MAP1A_MOUSE
ID MAP1A_MOUSE Reviewed; 2776 AA.
AC Q9QYR6; A2ARN9; Q3TQM8; Q3TUV8; Q3UHB7; Q9QZH9; Q9QZI0; Q9QZI1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Microtubule-associated protein 1A;
DE Short=MAP-1A;
DE Contains:
DE RecName: Full=MAP1A heavy chain;
DE Contains:
DE RecName: Full=MAP1 light chain LC2;
GN Name=Map1a; Synonyms=Mtap1, Mtap1a;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-224 (ISOFORMS 1 AND 2), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11311937; DOI=10.1016/s0167-4781(01)00173-7;
RA Nakayama A., Odajima T., Murakami H., Mori N., Takahashi M.;
RT "Characterization of two promoters that regulate alternative transcripts in
RT the microtubule-associated protein (MAP) 1A gene.";
RL Biochim. Biophys. Acta 1518:260-266(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633; SER-644; SER-667;
RP SER-981; SER-1768 AND SER-1772, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [5]
RP INTERACTION WITH TIAM2.
RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M.,
RA Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.;
RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-117; SER-118;
RP SER-121; SER-155; SER-384; SER-526; SER-527; THR-633; SER-667; SER-678;
RP SER-873; SER-876; SER-877; SER-890; THR-893; SER-895; SER-899; SER-908;
RP SER-981; SER-991; SER-999; SER-1008; SER-1023; SER-1062; THR-1068;
RP SER-1131; SER-1133; SER-1147; SER-1177; SER-1196; SER-1205; SER-1289;
RP SER-1310; SER-1313; SER-1316; SER-1516; SER-1606; SER-1747; SER-1762;
RP SER-1768; SER-1772; THR-1777; SER-1783; SER-1789 AND SER-2082, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [9]
RP INTERACTION WITH ELAVL4.
RX PubMed=21288476; DOI=10.1016/j.biochi.2011.01.008;
RA Fujiwara Y., Kasashima K., Saito K., Fukuda M., Fukao A., Sasano Y.,
RA Inoue K., Fujiwara T., Sakamoto H.;
RT "Microtubule association of a neuronal RNA-binding protein HuD through its
RT binding to the light chain of MAP1B.";
RL Biochimie 93:817-822(2011).
CC -!- FUNCTION: Structural protein involved in the filamentous cross-bridging
CC between microtubules and other skeletal elements.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins. Interacts with guanylate kinase-like domain
CC of DLG1, DLG2 and DLG4. Binds to CSNK1D (By similarity). Interacts with
CC TIAM2. MAP1 light chain LC2: Interacts with ELAVL4 (PubMed:21288476).
CC {ECO:0000250, ECO:0000269|PubMed:17320046,
CC ECO:0000269|PubMed:21288476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QYR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYR6-2; Sequence=VSP_003201;
CC -!- TISSUE SPECIFICITY: Both isoforms highly expressed in brain, and to a
CC lesser extent in embryo. Isoform 1 is also expressed at a low level in
CC other tissues including heart and muscle.
CC {ECO:0000269|PubMed:11311937}.
CC -!- DOMAIN: The basic region containing the repeats may be responsible for
CC the binding of MAP1A to microtubules.
CC -!- PTM: Phosphorylated by CSNK1D. {ECO:0000250}.
CC -!- PTM: LC2 is generated from MAP1A by proteolytic processing. It is free
CC to associate with both MAP1A and MAP1B (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
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DR EMBL; AK147474; BAE27940.1; -; mRNA.
DR EMBL; AK160546; BAE35863.1; -; mRNA.
DR EMBL; AK163468; BAE37354.1; -; mRNA.
DR EMBL; AL845466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF182211; AAF06164.1; -; Genomic_DNA.
DR EMBL; AF182208; AAF06164.1; JOINED; Genomic_DNA.
DR EMBL; AF182209; AAF06164.1; JOINED; Genomic_DNA.
