ID MTAP2_RAT Reviewed; 1861 AA. AC P15146; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 3. DT 27-MAR-2024, entry version 187. DE RecName: Full=Microtubule-associated protein 2; DE Short=MAP-2; GN Name=Map2; Synonyms=Mtap2; 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] (ISOFORM 2). RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=2339070; DOI=10.1093/nar/18.9.2822; RA Kindler S., Schwanke B., Schulz B., Garner C.C.; RT "Complete cDNA sequence encoding rat high and low molecular weight MAP2."; RL Nucleic Acids Res. 18:2822-2822(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), AND RP DEVELOPMENTAL STAGE (ISOFORM 3). RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=2174050; DOI=10.1016/s0021-9258(17)45425-1; RA Kindler S., Schulz B., Goedert M., Garner C.C.; RT "Molecular structure of microtubule-associated protein 2b and 2c from rat RT brain."; RL J. Biol. Chem. 265:19679-19684(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=2326166; DOI=10.1093/nar/18.2.361; RA Doll T., Papandrikopoulou A., Matus A.; RT "Nucleotide and amino acid sequences of embryonic rat MAP2c."; RL Nucleic Acids Res. 18:361-361(1990). RN [4] RP DISCUSSION OF SEQUENCE, TISSUE SPECIFICITY (ISOFORM 3), AND DEVELOPMENTAL RP STAGE (ISOFORM 3). RX PubMed=2770869; DOI=10.1038/340650a0; RA Papandrikopoulou A., Doll T., Tucker R.P., Garner C.C., Matus A.; RT "Embryonic MAP2 lacks the cross-linking sidearm sequences and dendritic RT targeting signal of adult MAP2."; RL Nature 340:650-652(1989). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1695-1725 (ISOFORM 1). RX PubMed=8282767; DOI=10.1242/jcs.106.2.633; RA Doll T., Meichsner M., Riederer B.M., Honegger P., Matus A.; RT "An isoform of microtubule-associated protein 2 (MAP2) containing four RT repeats of the tubulin-binding motif."; RL J. Cell Sci. 106:633-640(1993). RN [6] RP PHOSPHORYLATION AT SER-1682. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=9108484; DOI=10.1016/s0092-8674(00)80208-1; RA Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.; RT "MARK - a novel family of protein kinases that phosphorylate microtubule- RT associated proteins and trigger microtubule disruption."; RL Cell 89:297-308(1997). RN [7] RP PHOSPHORYLATION AT SER-319; SER-350 AND SER-382 (ISOFORM 3). RX PubMed=11029056; DOI=10.1091/mbc.11.10.3573; RA Ozer R.S., Halpain S.; RT "Phosphorylation-dependent localization of microtubule-associated protein RT MAP2c to the actin cytoskeleton."; RL Mol. Biol. Cell 11:3573-3587(2000). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-136; SER-140; RP SER-221; SER-224; SER-348; SER-498; SER-522; SER-610; SER-628; SER-741; RP SER-884; SER-893; SER-939; SER-1051; SER-1140; SER-1141; THR-1161; RP SER-1162; SER-1353; THR-1359; SER-1541; THR-1611; THR-1622; THR-1625; RP THR-1652; SER-1656; SER-1816; SER-1824; SER-1829 AND SER-1842, AND RP 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). RN [9] RP DEVELOPMENTAL STAGE. RX PubMed=29934347; DOI=10.1523/jneurosci.0699-18.2018; RA Lizama B.N., Palubinsky A.M., Raveendran V.A., Moore A.M., Federspiel J.D., RA Codreanu S.G., Liebler D.C., McLaughlin B.; RT "Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of RT HSC70-Interacting Protein."; RL J. Neurosci. 38:6825-6840(2018). 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 (By similarity). {ECO:0000250|UniProtKB:P11137, CC ECO:0000250|UniProtKB:P20357}. 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=MAP2x; CC IsoId=P15146-1; Sequence=Displayed; CC Name=2; Synonyms=MAP2b; CC IsoId=P15146-2; Sequence=VSP_003199; CC Name=3; Synonyms=MAP2c; CC IsoId=P15146-3; Sequence=VSP_003198, VSP_003199; CC Name=4; Synonyms=MAP2d; CC IsoId=P15146-4; Sequence=VSP_003198; CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in the liver. CC {ECO:0000269|PubMed:2174050}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in the entorhinal cortex and CC hippocampal neuronal cell bodies. {ECO:0000269|PubMed:2770869}. CC -!- DEVELOPMENTAL STAGE: Expressed in neurons at 18.5 dpc (at protein CC level). {ECO:0000269|PubMed:29934347}. CC -!- DEVELOPMENTAL STAGE: [Isoform 3]: Expressed in the brain at postnatal CC day 6 (PubMed:2770869). Expressed in the brain at postnatal day 7 CC (PubMed:2174050). {ECO:0000269|PubMed:2174050, CC ECO:0000269|PubMed:2770869}. 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. Isoform 3/MAP2c is CC probably phosphorylated by PKA at Ser-319, Ser-350 and Ser-382 and by CC FYN at Tyr-67. The interaction with KNDC1 enhances MAP2 threonine CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:P20357, CC ECO:0000269|PubMed:11029056, ECO:0000269|PubMed:9108484}. 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; X51842; CAA36135.1; -; mRNA. DR EMBL; X17682; CAA35667.1; -; mRNA. DR EMBL; X71487; CAA50588.1; -; mRNA. DR PIR; A37981; A37981. DR PIR; I55502; S33176. DR RefSeq; XP_008765430.1; XM_008767208.2. [P15146-3] DR AlphaFoldDB; P15146; -. DR SASBDB; P15146; -. DR BioGRID; 247625; 7. DR IntAct; P15146; 6. DR MINT; P15146; -. DR STRING; 10116.ENSRNOP00000042029; -. DR GlyGen; P15146; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P15146; -. DR PhosphoSitePlus; P15146; -. DR SwissPalm; P15146; -. DR PaxDb; 10116-ENSRNOP00000050877; -. DR GeneID; 25595; -. DR UCSC; RGD:3044; rat. [P15146-1] DR AGR; RGD:3044; -. DR CTD; 4133; -. DR RGD; 3044; Map2. DR eggNOG; KOG2418; Eukaryota. DR InParanoid; P15146; -. DR OrthoDB; 5406159at2759; -. DR PhylomeDB; P15146; -. DR PRO; PR:P15146; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0015629; C:actin cytoskeleton; IMP:CAFA. DR GO; GO:0097440; C:apical dendrite; ISO:RGD. DR GO; GO:0150014; C:apical distal dendrite; IDA:ARUK-UCL. DR GO; GO:0043203; C:axon hillock; IDA:ARUK-UCL. DR GO; GO:0043194; C:axon initial segment; IDA:ARUK-UCL. DR GO; GO:0097441; C:basal dendrite; IDA:ARUK-UCL. DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; ISO:RGD. DR GO; GO:0044297; C:cell body; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; IDA:ARUK-UCL. DR GO; GO:0044307; C:dendritic branch; IDA:ARUK-UCL. DR GO; GO:1902737; C:dendritic filopodium; IDA:ARUK-UCL. DR GO; GO:0044294; C:dendritic growth cone; IDA:ARUK-UCL. DR GO; GO:0043198; C:dendritic shaft; IDA:ARUK-UCL. DR GO; GO:0150002; C:distal dendrite; IDA:ARUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IMP:CAFA. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL. DR GO; GO:0034399; C:nuclear periphery; ISO:RGD. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; ISO:RGD. DR GO; GO:0150001; C:primary dendrite; IDA:ARUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:1990635; C:proximal dendrite; IDA:ARUK-UCL. DR GO; GO:1990769; C:proximal neuron projection; IDA:ARUK-UCL. DR GO; GO:0032587; C:ruffle membrane; IMP:CAFA. DR GO; GO:0003779; F:actin binding; IMP:CAFA. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD. DR GO; GO:0008017; F:microtubule binding; IMP:CAFA. DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL. DR GO; GO:0007409; P:axonogenesis; ISO:RGD. DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD. DR GO; GO:0021954; P:central nervous system neuron development; ISO:RGD. DR GO; GO:0016358; P:dendrite development; ISO:RGD. DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD. DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD. DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD. DR GO; GO:0030517; P:negative regulation of axon extension; IMP:ARUK-UCL. DR GO; GO:1904527; P:negative regulation of microtubule binding; IDA:ARUK-UCL. DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:CAFA. DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:ARUK-UCL. DR GO; GO:0031175; P:neuron projection development; ISO:RGD. DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IMP:ARUK-UCL. DR GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; IMP:ARUK-UCL. DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IMP:ARUK-UCL. DR GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL. DR GO; GO:0032355; P:response to estradiol; IEP:RGD. DR GO; GO:0032570; P:response to progesterone; IEP:RGD. DR DisProt; DP00122; -. DR InterPro; IPR027324; MAP2/MAP4/Tau. DR InterPro; IPR013588; MAP2_projctn. DR InterPro; IPR001084; MAP_tubulin-bd_rpt. DR PANTHER; PTHR11501; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR11501:SF15; MICROTUBULE-ASSOCIATED PROTEIN 2; 1. DR Pfam; PF08377; MAP2_projctn; 1. DR Pfam; PF00418; Tubulin-binding; 4. DR PROSITE; PS00229; TAU_MAP_1; 3. DR PROSITE; PS51491; TAU_MAP_2; 4. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Cell projection; Cytoplasm; KW Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..1861 FT /note="Microtubule-associated protein 2" FT /id="PRO_0000072749" FT REPEAT 1664..1694 FT /note="Tau/MAP 1" FT REPEAT 1695..1725 FT /note="Tau/MAP 2" FT REPEAT 1726..1756 FT /note="Tau/MAP 3" FT REPEAT 1757..1788 FT /note="Tau/MAP 4" FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 109..231 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 575..688 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 704..747 FT /note="Interaction with KNDC1" FT /evidence="ECO:0000250|UniProtKB:P20357" FT REGION 766..797 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 826..866 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 884..903 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 929..987 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1006..1026 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1087..1170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1207..1247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1343..1384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1406..1643 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1454..1474 FT /note="Calmodulin-binding" FT /evidence="ECO:0000255" FT REGION 1816..1835 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 63..80 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..382 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..439 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 440..466 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 579..610 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 631..652 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..684 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 777..792 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 884..898 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 949..987 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1107..1165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1355..1384 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1406..1486 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1507..1524 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1566..1582 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1589..1624 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 136 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 478 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 498 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 552 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 598 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:0007744|PubMed:22673903" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 728 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 732 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 736 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 739 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 741 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 748 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 884 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 939 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1051 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1146 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1161 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1166 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1359 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1562 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1594 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1608 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1611 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1622 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1625 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1652 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1656 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1682 FT /note="Phosphoserine; by MARK1" FT /evidence="ECO:0000269|PubMed:9108484" FT MOD_RES 1816 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1821 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20357" FT MOD_RES 1824 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1829 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1842 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT VAR_SEQ 152..1514 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:2326166" FT /id="VSP_003198" FT VAR_SEQ 1695..1725 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:2174050, FT ECO:0000303|PubMed:2326166, ECO:0000303|PubMed:2339070" FT /id="VSP_003199" FT MOD_RES P15146-3:319 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11029056" FT MOD_RES P15146-3:350 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11029056" FT MOD_RES P15146-3:382 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11029056" SQ SEQUENCE 1861 AA; 202411 MW; 42DCF116D21EF54E CRC64; MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGSGEG LSRSANGFPY REEEEGAFGE HGSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQP AALPLAAEET VNLPPSPPPS PASEQTAALE EDLLTASKME FPEQQKLPSS FAEPLDKEET EFKMQSKPGE DFEHAALVPQ PDTSKTPQDK KDPQDMEGEK SPASPFAQTF GTNLEDIKQI TEPSITVPSI GLSAEPLAPK DQKDWFIEMP VESKKDEWGL AAPISPGPLT PMREKDVLED IPRWEGKQFD SPMPSPFHGG SFTLPLDTVK DERVTEGSQP FAPVFFQSDD KMSLQDTSGS ATSKESSKDE EPQKDKADKV ADVPVSEATT VLGDVHSPAV EGFVGENISG EEKGTTDQEK KETSTPSVQE PTLTETEPQT KLEETSKVSI EETVAKEEES LKLKDDKAGV IQTSTEQSFS KEDQKGQEQT IEALKQDSFP ISLEQAVTDA AMATKTLEKV TSEPEAVSEK REIQGLFEED IADKSKLEGA GSATVAEVEM PFYEDKSGMS KYFETSALKE DVTRSTGLGS DYYELSDSRG NAQESLDTVS PKNQQDEKEL LAKASQPSPP AHEAGYSTLA QSYTSDHPSE LPEEPSSPQE RMFTIDPKVY GEKRDLHSKN KDDLTLSRSL GLGGRSAIEQ RSMSINLPMS CLDSIALGFN FGRGHDLSPL ASDILTNTSG SMDEGDDYLP PTTPAVEKIP CFPIESKEEE DKTEQAKVTG GQTTQVETSS ESPFPAKEYY KNGTVMAPDL PEMLDLAGTR SRLASVSADA EVARRKSVPS EAVVAESSTG LPPVADDSQP VKPDSQLEDM GYCVFNKYTV PLPSPVQDSE NLSGESGSFY EGTDDKVRRD LATDLSLIEV KLAAAGRVKD EFTAEKEASP PSSADKSGLS REFDQDRKAN DKLDTVLEKS EEHVDSKEHA KESEEVGDKV ELFGLGVTYE QTSAKELITT KETAPERAEK GLSSVPEVAE VETTTKADQG LDVAAKKDDQ SPLDIKVSDF GQMASGMSVD AGKTIELKFE VDQQLTLSSE APQETDSFMG IESSHVKDGA KVSETEVKEK VAKPDLVHQE AVDKEESYES SGEHESLTME SLKPDEGKKE TSPETSLIQD EVALKLSVEI PCPPPVSEAD SSIDEKAEVQ MEFIQLPKEE STETPDIPAI PSDVTQPQPE AVVSEPAEVR GEEEEIEAEG EYDKLLFRSD TLQITDLLVP GSREEFVETC PGEHKGVVES VVTIEDDFIT VVQTTTDEGE LGSHSVRFAA PVQPEEERRP YPHDEELEVL MAAEAQAEPK DGSPDAPATP EKEEVPFSEY KTETYDDYKD ETTIDDSIMD ADSLWVDTQD DDRSILTEQL ETIPKEERAE KEARRPSLEK HRKEKPFKTG RGRISTPERR EVAKKEPSTV SRDEVRRKKA VYKKAELAKE SEVQAHSPSR KLILKPAIKY TRPTHLSCVK RKTTATSGES AQAPSAFKQA KDKVTDGITK SPEKRSSLPR PSSILPPRRG VSGDREENSF SLNSSISSAR RTTRSEPIRR AGKSGTSTPT TPGSTAITPG TPPSYSSRTP GTPGTPSYPR TPGTPKSGIL VPSEKKVAII RTPPKSPATP KQLRLINQPL PDLKNVKSKI GSTDNIKYQP KGGQVRILNK KMDFSKVQSR CGSKDNIKHS AGGGNVQIVT KKIDLSHVTS KCGSLKNIRH RPGGGRVKIE SVKLDFKEKA QAKVGSLDNA HHVPGGGNVK IDSQKLNFRE HAKARVDHGA EIITQSPSRS SVASPRRLSN VSSSGSINLL ESPQLATLAE DVTAALAKQG L //