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Microtubule-associated protein 1A (MAP-1A) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]

 MAP1A_MOUSE             Reviewed;        2776 AA.
Q9QYR6; A2ARN9; Q3TQM8; Q3TUV8; Q3UHB7; Q9QZH9; Q9QZI0; Q9QZI1;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 2.
18-JUL-2018, entry version 144.
RecName: Full=Microtubule-associated protein 1A;
Short=MAP-1A;
Contains:
RecName: Full=MAP1A heavy chain;
Contains:
RecName: Full=MAP1 light chain LC2;
Name=Map1a; Synonyms=Mtap1, Mtap1a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-224 (ISOFORMS 1 AND 2),
AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11311937; DOI=10.1016/S0167-4781(01)00173-7;
Nakayama A., Odajima T., Murakami H., Mori N., Takahashi M.;
"Characterization of two promoters that regulate alternative
transcripts in the microtubule-associated protein (MAP) 1A gene.";
Biochim. Biophys. Acta 1518:260-266(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633; SER-644; SER-667;
SER-981; SER-1768 AND SER-1772, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[5]
INTERACTION WITH TIAM2.
PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
Amano M.;
"Rho-kinase modulates the function of STEF, a Rac GEF, through its
phosphorylation.";
Biochem. Biophys. Res. Commun. 355:788-794(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-117; SER-118;
SER-121; SER-155; SER-384; SER-526; SER-527; THR-633; SER-667;
SER-678; SER-873; SER-876; SER-877; SER-890; THR-893; SER-895;
SER-899; SER-908; SER-981; SER-991; SER-999; SER-1008; SER-1023;
SER-1062; THR-1068; SER-1131; SER-1133; SER-1147; SER-1177; SER-1196;
SER-1205; SER-1289; SER-1310; SER-1313; SER-1316; SER-1516; SER-1606;
SER-1747; SER-1762; SER-1768; SER-1772; THR-1777; SER-1783; SER-1789
AND SER-2082, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Structural protein involved in the filamentous cross-
bridging between microtubules and other skeletal elements.
-!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate
with MAP1A and MAP1B proteins. Interacts with guanylate kinase-
like domain of DLG1, DLG2 and DLG4. Binds to CSNK1D (By
similarity). Interacts with TIAM2. {ECO:0000250,
ECO:0000269|PubMed:17320046}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9QYR6-1; Sequence=Displayed;
Name=2;
IsoId=Q9QYR6-2; Sequence=VSP_003201;
-!- TISSUE SPECIFICITY: Both isoforms highly expressed in brain, and
to a lesser extent in embryo. Isoform 1 is also expressed at a low
level in other tissues including heart and muscle.
{ECO:0000269|PubMed:11311937}.
-!- DOMAIN: The basic region containing the repeats may be responsible
for the binding of MAP1A to microtubules.
-!- PTM: Phosphorylated by CSNK1D. {ECO:0000250}.
-!- PTM: LC2 is generated from MAP1A by proteolytic processing. It is
free to associate with both MAP1A and MAP1B (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
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EMBL; AK147474; BAE27940.1; -; mRNA.
EMBL; AK160546; BAE35863.1; -; mRNA.
EMBL; AK163468; BAE37354.1; -; mRNA.
EMBL; AL845466; CAM24218.1; -; Genomic_DNA.
EMBL; AF182211; AAF06164.1; -; Genomic_DNA.
EMBL; AF182208; AAF06164.1; JOINED; Genomic_DNA.
EMBL; AF182209; AAF06164.1; JOINED; Genomic_DNA.
EMBL; AF182211; AAF06163.1; -; Genomic_DNA.
EMBL; AF182213; AAD55790.1; -; mRNA.
EMBL; AF182212; AAD55789.1; -; mRNA.
CCDS; CCDS50685.1; -. [Q9QYR6-1]
RefSeq; NP_001166977.1; NM_001173506.1. [Q9QYR6-1]
RefSeq; NP_115769.1; NM_032393.2.
UniGene; Mm.36501; -.
PDB; 5GNV; X-ray; 2.60 A; B=1866-1891.
PDBsum; 5GNV; -.
ProteinModelPortal; Q9QYR6; -.
SMR; Q9QYR6; -.
BioGrid; 201583; 8.
IntAct; Q9QYR6; 7.
MINT; Q9QYR6; -.
STRING; 10090.ENSMUSP00000092223; -.
iPTMnet; Q9QYR6; -.
PhosphoSitePlus; Q9QYR6; -.
SwissPalm; Q9QYR6; -.
PaxDb; Q9QYR6; -.
PRIDE; Q9QYR6; -.
Ensembl; ENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254. [Q9QYR6-1]
GeneID; 17754; -.
KEGG; mmu:17754; -.
UCSC; uc008lyj.2; mouse. [Q9QYR6-1]
CTD; 4130; -.
MGI; MGI:1306776; Map1a.
eggNOG; KOG3592; Eukaryota.
eggNOG; ENOG410XRYM; LUCA.
GeneTree; ENSGT00550000074593; -.
HOVERGEN; HBG052408; -.
InParanoid; Q9QYR6; -.
KO; K10429; -.
PRO; PR:Q9QYR6; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027254; -.
CleanEx; MM_MTAP1A; -.
