MAP1A_RAT
ID MAP1A_RAT Reviewed; 2774 AA.
AC P34926;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 152.
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=Mtap1a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1379599; DOI=10.1016/s0021-9258(18)42039-x;
RA Langkopf A., Hammarback J.A., Mueller R., Vallee R.B., Garner C.C.;
RT "Microtubule-associated proteins 1A and LC2. Two proteins encoded in one
RT messenger RNA.";
RL J. Biol. Chem. 267:16561-16566(1992).
RN [2]
RP INTERACTION WITH DLG1; DLG2 AND DLG4.
RX PubMed=9786987; DOI=10.1523/jneurosci.18-21-08805.1998;
RA Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T.,
RA Ralston H.J., Bredt D.S.;
RT "Localization of postsynaptic density-93 to dendritic microtubules and
RT interaction with microtubule-associated protein 1A.";
RL J. Neurosci. 18:8805-8813(1998).
RN [3]
RP INTERACTION WITH CSNK1D, AND PHOSPHORYLATION BY CSNK1D.
RX PubMed=15961172; DOI=10.1016/j.bbamcr.2005.05.004;
RA Wolff S., Xiao Z., Wittau M., Suessner N., Stoeter M., Knippschild U.;
RT "Interaction of casein kinase 1 delta (CK1 delta) with the light chain LC2
RT of microtubule associated protein 1A (MAP1A).";
RL Biochim. Biophys. Acta 1745:196-206(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-319; SER-322;
RP SER-384; SER-526; SER-527; SER-611; SER-643; THR-663; SER-666; SER-690;
RP SER-889; THR-892; SER-894; SER-907; SER-980; SER-990; SER-1007; SER-1013;
RP SER-1022; SER-1029; SER-1037; SER-1132; SER-1134; SER-1178; SER-1188;
RP SER-1191; SER-1206; SER-1209; SER-1252; SER-1280; SER-1301; SER-1304;
RP SER-1574; SER-1594; SER-1622; SER-1643; SER-1742; SER-1757; SER-1763;
RP SER-1767; THR-1772; SER-1784; SER-1897; SER-1988; THR-2026; SER-2043;
RP SER-2077; SER-2204; SER-2221; SER-2225; SER-2228; SER-2229 AND SER-2260,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts with TIAM2 (By
CC similarity). MAP1 light chain LC2: Interacts with ELAVL4 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9QYR6,
CC ECO:0000269|PubMed:15961172, ECO:0000269|PubMed:9786987}.
CC -!- INTERACTION:
CC P34926; Q62696: Dlg1; NbExp=2; IntAct=EBI-631571, EBI-389325;
CC P34926; Q63622: Dlg2; NbExp=4; IntAct=EBI-631571, EBI-396947;
CC P34926; P31016: Dlg4; NbExp=16; IntAct=EBI-631571, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain, heart and muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed late during neuronal development
CC appearing when axons and dendrites begin to solidify and stabilize
CC their morphology.
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:0000269|PubMed:15961172}.
CC -!- PTM: LC2 is generated from MAP1A by proteolytic processing. It is free
CC to associate with both MAP1A and MAP1B.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
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DR EMBL; M83196; AAB48069.1; -; mRNA.
DR PIR; A43359; A43359.
DR RefSeq; NP_112257.1; NM_030995.1.
DR BioGRID; 247217; 8.
DR DIP; DIP-29265N; -.
DR IntAct; P34926; 8.
DR MINT; P34926; -.
DR STRING; 10116.ENSRNOP00000019320; -.
DR iPTMnet; P34926; -.
DR PhosphoSitePlus; P34926; -.
DR SwissPalm; P34926; -.
DR jPOST; P34926; -.
DR PaxDb; P34926; -.
DR PRIDE; P34926; -.
DR GeneID; 25152; -.
DR KEGG; rno:25152; -.
DR UCSC; RGD:3042; rat.
DR CTD; 4130; -.
DR RGD; 3042; Map1a.
DR eggNOG; KOG3592; Eukaryota.
DR InParanoid; P34926; -.
DR PhylomeDB; P34926; -.
DR PRO; PR:P34926; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0044307; C:dendritic branch; IDA:ARUK-UCL.
DR GO; GO:1901588; C:dendritic microtubule; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0150001; C:primary dendrite; IDA:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0005518; F:collagen binding; IPI:RGD.
DR GO; GO:0008093; F:cytoskeletal anchor activity; ISO:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:RGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; ISO:RGD.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD.
DR GO; GO:1990535; P:neuron projection maintenance; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0099642; P:retrograde axonal protein transport; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
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 Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..2774
FT /note="Microtubule-associated protein 1A"
FT /id="PRO_0000018602"
FT CHAIN 1..2541
FT /note="MAP1A heavy chain"
FT /id="PRO_0000418378"
FT CHAIN 2542..2774
FT /note="MAP1 light chain LC2"
FT /id="PRO_0000018603"
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..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..541
FT /note="11 X 3 AA repeats of K-K-[DE]"
FT REGION 342..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1693..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..2644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..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..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..2000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2042..2059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2060..2095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2109..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2221..2237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2354..2372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2377..2400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2474..2492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2530..2552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2562..2579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2614..2631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 663
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 892
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1772
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1923
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 1988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2026
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
FT MOD_RES 2635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78559"
SQ SEQUENCE 2774 AA; 299531 MW; 3DEF74427BA9D7D7 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 VSKLAKREEV LEEGAKEARS ELAKELAKTE
KKAKEPSEKP PEKPSKSERV RGESSEALKA EKRRLIKDKA GKKHLKEKIS KLEEKKDKEK
KEIKKERKEL KKEEGRKEEK KDAKKDEKRK DTKPEVKKLS KPDLKPFTPE VRKTLYKAKA
PGRVKVDKGR AARGEKELSS EPRTPPAQKG AAPPAAVSGH RELALSSPED LTQDFEELKR
EERGLLAEQR DTGLGEKPLP ADATEQGHPS AAIQVTQPSG PVLEGEHVER EKEVVPDSPG
DKGSTNRGPD SGAEVEKEKE TWEERKQREA ELGPENTAAR EESEAEVKED VIEKAELEEM
EETHPSDEEG EETKAESFYQ KHTQEALKAS PKSREALGGR DLGFQGKAPE KETASFLSSL
ATPAGATEHV SYIQDETIPG YSETEQTISD EEIHDEPDER PAPPRFPTST YDLSGPEGPG
PFEASQAADS AVPASSSKTY GAPETELTYP PNMVAAPLAE EEHVSSATSI TECDKLSSFA
TSVAEDQSVA SLTAPQTEET GKSSLLLDTV TSIPSSRTEA TQGLDYVPSA GTISPTSSLE
EDKGFKSPPC EDFSVTGESE KKGETVGRGL SGEKAVGKEE KYVVTSEKLS GQYAAVFGAP
GHTLPPGEPA LGEVEERCLS PDDSTVKMAS PPPSGPPSAA HTPFHQSPVE DKSEPRDFQE
DSWGETKHSP GVSKEDSEEQ TVKPGPEEGT SEEGKGPPTR SPQAQDMPVS IAGGQTGCTI
QLLPEQDKAI VFETGEAGSN LGAGTLPGEV RTSTEEATEP QKDEVLRFTD QSLSPEDAES
LSVLSVVSPD TTKQEATPRS PCSLKEQQPH KDLWPMVSPE DTQSLSFSEE SPSKETSLDI
SSKQLSPESL GTLQFGELNL GKEERGPVMK AEDDSCHLAP VSIPEPHRAT VSPSTDETPA
GTLPGGSFSH SALSVDRKHS PGEITGPGGH FMTSDSSLTK SPESLSSPAM EDLAVEWEGK
APGKEKEPEL KSETRQQKGQ ILPEKVAVVE QDLIIHQKDG ALDEENKPGR QQDKTPEQKG
RDLDEKDTAA ELDKGPEPKE KDLDREDQGQ RAGPPAEKDK ASEQRDTDLQ QTQATEPRDR
AQERRDSEEK DKSLELRDRT PEEKDRILVQ EDRAPEHSIP EPTQTDRAPD RKGTDDKEQK
EEASEEKEQV LEQKDWALGK EGETLDQEAR TAEQKDETLK EDKTQGQKSS FVEDKTTTSK
ETVLDQKSAE KADSVEQQDG AALEKTRALG LEESPAEGSK AREQEKKYWK EQDVVQGWRE
TSPTRGEPVG GQKEPVPAWE GKSPEQEVRY WRDRDITLQQ DAYWRELSCD RKVWFPHELD
GQGARPRYCE ERESTFLDEG PDEQEITPLQ HTPRSPWTSD FKDFQEPLPQ KGLEVERWLA
ESPVGLPPEE EDKLTRSPFE IISPPASPPE MTGQRVPSAP GQESPVPDTE STAPMRNEPT
TPSWLAEIPP WVPKDRPLPP APLSPAPAPP TPAPEPHTPV PFSWGLAEYD SVVAAVQEGA
AELEGGPYSP LGKDYRKAEG EREGEGGAGA PDSSSFSPKV PEAGESLATR DTEQTEPEQR
EPTPYPDERS FQYADIYEQM MLTGLGPACP TREPPLGASG DWPPHLSTKE EAAGCNTSAE
KETSSPASPQ NLQSDTPAFS YASLAGPAVP PRQEPDPGPN VEPSITPPAV PPRAPISLSK
DLSPPLNGST VSCSPDRRTP SPKETGRGHW DDGTNDSDLE KGAREQPEKE TRSPSPHHPM
PMGHSSLWPE TEAYSSLSSD SHLGSVRPSL DFPASAFGFS SLQPAPPQLP SPAEPRSAPC
GSLAFSGDRA LALVPGTPTR TRHDEYLEVT KAPSLDSSLP QLPSPSSPGG PLLSNLPRPA
SPALSEGSSS EATTPVISSV AERFPPGLEA AEQSAEGLGS GKESAAHSLW DLTPLSPAPS
ASLDLAPAPA PAPAPAPGLP GDLGDGTLPC RPECTGELTK KPSPFLSPSG DHEANGPGET
SLNPPGFVTA TAEKEEAEAP HAWERGSWPE GAERSSRPDT LLSSEQPLRP GKSSGGPPCS
LSSEVEAGPQ GCATDPRPHC GELSPSFLNP PLPPSTDDSD LSTEEARLAG KGGRRRVGRP
GATGGPCPMA DETPPTSASD SGSSQSDSDV PPETEECPSI TAEAALDSDE DGDFLPVDKA
GGVSGTHHPR PGHDPPPTPL PDPRPSPPRP DVCMADPEGL SSESGRVERL REKGRPGRRA
PGRAKPASPA RRLDIRGKRS PTPGKGPVDR TSRTVPRPRS TPSQVTSAEE KDGHSPMSKG
LVNGLKAGST ALGSKGGSGP PVYVDLAYIP NHCSGKTADQ DFFRRVRASY YVVSGNDPAN
GEPSRAVLDA LLEGKAQWGE NLQVTLIPTH DTEVTREWYQ QTHEQQQQLN VLVLASSSTV
VMQDESFPAC KIEF
