ID   MTAP2_HUMAN             Reviewed;        1827 AA.
AC   P11137; Q17S04; Q8IUX2; Q99975; Q99976;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 4.
DT   24-JAN-2024, entry version 215.
DE   RecName: Full=Microtubule-associated protein 2;
DE            Short=MAP-2;
GN   Name=MAP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Price R.;
RT   "Complete cDNA of human MAP2 gene and a profile of two RFLPs for
RT   BglII/BclI.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Brain;
RX   PubMed=8294038; DOI=10.1016/0378-1119(93)90502-t;
RA   Albala J.S., Kalcheva N., Shafit-Zagardo B.;
RT   "Characterization of the transcripts encoding two isoforms of human
RT   microtubule-associated protein-2 (MAP-2).";
RL   Gene 136:377-378(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   TISSUE=Brain, and Pancreas;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 77-649 (ISOFORM 1).
RX   PubMed=2481044; DOI=10.1002/jnr.490240405;
RA   Dammerman M., Yen S.H., Shafit-Zagardo B.;
RT   "Sequence of a human MAP-2 region sharing epitopes with Alzheimer
RT   neurofibrillary tangles.";
RL   J. Neurosci. Res. 24:487-495(1989).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 494-1562 (ISOFORM 1).
RX   PubMed=2455776; DOI=10.1111/j.1471-4159.1988.tb01079.x;
RA   Kosik K.S., Orecchio L.D., Bakalis S., Duffy L., Neve R.L.;
RT   "Partial sequence of MAP2 in the region of a shared epitope with Alzheimer
RT   neurofibrillary tangles.";
RL   J. Neurochem. 51:587-598(1988).
RN   [8]
RP   PHOSPHORYLATION AT TYR-67 (ISOFORM 2) BY FYN.
RX   PubMed=15536091; DOI=10.1074/jbc.m411380200;
RA   Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.;
RT   "Fyn phosphorylates human MAP-2c on tyrosine 67.";
RL   J. Biol. Chem. 280:1962-1970(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1347 AND SER-1353, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1782, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   INTERACTION WITH DPYSL5.
RX   PubMed=33894126; DOI=10.1016/j.ajhg.2021.04.004;
RA   Jeanne M., Demory H., Moutal A., Vuillaume M.L., Blesson S., Thepault R.A.,
RA   Marouillat S., Halewa J., Maas S.M., Motazacker M.M., Mancini G.M.S.,
RA   van Slegtenhorst M.A., Andreou A., Cox H., Vogt J., Laufman J.,
RA   Kostandyan N., Babikyan D., Hancarova M., Bendova S., Sedlacek Z.,
RA   Aldinger K.A., Sherr E.H., Argilli E., England E.M., Audebert-Bellanger S.,
RA   Bonneau D., Colin E., Denomme-Pichon A.S., Gilbert-Dussardier B.,
RA   Isidor B., Kuery S., Odent S., Redon R., Khanna R., Dobyns W.B.,
RA   Bezieau S., Honnorat J., Lohkamp B., Toutain A., Laumonnier F.;
RT   "Missense variants in DPYSL5 cause a neurodevelopmental disorder with
RT   corpus callosum agenesis and cerebellar abnormalities.";
RL   Am. J. Hum. Genet. 108:951-961(2021).
RN   [14]
RP   VARIANTS [LARGE SCALE ANALYSIS] ASP-277 AND LEU-705.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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 (PubMed:33894126). {ECO:0000250|UniProtKB:P20357,
CC       ECO:0000269|PubMed:33894126}.
CC   -!- INTERACTION:
CC       P11137; Q13951: CBFB; NbExp=2; IntAct=EBI-2682460, EBI-718750;
CC       P11137-4; P02649: APOE; NbExp=3; IntAct=EBI-25832133, EBI-1222467;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC       projection, dendrite {ECO:0000250|UniProtKB:P20357}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=MAP2b;
CC         IsoId=P11137-1; Sequence=Displayed;
CC       Name=2; Synonyms=MAP2c;
CC         IsoId=P11137-2; Sequence=VSP_003197;
CC       Name=3;
CC         IsoId=P11137-3; Sequence=VSP_011302;
CC       Name=4;
CC         IsoId=P11137-4; Sequence=VSP_043596, VSP_043597, VSP_043598;
CC   -!- PTM: Phosphorylated at serine residues in K-X-G-S motifs by
CC       MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing
CC       detachment from microtubules, and their disassembly (By similarity).
