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   02-SEP-2026, entry version 201.
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,
RC   Pancreas, 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_001310634.2.
DR   RefSeq; NP_001418677.1; NM_001431748.1.
DR   AlphaFoldDB; P20357; -.
DR   BioGRID; 201585; 45.
DR   CORUM; P20357; -.
DR   FunCoup; P20357; 1150.
DR   IntAct; P20357; 17.
DR   MINT; P20357; -.
DR   STRING; 10090.ENSMUSP00000109646; -.
DR   GlyGen; P20357; 17 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (13 sites).
DR   iPTMnet; P20357; -.
DR   PhosphoSitePlus; P20357; -.
DR   SwissPalm; P20357; -.
DR   jPOST; P20357; -.
DR   PaxDb; 10090-ENSMUSP00000109646; -.
DR   PeptideAtlas; P20357; -.
DR   ProteomicsDB; 291359; -.
DR   Pumba; P20357; -.
DR   ABCD; P20357; 2 sequenced antibodies.
DR   Antibodypedia; 2169; 1410 antibodies from 50 providers.
DR   DNASU; 17756; -.
DR   Ensembl; ENSMUST00000114013.8; ENSMUSP00000109646.2; ENSMUSG00000015222.19.
DR   GeneID; 17756; -.
DR   KEGG; mmu:17756; -.
DR   UCSC; uc007bhz.1; mouse.
DR   AGR; MGI:97175; -.
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   PhylomeDB; P20357; -.
DR   BioGRID-ORCS; 17756; 1 hit in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P20357; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P20357; protein.
DR   Bgee; ENSMUSG00000015222; Expressed in anterior amygdaloid area and 218 other cell types or tissues.
DR   ExpressionAtlas; P20357; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:GO_Central.
DR   GO; GO:0097440; C:apical dendrite; IDA:MGI.
DR   GO; GO:0150014; C:apical distal dendrite; ISO:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
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:GO_Central.
DR   GO; GO:0097442; C:CA3 pyramidal cell dendrite; IDA:MGI.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0005929; C:cilium; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISO:GO_Central.
DR   GO; GO:0044307; C:dendritic branch; ISO:GO_Central.
DR   GO; GO:1902737; C:dendritic filopodium; ISO:GO_Central.
DR   GO; GO:0044294; C:dendritic growth cone; ISO:GO_Central.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0150002; C:distal dendrite; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:GO_Central.
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:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0098794; C:postsynapse; ISO:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0150001; C:primary dendrite; ISO:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:GO_Central.
DR   GO; GO:1990635; C:proximal dendrite; ISO:GO_Central.
DR   GO; GO:1990769; C:proximal neuron projection; IDA:ARUK-UCL.
DR   GO; GO:0032587; C:ruffle membrane; ISO:GO_Central.
DR   GO; GO:0003779; F:actin binding; ISO:GO_Central.
DR   GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI.
DR   GO; GO:0002162; F:dystroglycan binding; ISO:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0140778; F:microtubule stabilizing activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:GO_Central.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
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:0007026; P:negative regulation of microtubule depolymerization; ISO:GO_Central.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; ISO:GO_Central.
DR   GO; GO:0060632; P:regulation of microtubule-based movement; IBA:GO_Central.
DR   GO; GO:1902996; P:regulation of neurofibrillary tangle assembly; ISO:GO_Central.
DR   GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:GO_Central.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL.
DR   InterPro; IPR027324; MAP2/MAP4/Tau.
DR   InterPro; IPR013588; MAP2_projctn.
DR   InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR   PANTHER; PTHR11501; MICROTUBULE-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR11501:SF15; MICROTUBULE-ASSOCIATED PROTEIN 2; 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        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..133
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..790
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1412..1430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1440
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1445..1464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1471..1481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1527..1544
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1546..1557
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1567..1578
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1591..1607
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1613..1623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1783..1796
FT                   /note="Low complexity"
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
//