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NFM_MOUSE
ID   NFM_MOUSE               Reviewed;         848 AA.
AC   P08553; A2VCT5; Q0VDM8; Q3HRJ6; Q3TNS4; Q3TPK2; Q61961; Q8BQ20;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   03-AUG-2022, entry version 201.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036526; DOI=10.1111/j.1432-1033.1987.tb13485.x;
RA   Levy E., Liem R.K.H., D'Eustachio P., Cowan N.J.;
RT   "Structure and evolutionary origin of the gene encoding mouse NF-M, the
RT   middle-molecular-mass neurofilament protein.";
RL   Eur. J. Biochem. 166:71-77(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RA   Jensen K.H., Brown A.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-848.
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   [5]
RP   PROTEIN SEQUENCE OF 167-182; 222-233 AND 410-425, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 322-540.
RX   PubMed=3103856; DOI=10.1016/0169-328x(86)90030-6;
RA   Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.;
RT   "Cloning and developmental expression of the murine neurofilament gene
RT   family.";
RL   Brain Res. 387:243-250(1986).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; THR-642; SER-669 AND
RP   SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-430.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA   Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA   Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-224; SER-550;
RP   SER-551; THR-565; SER-605; SER-610; SER-715; SER-723 AND SER-769, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=22723690; DOI=10.1523/jneurosci.1081-12.2012;
RA   Yuan A., Sasaki T., Kumar A., Peterhoff C.M., Rao M.V., Liem R.K.,
RA   Julien J.P., Nixon R.A.;
RT   "Peripherin is a subunit of peripheral nerve neurofilaments: implications
RT   for differential vulnerability of CNS and peripheral nervous system
RT   axons.";
RL   J. Neurosci. 32:8501-8508(2012).
RN   [14]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-42, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
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 (PubMed:22723690). {ECO:0000269|PubMed:22723690}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:22723690}. Cell projection, axon
CC       {ECO:0000269|PubMed:22723690}.
CC   -!- TISSUE SPECIFICITY: Expressed in the sciatic nerve (at protein level).
CC       {ECO:0000269|PubMed:22723690}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; X05640; CAA29127.1; -; Genomic_DNA.
DR   EMBL; DQ201636; ABA46749.1; -; mRNA.
DR   EMBL; AK051696; BAC34724.1; -; mRNA.
DR   EMBL; AK164318; BAE37734.1; -; mRNA.
DR   EMBL; AK165041; BAE38014.1; -; mRNA.
DR   EMBL; BC119602; AAI19603.1; -; mRNA.
DR   EMBL; BC128564; AAI28565.1; -; mRNA.
DR   EMBL; M20481; AAA39815.1; -; mRNA.
DR   CCDS; CCDS27233.1; -.
DR   PIR; B43772; B43772.
DR   PIR; S00030; S00030.
DR   RefSeq; NP_032717.2; NM_008691.2.
DR   AlphaFoldDB; P08553; -.
DR   SMR; P08553; -.
DR   BioGRID; 201758; 22.
DR   IntAct; P08553; 13.
DR   MINT; P08553; -.
DR   STRING; 10090.ENSMUSP00000022638; -.
DR   GlyGen; P08553; 2 sites.
DR   iPTMnet; P08553; -.
DR   PhosphoSitePlus; P08553; -.
DR   SwissPalm; P08553; -.
DR   UCD-2DPAGE; P08553; -.
DR   EPD; P08553; -.
DR   jPOST; P08553; -.
DR   MaxQB; P08553; -.
DR   PaxDb; P08553; -.
DR   PeptideAtlas; P08553; -.
DR   PRIDE; P08553; -.
DR   ProteomicsDB; 252818; -.
DR   DNASU; 18040; -.
DR   GeneID; 18040; -.
DR   KEGG; mmu:18040; -.
DR   UCSC; uc007ulo.1; mouse.
DR   CTD; 4741; -.
DR   MGI; MGI:97314; Nefm.
DR   eggNOG; KOG1216; Eukaryota.
DR   InParanoid; P08553; -.
DR   OrthoDB; 898483at2759; -.
DR   PhylomeDB; P08553; -.
DR   TreeFam; TF330122; -.
DR   BioGRID-ORCS; 18040; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Nefm; mouse.
DR   PRO; PR:P08553; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P08553; protein.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR   GO; GO:0005882; C:intermediate filament; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0097418; C:neurofibrillary tangle; ISO:MGI.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IDA:SynGO.