CC       Isoform 2 is probably phosphorylated by PKA at Ser-323, Ser-354 and
CC       Ser-386 and by FYN at Tyr-67. The interaction with KNDC1 enhances MAP2
CC       threonine phosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:P15146, ECO:0000250|UniProtKB:P20357}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44216/MAP2";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U01828; AAA03354.1; -; mRNA.
DR   EMBL; U89330; AAB48098.1; -; mRNA.
DR   EMBL; U89329; AAB48097.1; -; mRNA.
DR   EMBL; AC006385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC019106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471063; EAW70459.1; -; Genomic_DNA.
DR   EMBL; BC038857; AAH38857.1; -; mRNA.
DR   EMBL; BC110423; AAI10424.1; -; mRNA.
DR   EMBL; BC117123; AAI17124.1; -; mRNA.
DR   EMBL; BC143245; AAI43246.1; -; mRNA.
DR   EMBL; M25668; AAA59552.1; -; mRNA.
DR   CCDS; CCDS2384.1; -. [P11137-1]
DR   CCDS; CCDS2385.1; -. [P11137-2]
DR   CCDS; CCDS33369.1; -. [P11137-4]
DR   CCDS; CCDS86916.1; -. [P11137-3]
DR   PIR; I53693; QRHUMT.
DR   PIR; I67793; I67793.
DR   RefSeq; NP_001034627.1; NM_001039538.1. [P11137-4]
DR   RefSeq; NP_002365.3; NM_002374.3. [P11137-1]
DR   RefSeq; NP_114033.2; NM_031845.2. [P11137-2]
DR   RefSeq; NP_114035.2; NM_031847.2.
DR   RefSeq; XP_016859607.1; XM_017004118.1.
DR   RefSeq; XP_016859612.1; XM_017004123.1.
DR   RefSeq; XP_016859613.1; XM_017004124.1.
DR   RefSeq; XP_016859627.1; XM_017004138.1.
DR   RefSeq; XP_016859628.1; XM_017004139.1.
DR   RefSeq; XP_016859629.1; XM_017004140.1.
DR   AlphaFoldDB; P11137; -.
DR   SMR; P11137; -.
DR   BioGRID; 110305; 74.
DR   DIP; DIP-577N; -.
DR   IntAct; P11137; 27.
DR   MINT; P11137; -.
DR   STRING; 9606.ENSP00000353508; -.
DR   BindingDB; P11137; -.
DR   ChEMBL; CHEMBL2390810; -.
DR   DrugBank; DB01248; Docetaxel.
DR   DrugBank; DB01196; Estramustine.
DR   DrugBank; DB01229; Paclitaxel.
DR   GlyCosmos; P11137; 7 sites, 1 glycan.
DR   GlyGen; P11137; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P11137; -.
DR   PhosphoSitePlus; P11137; -.
DR   BioMuta; MAP2; -.
DR   DMDM; 215274255; -.
DR   EPD; P11137; -.
DR   jPOST; P11137; -.
DR   MassIVE; P11137; -.
DR   MaxQB; P11137; -.
DR   PaxDb; 9606-ENSP00000353508; -.
DR   PeptideAtlas; P11137; -.
DR   ProteomicsDB; 52694; -. [P11137-1]
DR   ProteomicsDB; 52695; -. [P11137-2]
DR   ProteomicsDB; 52696; -. [P11137-3]
DR   ProteomicsDB; 52697; -. [P11137-4]
DR   Pumba; P11137; -.
DR   Antibodypedia; 2169; 1585 antibodies from 47 providers.
DR   DNASU; 4133; -.
