MTAP2_HUMAN
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 03-AUG-2022, entry version 207.
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="http://atlasgeneticsoncology.org/Genes/MAP2ID44216ch2q34.html";
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. [P11137-4]
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; 62.
DR DIP; DIP-577N; -.
DR IntAct; P11137; 18.
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 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; P11137; -.
DR PeptideAtlas; P11137; -.
DR PRIDE; P11137; -.
DR ProteomicsDB; 52694; -. [P11137-1]
DR ProteomicsDB; 52695; -. [P11137-2]
DR ProteomicsDB; 52696; -. [P11137-3]
DR ProteomicsDB; 52697; -. [P11137-4]
DR Antibodypedia; 2169; 1352 antibodies from 47 providers.
DR DNASU; 4133; -.
DR Ensembl; ENST00000199940.10; ENSP00000199940.6; ENSG00000078018.21. [P11137-4]
DR Ensembl; ENST00000360351.8; ENSP00000353508.4; ENSG00000078018.21. [P11137-1]
DR Ensembl; ENST00000361559.8; ENSP00000355290.4; ENSG00000078018.21. [P11137-2]
DR Ensembl; ENST00000392194.5; ENSP00000376032.1; ENSG00000078018.21. [P11137-2]
DR Ensembl; ENST00000447185.5; ENSP00000392164.1; ENSG00000078018.21. [P11137-3]
DR Ensembl; ENST00000682079.1; ENSP00000507035.1; ENSG00000078018.21. [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 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; 716848at2759; -.
DR PhylomeDB; P11137; -.
DR TreeFam; TF316358; -.
DR PathwayCommons; P11137; -.
DR SignaLink; P11137; -.
DR SIGNOR; P11137; -.
DR BioGRID-ORCS; 4133; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; MAP2; human.
DR GeneWiki; MAP2; -.
DR GenomeRNAi; 4133; -.
DR Pharos; P11137; Tbio.
DR PRO; PR:P11137; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P11137; protein.
DR Bgee; ENSG00000078018; Expressed in Brodmann (1909) area 23 and 184 other tissues.
DR ExpressionAtlas; P11137; baseline and differential.
DR Genevisible; P11137; HS.
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:0001578; P:microtubule bundle formation; IEA:InterPro.
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; 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 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