DR EMBL; AF182211; AAF06163.1; -; Genomic_DNA.
DR EMBL; AF182213; AAD55790.1; -; mRNA.
DR EMBL; AF182212; AAD55789.1; -; mRNA.
DR CCDS; CCDS50685.1; -. [Q9QYR6-1]
DR RefSeq; NP_001166977.1; NM_001173506.1. [Q9QYR6-1]
DR RefSeq; NP_115769.1; NM_032393.2.
DR PDB; 5GNV; X-ray; 2.60 A; B=1866-1891.
DR PDBsum; 5GNV; -.
DR SMR; Q9QYR6; -.
DR BioGRID; 201583; 21.
DR IntAct; Q9QYR6; 7.
DR MINT; Q9QYR6; -.
DR STRING; 10090.ENSMUSP00000092223; -.
DR iPTMnet; Q9QYR6; -.
DR PhosphoSitePlus; Q9QYR6; -.
DR SwissPalm; Q9QYR6; -.
DR jPOST; Q9QYR6; -.
DR MaxQB; Q9QYR6; -.
DR PaxDb; Q9QYR6; -.
DR PRIDE; Q9QYR6; -.
DR ProteomicsDB; 292166; -. [Q9QYR6-1]
DR ProteomicsDB; 292167; -. [Q9QYR6-2]
DR Antibodypedia; 6277; 147 antibodies from 24 providers.
DR DNASU; 17754; -.
DR Ensembl; ENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254. [Q9QYR6-1]
DR GeneID; 17754; -.
DR KEGG; mmu:17754; -.
DR UCSC; uc008lyj.2; mouse. [Q9QYR6-1]
DR CTD; 4130; -.
DR MGI; MGI:1306776; Map1a.
DR VEuPathDB; HostDB:ENSMUSG00000027254; -.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000158701; -.
DR InParanoid; Q9QYR6; -.
DR OrthoDB; 86642at2759; -.
DR BioGRID-ORCS; 17754; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Map1a; mouse.
DR PRO; PR:Q9QYR6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QYR6; protein.
DR Bgee; ENSMUSG00000027254; Expressed in primary visual cortex and 195 other tissues.
DR ExpressionAtlas; Q9QYR6; baseline and differential.
DR Genevisible; Q9QYR6; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0044307; C:dendritic branch; ISO:MGI.
DR GO; GO:1901588; C:dendritic microtubule; IDA:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0150001; C:primary dendrite; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:ARUK-UCL.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IDA:ARUK-UCL.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:ARUK-UCL.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0015631; F:tubulin binding; IDA:ARUK-UCL.
DR GO; GO:0099641; P:anterograde axonal protein transport; IGI:ARUK-UCL.
DR GO; GO:0008306; P:associative learning; IMP:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0007613; P:memory; IMP:ARUK-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:ARUK-UCL.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ARUK-UCL.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; IMP:ARUK-UCL.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:ARUK-UCL.
DR GO; GO:1990535; P:neuron projection maintenance; IMP:ARUK-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IGI:MGI.
DR GO; GO:1903829; P:positive regulation of protein localization; IMP:ARUK-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:ARUK-UCL.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:ARUK-UCL.
