P08553 (NFM_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 134.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Neurofilament medium polypeptide Short name=NF-M Alternative name(s): 160 kDa neurofilament protein Neurofilament 3 Neurofilament triplet M protein | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 848 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber. |
| Post-translational modification | There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber. Phosphorylation seems to play a major role in the functioning of the larger neurofilament polypeptides (NF-M and NF-H), the levels of phosphorylation being altered developmentally and coincidentally with a change in the neurofilament function. Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization By similarity. |
| Sequence similarities | Belongs to the intermediate filament family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 848 | 847 | Neurofilament medium polypeptide | PRO_0000063795 | |||||
Regions | |||||||||
| Region | 2 – 102 | 101 | Head | ||||||
| Region | 103 – 410 | 308 | Rod | ||||||
| Region | 103 – 134 | 32 | Coil 1A | ||||||
| Region | 135 – 147 | 13 | Linker 1 | ||||||
| Region | 148 – 246 | 99 | Coil 1B | ||||||
| Region | 247 – 263 | 17 | Linker 12 | ||||||
| Region | 264 – 285 | 22 | Coil 2A | ||||||
| Region | 286 – 289 | 4 | Linker 2 | ||||||
| Region | 290 – 410 | 121 | Coil 2B | ||||||
| Region | 411 – 848 | 438 | Tail | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 318 | 1 | Phosphotyrosine Ref.10 | ||||||
| Modified residue | 502 | 1 | Phosphoserine Ref.7 Ref.12 | ||||||
| Modified residue | 506 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 537 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 545 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 551 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 605 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 610 | 1 | Phosphoserine Ref.8 Ref.12 | ||||||
| Modified residue | 642 | 1 | Phosphothreonine Ref.8 | ||||||
| Modified residue | 645 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 669 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 689 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 715 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 769 | 1 | Phosphoserine Ref.11 | ||||||
| Glycosylation | 47 | 1 | O-linked (GlcNAc) Probable | ||||||
| Glycosylation | 430 | 1 | O-linked (GlcNAc) Probable | ||||||
Experimental info | |||||||||
| Sequence conflict | 17 | 1 | V → VP in CAA29127. Ref.1 | ||||||
| Sequence conflict | 53 | 1 | K → T in CAA29127. Ref.1 | ||||||
| Sequence conflict | 57 | 1 | L → V in CAA29127. Ref.1 | ||||||
| Sequence conflict | 234 | 1 | S → R in CAA29127. Ref.1 | ||||||
| Sequence conflict | 432 | 1 | S → F in AAA39815. Ref.6 | ||||||
| Sequence conflict | 539 – 540 | 2 | QA → RR in AAA39815. Ref.6 | ||||||
| Sequence conflict | 628 | 1 | Q → H in ABA46749. Ref.2 | ||||||
| Sequence conflict | 628 | 1 | Q → H in BAC34724. Ref.3 | ||||||
| Sequence conflict | 628 | 1 | Q → H in BAE37734. Ref.3 | ||||||
| Sequence conflict | 696 | 1 | E → K in BAC34724. Ref.3 | ||||||
| Sequence conflict | 699 | 1 | P → L in ABA46749. Ref.2 | ||||||
| Sequence conflict | 699 | 1 | P → L in BAC34724. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structure and evolutionary origin of the gene encoding mouse NF-M, the middle-molecular-mass neurofilament protein." Levy E., Liem R.K.H., D'Eustachio P., Cowan N.J. Eur. J. Biochem. 166:71-77(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Jensen K.H., Brown A. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Eye and Spinal ganglion. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-848. |
| [5] | Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 167-182; 222-233 AND 410-425, MASS SPECTROMETRY. Tissue: Hippocampus. |
| [6] | "Cloning and developmental expression of the murine neurofilament gene family." Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F. Brain Res. 387:243-250(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 322-540. |
| [7] | "Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-506, MASS SPECTROMETRY. Tissue: Forebrain. |
| [8] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605; SER-610; THR-642; SER-669 AND SER-715, MASS SPECTROMETRY. Tissue: Brain. |
| [9] | "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry." Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-430, MASS SPECTROMETRY. Tissue: Brain. |
| [10] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, MASS SPECTROMETRY. Tissue: Brain. |
| [11] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [12] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502; SER-610 AND SER-645, MASS SPECTROMETRY. Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X05640 Genomic DNA. Translation: CAA29127.1. DQ201636 mRNA. Translation: ABA46749.1. AK051696 mRNA. Translation: BAC34724.1. AK164318 mRNA. Translation: BAE37734.1. AK165041 mRNA. Translation: BAE38014.1. BC119602 mRNA. Translation: AAI19603.1. BC128564 mRNA. Translation: AAI28565.1. M20481 mRNA. Translation: AAA39815.1. |
| IPI | IPI00323800. |
| PIR | B43772. S00030. |
| RefSeq | NP_032717.2. NM_008691.2. |
| UniGene | Mm.390700. |
3D structure databases | |
| ProteinModelPortal | P08553. |
| SMR | P08553. Positions 98-247, 263-332, 337-405. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P08553. 6 interactions. |
PTM databases | |
| PhosphoSite | P08553. |
2D gel databases | |
| UCD-2DPAGE | P08553. |
Proteomic databases | |
| PaxDb | P08553. |
| PRIDE | P08553. |
Protocols and materials databases | |
| DNASU | 18040. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000022638; ENSMUSP00000022638; ENSMUSG00000022054. |
| GeneID | 18040. |
| KEGG | mmu:18040. |
| UCSC | uc007ulo.1. mouse. |
Organism-specific databases | |
| CTD | 4741. |
| MGI | MGI:97314. Nefm. |
Phylogenomic databases | |
| eggNOG | NOG151229. |
| GeneTree | ENSGT00560000076873. |
| HOVERGEN | HBG013015. |
| InParanoid | P08553. |
| KO | K04573. |
| OrthoDB | EOG4VMFFD. |
Gene expression databases | |
| ArrayExpress | P08553. |
| Bgee | P08553. |
| CleanEx | MM_NEFM. |
| Genevestigator | P08553. |
| GermOnline | ENSMUSG00000022054. Mus musculus. |
Family and domain databases | |
| InterPro | IPR016044. F. IPR001664. IF. IPR006821. Intermed_filament_DNA-bd. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [Graphical view] |
| PANTHER | PTHR23239. PTHR23239. 1 hit. |
| Pfam | PF00038. Filament. 1 hit. PF04732. Filament_head. 1 hit. [Graphical view] |
| PRINTS | PR01248. TYPE1KERATIN. |
| PROSITE | PS00226. IF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 293149. |
| SOURCE | Search... |
Entry information
| Entry name | NFM_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P08553 Secondary accession number(s): A2VCT5 Q8BQ20 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
