NFM_HUMAN
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 03-AUG-2022, entry version 212.
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 -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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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; 112.
DR IntAct; P07197; 48.
DR MINT; P07197; -.
DR STRING; 9606.ENSP00000221166; -.
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 UCD-2DPAGE; P07197; -.
DR EPD; P07197; -.
DR jPOST; P07197; -.
DR MassIVE; P07197; -.
DR MaxQB; P07197; -.
DR PaxDb; P07197; -.
DR PeptideAtlas; P07197; -.
DR PRIDE; P07197; -.
DR ProteomicsDB; 19213; -.
DR ProteomicsDB; 51962; -. [P07197-1]
DR Antibodypedia; 4396; 713 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 CTD; 4741; -.
DR DisGeNET; 4741; -.
DR GeneCards; NEFM; -.
DR HGNC; HGNC:7734; NEFM.
DR HPA; ENSG00000104722; Tissue enriched (brain).
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; GPIFTHR; -.
DR OrthoDB; 898483at2759; -.
DR PhylomeDB; P07197; -.
DR TreeFam; TF330122; -.
DR PathwayCommons; P07197; -.
DR SignaLink; P07197; -.
DR SIGNOR; P07197; -.
DR BioGRID-ORCS; 4741; 32 hits in 1066 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 147 other tissues.
DR ExpressionAtlas; P07197; baseline and differential.
DR Genevisible; P07197; HS.
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:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0033693; P:neurofilament bundle assembly; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027697; NF-M.
DR PANTHER; PTHR45652:SF3; PTHR45652:SF3; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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