DR GO; GO:0099642; P:retrograde axonal protein transport; IGI:ARUK-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IDA:MGI.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:ARUK-UCL.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR015656; MAP1A.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF6; PTHR13843:SF6; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2776
FT /note="Microtubule-associated protein 1A"
FT /id="PRO_0000072753"
FT CHAIN 1..2542
FT /note="MAP1A heavy chain"
FT /id="PRO_0000418377"
FT CHAIN 2543..2776
FT /note="MAP1 light chain LC2"
FT /id="PRO_0000269727"
FT REPEAT 336..338
FT /note="1"
FT REPEAT 415..417
FT /note="2"
FT REPEAT 420..422
FT /note="3"
FT REPEAT 424..426
FT /note="4"
FT REPEAT 427..429
FT /note="5"
FT REPEAT 431..433
FT /note="6"
FT REPEAT 436..438
FT /note="7"
FT REPEAT 440..442
FT /note="8"
FT REPEAT 444..446
FT /note="9"
FT REPEAT 449..451
FT /note="10"
FT REPEAT 539..541
FT /note="11"
FT REGION 310..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..541
FT /note="11 X 3 AA approximate repeats of K-K-[DE]"
FT REGION 345..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..2648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1986..2008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2015..2044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2226..2242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2380..2401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2475..2493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2531..2554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2563..2580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2619..2633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 633
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 893
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1068
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1777
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1928
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2031
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2048
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT VAR_SEQ 1
FT /note="M -> METTPELGLQSLGAPPAQNPAEPLCEAGAAVAAARWDLRKYSLLIVI
FT GDIGTESQLRAVRAHLEQGILSWNIDLSSFDLNQQLRLFITRHLAHFSSEVKGQRTLCH
FT QSETLETIILVNPTADSISSEVHHLLSSPSAHKLLILSGQTLEPEGDLILQSGTYSYQN
FT FAQVLHKPEIAQLLSNRDPGIQAFLTVSCLGEGDWSHLGLSSSQETLHLRLNPEPVLPT
FT M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11311937"
FT /id="VSP_003201"
FT CONFLICT 349
FT /note="R -> C (in Ref. 1; BAE27940)"
FT /evidence="ECO:0000305"
FT HELIX 1877..1880
FT /evidence="ECO:0007829|PDB:5GNV"
FT HELIX 1882..1884
FT /evidence="ECO:0007829|PDB:5GNV"
SQ SEQUENCE 2776 AA; 300140 MW; 62A8CC584CCAB21A CRC64;
MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS ALFAVNGFNI
LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING LLQRKVAELE EEQSQGSSSY
SDWVKNLISP ELGVVFFNVP DKLRLPDASR KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV
SNTIEPLTLF HKMGVGRLDM YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LANGKEAEIS
VPYLTSITAL VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
AGAVPANLKP SKIKHRADSK ESLKAAPKTA MSKLAKREEV LEEGAKEARS ELAKELAKSE
KKAKEPSEKP PEKPSKPERV RTESSEALKA EKRKLIKDKV GKKHLKEKIS KLEEKRDKEK
KEIKKERKEL KKEEGRKEEK KDAKKDEKRK DTKPELKKFS KPDLKPFTPE VRKTLYKAKA
PGRLKVDKGR AARGEKELSS EPRTPPAQKG AAPPPAASGH RELALSSPED LTQDFEELKR
EERGLLAEPR DTELGEKPLP ADASEQGRPS TAIQVTQPPA SVLEQEQVER EKEVVPDFPE
DKGSKNRAPD SGAEVEREKE TWEERKPREA ELTPENIAAA REESEPEVKE DVIEKAELEE
MEEVHPSDEE EEETKAESFY QKHMQEALKV IPKGREALGG RELGFQGKAP EKETASFLSS
LATPAGAAEH VSYIQDETIP GYSETEQTIS DEEIHDEPDE RPAPPRFPTS TYDLSGPEGP
GPFEASQSAE SAVPASSSKT YGAPETELTY PPNMVAAPLA EEEHVSSATS ITECDKLSSF
ATSVAEDQSV ASLTAPQTEE TGKSSLLLDT VTSIPSSRTE ATQGLDYVPS AGTISPTSSL
EEDKGFKSPP CEDFSVTGES EKKGESVGRG LTGEKAVGKE EKNVTTSEKL SSQYAAVFGA
PGHALHPGEP ALGEVEERCL SPDDSTVKMA SPPPSGPPSA AHTPFHQSPV EEKSEPQDFQ
EDSWGDTKHA PGVSKEDAEE QTVKPGPEEA MSEEGKVPLS RSPQAQDTLG SLAGGQTGCT
IQLLPEQDKA VVFETGEAGA ASGAGSLPGE VRTQEPAEPQ KDELLGFTDQ SFSPEDAESL
SVLSVVSPDT AKQEATPRSP CTPKEQQLHK DLWPMVSPED TQSLSFSEES PSKETSLDIS
SKQLSPESLG TLQFGELSLG KEEKGPLVKA EDNSCHLAPV SIPEPHTATV SPPTDEAAGE
AGLTDESPAG NLPGSSFSHS ALSGDRKHSP GEITGPGGHF MTSDSSLTKS PESLSSPAME
DLAMEWGGKA PGSEDRATEQ KEKELERKSE TLQQKDQILS EKAALVQRDS VMHQKDEALD
EENKPGGQQD KTSEQKGRDL DKKDTAVELG KGPEPKGKDL YLEDQGLAEK DKALEQRGAA
LQQTQAPEPR ARAQEHRDLE QKDEHLELRD KTPEEKDKVL VLEDRAPEHI IPQPTQTDRA
PEHRSKVDKE QKDEASEEKE QVLEQKDWAR EKEGAALDQD NRAAGQKDGT LKEDKTQGQK
SSFLEDKSTT PKEMTLDQKS PEKAKGVEQQ DGAVPEKTRA LGLEESPEEE GKAREQEEKY
WKEQDVVQGW RETSPTRGEP VPAWEGKSPE QEVRYWRDRD ITLQQDAYWK ELSCERKVWF
PHELDGQGAR PRYSEEREST FLDEGPNEQE ITPLQHTPRS PWASDFKDFQ EPLPQKGLEV
ERWLAESPVG LPPEEEDKLT RSPFEIISPP ASPPEMTGQR VPSAPGQESP VPDTKSTPPT
RNEPTTPSWL AEIPPWVPKD RPLPPAPLSP APAPPTPAPD PHAPAPFSWG IAEYDSVVAA
VQEGAAELEG GPYSPLGKDY RKAEGEREGE GGAGAPDSSS FSSKVPEVTE SHTTRDAEQT
EPEQREPTPY PDERSFQYAD IYEQMMLTGL GPACPTREPP LGASGDWPPH LSTKEEAAGR
NKSAEKELSS AVSPPNLHSD TPTFSYASLA GPTIPPRQEP EPGPNVEPSF TPPAVPPRAP
ISLSQDPSPP LNGSTTSCGP DRRTPSPKEA GRSHWDDGTN DSDLEKGARE QPEKETQSPS
PHHPMPVGHP SLWPETEAHS SLSSDSHLGP VRPSLDFPAS AFGFSSLQPA PPQLPSPAEP
RSAPCGSLAF SGDRALALVP GTPTRTRHDE YLEVTKAPSL DSSLPQLPSP SSPGAPLLSN
LPRPASPALS EGSSSEATTP VISSVAERFP PGLEVAEQSS GELGPGNEPA AHSLWDLTPL
SPAPLASRDL APAPAPAPAP SLPGNLGDGT LSCRPECSGE LTKKPSPFLS HSGDHEANGP
GETSLNPPGF ATATAEKEEA EALHAWERGS WPEGAERSSR PDTLLSSEQR PGKSSGGPPC
SLSSEVEAGP QGCATDPRPH CGELSPSFLN PPLPPSTDDS DLSTEEARLA GKGGRRRAGR
PGATGGPCPM ADETPPTSAS DSGSSQSDSD VPPETEECPS ITAEAALDSD EDGDFLPVDK
AGGVSGTHHP RPGHDPPPAP LPDPRPPPPR PDVCMADPEG LSSESGRVER LREKVQGRPG
RKAPGRAKPA SPARRLDIRG KRSPTPGKGP VDRTSRALPR PRSTPSQVTS EEKDGHSPMS
KGLVNGLKAG STALGSKGSS GPPVYVDLAY IPNHCSGKTA DQDFFRRVRA SYYVVSGNDP
ANGEPSRAVL DALLEGKAQW GENLQVTLIP THDTEVTREW YQQTHEQQQQ LNVLVLASSS
TVVMQDESFP ACKIEF
