P19246 · NFH_MOUSE

  • Protein
    Neurofilament heavy polypeptide
  • Gene
    Nefh
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NF proteins. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical dendrite
Cellular Componentaxon
Cellular Componentbasal proximal dendrite
Cellular Componentcytoplasm
Cellular Componentintermediate filament
Cellular Componentmitochondrion
Cellular Componentmyelin sheath
Cellular Componentneurofibrillary tangle
Cellular Componentneurofilament
Cellular Componentneuronal cell body
Cellular Componentperikaryon
Cellular Componentpostsynaptic density
Cellular Componentpostsynaptic intermediate filament cytoskeleton
Cellular ComponentSchaffer collateral - CA1 synapse
Molecular Functionprotein kinase binding
Molecular Functionprotein-containing complex binding
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functionstructural constituent of cytoskeleton
Molecular Functionstructural constituent of postsynaptic intermediate filament cytoskeleton
Molecular Functiontoxic substance binding
Biological Processaxon development
Biological Processaxon regeneration
Biological Processcellular response to leukemia inhibitory factor
Biological Processintermediate filament bundle assembly
Biological Processintermediate filament cytoskeleton organization
Biological Processmicrotubule cytoskeleton organization
Biological Processneurofilament bundle assembly
Biological Processneurofilament cytoskeleton organization
Biological Processovarian follicle atresia
Biological Processperipheral nervous system neuron axonogenesis
Biological Processpostsynaptic modulation of chemical synaptic transmission
Biological Processregulation of organelle transport along microtubule
Biological Processresponse to sodium arsenite

Names & Taxonomy

Protein names

  • Recommended name
    Neurofilament heavy polypeptide
  • Short names
    NF-H
  • Alternative names
    • 200 kDa neurofilament protein
    • Neurofilament triplet H protein

Gene names

    • Name
      Nefh
    • Synonyms
      Kiaa0845, Nfh

Organism names

  • Taxonomic identifier
  • Strains
    • Swiss Webster
    • C57BL/6J
    • OF1
    • VM
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P19246
  • Secondary accessions
    • A1E2H9
    • Q5SVF6
    • Q61959

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000638011-1090Neurofilament heavy polypeptide
Modified residue74Phosphoserine
Modified residue122Phosphoserine
Modified residue345Phosphoserine
Modified residue416Phosphoserine
Modified residue419Phosphoserine
Modified residue508Phosphoserine
Modified residue523Phosphoserine
Modified residue529Phosphoserine
Modified residue535Phosphoserine
Modified residue541Phosphoserine
Modified residue547Phosphoserine
Modified residue553Phosphoserine
Modified residue559Phosphoserine
Modified residue565Phosphoserine
Modified residue571Phosphoserine
Modified residue577Phosphoserine
Modified residue583Phosphoserine
Modified residue589Phosphoserine
Modified residue595Phosphoserine
Modified residue601Phosphoserine
Modified residue607Phosphoserine
Modified residue613Phosphoserine
Modified residue619Phosphoserine
Modified residue625Phosphoserine
Modified residue631Phosphoserine
Modified residue637Phosphoserine
Modified residue643Phosphoserine
Modified residue649Phosphoserine
Modified residue655Phosphoserine
Modified residue661Phosphoserine
Modified residue667Phosphoserine
Modified residue673Phosphoserine
Modified residue679Phosphoserine
Modified residue685Phosphoserine
Modified residue691Phosphoserine
Modified residue697Phosphoserine
Modified residue703Phosphoserine
Modified residue709Phosphoserine
Modified residue715Phosphoserine
Modified residue721Phosphoserine
Modified residue727Phosphoserine
Modified residue733Phosphoserine
Modified residue739Phosphoserine
Modified residue745Phosphoserine
Modified residue751Phosphoserine
Modified residue757Phosphoserine
Modified residue763Phosphoserine
Modified residue769Phosphoserine
Modified residue783Phosphoserine
Modified residue789Phosphoserine
Modified residue795Phosphoserine
Modified residue809Phosphoserine
Modified residue815Phosphoserine
Modified residue834Phosphoserine
Modified residue839Phosphothreonine
Modified residue859Phosphoserine
Modified residue867Phosphoserine
Modified residue888Phosphoserine
Modified residue947Phosphoserine

Post-translational modification

There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH 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.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the sciatic nerve (at protein level).

