EP15R_MOUSE
ID EP15R_MOUSE Reviewed; 907 AA.
AC Q60902; Q3U7L9; Q3UIS9; Q8CB60; Q8CB70; Q91WH8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Epidermal growth factor receptor substrate 15-like 1;
DE AltName: Full=Epidermal growth factor receptor pathway substrate 15-related sequence;
DE Short=Eps15-rs;
DE AltName: Full=Eps15-related protein;
DE Short=Eps15R;
GN Name=Eps15l1; Synonyms=Eps15-rs, Eps15R;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=7568168; DOI=10.1073/pnas.92.21.9530;
RA Wong W.T., Schumacher C., Salcini A.E., Romano A., Castagnino P.,
RA Pelicci P.G., Di Fiore P.;
RT "A protein-binding domain, EH, identified in the receptor tyrosine kinase
RT substrate Eps15 and conserved in evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9530-9534(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Kidney;
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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
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 [5]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH EPS15; AP-2
RP COMPLEX; AGFG1 AND AGFG2.
RX PubMed=9446614; DOI=10.1074/jbc.273.5.3003;
RA Coda L., Salcini A.E., Confalonieri S., Pelicci G., Sorkina T., Sorkin A.,
RA Pelicci P.G., Di Fiore P.P.;
RT "Eps15R is a tyrosine kinase substrate with characteristics of a docking
RT protein possibly involved in coated pits-mediated internalization.";
RL J. Biol. Chem. 273:3003-3012(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-562, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-255, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-108; SER-244;
RP SER-253; SER-255; SER-360; THR-364 AND SER-610, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [12]
RP INTERACTION WITH FCHO2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [13]
RP INTERACTION WITH DAB2.
RX PubMed=22648170; DOI=10.1091/mbc.e11-12-1007;
RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate
RT integrin beta1 endocytosis.";
RL Mol. Biol. Cell 23:2905-2916(2012).
CC -!- FUNCTION: Seems to be a constitutive component of clathrin-coated pits
CC that is required for receptor-mediated endocytosis. Involved in
CC endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR);
CC internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to
CC require association with DAB2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL. Associates
CC with the clathrin-associated adapter protein complex 2 (AP-2).
CC Interacts with FCHO1 (By similarity). Interacts with FCHO2. Interacts
CC (via EH domains) with DAB2. Interacts with UBQLN1 (via ubiquitin-like
CC domain). Interacts with CAVIN3 (via leucine-zipper domain) (By
CC similarity). Interacts with REPS2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBC2, ECO:0000269|PubMed:20448150,
CC ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:9446614}.
CC -!- INTERACTION:
CC Q60902; P98078: Dab2; NbExp=2; IntAct=EBI-443931, EBI-1391846;
CC Q60902; P42567: Eps15; NbExp=2; IntAct=EBI-443931, EBI-443923;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9446614};
CC Peripheral membrane protein {ECO:0000269|PubMed:9446614}. Nucleus
CC {ECO:0000269|PubMed:9446614}. Membrane, coated pit
CC {ECO:0000269|PubMed:9446614}. Note=Localized to plasma membrane coated
CC pits.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q60902-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60902-2; Sequence=VSP_010683, VSP_010684;
CC Name=3;
CC IsoId=Q60902-3; Sequence=VSP_010681, VSP_010682;
CC Name=4;
CC IsoId=Q60902-4; Sequence=VSP_022638, VSP_022639;
CC -!- PTM: Phosphorylated on tyrosine residues by EGFR.
CC {ECO:0000269|PubMed:9446614}.
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DR EMBL; U29156; AAA87202.1; -; mRNA.
DR EMBL; AK036662; BAC29523.1; -; mRNA.
DR EMBL; AK036728; BAC29554.1; -; mRNA.
DR EMBL; AK146781; BAE27427.1; -; mRNA.
DR EMBL; AK152602; BAE31350.1; -; mRNA.
DR EMBL; CH466525; EDL10796.1; -; Genomic_DNA.
DR EMBL; BC015259; AAH15259.1; -; mRNA.
DR CCDS; CCDS52597.1; -. [Q60902-1]
DR CCDS; CCDS85561.1; -. [Q60902-4]
DR RefSeq; NP_001116304.1; NM_001122832.1.
DR RefSeq; NP_001276788.1; NM_001289859.1. [Q60902-4]
DR RefSeq; NP_031970.2; NM_007944.3. [Q60902-1]
DR AlphaFoldDB; Q60902; -.
DR SMR; Q60902; -.
DR BioGRID; 199490; 21.
DR IntAct; Q60902; 8.
DR MINT; Q60902; -.
DR STRING; 10090.ENSMUSP00000129739; -.
DR iPTMnet; Q60902; -.
DR PhosphoSitePlus; Q60902; -.
DR EPD; Q60902; -.
DR jPOST; Q60902; -.
DR MaxQB; Q60902; -.
DR PaxDb; Q60902; -.
DR PeptideAtlas; Q60902; -.
DR PRIDE; Q60902; -.
DR ProteomicsDB; 275924; -. [Q60902-1]
DR ProteomicsDB; 275925; -. [Q60902-2]
DR ProteomicsDB; 275926; -. [Q60902-3]
DR ProteomicsDB; 275927; -. [Q60902-4]
DR Antibodypedia; 14142; 213 antibodies from 31 providers.
