STYL2_MOUSE
ID STYL2_MOUSE Reviewed; 1138 AA.
AC Q148W8; Q3UQN8; Q6PCZ9; Q8BX87;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine/threonine/tyrosine-interacting-like protein 2;
DE AltName: Full=Inactive dual specificity phosphatase 27 {ECO:0000305};
GN Name=Styxl2; Synonyms=Dusp27 {ECO:0000312|MGI:MGI:2685055};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-373; THR-427;
RP SER-503; SER-555; SER-862; SER-929; SER-966 AND SER-1016, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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: 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}.
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DR EMBL; AK048603; BAC33386.1; -; mRNA.
DR EMBL; AK142263; BAE25001.1; -; mRNA.
DR EMBL; BC059034; AAH59034.1; -; mRNA.
DR EMBL; BC117936; AAI17937.1; -; mRNA.
DR CCDS; CCDS15446.1; -.
DR RefSeq; NP_001028516.2; NM_001033344.3.
DR RefSeq; NP_001153521.1; NM_001160049.1.
DR AlphaFoldDB; Q148W8; -.
DR SMR; Q148W8; -.
DR BioGRID; 232253; 2.
DR STRING; 10090.ENSMUSP00000083155; -.
DR iPTMnet; Q148W8; -.
DR PhosphoSitePlus; Q148W8; -.
DR PaxDb; Q148W8; -.
DR PeptideAtlas; Q148W8; -.
DR PRIDE; Q148W8; -.
DR ProteomicsDB; 277638; -.
DR Antibodypedia; 2486; 22 antibodies from 10 providers.
DR DNASU; 240892; -.
DR Ensembl; ENSMUST00000085992; ENSMUSP00000083155; ENSMUSG00000026564.
DR Ensembl; ENSMUST00000192369; ENSMUSP00000141564; ENSMUSG00000026564.
DR GeneID; 240892; -.
DR KEGG; mmu:240892; -.
DR UCSC; uc007dkh.2; mouse.
DR CTD; 240892; -.
DR MGI; MGI:2685055; Dusp27.
DR VEuPathDB; HostDB:ENSMUSG00000026564; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159723; -.
DR HOGENOM; CLU_009343_0_0_1; -.
DR InParanoid; Q148W8; -.
DR OMA; FNTPCVM; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q148W8; -.
DR TreeFam; TF351505; -.
DR BioGRID-ORCS; 240892; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q148W8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q148W8; protein.
DR Bgee; ENSMUSG00000026564; Expressed in interventricular septum and 72 other tissues.
DR Genevisible; Q148W8; MM.
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 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1138
FT /note="Serine/threonine/tyrosine-interacting-like protein
FT 2"
FT /id="PRO_0000302839"
FT DOMAIN 132..280
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 145
FT /note="E -> D (in Ref. 1; BAE25001)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="K -> R (in Ref. 1; BAC33386)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1138 AA; 128575 MW; 0187A4C2D943AA11 CRC64;
MATGGDAEEE QVVPNEEDEA DVRAVQARYL RSPSPSQYSV VSEAETESIF MEPIHLSSAV
AAKQIINEEL KPRGLRTDTE CPGMLESAEQ LLVEDLYNRV REKMDDRSLF NTPCVLDLQR
ALTQDRQEAP RNEVDEVWPN VFIAEKSVAV NKGRLKRLGI THILNAAHGT GVYTGSEFYT
GLEIQYLGVE VDDFPEVDIS QHFRKAAEFL DEALLTYRGK VLVSSEMGIS RSAVLVVAYL
MIFHSMAILE ALMTVRRKRA IYPNDGFLKQ LRELNEKLME EREEEDGEEE SEEDAGSMLG
ARVNSLMVEE EDDATSHLSG SSLGKASQVS KPVTLIDDEE EEKKLYEEWR KGQGFPKGEA
AQGRKGRSCS MSSAQDGDDC EDEDVERIIQ EWQSRNERYQ AKGREQWNRE EEEEEENSYS
SRRRRHTLSE SSASESVSSH DIRILKQQLE RSTQSRRGRY RSDSESSEST WDMWNERLVE
IEKEAARKYR SKSKREELDG DCSEAGGRVR EDDEESVLSE ASSFYNFCSR NKDKLTPLER
WKIKRIQFGF HKKDSEAGDG GSEHGTEEAA AGEKNLSDVN LTAYQAWKLK HQKKVGSENK
EEVVEMSKGE DTVLAKKRQR RLELLERSRQ TLEESQSMGS WEADSSTASR SIPLSAFSSA
APSVSADGDT ASVLSTQSHR SHASNMPATP LPNLPVGPGD TISIASIQNW IANVVNETLA
QKQNEMLLLS RPPSVASMKA APAACGLGGD DQLSVLSTSL SGCLPPPSQG RPSSDVQSVL
SSTSSLTSRA EGSGNKVRGT SKPIYSLFAD NVDLKELGRK EKEMQMELQE KMSEYKMEKL
ASDNKRSSLF KKKKAKDDED MSVGDRDEDT DSAIGSFRYS SRSNSQKPET DASSSLAISD
HYRNGRSMGN EMDSNINTWL SGLRMEEKSP PQSDWSGSSR GRYTRSSLLR ETESKSCSYK
FSKSRSQEQD TSFHEANGDT VRNTSRFSSS TTKEAREMHK FSRSTFSETS SSREESPEPY
FFRRTPEPSD GEESPEPRRP NWTRPRDWED VEESSKSDFA EFGAKRKFTQ SFMRSEEEGE
KERTENREEG RFASGRQSQY RRSTNQQEEE EMDDEAIIAA WRKRQEETRT KLQRRRED