DR   Ensembl; ENST00000199940.10; ENSP00000199940.6; ENSG00000078018.22. [P11137-4]
DR   Ensembl; ENST00000360351.8; ENSP00000353508.4; ENSG00000078018.22. [P11137-1]
DR   Ensembl; ENST00000361559.8; ENSP00000355290.4; ENSG00000078018.22. [P11137-2]
DR   Ensembl; ENST00000392194.5; ENSP00000376032.1; ENSG00000078018.22. [P11137-2]
DR   Ensembl; ENST00000447185.5; ENSP00000392164.1; ENSG00000078018.22. [P11137-3]
DR   Ensembl; ENST00000682079.1; ENSP00000507035.1; ENSG00000078018.22. [P11137-1]
DR   GeneID; 4133; -.
DR   KEGG; hsa:4133; -.
DR   MANE-Select; ENST00000682079.1; ENSP00000507035.1; NM_001375505.1; NP_001362434.1.
DR   UCSC; uc002vdd.2; human. [P11137-1]
DR   AGR; HGNC:6839; -.
DR   CTD; 4133; -.
DR   DisGeNET; 4133; -.
DR   GeneCards; MAP2; -.
DR   HGNC; HGNC:6839; MAP2.
DR   HPA; ENSG00000078018; Group enriched (brain, retina).
DR   MIM; 157130; gene.
DR   neXtProt; NX_P11137; -.
DR   OpenTargets; ENSG00000078018; -.
DR   PharmGKB; PA30583; -.
DR   VEuPathDB; HostDB:ENSG00000078018; -.
DR   eggNOG; KOG2418; Eukaryota.
DR   GeneTree; ENSGT00940000156597; -.
DR   HOGENOM; CLU_021741_3_0_1; -.
DR   InParanoid; P11137; -.
DR   OrthoDB; 5406159at2759; -.
DR   PhylomeDB; P11137; -.
DR   TreeFam; TF316358; -.
DR   PathwayCommons; P11137; -.
DR   SignaLink; P11137; -.
DR   SIGNOR; P11137; -.
DR   BioGRID-ORCS; 4133; 9 hits in 1157 CRISPR screens.
DR   ChiTaRS; MAP2; human.
DR   GeneWiki; MAP2; -.
DR   GenomeRNAi; 4133; -.
DR   Pharos; P11137; Tchem.
DR   PRO; PR:P11137; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P11137; Protein.
DR   Bgee; ENSG00000078018; Expressed in Brodmann (1909) area 23 and 186 other cell types or tissues.
DR   ExpressionAtlas; P11137; baseline and differential.
DR   GO; GO:0150014; C:apical distal dendrite; ISS:ARUK-UCL.
DR   GO; GO:0043203; C:axon hillock; ISS:ARUK-UCL.
DR   GO; GO:0043194; C:axon initial segment; ISS:ARUK-UCL.
DR   GO; GO:0097441; C:basal dendrite; ISS:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR   GO; GO:0005829; C:cytosol; ISS:ARUK-UCL.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:ARUK-UCL.
DR   GO; GO:0044307; C:dendritic branch; ISS:ARUK-UCL.
DR   GO; GO:1902737; C:dendritic filopodium; ISS:ARUK-UCL.
DR   GO; GO:0044294; C:dendritic growth cone; ISS:ARUK-UCL.
DR   GO; GO:0043198; C:dendritic shaft; ISS:ARUK-UCL.
DR   GO; GO:0150002; C:distal dendrite; ISS:ARUK-UCL.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR   GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR   GO; GO:0150001; C:primary dendrite; ISS:ARUK-UCL.
DR   GO; GO:1990635; C:proximal dendrite; ISS:ARUK-UCL.
DR   GO; GO:1990769; C:proximal neuron projection; ISS:ARUK-UCL.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR   GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR   GO; GO:0021954; P:central nervous system neuron development; IEP:DFLAT.
DR   GO; GO:0016358; P:dendrite development; TAS:ARUK-UCL.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEP:DFLAT.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:ARUK-UCL.
DR   GO; GO:0030517; P:negative regulation of axon extension; ISS:ARUK-UCL.
DR   GO; GO:1904527; P:negative regulation of microtubule binding; ISS:ARUK-UCL.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:ARUK-UCL.
DR   GO; GO:0031175; P:neuron projection development; IEP:DFLAT.
DR   GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISS:ARUK-UCL.
DR   GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; ISS:ARUK-UCL.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; TAS:ARUK-UCL.