DR   GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; IDA:SynGO.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR   GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; IGI:MGI.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0045105; P:intermediate filament polymerization or depolymerization; ISO:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR   GO; GO:0033693; P:neurofilament bundle assembly; ISO:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
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; 2.
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; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Glycoprotein; Intermediate filament;
KW   Methylation; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   CHAIN           2..848
FT                   /note="Neurofilament medium polypeptide"
FT                   /id="PRO_0000063795"
FT   DOMAIN          99..410
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..102
FT                   /note="Head"
FT   REGION          103..134
FT                   /note="Coil 1A"
FT   REGION          135..147
FT                   /note="Linker 1"
FT   REGION          148..246
FT                   /note="Coil 1B"
FT   REGION          247..263
FT                   /note="Linker 12"
FT   REGION          264..285
FT                   /note="Coil 2A"
FT   REGION          286..289
FT                   /note="Linker 2"
FT   REGION          290..410
FT                   /note="Coil 2B"
FT   REGION          411..848
FT                   /note="Tail"
FT   REGION          482..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..537
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..573
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..762
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..785
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:0007744|PubMed:24129315"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         318
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         482
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         537
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         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         565
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         610
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         642
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O77788"
FT   MOD_RES         715
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         753
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12839"
FT   MOD_RES         769
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   CARBOHYD        47
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000305|PubMed:16452088"
FT   CARBOHYD        430
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000305|PubMed:16452088"
FT   CONFLICT        17
FT                   /note="V -> VP (in Ref. 1; CAA29127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="K -> T (in Ref. 1; CAA29127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="L -> V (in Ref. 1; CAA29127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="S -> R (in Ref. 1; CAA29127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="S -> F (in Ref. 6; AAA39815)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539..540
FT                   /note="QA -> RR (in Ref. 6; AAA39815)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        628
FT                   /note="Q -> H (in Ref. 2; ABA46749 and 3; BAC34724/
FT                   BAE37734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="E -> K (in Ref. 3; BAC34724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        699
FT                   /note="P -> L (in Ref. 2; ABA46749 and 3; BAC34724)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   848 AA;  95916 MW;  0783F50558A7D4C3 CRC64;
     MSYTLDSLGN PSAYRRVTET RSSFSRVSGS PSSGFRSQSW SRGSPSTVSS SYKRSALAPR
     LAYSSAMLSS AESSLDFSQS SSLLNGGSGG DYKLSRSNEK EQLQGLNDRF AGYIEKVHYL
     EQQNKEIEAE IQALRQKQAS HAQLGDAYDQ EIRELRATLE MVNHEKAQVQ LDSDHLEEDI
     HRLKERFEEE ARLRDDTEAA IRALRKDIEE SSMVKVELDK KVQSLQDEVA FLRSNHEEEV
     ADLLAQIQAS HITVERKDYL KTDISTALKE IRSQLECHSD QNMHQAEEWF KCRYAKLTEA
     AEQNKEAIRS AKEEIAEYRR QLQSKSIELE SVRGTKESLE RQLSDIEERH NHDLSSYQDT
     IQQLENELRG TKWEMARHLR EYQDLLNVKM ALDIEIAAYR KLLEGEETRF STFSGSITGP
     LYTHRQPSVT ISSKIQKTKV EAPKLKVQHK FVEEIIEETK VEDEKSEMEE TLTAIAEELA
     ASAKEEKEEA EEKEEEPEAE KSPVKSPEAK EEEEEGEKEE EEEGQEEEEE EDEGVKSDQA
     EEGGSEKEGS SEKDEGEQEE EEGETEAEGE GEEAEAKEEK KIEGKVEEVA VKEEIKVEKP
     EKAKSPMPKS PVEEVKPKPE AKAGKGEQKE EEKVEEEKKE VTKESPKEEK VEKKEEKPKD
     VADKKKAESP VKEKAVEEVI TISKSVKVSL EKDTKEEKPQ PQEKVKEKAE EEGGSEEEGS
     DRSPQESKKE DIAINGEVEG KEEEEQETQE KGSGREEEKG VVTNGLDVSP AEEKKGEDSS
     DDKVVVTKKV EKITSEGGDG ATKYITKSVT VTQKVEEHEE TFEEKLVSTK KVEKVTSHAI
     VKEVTQGD
 
 
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