed:23163895, ECO:0000269|PubMed:24709986,
CC ECO:0000269|PubMed:29250526}.
CC -!- SUBUNIT: Interacts with G3BP1 (PubMed:20180778). Interacts with PTPMT1;
CC the interaction inhibits PTPMT1 catalytic activity (PubMed:24709986).
CC {ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:24709986}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:21262771}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9Y6J8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6J8-2; Sequence=VSP_005178, VSP_005179;
CC Name=3;
CC IsoId=Q9Y6J8-3; Sequence=VSP_005180;
CC Name=4;
CC IsoId=Q9Y6J8-4; Sequence=VSP_005175;
CC Name=5;
CC IsoId=Q9Y6J8-5; Sequence=VSP_005176, VSP_005177;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the two active site residues His and Cys at position 245
CC and 246 which are essential for dual-specificity phosphatase activity.
CC Lacks phosphatase activity. {ECO:0000269|PubMed:20180778,
CC ECO:0000269|PubMed:23163895}.
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DR EMBL; AF069762; AAD36983.1; -; mRNA.
DR EMBL; AC006330; AAS07535.1; -; Genomic_DNA.
DR EMBL; BC024035; AAH24035.1; -; mRNA.
DR EMBL; AF188201; AAF04111.1; -; mRNA.
DR EMBL; AF188202; AAF04112.1; -; mRNA.
DR EMBL; AF188203; AAF04113.1; -; mRNA.
DR EMBL; AF188204; AAF04114.1; -; mRNA.
DR EMBL; AF169647; AAD53723.1; -; mRNA.
DR EMBL; AF169648; AAD53724.1; -; mRNA.
DR CCDS; CCDS5580.1; -. [Q9Y6J8-1]
DR CCDS; CCDS83193.1; -. [Q9Y6J8-4]
DR RefSeq; NP_001304714.1; NM_001317785.1. [Q9Y6J8-1]
DR RefSeq; NP_001304715.1; NM_001317786.1. [Q9Y6J8-1]
DR RefSeq; NP_001304716.1; NM_001317787.1. [Q9Y6J8-4]
DR RefSeq; NP_001304717.1; NM_001317788.1.
DR RefSeq; NP_001304718.1; NM_001317789.1.
DR RefSeq; NP_057170.1; NM_016086.2. [Q9Y6J8-1]
DR RefSeq; XP_011514595.1; XM_011516293.2. [Q9Y6J8-1]
DR AlphaFoldDB; Q9Y6J8; -.
DR SMR; Q9Y6J8; -.
DR BioGRID; 119663; 47.
DR IntAct; Q9Y6J8; 7.
DR MINT; Q9Y6J8; -.
DR STRING; 9606.ENSP00000248600; -.
DR DEPOD; STYXL1; -.
DR iPTMnet; Q9Y6J8; -.
DR PhosphoSitePlus; Q9Y6J8; -.
DR BioMuta; STYXL1; -.
DR DMDM; 29840801; -.
DR jPOST; Q9Y6J8; -.
DR MassIVE; Q9Y6J8; -.
DR MaxQB; Q9Y6J8; -.
DR PaxDb; 9606-ENSP00000248600; -.
DR PeptideAtlas; Q9Y6J8; -.
DR ProteomicsDB; 86702; -. [Q9Y6J8-1]
DR ProteomicsDB; 86703; -. [Q9Y6J8-2]
DR ProteomicsDB; 86704; -. [Q9Y6J8-3]
DR ProteomicsDB; 86705; -. [Q9Y6J8-4]
DR ProteomicsDB; 86706; -. [Q9Y6J8-5]
DR Antibodypedia; 29274; 61 antibodies from 18 providers.
DR DNASU; 51657; -.
DR Ensembl; ENST00000248600.5; ENSP00000248600.1; ENSG00000127952.17. [Q9Y6J8-1]
DR Ensembl; ENST00000340062.9; ENSP00000343383.5; ENSG00000127952.17. [Q9Y6J8-4]
DR Ensembl; ENST00000359697.8; ENSP00000352726.3; ENSG00000127952.17. [Q9Y6J8-1]
DR Ensembl; ENST00000360591.7; ENSP00000353798.4; ENSG00000127952.17. [Q9Y6J8-4]
DR Ensembl; ENST00000431581.5; ENSP00000392221.1; ENSG00000127952.17. [Q9Y6J8-1]
DR GeneID; 51657; -.
DR KEGG; hsa:51657; -.
DR MANE-Select; ENST00000359697.8; ENSP00000352726.3; NM_001317785.2; NP_001304714.1.
