PTN18_MOUSE
ID PTN18_MOUSE Reviewed; 453 AA.
AC Q61152; Q4JFH4; Q62404; Q922E3;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 18;
DE EC=3.1.3.48;
DE AltName: Full=Fetal liver phosphatase 1;
DE Short=FLP-1;
DE AltName: Full=PTP-K1;
GN Name=Ptpn18; Synonyms=Flp1, Ptpk1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8695832;
RA Cheng J., Daimaru L., Fennie C., Lasky L.A.;
RT "A novel protein tyrosine phosphatase expressed in lin(lo)CD34(hi)Sca(hi)
RT hematopoietic progenitor cells.";
RL Blood 88:1156-1167(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8875997;
RA Huang K., Sommers C.L., Grinberg A., Kozak C.A., Love P.E.;
RT "Cloning and characterization of PTP-K1, a novel nonreceptor protein
RT tyrosine phosphatase highly expressed in bone marrow.";
RL Oncogene 13:1567-1573(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Fetal liver;
RX PubMed=8977243;
RA Dosil M., Leibman N., Lemischka I.R.;
RT "Cloning and characterization of fetal liver phosphatase 1, a nuclear
RT protein tyrosine phosphatase isolated from hematopoietic stem cells.";
RL Blood 88:4510-4525(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Intestinal mucosa;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [6]
RP INTERACTION WITH PSTPIP1.
RX PubMed=9265651; DOI=10.1083/jcb.138.4.845;
RA Spencer S., Dowbenko D., Cheng J., Li W., Brush J., Utzig S., Simanis V.,
RA Lasky L.A.;
RT "PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that
RT is a substrate for a PEST tyrosine phosphatase.";
RL J. Cell Biol. 138:845-860(1997).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381 AND TYR-419, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 involved in growth and differentiation of
CC hematopoietic cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with PSTPIP1. {ECO:0000269|PubMed:9265651}.
CC -!- INTERACTION:
CC Q61152; P97814: Pstpip1; NbExp=3; IntAct=EBI-7074223, EBI-7484574;
CC Q61152; Q99M15: Pstpip2; NbExp=7; IntAct=EBI-7074223, EBI-8653964;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8977243}. Cytoplasm
CC {ECO:0000269|PubMed:8977243}.
CC -!- TISSUE SPECIFICITY: Highest expression in bone marrow. Also expressed
CC in kidney, lung, ovary, spleen, thymus and lymph node.
CC {ECO:0000269|PubMed:8695832, ECO:0000269|PubMed:8875997,
CC ECO:0000269|PubMed:8977243}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo from day 15.5.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; U49853; AAB18623.1; -; mRNA.
DR EMBL; U35124; AAB82736.1; -; mRNA.
DR EMBL; U52523; AAC52991.1; -; mRNA.
DR EMBL; AK144353; BAE25845.1; -; mRNA.
DR EMBL; BC008512; AAH08512.1; -; mRNA.
DR CCDS; CCDS14867.1; -.
DR RefSeq; NP_035336.2; NM_011206.2.
DR AlphaFoldDB; Q61152; -.
DR SMR; Q61152; -.
DR BioGRID; 202483; 2.
DR IntAct; Q61152; 2.
DR MINT; Q61152; -.
DR STRING; 10090.ENSMUSP00000027302; -.
DR iPTMnet; Q61152; -.
DR PhosphoSitePlus; Q61152; -.
DR EPD; Q61152; -.
DR jPOST; Q61152; -.
DR MaxQB; Q61152; -.
DR PaxDb; Q61152; -.
DR PeptideAtlas; Q61152; -.
DR PRIDE; Q61152; -.
DR ProteomicsDB; 291541; -.
DR Antibodypedia; 33499; 124 antibodies from 25 providers.
DR DNASU; 19253; -.
DR Ensembl; ENSMUST00000027302; ENSMUSP00000027302; ENSMUSG00000026126.
DR GeneID; 19253; -.
DR KEGG; mmu:19253; -.
DR UCSC; uc007aos.1; mouse.
DR CTD; 26469; -.
DR MGI; MGI:108410; Ptpn18.
DR VEuPathDB; HostDB:ENSMUSG00000026126; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000162860; -.
DR HOGENOM; CLU_015557_0_0_1; -.
DR InParanoid; Q61152; -.
DR OMA; LVWEFRV; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q61152; -.
DR TreeFam; TF351977; -.
DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR BioGRID-ORCS; 19253; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Ptpn18; mouse.
DR PRO; PR:Q61152; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61152; protein.
DR Bgee; ENSMUSG00000026126; Expressed in granulocyte and 145 other tissues.
DR ExpressionAtlas; Q61152; baseline and differential.
DR Genevisible; Q61152; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..453
FT /note="Tyrosine-protein phosphatase non-receptor type 18"
FT /id="PRO_0000094774"
FT DOMAIN 26..291
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 384..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229..235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 381
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 419
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CONFLICT 11
FT /note="F -> L (in Ref. 3; AAC52991)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="T -> M (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="I -> T (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="F -> S (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..368
FT /note="ASAGTGP -> LRRHRA (in Ref. 3; AAC52991)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="G -> V (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="T -> N (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="T -> I (in Ref. 5; AAH08512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50202 MW; 88AD7E73CE8136B0 CRC64;
MSRHTDLVRS FLEQLEARDY REGAILAREF SDIKARSVAW KSEGVCSTKA GSRLGNTNKN
RYKDVVAYDE TRVILSLLQE EGHGDYINAN FIRGIDGSQA YIATQGPLPH TLLDFWRLVW
EFGVKVILMA CQETENGRRK CERYWAREQE PLKAGPFCIT LTKETTLNAD ITLRTLQVTF
QKEFRSVHQL QYMSWPDHGV PSSSDHILTM VEEARCLQGL GPGPLCVHCS AGCGRTGVLC
AVDYVRQLLL TQTIPPNFSL FQVVLEMRKQ RPAAVQTEEQ YRFLYHTVAQ LFSRTLQDTS
PHYQNLKENC APICKEAFSL RTSSALPATS RPPGGVLRSI SVPAPPTLPM ADTYAVVQKR
GASAGTGPGP RAPTSTDTPI YSQVAPRAQR PVAHTEDAQG TTALRRVPAD QNSSGPDAYE
EVTDGAQTGG LGFNLRIGRP KGPRDPPAEW TRV
