ID   NFM_HUMAN               Reviewed;         916 AA.
AC   P07197; B4DGN2; E9PBF7; Q4QRK6;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 3.
DT   27-MAR-2024, entry version 221.
DE   RecName: Full=Neurofilament medium polypeptide;
DE            Short=NF-M;
DE   AltName: Full=160 kDa neurofilament protein;
DE   AltName: Full=Neurofilament 3;
DE   AltName: Full=Neurofilament triplet M protein;
GN   Name=NEFM; Synonyms=NEF3, NFM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-439.
RX   PubMed=3608989; DOI=10.1002/j.1460-2075.1987.tb02409.x;
RA   Myers M.W., Lazzarini R.A., Lee V.M.-Y., Schlaepfer W.W., Nelson D.L.;
RT   "The human mid-size neurofilament subunit: a repeated protein sequence and
RT   the relationship of its gene to the intermediate filament gene family.";
RL   EMBO J. 6:1617-1626(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-439.
RC   TISSUE=Retina;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-439.
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-439.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-439.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2450354; DOI=10.1073/pnas.85.6.1998;
RA   Lee V.M.-Y., Otvos L. Jr., Carden M.J., Hollosi M., Dietzschold B.,
RA   Lazzarini R.A.;
RT   "Identification of the major multiphosphorylation site in mammalian
RT   neurofilaments.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1998-2002(1988).
RN   [8]
RP   PROTEIN SEQUENCE OF 128-137; 140-155; 169-184 AND 592-606, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   PHOSPHORYLATION BY PKN1.
RX   PubMed=8621664; DOI=10.1074/jbc.271.16.9816;
RA   Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M.,
RA   Sunakawa H., Ono Y.;
RT   "PKN associates and phosphorylates the head-rod domain of neurofilament
RT   protein.";
RL   J. Biol. Chem. 271:9816-9822(1996).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-439, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Neurofilaments usually contain three intermediate filament
CC       proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC       neuronal caliber. May additionally cooperate with the neuronal
CC       intermediate filament proteins PRPH and INA to form neuronal
CC       filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}.
CC   -!- SUBUNIT: Forms heterodimers with NEFL; which can further hetero-
CC       oligomerize (in vitro) (By similarity). Forms heterodimers with INA (in
CC       vitro) (By similarity). {ECO:0000250|UniProtKB:P12839}.
CC   -!- INTERACTION:
CC       P07197; P05412: JUN; NbExp=2; IntAct=EBI-1105035, EBI-852823;
CC       P07197; P07196: NEFL; NbExp=4; IntAct=EBI-1105035, EBI-475646;
CC       P07197; P06400: RB1; NbExp=2; IntAct=EBI-1105035, EBI-491274;
CC       P07197; Q15796: SMAD2; NbExp=3; IntAct=EBI-1105035, EBI-1040141;
CC       P07197; P08670: VIM; NbExp=5; IntAct=EBI-1105035, EBI-353844;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P08553}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P08553}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P07197-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P07197-2; Sequence=VSP_046306;
CC   -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFM is
CC       phosphorylated on a number of the serines in this motif. It is thought
CC       that phosphorylation of NFM results in the formation of interfilament
CC       cross bridges that are important in the maintenance of axonal caliber.
CC   -!- PTM: Phosphorylation seems to play a major role in the functioning of
CC       the larger neurofilament polypeptides (NF-M and NF-H), the levels of
CC       phosphorylation being altered developmentally and coincidentally with a
CC       change in the neurofilament function.
CC   -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC       leading to the inhibition of polymerization.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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; Y00067; CAA68276.1; -; Genomic_DNA.
DR   EMBL; EF560736; ABQ59046.1; -; mRNA.
DR   EMBL; AK294681; BAG57843.1; -; mRNA.
DR   EMBL; AF106564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63602.1; -; Genomic_DNA.
DR   EMBL; BC096757; AAH96757.1; -; mRNA.
DR   CCDS; CCDS47831.1; -. [P07197-2]
DR   CCDS; CCDS6046.1; -. [P07197-1]
DR   PIR; A27864; A27864.
