STYL2_HUMAN
ID STYL2_HUMAN Reviewed; 1158 AA.
AC Q5VZP5; A0AUM4; Q9C074;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine/threonine/tyrosine-interacting-like protein 2;
DE AltName: Full=Inactive dual specificity phosphatase 27 {ECO:0000305};
GN Name=STYXL2 {ECO:0000312|HGNC:HGNC:25034}; Synonyms=DUSP27;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1157, AND VARIANTS ASP-265 AND
RP GLN-855.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 501-1158.
RA Li D.X., Bachinski L.L., Shaffer L., Roberts R.;
RT "Isolation of a novel gene preferably expressed in cardiac and skeletal
RT muscles by mRNA differential display.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for myofiber maturation.
CC {ECO:0000250|UniProtKB:F1QWM2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:F1QWM2}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-225 is present instead of the conserved Cys which is
CC expected to be an active site residue suggesting that this protein has
CC lost its phosphatase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK02011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL158837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115387; AAI15388.1; -; mRNA.
DR EMBL; AF119045; AAK02011.1; ALT_INIT; mRNA.
DR CCDS; CCDS30932.1; -.
DR RefSeq; NP_001073895.1; NM_001080426.2.
DR AlphaFoldDB; Q5VZP5; -.
DR SMR; Q5VZP5; -.
DR BioGRID; 124920; 3.
DR IntAct; Q5VZP5; 2.
DR STRING; 9606.ENSP00000354483; -.
DR DEPOD; DUSP27; -.
DR iPTMnet; Q5VZP5; -.
DR PhosphoSitePlus; Q5VZP5; -.
DR BioMuta; DUSP27; -.
DR DMDM; 74747829; -.
DR EPD; Q5VZP5; -.
DR jPOST; Q5VZP5; -.
DR MassIVE; Q5VZP5; -.
DR PaxDb; Q5VZP5; -.
DR PeptideAtlas; Q5VZP5; -.
DR PRIDE; Q5VZP5; -.
DR ProteomicsDB; 65715; -.
DR Antibodypedia; 2486; 22 antibodies from 10 providers.
DR DNASU; 92235; -.
DR Ensembl; ENST00000271385.9; ENSP00000271385.5; ENSG00000198842.10.
DR Ensembl; ENST00000361200.7; ENSP00000354483.2; ENSG00000198842.10.
DR Ensembl; ENST00000443333.1; ENSP00000404874.1; ENSG00000198842.10.
DR GeneID; 92235; -.
DR KEGG; hsa:92235; -.
DR MANE-Select; ENST00000361200.7; ENSP00000354483.2; NM_001080426.3; NP_001073895.1.
DR UCSC; uc001geb.2; human.
DR CTD; 92235; -.
DR DisGeNET; 92235; -.
DR GeneCards; STYXL2; -.
DR HGNC; HGNC:25034; STYXL2.
DR HPA; ENSG00000198842; Group enriched (heart muscle, skeletal muscle, tongue).
DR neXtProt; NX_Q5VZP5; -.
DR OpenTargets; ENSG00000198842; -.
DR VEuPathDB; HostDB:ENSG00000198842; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159723; -.
DR HOGENOM; CLU_009343_0_0_1; -.
DR InParanoid; Q5VZP5; -.
DR OMA; FNTPCVM; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q5VZP5; -.
DR TreeFam; TF351505; -.
DR PathwayCommons; Q5VZP5; -.
DR SignaLink; Q5VZP5; -.
DR BioGRID-ORCS; 92235; 15 hits in 1067 CRISPR screens.
DR ChiTaRS; DUSP27; human.
DR GenomeRNAi; 92235; -.
DR Pharos; Q5VZP5; Tdark.
DR PRO; PR:Q5VZP5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VZP5; protein.
DR Bgee; ENSG00000198842; Expressed in left ventricle myocardium and 88 other tissues.
DR Genevisible; Q5VZP5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
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 PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..1158
FT /note="Serine/threonine/tyrosine-interacting-like protein
FT 2"
FT /id="PRO_0000302838"
FT DOMAIN 132..280
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148W8"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q148W8"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148W8"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148W8"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148W8"
FT VARIANT 265
FT /note="E -> D (in dbSNP:rs267745)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034964"
FT VARIANT 466
FT /note="R -> H (in dbSNP:rs6668826)"
FT /id="VAR_034965"
FT VARIANT 505
FT /note="A -> T (in dbSNP:rs3795605)"
FT /id="VAR_034966"
FT VARIANT 855
FT /note="K -> Q (in dbSNP:rs267746)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034967"
FT VARIANT 1124
FT /note="T -> N (in dbSNP:rs2281959)"
FT /id="VAR_034968"
SQ SEQUENCE 1158 AA; 130176 MW; 6843A7062D80CBB2 CRC64;
MATRKDTEEE QVVPSEEDEA NVRAVQAHYL RSPSPSQYSM VSDAETESIF MEPIHLSSAI
AAKQIINEEL KPPGVRADAE CPGMLESAEQ LLVEDLYNRV REKMDDTSLY NTPCVLDLQR
ALVQDRQEAP WNEVDEVWPN VFIAEKSVAV NKGRLKRLGI THILNAAHGT GVYTGPEFYT
GLEIQYLGVE VDDFPEVDIS QHFRKASEFL DEALLTYRGK VLVSSEMGIS RSAVLVVAYL
MIFHNMAILE ALMTVRKKRA IYPNEGFLKQ LRELNEKLME EREEDYGREG GSAEAEEGEG
TGSMLGARVH ALTVEEEDDS ASHLSGSSLG KATQASKPLT LIDEEEEEKL YEQWKKGQGL
LSDKVPQDGG GWRSASSGQG GEELEDEDVE RIIQEWQSRN ERYQAEGYRR WGREEEKEEE
SDAGSSVGRR RRTLSESSAW ESVSSHDIWV LKQQLELNRP DHGRRRRADS MSSESTWDAW
NERLLEIEKE ASRRYHAKSK REEAADRSSE AGSRVREDDE DSVGSEASSF YNFCSRNKDK
LTALERWKIK RIQFGFHKKD LGAGDSSGEP GAEEAVGEKN PSDVSLTAYQ AWKLKHQKKV
GSENKEEVVE LSKGEDSALA KKRQRRLELL ERSRQTLEES QSMASWEADS STASGSIPLS
AFWSADPSVS ADGDTTSVLS TQSHRSHLSQ AASNIAGCST SNPTTPLPNL PVGPGDTISI
ASIQNWIANV VSETLAQKQN EMLLLSRSPS VASMKAVPAA SCLGDDQVSM LSGHSSSSLG
GCLLPQSQAR PSSDMQSVLS CNTTLSSPAE SCRSKVRGTS KPIFSLFADN VDLKELGRKE
KEMQMELREK MSEYKMEKLA SDNKRSSLFK KKKVKEDEDD GVGDGDEDTD SAIGSFRYSS
RSNSQKPETD TCSSLAVCDH YASGSRVGKE MDSSINKWLS GLRTEEKPPF QSDWSGSSRG
KYTRSSLLRE TESKSSSYKF SKSQSEEQDT SSYHEANGNS VRSTSRFSSS STREGREMHK
FSRSTYNETS SSREESPEPY FFRRTPESSE REESPEPQRP NWARSRDWED VEESSKSDFS
EFGAKRKFTQ SFMRSEEEGE KERTENREEG RFASGRRSQY RRSTDREEEE EMDDEAIIAA
WRRRQEETRT KLQKRRED
