ID PTN12_MOUSE Reviewed; 775 AA.
AC P35831; Q80UM4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 191.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 12;
DE EC=3.1.3.48 {ECO:0000269|PubMed:7772023};
DE AltName: Full=MPTP-PEST;
DE AltName: Full=Protein-tyrosine phosphatase P19;
DE Short=P19-PTP;
GN Name=Ptpn12;
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].
RX PubMed=1590786; DOI=10.1016/s0006-291x(05)80015-4;
RA den Hertog J., Pals C.E., Jonk L.J., Kruijer W.;
RT "Differential expression of a novel murine non-receptor protein tyrosine
RT phosphatase during differentiation of P19 embryonal carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 184:1241-1249(1992).
RN [2]
RP SEQUENCE REVISION TO 297-416.
RX PubMed=1472029; DOI=10.1016/0006-291x(92)92335-u;
RA Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M.,
RA Adachi M., Imai K., Yachi A.;
RT "Cloning and characterization of a human cDNA encoding a novel putative
RT cytoplasmic protein-tyrosine-phosphatase.";
RL Biochem. Biophys. Res. Commun. 189:1223-1230(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=7772023; DOI=10.1042/bj3080425;
RA Charest A., Wagner J., Shen S.H., Tremblay M.L.;
RT "Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein
RT tyrosine phosphatase.";
RL Biochem. J. 308:425-432(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [7]
RP INTERACTION WITH TGFB1I1.
RX PubMed=10092676; DOI=10.1074/jbc.274.14.9847;
RA Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L., Nose K.;
RT "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase
RT PEST (PTP-PEST) through its LIM 3 domain.";
RL J. Biol. Chem. 274:9847-9853(1999).
RN [8]
RP INTERACTION WITH PSTPIP1.
RX PubMed=11711533; DOI=10.1074/jbc.m106428200;
RA Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S., Lasky L.A.,
RA Tremblay M.L.;
RT "PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-
RT PEST toward a specific dephosphorylation of WASP.";
RL J. Biol. Chem. 277:2973-2986(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LPXN AND PTK2B/PYK2.
RX PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669;
RA Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y.,
RA Goldknopf J., Hruska K.A.;
RT "Leupaxin is a critical adaptor protein in the adhesion zone of the
RT osteoclast.";
RL J. Bone Miner. Res. 18:669-685(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [11]
RP INTERACTION WITH LPXN.
RX PubMed=15786712; DOI=10.1007/s11010-005-2149-6;
RA Watanabe N., Amano N., Ishizuka H., Mashima K.;
RT "Leupaxin binds to PEST domain tyrosine phosphatase PEP.";
RL Mol. Cell. Biochem. 269:13-17(2005).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17070019; DOI=10.1016/j.mod.2006.08.011;
RA Sirois J., Cote J.F., Charest A., Uetani N., Bourdeau A., Duncan S.A.,
RA Daniels E., Tremblay M.L.;
RT "Essential function of PTP-PEST during mouse embryonic vascularization,
RT mesenchyme formation, neurogenesis and early liver development.";
RL Mech. Dev. 123:869-880(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-596; THR-598;
RP SER-603; SER-606 AND SER-608, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-434, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; SER-550; SER-603;
RP SER-606; SER-608 AND SER-748, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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: Dephosphorylates a range of proteins, and thereby regulates
CC cellular signaling cascades (PubMed:17070019). Dephosphorylates
CC cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby
CC regulates signaling via ERBB2 and PTK2B/PYK2. Selectively
CC dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or
CC 'Tyr-1248' (By similarity). {ECO:0000250|UniProtKB:Q05209,
CC ECO:0000269|PubMed:17070019}.
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, ECO:0000269|PubMed:7772023};
CC -!- SUBUNIT: Interacts with PSTPIP1 and TGFB1I1 (PubMed:10092676,
CC PubMed:11711533). Interacts with PTK2B/PYK2 (PubMed:12674328).
CC Interacts with LPXN (PubMed:12674328, PubMed:15786712). Interacts with
CC SORBS2; this interaction greatly enhances WASF1 dephosphorylation and
CC might mediate partial translocation to focal adhesion sites (By
CC similarity). {ECO:0000250|UniProtKB:Q05209,
CC ECO:0000269|PubMed:10092676, ECO:0000269|PubMed:11711533,
CC ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:15786712}.
CC -!- INTERACTION:
CC P35831; P97814: Pstpip1; NbExp=5; IntAct=EBI-2642957, EBI-7484574;
CC P35831; P98083: Shc1; NbExp=2; IntAct=EBI-2642957, EBI-300201;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12674328,
CC ECO:0000269|PubMed:7772023}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q05209}. Cell projection, podosome
CC {ECO:0000269|PubMed:12674328}. Note=Partial translocation to focal
CC adhesion sites might be mediated by interaction with SORBS2.