ExpressionAtlas; Q9QYR6; baseline and differential.
Genevisible; Q9QYR6; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043194; C:axon initial segment; IDA:ARUK-UCL.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
GO; GO:0044307; C:dendritic branch; ISO:MGI.
GO; GO:1901588; C:dendritic microtubule; IDA:ARUK-UCL.
GO; GO:0043198; C:dendritic shaft; ISO:MGI.
GO; GO:0005875; C:microtubule associated complex; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0150001; C:primary dendrite; ISO:MGI.
GO; GO:0003779; F:actin binding; IDA:ARUK-UCL.
GO; GO:0005518; F:collagen binding; ISO:MGI.
GO; GO:0008093; F:cytoskeletal adaptor activity; IDA:ARUK-UCL.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:ARUK-UCL.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0015631; F:tubulin binding; IDA:ARUK-UCL.
GO; GO:0099641; P:anterograde axonal protein transport; IGI:ARUK-UCL.
GO; GO:0008306; P:associative learning; IMP:ARUK-UCL.
GO; GO:0007613; P:memory; IMP:ARUK-UCL.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:ARUK-UCL.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ARUK-UCL.
GO; GO:1902817; P:negative regulation of protein localization to microtubule; IMP:ARUK-UCL.
GO; GO:0070050; P:neuron cellular homeostasis; IMP:ARUK-UCL.
GO; GO:1990535; P:neuron projection maintenance; IMP:ARUK-UCL.
GO; GO:0045494; P:photoreceptor cell maintenance; IGI:MGI.
GO; GO:1903829; P:positive regulation of cellular protein localization; IMP:ARUK-UCL.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:ARUK-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:ARUK-UCL.
GO; GO:0099642; P:retrograde axonal protein transport; IGI:ARUK-UCL.
GO; GO:0007605; P:sensory perception of sound; IDA:MGI.
GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:ARUK-UCL.
InterPro; IPR026074; MAP1.
InterPro; IPR015656; MAP1A.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
PANTHER; PTHR13843; PTHR13843; 2.
PANTHER; PTHR13843:SF6; PTHR13843:SF6; 2.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 2776 Microtubule-associated protein 1A.
/FTId=PRO_0000072753.
CHAIN 1 2542 MAP1A heavy chain.
/FTId=PRO_0000418377.
CHAIN 2543 2776 MAP1 light chain LC2.
/FTId=PRO_0000269727.
REPEAT 336 338 1.
REPEAT 415 417 2.
REPEAT 420 422 3.
REPEAT 424 426 4.
REPEAT 427 429 5.
REPEAT 431 433 6.
REPEAT 436 438 7.
REPEAT 440 442 8.
REPEAT 444 446 9.
REPEAT 449 451 10.
REPEAT 539 541 11.
REGION 336 541 11 X 3 AA approximate repeats of K-K-
[DE].
COMPBIAS 338 677 Glu-rich.
COMPBIAS 1748 2303 Pro-rich.
COMPBIAS 2530 2551 Pro-rich.
COMPBIAS 2747 2750 Poly-Gln.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 177 177 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 504 504 Phosphothreonine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 633 633 Phosphothreonine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 644 644 Phosphoserine.
{ECO:0000244|PubMed:16452087}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 877 877 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 893 893 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 895 895 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 899 899 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 981 981 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1008 1008 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1014 1014 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 1023 1023 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1068 1068 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1131 1131 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1177 1177 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1187 1187 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1190 1190 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1196 1196 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1205 1205 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1208 1208 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 1251 1251 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 1289 1289 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1310 1310 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1313 1313 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1316 1316 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1516 1516 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1580 1580 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1606 1606 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1634 1634 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1648 1648 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1720 1720 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1747 1747 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1762 1762 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1768 1768 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 1772 1772 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 1777 1777 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1783 1783 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1789 1789 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1902 1902 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 1928 1928 Phosphothreonine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 1993 1993 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 2031 2031 Phosphothreonine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2048 2048 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 2082 2082 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2209 2209 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2226 2226 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2230 2230 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2233 2233 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2234 2234 Phosphoserine.
{ECO:0000250|UniProtKB:P34926}.
MOD_RES 2425 2425 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 2623 2623 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
MOD_RES 2637 2637 Phosphoserine.
{ECO:0000250|UniProtKB:P78559}.
VAR_SEQ 1 1 M -> METTPELGLQSLGAPPAQNPAEPLCEAGAAVAAARW
DLRKYSLLIVIGDIGTESQLRAVRAHLEQGILSWNIDLSSF
DLNQQLRLFITRHLAHFSSEVKGQRTLCHQSETLETIILVN
PTADSISSEVHHLLSSPSAHKLLILSGQTLEPEGDLILQSG
TYSYQNFAQVLHKPEIAQLLSNRDPGIQAFLTVSCLGEGDW
SHLGLSSSQETLHLRLNPEPVLPTM (in isoform 2).
{ECO:0000303|PubMed:11311937}.
/FTId=VSP_003201.
CONFLICT 349 349 R -> C (in Ref. 1; BAE27940).
{ECO:0000305}.
HELIX 1877 1880 {ECO:0000244|PDB:5GNV}.
HELIX 1882 1884 {ECO:0000244|PDB:5GNV}.
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


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