DR   GO; GO:1902513; P:regulation of organelle transport along microtubule; ISS:ARUK-UCL.
DR   GO; GO:0032880; P:regulation of protein localization; ISS: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.
DR   Genevisible; P11137; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Cell projection; Cytoplasm;
KW   Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1827
FT                   /note="Microtubule-associated protein 2"
FT                   /id="PRO_0000072747"
FT   REPEAT          1661..1691
FT                   /note="Tau/MAP 1"
FT   REPEAT          1692..1722
FT                   /note="Tau/MAP 2"
FT   REPEAT          1723..1754
FT                   /note="Tau/MAP 3"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..744
FT                   /note="Interaction with KNDC1"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   REGION          931..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1073..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1403..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1447..1467
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          1471..1490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1506..1638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1779..1801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..986
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1100..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1314..1329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1349..1378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1559..1576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1583..1618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1780..1801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         629
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         733
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         736
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         738
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         745
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         890
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         936
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         1133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         1155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1602
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1605
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1616
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1619
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1649
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         1679
FT                   /note="Phosphoserine; by MARK1"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         1782
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1790
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20357"
FT   MOD_RES         1795
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   MOD_RES         1808
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15146"
FT   VAR_SEQ         152..1507
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8294038"
FT                   /id="VSP_003197"
FT   VAR_SEQ         152..229
FT                   /note="DLLTASKMEFHDQQELTPSTAEPSDQKEKESEKQSKPGEDLKHAALVSQPET
FT                   TKTYPDKKDMQGTEEEKAPLALFGHT -> AAGGESALAPSVFKQAKDKVSNSTLSKIP
FT                   ALQGSTKSPRYSSACPSTTKRATFSDSLLIQPTSAGSTDRLPYSKSGNK (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043596"
FT   VAR_SEQ         152..155
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8294038"
FT                   /id="VSP_011302"
FT   VAR_SEQ         230..1528
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043597"
FT   VAR_SEQ         1691
FT                   /note="Q -> QVRILNKKIDFSKVQSRCGSKDNIKHSAGGGN (in isoform
FT                   4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043598"
FT   VARIANT         82
FT                   /note="A -> G (in dbSNP:rs2271251)"
FT                   /id="VAR_019612"
FT   VARIANT         179
FT                   /note="E -> G (in dbSNP:rs6749066)"
FT                   /id="VAR_050019"
FT   VARIANT         277
FT                   /note="E -> D (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036014"
FT   VARIANT         423
FT                   /note="R -> K (in dbSNP:rs741006)"
FT                   /id="VAR_019613"
FT   VARIANT         705
FT                   /note="P -> L (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs146432517)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036015"
FT   VARIANT         976
FT                   /note="H -> L (in dbSNP:rs13425372)"
FT                   /id="VAR_050020"
FT   VARIANT         991
FT                   /note="G -> R (in dbSNP:rs35927101)"
FT                   /id="VAR_050021"
FT   VARIANT         1099
FT                   /note="M -> V (in dbSNP:rs17745550)"
FT                   /id="VAR_050022"
FT   CONFLICT        9
FT                   /note="A -> G (in Ref. 2; AAB48098/AAB48097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="A -> R (in Ref. 1; AAA03354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="G -> A (in Ref. 1; AAA03354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="K -> S (in Ref. 1; AAA03354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1112
FT                   /note="E -> Q (in Ref. 1; AAA03354, 2; AAB48098 and 5;
FT                   AAA59552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1655
FT                   /note="A -> GL (in Ref. 2; AAB48098/AAB48097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1715..1716
FT                   /note="RH -> D (in Ref. 1; AAA03354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1736
FT                   /note="A -> V (in Ref. 1; AAA03354)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         P11137-2:67
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:15536091"
FT   MOD_RES         P11137-2:323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         P11137-2:354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         P11137-2:386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1827 AA;  199526 MW;  2C4801C589086603 CRC64;
     MADERKDEAK APHWTSAPLT EASAHSHPPE IKDQGGAGEG LVRSANGFPY REDEEGAFGE
     HGSQGTYSNT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQT
     AALPLAAEET ANLPPSPPPS PASEQTVTVE EDLLTASKME FHDQQELTPS TAEPSDQKEK
     ESEKQSKPGE DLKHAALVSQ PETTKTYPDK KDMQGTEEEK APLALFGHTL VASLEDMKQK
     TEPSLVVPGI DLPKEPPTPK EQKDWFIEMP TEAKKDEWGL VAPISPGPLT PMREKDVFDD
     IPKWEGKQFD SPMPSPFQGG SFTLPLDVMK NEIVTETSPF APAFLQPDDK KSLQQTSGPA
     TAKDSFKIEE PHEAKPDKMA EAPPSEAMTL PKDAHIPVVE EHVMGKVLEE EKEAINQETV
     QQRDTFTPSG QEPILTEKET ELKLEEKTTI SDKEAVPKES KPPKPADEEI GIIQTSTEHT
     FSEQKDQEPT TDMLKQDSFP VSLEQAVTDS AMTSKTLEKA MTEPSALIEK SSIQELFEMR
     VDDKDKIEGV GAATSAELDM PFYEDKSGMS KYFETSALKE EATKSIEPGS DYYELSDTRE
     SVHESIDTMS PMHKNGDKEF QTGKESQPSP PAQEAGYSTL AQSYPSDLPE EPSSPQERMF
     TIDPKVYGEK RDLHSKNKDD LTLSRSLGLG GRSAIEQRSM SINLPMSCLD SIALGFNFGR
     GHDLSPLASD ILTNTSGSMD EGDDYLPATT PALEKAPCFP VESKEEEQIE KVKATGEEST
     QAEISCESPF LAKDFYKNGT VMAPDLPEML DLAGTRSRLA SVSADAEVAR RKSVPSETVV
     EDSRTGLPPV TDENHVIVKT DSQLEDLGYC VFNKYTVPLP SPVQDSENLS GESGTFYEGT
     DDKVRRDLAT DLSLIEVKLA AAGRVKDEFS VDKEASAHIS GDKSGLSKEF DQEKKANDRL
     DTVLEKSEEH ADSKEHAKKT EEAGDEIETF GLGVTYEQAL AKDLSIPTDA SSEKAEKGLS
     SVPEIAEVEP SKKVEQGLDF AVQGQLDVKI SDFGQMASGL NIDDRRATEL KLEATQDMTP
     SSKAPQEADA FMGVESGHMK EGTKVSETEV KEKVAKPDLV HQEAVDKEES YESSGEHESL
     TMESLKADEG KKETSPESSL IQDEIAVKLS VEIPCPPAVS EADLATDERA DVQMEFIQGP
     KEESKETPDI SITPSDVAEP LHETIVSEPA EIQSEEEEIE AQGEYDKLLF RSDTLQITDL
     GVSGAREEFV ETCPSEHKGV IESVVTIEDD FITVVQTTTD EGESGSHSVR FAALEQPEVE
     RRPSPHDEEE FEVEEAAEAQ AEPKDGSPEA PASPEREEVA LSEYKTETYD DYKDETTIDD
     SIMDADSLWV DTQDDDRSIM TEQLETIPKE EKAEKEARRS SLEKHRKEKP FKTGRGRIST
     PERKVAKKEP STVSRDEVRR KKAVYKKAEL AKKTEVQAHS PSRKFILKPA IKYTRPTHLS
     CVKRKTTAAG GESALAPSVF KQAKDKVSDG VTKSPEKRSS LPRPSSILPP RRGVSGDRDE
     NSFSLNSSIS SSARRTTRSE PIRRAGKSGT STPTTPGSTA ITPGTPPSYS SRTPGTPGTP
     SYPRTPHTPG TPKSAILVPS EKKVAIIRTP PKSPATPKQL RLINQPLPDL KNVKSKIGST
     DNIKYQPKGG QVQIVTKKID LSHVTSKCGS LKNIRHRPGG GRVKIESVKL DFKEKAQAKV
     GSLDNAHHVP GGGNVKIDSQ KLNFREHAKA RVDHGAEIIT QSPGRSSVAS PRRLSNVSSS
     GSINLLESPQ LATLAEDVTA ALAKQGL
//