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Protein

Neurofilament light polypeptide

Gene

NEFL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.

GO - Molecular functioni

  1. identical protein binding Source: UniProtKB
  2. protein binding, bridging Source: BHF-UCL
  3. protein C-terminus binding Source: UniProtKB
  4. structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  1. anterograde axon cargo transport Source: UniProtKB
  2. axon transport of mitochondrion Source: UniProtKB
  3. intermediate filament organization Source: UniProtKB
  4. locomotion Source: Ensembl
  5. microtubule cytoskeleton organization Source: Ensembl
  6. negative regulation of neuron apoptotic process Source: Ensembl
  7. neurofilament bundle assembly Source: UniProtKB
  8. neuromuscular process controlling balance Source: Ensembl
  9. neuron projection morphogenesis Source: Ensembl
  10. peripheral nervous system axon regeneration Source: Ensembl
  11. positive regulation of axonogenesis Source: Ensembl
  12. protein polymerization Source: Ensembl
  13. regulation of axon diameter Source: Ensembl
  14. response to corticosterone Source: Ensembl
  15. response to peptide hormone Source: Ensembl
  16. response to toxic substance Source: Ensembl
  17. retrograde axon cargo transport Source: UniProtKB
  18. synaptic transmission Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament light polypeptide
Short name:
NF-L
Alternative name(s):
68 kDa neurofilament protein
Neurofilament triplet L protein
Gene namesi
Name:NEFL
Synonyms:NF68, NFL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:7739. NEFL.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cytoplasm Source: BHF-UCL
  3. cytosol Source: Reactome
  4. growth cone Source: Ensembl
  5. neurofilament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 1F (CMT1F)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. CMT1F is characterized by onset in infancy or childhood (range 1 to 13 years).

See also OMIM:607734
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81P → L in CMT1F. 1 Publication
VAR_016018
Natural varianti8 – 81P → Q in CMT1F. 1 Publication
VAR_016019
Natural varianti8 – 81P → R in CMT2E and CMT1F. 3 Publications
Corresponds to variant rs60261494 [ dbSNP | Ensembl ].
VAR_016020
Natural varianti90 – 901E → K in CMT1F. 1 Publication
Corresponds to variant rs58332872 [ dbSNP | Ensembl ].
VAR_016022
Natural varianti98 – 981N → S in CMT1F. 1 Publication
Corresponds to variant rs58982919 [ dbSNP | Ensembl ].
VAR_016023
Natural varianti396 – 3961E → K in CMT1F and CMT2E. 3 Publications
VAR_021614
Natural varianti527 – 5271Missing in CMT1F. 1 Publication
VAR_016025
Charcot-Marie-Tooth disease 2E (CMT2E)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.

See also OMIM:607684
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81P → R in CMT2E and CMT1F. 3 Publications
Corresponds to variant rs60261494 [ dbSNP | Ensembl ].
VAR_016020
Natural varianti22 – 221P → S in CMT2E. 2 Publications
Corresponds to variant rs28928910 [ dbSNP | Ensembl ].
VAR_016021
Natural varianti332 – 3321Q → P in CMT2E. 1 Publication
Corresponds to variant rs59443585 [ dbSNP | Ensembl ].
VAR_009703
Natural varianti336 – 3361L → P in CMT2E. 1 Publication
VAR_021613
Natural varianti396 – 3961E → K in CMT1F and CMT2E. 3 Publications
VAR_021614

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi607684. phenotype.
607734. phenotype.
Orphaneti99939. Autosomal dominant Charcot-Marie-Tooth disease type 2E.
101085. Charcot-Marie-Tooth disease type 1F.
228374. Severe early-onset axonal neuropathy due to NEFL deficiency.
PharmGKBiPA31542.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 543542Neurofilament light polypeptidePRO_0000063787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Glycosylationi21 – 211O-linked (GlcNAc)By similarity
Glycosylationi27 – 271O-linked (GlcNAc)By similarity
Modified residuei43 – 431PhosphotyrosineBy similarity
Modified residuei56 – 561PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei472 – 4721PhosphoserineBy similarity

Post-translational modificationi

O-glycosylated.By similarity
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.1 Publication
Ubiquitinated in the presence of TRIM2 and UBE2D1.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07196.
PaxDbiP07196.
PRIDEiP07196.

2D gel databases

UCD-2DPAGEP07196.

PTM databases

PhosphoSiteiP07196.

Expressioni

Gene expression databases

CleanExiHS_NEFL.
ExpressionAtlasiP07196. baseline and differential.
GenevestigatoriP07196.

