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STYL1_HUMAN
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   03-AUG-2022, entry version 172.
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; Q9Y6J8; -.
DR   PeptideAtlas; Q9Y6J8; -.
DR   PRIDE; 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; 55 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   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; TMAYLMH; -.
DR   OrthoDB; 845704at2759; -.
DR   PhylomeDB; Q9Y6J8; -.
DR   TreeFam; TF352452; -.
DR   PathwayCommons; Q9Y6J8; -.
DR   SignaLink; Q9Y6J8; -.
DR   BioGRID-ORCS; 51657; 9 hits in 1079 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 189 other 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: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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IGI:UniProtKB.
DR   Gene3D; 3.40.250.10; -; 1.
DR   Gene3D; 3.90.190.10; -; 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   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF52821; SSF52821; 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
 
 
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