Gene expression databases

Interaction

Subunit

Forms heterodimers with NEFL; which can further hetero-oligomerize (in vitro) (By similarity).
Forms heterodimers with INA (in vitro) (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias, repeat.

TypeIDPosition(s)Description
Region2-98Head
Domain95-411IF rod
Region99-130Coil 1A
Region131-143Linker 1
Region144-242Coil 1B
Region243-264Linker 12
Region265-286Coil 2A
Region287-290Linker 2
Region291-411Coil 2B
Region412-1090Tail
Compositional bias456-474Basic and acidic residues
Region456-1090Disordered
Compositional bias475-493Acidic residues
Compositional bias507-527Basic and acidic residues
Repeat522-5271
Region522-89252 X 6 AA approximate tandem repeats of K-S-P-[AGISV]-[EATK]-[APVQ]
Repeat528-5332
Repeat534-5393
Repeat540-5454
Repeat546-5515
Repeat552-5576
Repeat558-5637
Repeat564-5698
Repeat570-5759
Repeat576-58110
Repeat582-58711
Repeat588-59312
Repeat594-59913
Repeat600-60514
Repeat606-61115
Repeat612-61716
Repeat618-62317
Repeat624-62918
Repeat630-63519
Repeat636-64120
Repeat642-64721
Repeat648-65322
Repeat654-65923
Repeat660-66524
Repeat666-67125
Repeat672-67726
Repeat678-68327
Repeat684-68928
Repeat690-69529
Repeat696-70130
Repeat702-70731
Repeat708-71332
Repeat714-71933
Repeat720-72534
Repeat726-73135
Repeat732-73736
Repeat738-74337
Repeat744-74938
Repeat750-75539
Repeat756-76140
Repeat762-76741
Compositional bias765-832Basic and acidic residues
Repeat768-77342
Repeat774-77943; approximate
Repeat782-78744
Repeat788-79345
Repeat794-79946
Repeat808-81347
Repeat814-81948
Repeat833-83849
Compositional bias843-1090Basic and acidic residues
Repeat858-86350
Repeat866-87151
Repeat887-89252

Sequence similarities

Belongs to the intermediate filament family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,090
  • Mass (Da)
    116,994
  • Last updated
    2006-05-02 v3
  • Checksum
    B2A7D7D36FF2F448
MMSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQQAGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEEGAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK

Sequence caution

The sequence AAA39813.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence CAA83229.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict134-135in Ref. 2; AAA39813
Sequence conflict202in Ref. 2; AAA39813
Sequence conflict284in Ref. 2; AAA39813
Compositional bias456-474Basic and acidic residues
Compositional bias475-493Acidic residues
Sequence conflict495in Ref. 2; AAA39813
Compositional bias507-527Basic and acidic residues
Sequence conflict519in Ref. 1; AAA39809 and 3; CAA83229
Sequence conflict549in Ref. 1; AAA39809 and 3; CAA83229
Sequence conflict694-717in Ref. 1; AAA39809 and 3; CAA83229
Compositional bias765-832Basic and acidic residues
Sequence conflict817in Ref. 1; AAA39809, 3; CAA83229 and 6; ABK96805
Compositional bias843-1090Basic and acidic residues
Sequence conflict846-847in Ref. 1; AAA39809, 3; CAA83229 and 6; ABK96805
Sequence conflict846-847in Ref. 2; AAA39813

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M35131
EMBL· GenBank· DDBJ
AAA39809.1
EMBL· GenBank· DDBJ
mRNA
M24496
EMBL· GenBank· DDBJ
AAA39813.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
M23349
EMBL· GenBank· DDBJ
AAA39813.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
M24494
EMBL· GenBank· DDBJ
AAA39813.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
M24495
EMBL· GenBank· DDBJ
AAA39813.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
Z31012
EMBL· GenBank· DDBJ
CAA83229.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
AL645522
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
EF101556
EMBL· GenBank· DDBJ
ABK96805.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp