MTAP2_MOUSE
ID MTAP2_MOUSE Reviewed; 1828 AA.
AC P20357; E9QLE1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Microtubule-associated protein 2;
DE Short=MAP-2;
GN Name=Map2; Synonyms=Mtap2;
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=3205744; DOI=10.1093/nar/16.23.11369;
RA Wang D., Lewis S.A., Cowan N.J.;
RT "Complete sequence of a cDNA encoding mouse MAP2.";
RL Nucleic Acids Res. 16:11369-11370(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3142041; DOI=10.1126/science.3142041;
RA Lewis S.A., Wang D., Cowan N.J.;
RT "Microtubule-associated protein MAP2 shares a microtubule binding motif
RT with tau protein.";
RL Science 242:936-939(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PROTEIN SEQUENCE OF 94-107; 583-597; 909-920; 989-1004; 1159-1174;
RP 1403-1414 AND 1511-1538, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-726; SER-1352; THR-1358;
RP THR-1606 AND THR-1609, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352; THR-1358 AND THR-1609,
RP AND IDENTIFICATION BY 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 [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH KNDC1, AND PHOSPHORYLATION.
RX PubMed=17984326; DOI=10.1083/jcb.200702036;
RA Huang J., Furuya A., Furuichi T.;
RT "Very-KIND, a KIND domain containing RasGEF, controls dendrite growth by
RT linking Ras small GTPases and MAP2.";
RL J. Cell Biol. 179:539-552(2007).
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-28; SER-136; SER-140;
RP SER-143; SER-283; SER-333; SER-476; SER-496; SER-550; SER-596; SER-599;
RP SER-603; SER-608; SER-726; SER-730; THR-734; SER-737; SER-739; TYR-746;
RP SER-823; SER-1139; SER-1140; SER-1145; SER-1161; SER-1165; SER-1352;
RP THR-1358; SER-1539; SER-1560; SER-1592; THR-1606; THR-1609; THR-1620;
RP THR-1623; THR-1650; SER-1783; SER-1788 AND SER-1791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP INTERACTION WITH KNDC1.
RX PubMed=21385318; DOI=10.1111/j.1742-4658.2011.08085.x;
RA Huang J., Furuya A., Hayashi K., Furuichi T.;
RT "Interaction between very-KIND Ras guanine exchange factor and microtubule-
RT associated protein 2, and its role in dendrite growth -- structure and
RT function of the second kinase noncatalytic C-lobe domain.";
RL FEBS J. 278:1651-1661(2011).
CC -!- FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize
CC the microtubules against depolymerization. They also seem to have a
CC stiffening effect on microtubules.
CC -!- SUBUNIT: Interacts with KNDC1 (via KIND2); the interaction enhances
CC MAP2 phosphorylation and localizes KNDC1 to dendrites. Interacts with
CC DPYSL5 (By similarity). {ECO:0000250|UniProtKB:P11137,
CC ECO:0000269|PubMed:17984326}.
CC -!- INTERACTION:
CC P20357; Q0KK55: Kndc1; NbExp=9; IntAct=EBI-397863, EBI-8605532;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, dendrite {ECO:0000269|PubMed:17984326}.
CC -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by causing
CC MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), detachment
CC from microtubules, and their disassembly (By similarity). The
CC interaction with KNDC1 enhances MAP2 threonine phosphorylation
CC (PubMed:17984326). {ECO:0000250|UniProtKB:P15146,
CC ECO:0000269|PubMed:17984326}.
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DR EMBL; M21041; AAA39490.1; -; mRNA.
DR EMBL; AC091465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS83550.1; -.
DR PIR; A40115; A40115.
DR RefSeq; NP_001297563.1; NM_001310634.1.
DR RefSeq; XP_006495817.1; XM_006495754.2.
DR AlphaFoldDB; P20357; -.
DR BioGRID; 201585; 31.
DR IntAct; P20357; 17.
DR MINT; P20357; -.
DR STRING; 10090.ENSMUSP00000076577; -.
DR iPTMnet; P20357; -.
DR PhosphoSitePlus; P20357; -.
DR SwissPalm; P20357; -.
DR jPOST; P20357; -.
DR MaxQB; P20357; -.
DR PaxDb; P20357; -.
DR PeptideAtlas; P20357; -.
DR PRIDE; P20357; -.
DR ProteomicsDB; 291359; -.
DR ABCD; P20357; 2 sequenced antibodies.
DR Antibodypedia; 2169; 1352 antibodies from 47 providers.
DR DNASU; 17756; -.
DR Ensembl; ENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222.
DR GeneID; 17756; -.
DR KEGG; mmu:17756; -.
DR UCSC; uc007bhz.1; mouse.
DR CTD; 4133; -.
DR MGI; MGI:97175; Map2.
DR VEuPathDB; HostDB:ENSMUSG00000015222; -.
DR eggNOG; KOG2418; Eukaryota.
DR GeneTree; ENSGT00940000156597; -.
DR HOGENOM; CLU_002538_0_0_1; -.
DR InParanoid; P20357; -.
DR OrthoDB; 716848at2759; -.
DR PhylomeDB; P20357; -.
DR BioGRID-ORCS; 17756; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Map2; mouse.
DR PRO; PR:P20357; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P20357; protein.
DR Bgee; ENSMUSG00000015222; Expressed in anterior amygdaloid area and 215 other tissues.
DR ExpressionAtlas; P20357; baseline and differential.
DR Genevisible; P20357; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0097440; C:apical dendrite; IDA:MGI.
DR GO; GO:0150014; C:apical distal dendrite; ISO:MGI.
DR GO; GO:0043203; C:axon hillock; IDA:ARUK-UCL.
DR GO; GO:0043194; C:axon initial segment; IDA:ARUK-UCL.
DR GO; GO:0097441; C:basal dendrite; ISO:MGI.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0044307; C:dendritic branch; ISO:MGI.
DR GO; GO:1902737; C:dendritic filopodium; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0150002; C:distal dendrite; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; TAS:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0034399; C:nuclear periphery; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0150001; C:primary dendrite; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR GO; GO:1990769; C:proximal neuron projection; IDA:ARUK-UCL.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:InterPro.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:ARUK-UCL.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:ARUK-UCL.
DR GO; GO:1904527; P:negative regulation of microtubule binding; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISO:MGI.
DR GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; ISO:MGI.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL.
DR InterPro; IPR030797; MAP2.
DR InterPro; IPR013588; MAP2_projctn.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR PANTHER; PTHR11501:SF15; PTHR11501:SF15; 1.
DR Pfam; PF08377; MAP2_projctn; 1.
DR Pfam; PF00418; Tubulin-binding; 3.
DR PROSITE; PS00229; TAU_MAP_1; 2.
DR PROSITE; PS51491; TAU_MAP_2; 3.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1828
FT /note="Microtubule-associated protein 2"
FT /id="PRO_0000072748"
FT REPEAT 1662..1692
FT /note="Tau/MAP 1"
FT REPEAT 1693..1723
FT /note="Tau/MAP 2"
FT REPEAT 1724..1755
FT /note="Tau/MAP 3"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..745
FT /note="Interaction with KNDC1"
FT /evidence="ECO:0000269|PubMed:21385318"
FT REGION 765..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1472
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 1778..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 746
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"
FT MOD_RES 1358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"
FT MOD_RES 1620
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1623
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1650
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1680
FT /note="Phosphoserine; by MARK1"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT MOD_RES 1809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15146"
FT CONFLICT 116
FT /note="H -> Y (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="K -> E (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="F -> L (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="D -> G (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="S -> T (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="R -> G (in Ref. 1; no nucleotide entry and 2;
FT AAA39490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1828 AA; 199132 MW; E8FA7621C45D5A0D CRC64;
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGAGEG LSRNANGFPY REEEEGAFGE
HRSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQP
AALPLAAEET ANLPPSPPPS PASEQTATVE EDLLTASKME FPEQEKFPSS FAEPLDKGEM
EFKMPSKPGE DFEHAALVPD TSKTPQDKKD LQGMEGEKLP PVPFAQTFGT NLEDRKQSTE
PSIVMPSIGL SAEPPAPKEP KDWFIEMPTE SKKDEWGLAA PISPGPLTPM REKDVLEDIP
RWEGKQFDSP MPSPFHGGSF TLPLDTMKNE RVSEGPRPFA PVFFQSDDKV SLQDPSALAT
SKESSKDEEP LKDKADKVAD VSISEVTTLL GNVHSPVVEG YVGENISGEV KVTTDQEKKE
TSAPSVQEPT LTETEPQTKL DEKSTVSIEE AVAKKEESFK LRDDKTGVIQ TSTEQSFSKE
DQKGQEHTID ELKQDSFPIS LEQAVTDAAM TSKTLGKVTS EPEAVSERRE IQGLFEEKTA
DKNKLEGAGS ATIAEVEMPF YEDKSGMSKY FETSALKEDM TRSTELGSDY YELSDSRGSA
QESLDTISPK NQHDEKELQA KASQPSPPAQ EAGYSTLAQS YTPDHPSELP EEPSSPQERM
FTIDPKVYGE KRDLHSKNKD DLTLSRSLGL GGRSAIEQRS MSINLPMSCL DSIALGFNFG
RGHDLSPLAS DILTNTSGSM DEGDDYLPPT TPAVEKMPCF PIESKEEEDK AEQAKVTGGQ
TIQVETSSES PFPAKEYYKN GTVMAPDLPE MLDLAGTRSR LASVSADAEV ARRKSVPSEA
MLAESSTSLP PVADESPVTV KPDSQLEDMG YCVFNKYTVP LPSPVQDSEN LSGESGSFYE
GTDDKVRRDL ATDLSLIEVK LAAAGRVKDE FTAEKEASPP TSADKSRLSR EFDHDRKAND
KLDTVLEKSE EHIDSKEHAK ESEEMGGKVE LFGLGITYDQ ASTKELITTK DTSPEKTEKG
LSSVPEVAEV EPTTKADQGL DFAATKAEPS QLDIKVSDFG QMASGMNVDA GKAIELKFEV
AQELTLSSEA PQEADSFMGV ESGHIKEGGK VNETEVKEKV TKPDLVHQEA VDKEESYESS
GEHESLTMES LKPDEGKKET SPETSLIQDE VALKLSVEIP CPPPVSEADL STDEKGEVQM
EFIQLPKEES TETPDIPAIP SDVTQPQPEA IVSEPAEVPS EEEEIEAGGE YDKLLFRSDT
LQISDLLVSE SREEFVETCP GELKGVVESV VTIEDDFITV VQTTTDEGES GSHSVRFAAP
AQPEEERRPR PHDEELEIEM AAEAQAEPKD GSPDAPATPE KEEVAFSEYK TETYDDYKDE
TTIDDSIMDA DSLWVDTQDD DRSILTEQLE TIPKEERAEK DARRPSLEKH RKEKPFKTGR
GRISTPERKV AKKEPSTVSR DEVRRKKAVY KKAELAKKSE VQAHSPSRKL ILKPAIKYTR
PTHLSCVKRK TTAASGDLAQ APGAFKQAKD KVTDGISKSP EKRSSLPRPS SILPPRRGVS
GDREENSFSL NSSISSARRT TRSEPIRRAG KSGTSTPTTP GSTAITPGTP PSYSSRTPGT
PGTPSYPRTP GTPKSGILVP SEKKVAIIRT PPKSPATPKQ LRLINQPLPD LKNVKSKIGS
TDNIKYQPKG GQVQIVTKKI DLSHVTSKCG SLKNIRHRPG GGRVKIESVK LDFKEKAQAK
VGSLDNAHHV PGGGNVKIDS QKLNFREHAK ARVDHGAEII TQSPSRSSVA SPRRLSNVSS
SGSINLLESP QLATLAEDVT AALAKQGL