DR UCSC; uc003uek.5; human. [Q9Y6J8-1]
DR AGR; HGNC:18165; -.
DR CTD; 51657; -.
DR DisGeNET; 51657; -.
DR GeneCards; STYXL1; -.
DR HGNC; HGNC:18165; STYXL1.
DR HPA; ENSG00000127952; Low tissue specificity.
DR neXtProt; NX_Q9Y6J8; -.
DR OpenTargets; ENSG00000127952; -.
DR PharmGKB; PA134942462; -.
DR VEuPathDB; HostDB:ENSG00000127952; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00390000010113; -.
DR HOGENOM; CLU_027074_1_0_1; -.
DR InParanoid; Q9Y6J8; -.
DR OMA; RFCVVYD; -.
DR OrthoDB; 5382152at2759; -.
DR PhylomeDB; Q9Y6J8; -.
DR TreeFam; TF352452; -.
DR PathwayCommons; Q9Y6J8; -.
DR SignaLink; Q9Y6J8; -.
DR BioGRID-ORCS; 51657; 9 hits in 1171 CRISPR screens.
DR ChiTaRS; STYXL1; human.
DR GeneWiki; STYXL1; -.
DR GenomeRNAi; 51657; -.
DR Pharos; Q9Y6J8; Tbio.
DR PRO; PR:Q9Y6J8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y6J8; Protein.
DR Bgee; ENSG00000127952; Expressed in right uterine tube and 191 other cell types or tissues.
DR ExpressionAtlas; Q9Y6J8; baseline and differential.
DR Genevisible; Q9Y6J8; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0001691; F:pseudophosphatase activity; IMP:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0062030; P:negative regulation of stress granule assembly; IMP:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IGI:UniProtKB.
DR CDD; cd14517; DSP_STYXL1; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR46659; SERINE/THREONINE/TYROSINE-INTERACTING-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR46659:SF1; SERINE_THREONINE_TYROSINE-INTERACTING-LIKE PROTEIN 1; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; Reference proteome.
FT CHAIN 1..313
FT /note="Serine/threonine/tyrosine-interacting-like protein
FT 1"
FT /id="PRO_0000094837"
FT DOMAIN 27..138
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 159..302
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 56..151
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005175"
FT VAR_SEQ 103..138
FT /note="DLVPQAAIEYGRILTRLTHHPVYILKGGYERFSGTY -> GTGCISAIP
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005176"
FT VAR_SEQ 139..313
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005177"
FT VAR_SEQ 233..287
FT /note="EIHHHLGSVILIFSTQGISRSCAAIIAYLMHSNEQTLQRSWAYVKKCKNNMC
FT PNR -> GYQPQLCRHHSLPHA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005178"
FT VAR_SEQ 234..313
FT /note="IHHHLGSVILIFSTQGISRSCAAIIAYLMHSNEQTLQRSWAYVKKCKNNMCP
FT NRGLVSQLLEWEKTILGDSITNIMDPLY -> VLGLCQEVQKQHVSKSGIGEPAAGMGE
FT DYPWRFHHKHHGSALLIFSEAHRRVLKSLTWGHFVGGGPECVYPGLSGRRRPLLPESL
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005180"
FT VAR_SEQ 288..313
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005179"
FT MUTAGEN 245..246
FT /note="FS->HC: Confers phosphatase activity.
FT Dephosphorylates G3BP1 at 'Ser-149'. Loss of interaction
FT with G3BP1. Reduces arsenite-induced stress granule
FT formation."
FT /evidence="ECO:0000269|PubMed:20180778,
FT ECO:0000269|PubMed:23163895"
SQ SEQUENCE 313 AA; 35818 MW; 5EDB25AB4EB60419 CRC64;
MPGLLLCEPT ELYNILNQAT KLSRLTDPNY LCLLDVRSKW EYDESHVITA LRVKKKNNEY
LLPESVDLEC VKYCVVYDNN SSTLEILLKD DDDDSDSDGD GKDLVPQAAI EYGRILTRLT
HHPVYILKGG YERFSGTYHF LRTQKIIWMP QELDAFQPYP IEIVPGKVFV GNFSQACDPK
IQKDLKIKAH VNVSMDTGPF FAGDADKLLH IRIEDSPEAQ ILPFLRHMCH FIEIHHHLGS
VILIFSTQGI SRSCAAIIAY LMHSNEQTLQ RSWAYVKKCK NNMCPNRGLV SQLLEWEKTI
LGDSITNIMD PLY
//