DR   RefSeq; NP_005373.2; NM_005382.2. [P07197-1]
DR   AlphaFoldDB; P07197; -.
DR   SMR; P07197; -.
DR   BioGRID; 110818; 135.
DR   IntAct; P07197; 54.
DR   MINT; P07197; -.
DR   STRING; 9606.ENSP00000221166; -.
DR   GlyCosmos; P07197; 7 sites, 1 glycan.
DR   GlyGen; P07197; 7 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P07197; -.
DR   PhosphoSitePlus; P07197; -.
DR   SwissPalm; P07197; -.
DR   BioMuta; NEFM; -.
DR   DMDM; 281185500; -.
DR   EPD; P07197; -.
DR   jPOST; P07197; -.
DR   MassIVE; P07197; -.
DR   MaxQB; P07197; -.
DR   PaxDb; 9606-ENSP00000221166; -.
DR   PeptideAtlas; P07197; -.
DR   ProteomicsDB; 19213; -.
DR   ProteomicsDB; 51962; -. [P07197-1]
DR   Pumba; P07197; -.
DR   Antibodypedia; 4396; 763 antibodies from 47 providers.
DR   DNASU; 4741; -.
DR   Ensembl; ENST00000221166.10; ENSP00000221166.5; ENSG00000104722.14. [P07197-1]
DR   Ensembl; ENST00000433454.3; ENSP00000412295.2; ENSG00000104722.14. [P07197-2]
DR   GeneID; 4741; -.
DR   KEGG; hsa:4741; -.
DR   MANE-Select; ENST00000221166.10; ENSP00000221166.5; NM_005382.2; NP_005373.2.
DR   UCSC; uc003xed.5; human. [P07197-1]
DR   AGR; HGNC:7734; -.
DR   CTD; 4741; -.
DR   DisGeNET; 4741; -.
DR   GeneCards; NEFM; -.
DR   HGNC; HGNC:7734; NEFM.
DR   HPA; ENSG00000104722; Group enriched (brain, retina).
DR   MIM; 162250; gene.
DR   neXtProt; NX_P07197; -.
DR   OpenTargets; ENSG00000104722; -.
DR   PharmGKB; PA162397442; -.
DR   VEuPathDB; HostDB:ENSG00000104722; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   GeneTree; ENSGT00940000154418; -.
DR   HOGENOM; CLU_524743_0_0_1; -.
DR   InParanoid; P07197; -.
DR   OMA; TTYQDTI; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; P07197; -.
DR   TreeFam; TF330122; -.
DR   PathwayCommons; P07197; -.
DR   SignaLink; P07197; -.
DR   SIGNOR; P07197; -.
DR   BioGRID-ORCS; 4741; 32 hits in 1148 CRISPR screens.
DR   ChiTaRS; NEFM; human.
DR   GeneWiki; NEFM; -.
DR   GenomeRNAi; 4741; -.
DR   Pharos; P07197; Tbio.
DR   PRO; PR:P07197; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P07197; Protein.
DR   Bgee; ENSG00000104722; Expressed in dorsal root ganglion and 148 other cell types or tissues.
DR   ExpressionAtlas; P07197; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0097418; C:neurofibrillary tangle; IDA:BHF-UCL.
DR   GO; GO:0005883; C:neurofilament; TAS:ProtInc.
DR   GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; TAS:BHF-UCL.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0033693; P:neurofilament bundle assembly; IBA:GO_Central.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR   PANTHER; PTHR45652:SF3; NEUROFILAMENT MEDIUM POLYPEPTIDE; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
DR   UCD-2DPAGE; P07197; -.