DR DNASU; 13859; -.
DR Ensembl; ENSMUST00000163643; ENSMUSP00000129739; ENSMUSG00000006276. [Q60902-1]
DR Ensembl; ENSMUST00000212121; ENSMUSP00000148468; ENSMUSG00000006276. [Q60902-4]
DR GeneID; 13859; -.
DR KEGG; mmu:13859; -.
DR UCSC; uc009mfr.3; mouse. [Q60902-1]
DR UCSC; uc009mfs.3; mouse. [Q60902-4]
DR UCSC; uc009mft.2; mouse. [Q60902-2]
DR UCSC; uc009mfu.2; mouse. [Q60902-3]
DR CTD; 58513; -.
DR MGI; MGI:104582; Eps15l1.
DR VEuPathDB; HostDB:ENSMUSG00000006276; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00940000155438; -.
DR HOGENOM; CLU_007270_1_1_1; -.
DR InParanoid; Q60902; -.
DR OMA; AMYLVRQ; -.
DR OrthoDB; 597979at2759; -.
DR PhylomeDB; Q60902; -.
DR TreeFam; TF324293; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 13859; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Eps15l1; mouse.
DR PRO; PR:Q60902; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60902; protein.
DR Bgee; ENSMUSG00000006276; Expressed in undifferentiated genital tubercle and 253 other tissues.
DR ExpressionAtlas; Q60902; baseline and differential.
DR Genevisible; Q60902; MM.
DR GO; GO:0030132; C:clathrin coat of coated pit; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR CDD; cd00052; EH; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR003903; UIM_dom.
DR Pfam; PF12763; EF-hand_4; 3.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 3.
DR SUPFAM; SSF47473; SSF47473; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50330; UIM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane; Coated pit;
KW Coiled coil; Endocytosis; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT CHAIN 2..907
FT /note="Epidermal growth factor receptor substrate 15-like
FT 1"
FT /id="PRO_0000146119"
FT DOMAIN 15..104
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 48..83
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..215
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 159..194
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 272..307
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 273..363
FT /note="EH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 308..341
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 863..882
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 889..907
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 15..368
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000269|PubMed:22648170"
FT REGION 229..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 384..551
FT /evidence="ECO:0000255"
FT COMPBIAS 235..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 74
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 562
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC2"
FT VAR_SEQ 565..595
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022638"
FT VAR_SEQ 596..599
FT /note="DDPF -> VKVE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010681"
FT VAR_SEQ 600..819
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010682"
FT VAR_SEQ 748..860
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022639"
FT VAR_SEQ 794..819
FT /note="STPVSQLGSSDFPESPDPFQPLGADS -> YASSSRGTRRWGQGGGHRAPPL
FT SSPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010683"
FT VAR_SEQ 820..907
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010684"
FT CONFLICT 14
FT /note="G -> S (in Ref. 1; AAA87202 and 4; AAH15259)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> P (in Ref. 1; AAA87202)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> V (in Ref. 2; BAE31350)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="R -> K (in Ref. 1; AAA87202 and 4; AAH15259)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="D -> H (in Ref. 2; BAC29523)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="D -> E (in Ref. 1; AAA87202)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="T -> A (in Ref. 1; AAA87202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 99309 MW; B5AF1A89B445E8A7 CRC64;
MAAPLVPLSQ QIPGGNPLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA
DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSSLSLTMPP PKFHDTSSPL MATQSSAETH
WAVRVEEKAK FDGIFESLLP VNGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD
RDEFAVAMHL VYRALEKEPV PSILPPPLIP PSKRKKTVFA GAVPVLPASP PPKDSLRSTP
SHGSVSSLNS TGSLSPKHSV KQPPVAWVVP VADKMRFDEI FLKTDLDLDG YVSGQEVKEI
FMHSGLTQNL LAHIWALADT RQTGKLSKEQ FALAMYFIQQ KVSKGIDPPQ VLSPDMVPPS
ERGTPIPDSS STLASGEFTG VKELDDISQE IAQLQREKYS LEQDIREKEE AIRQKTSEVQ
ELQNDLDRET SSLQELEAQK QDAQDRLDEM DQQKAKLRDM LSDVRQKCQD ETQTISSLKT
QIQSQESDLK SQEDDLNRAK SELNRLQQEE TQLEQSIQAG RAQLETILRS LKCTQDDINQ
ARSKLSQLQE SHLEAHRSLE QYDQVPDGVS GTSLPDLATL NEGILLAERG GFGAMDDPFK
NKALLFSNNS QELHPDPFQA EDPFKSDPFK GADPFKGDPF QSDPFSEQQT AATDPFGGDP
FKESDPFHSS SSDDFFKKQT KNDPFTSDPF TKNPSLPSKL DPFESSDPFS SSSISSKGSD
PFGTLDPFGS SSFSSAEGFA DFSQMSKPPP SGPFSSSLGG TGFSDDPFKS KQDTPALPPK
KPAPPRPKPP SGQSTPVSQL GSSDFPESPD PFQPLGADSG DPFQNKKGFG DPFSGKDPFA
PSSSAKPPKT SSSGFADFTS FGNEEQQLAW AKRESEKAEQ ERLARLRRQE QEDLELAIAL
SKADMPA