CC {ECO:0000250|UniProtKB:Q05209}.
CC -!- PTM: Phosphorylated by STK24/MST3 and this results in inhibition of its
CC activity. {ECO:0000250|UniProtKB:Q05209}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality at 9.5 to 10.5 dpc.
CC Heterozygous mice have no obvious phenotype.
CC {ECO:0000269|PubMed:17070019}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; X63440; CAA45037.1; ALT_SEQ; mRNA.
DR EMBL; X86781; CAA60477.1; -; Genomic_DNA.
DR EMBL; AK154107; BAE32381.1; -; mRNA.
DR EMBL; CH466586; EDL03216.1; -; Genomic_DNA.
DR EMBL; BC051980; AAH51980.1; -; mRNA.
DR CCDS; CCDS19102.1; -.
DR PIR; JH0609; JH0609.
DR PIR; S55345; S55345.
DR RefSeq; NP_035333.2; NM_011203.2.
DR AlphaFoldDB; P35831; -.
DR SMR; P35831; -.
DR BioGRID; 202478; 7.
DR IntAct; P35831; 4.
DR MINT; P35831; -.
DR STRING; 10090.ENSMUSP00000030556; -.
DR GlyGen; P35831; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P35831; -.
DR PhosphoSitePlus; P35831; -.
DR SwissPalm; P35831; -.
DR EPD; P35831; -.
DR jPOST; P35831; -.
DR MaxQB; P35831; -.
DR PaxDb; 10090-ENSMUSP00000030556; -.
DR PeptideAtlas; P35831; -.
DR ProteomicsDB; 301872; -.
DR Pumba; P35831; -.
DR Antibodypedia; 2052; 268 antibodies from 33 providers.
DR DNASU; 19248; -.
DR Ensembl; ENSMUST00000030556.8; ENSMUSP00000030556.8; ENSMUSG00000028771.14.
DR GeneID; 19248; -.
DR KEGG; mmu:19248; -.
DR UCSC; uc008woh.1; mouse.
DR AGR; MGI:104673; -.
DR CTD; 5782; -.
DR MGI; MGI:104673; Ptpn12.
DR VEuPathDB; HostDB:ENSMUSG00000028771; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000156909; -.
DR HOGENOM; CLU_015557_2_0_1; -.
DR InParanoid; P35831; -.
DR OMA; GPFHISC; -.
DR OrthoDB; 5489271at2759; -.
DR PhylomeDB; P35831; -.
DR TreeFam; TF351977; -.
DR Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR BioGRID-ORCS; 19248; 6 hits in 80 CRISPR screens.
DR ChiTaRS; Ptpn12; mouse.
DR PRO; PR:P35831; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P35831; Protein.
DR Bgee; ENSMUSG00000028771; Expressed in embryonic post-anal tail and 258 other cell types or tissues.
DR ExpressionAtlas; P35831; baseline and differential.
DR Genevisible; P35831; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
DR CDD; cd14604; PTPc-N12; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR012266; PTN12.
DR InterPro; IPR047170; PTN12/18/22.
DR InterPro; IPR047251; PTN12_cat.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45983; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR45983:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 12; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000932; Tyr-Ptase_nr12; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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 Acetylation; Cell junction; Cell projection; Cytoplasm; Hydrolase;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..775
FT /note="Tyrosine-protein phosphatase non-receptor type 12"
FT /id="PRO_0000094772"
FT DOMAIN 28..293
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..437
FT /note="Interaction with TGFB1I1"
FT /evidence="ECO:0000269|PubMed:10092676"
FT REGION 462..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231..237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05209"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 110..111
FT /note="LA -> FR (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="I -> M (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="K -> N (in Ref. 1; CAA45037)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> R (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..332
FT /note="KQDSP -> DETS (in Ref. 1; CAA45037)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="W -> V (in Ref. 1; CAA45037)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..415
FT /note="PM -> QW (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
FT CONFLICT 606..607
FT /note="SD -> WH (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="T -> H (in Ref. 3; CAA60477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 86526 MW; ED1A7A577CE4352C CRC64;
MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK
KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM
IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCENEQAR TDYFIRTLLL
EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA
ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL
YEIHGAQKIA DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE EILQPPEPHP
VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH PADLNRSYDK SADPMGKSES
AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD GNTLLNRGHA IKIKSASSSV VDRTSKPQEL
SAGALKVDDV SQNSCADCSA AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG
PENATPVPDS PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP
LHSDDSDSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CTRRVLPMSI ARQEVAGTPH
SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP NQEWSEQRES EGLTTSGNEK
HDAGGIHTEA SADSPPAFSD KKDQITKSPA EVTDIGFGNR CGKPKGPREP PSEWT
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