DR   Genevisible; P07197; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Glycoprotein;
KW   Intermediate filament; Methylation; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   CHAIN           2..916
FT                   /note="Neurofilament medium polypeptide"
FT                   /id="PRO_0000063794"
FT   DOMAIN          101..412
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REPEAT          614..626
FT                   /note="1"
FT   REPEAT          627..639
FT                   /note="2"
FT   REPEAT          640..652
FT                   /note="3"
FT   REPEAT          653..665
FT                   /note="4"
FT   REPEAT          666..678
FT                   /note="5"
FT   REPEAT          679..691
FT                   /note="6"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..104
FT                   /note="Head"
FT   REGION          105..136
FT                   /note="Coil 1A"
FT   REGION          137..149
FT                   /note="Linker 1"
FT   REGION          150..248
FT                   /note="Coil 1B"
FT   REGION          249..265
FT                   /note="Linker 12"
FT   REGION          266..287
FT                   /note="Coil 2A"
FT   REGION          288..291
FT                   /note="Linker 2"
FT   REGION          292..412
FT                   /note="Coil 2B"
FT   REGION          413..916
FT                   /note="Tail"
FT   REGION          485..851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..691
FT                   /note="6 X 13 AA approximate tandem repeats of K-S-P-V-
FT                   [PS]-K-S-P-V-E-E-[KA]-[GAK]"
FT   COMPBIAS        504..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..545
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..579
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         42
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         320
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         571
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         641
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         736
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08553"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         837
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CARBOHYD        47
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        431
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..376
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046306"
FT   VARIANT         439
FT                   /note="P -> T (in dbSNP:rs196864)"
FT                   /evidence="ECO:0000269|PubMed:11230166,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:3608989, ECO:0000269|Ref.5,
FT                   ECO:0007744|PubMed:21269460"
FT                   /id="VAR_060732"
FT   VARIANT         725
FT                   /note="P -> Q (in dbSNP:rs196863)"
FT                   /id="VAR_056024"
FT   CONFLICT        482
FT                   /note="V -> A (in Ref. 1; CAA68276)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   916 AA;  102472 MW;  187B16CA6C6BF092 CRC64;
     MSYTLDSLGN PSAYRRVTET RSSFSRVSGS PSSGFRSQSW SRGSPSTVSS SYKRSMLAPR
     LAYSSAMLSS AESSLDFSQS SSLLNGGSGP GGDYKLSRSN EKEQLQGLND RFAGYIEKVH
     YLEQQNKEIE AEIQALRQKQ ASHAQLGDAY DQEIRELRAT LEMVNHEKAQ VQLDSDHLEE
     DIHRLKERFE EEARLRDDTE AAIRALRKDI EEASLVKVEL DKKVQSLQDE VAFLRSNHEE
     EVADLLAQIQ ASHITVERKD YLKTDISTAL KEIRSQLESH SDQNMHQAEE WFKCRYAKLT
     EAAEQNKEAI RSAKEEIAEY RRQLQSKSIE LESVRGTKES LERQLSDIEE RHNHDLSSYQ
     DTIQQLENEL RGTKWEMARH LREYQDLLNV KMALDIEIAA YRKLLEGEET RFSTFAGSIT
     GPLYTHRPPI TISSKIQKPK VEAPKLKVQH KFVEEIIEET KVEDEKSEME EALTAITEEL
     AVSMKEEKKE AAEEKEEEPE AEEEEVAAKK SPVKATAPEV KEEEGEKEEE EGQEEEEEED
     EGAKSDQAEE GGSEKEGSSE KEEGEQEEGE TEAEAEGEEA EAKEEKKVEE KSEEVATKEE
     LVADAKVEKP EKAKSPVPKS PVEEKGKSPV PKSPVEEKGK SPVPKSPVEE KGKSPVPKSP
     VEEKGKSPVS KSPVEEKAKS PVPKSPVEEA KSKAEVGKGE QKEEEEKEVK EAPKEEKVEK
     KEEKPKDVPE KKKAESPVKE EAVAEVVTIT KSVKVHLEKE TKEEGKPLQQ EKEKEKAGGE
     GGSEEEGSDK GAKGSRKEDI AVNGEVEGKE EVEQETKEKG SGREEEKGVV TNGLDLSPAD
     EKKGGDKSEE KVVVTKTVEK ITSEGGDGAT KYITKSVTVT QKVEEHEETF EEKLVSTKKV
     EKVTSHAIVK EVTQSD
//