Interactioni

Subunit structurei

Interacts with ARHGEF28. Interacts with TRIM2.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050672EBI-475646,EBI-77613
MTMR2Q136142EBI-475646,EBI-475631
taxP140794EBI-475646,EBI-9675698From a different organism.

Protein-protein interaction databases

BioGridi110822. 39 interactions.
IntActiP07196. 15 interactions.
MINTiMINT-1370620.
STRINGi9606.ENSP00000221169.

Structurei

3D structure databases

ProteinModelPortaliP07196.
SMRiP07196. Positions 133-238, 252-321, 326-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9291HeadAdd
BLAST
Regioni93 – 396304RodAdd
BLAST
Regioni93 – 12432Coil 1AAdd
BLAST
Regioni125 – 13713Linker 1Add
BLAST
Regioni138 – 23497Coil 1BAdd
BLAST
Regioni235 – 25218Linker 12Add
BLAST
Regioni253 – 27119Coil 2AAdd
BLAST
Regioni272 – 2809Linker 2
Regioni281 – 396116Coil 2BAdd
BLAST
Regioni381 – 39111Epitope; recognized by IF-specific monoclonal antibodyAdd
BLAST
Regioni397 – 543147TailAdd
BLAST
Regioni397 – 44347Tail, subdomain AAdd
BLAST
Regioni444 – 543100Tail, subdomain B (acidic)Add
BLAST

Domaini

The extra mass and high charge density that distinguish the neurofilament proteins from all other intermediate filament proteins are due to the tailpiece extensions. This region may form a charged scaffolding structure suitable for interaction with other neuronal components or ions.

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG145720.
GeneTreeiENSGT00760000118905.
HOVERGENiHBG013015.
InParanoidiP07196.
KOiK04572.
PhylomeDBiP07196.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS
60 70 80 90 100
LSVRRSYSSS SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR
110 120 130 140 150
FASFIERVHE LEQQNKVLEA ELLVLRQKHS EPSRFRALYE QEIRDLRLAA
160 170 180 190 200
EDATNEKQAL QGEREGLEET LRNLQARYEE EVLSREDAEG RLMEARKGAD
210 220 230 240 250
EAALARAELE KRIDSLMDEI SFLKKVHEEE IAELQAQIQY AQISVEMDVT
260 270 280 290 300
KPDLSAALKD IRAQYEKLAA KNMQNAEEWF KSRFTVLTES AAKNTDAVRA
310 320 330 340 350
AKDEVSESRR LLKAKTLEIE ACRGMNEALE KQLQELEDKQ NADISAMQDT
360 370 380 390 400
INKLENELRT TKSEMARYLK EYQDLLNVKM ALDIEIAAYR KLLEGEETRL
410 420 430 440 450
SFTSVGSITS GYSQSSQVFG RSAYGGLQTS SYLMSTRSFP SYYTSHVQEE
460 470 480 490 500
QIEVEETIEA AKAEEAKDEP PSEGEAEEEE KDKEEAEEEE AAEEEEAAKE
510 520 530 540
ESEEAKEEEE GGEGEEGEET KEAEEEEKKV EGAGEEQAAK KKD
Length:543
Mass (Da):61,517
Last modified:January 23, 2007 - v3
Checksum:i98C1712D8ACFF33A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281Missing in CAA29097 (PubMed:3034332).Curated
Sequence conflicti155 – 1551N → TN (PubMed:3034332).Curated
Sequence conflicti161 – 1611Q → R in CAA29097 (PubMed:3034332).Curated
Sequence conflicti165 – 1651E → EE in CAA29097 (PubMed:3034332).Curated
Sequence conflicti195 – 1951A → R in CAA29097 (PubMed:3034332).Curated
Sequence conflicti452 – 4521I → T in CAA29097 (PubMed:3034332).Curated
Sequence conflicti461 – 4611A → S in CAA29097 (PubMed:3034332).Curated
Sequence conflicti472 – 4721S → D AA sequence (PubMed:6135695).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71E → K in a Charcot-Marie-Tooth disease patient. 1 Publication
Corresponds to variant rs57848467 [ dbSNP | Ensembl ].
VAR_016017
Natural varianti8 – 81P → L in CMT1F. 1 Publication
VAR_016018
Natural varianti8 – 81P → Q in CMT1F. 1 Publication
VAR_016019
Natural varianti8 – 81P → R in CMT2E and CMT1F. 3 Publications
Corresponds to variant rs60261494 [ dbSNP | Ensembl ].
VAR_016020
Natural varianti22 – 221P → S in CMT2E. 2 Publications
Corresponds to variant rs28928910 [ dbSNP | Ensembl ].
VAR_016021
Natural varianti90 – 901E → K in CMT1F. 1 Publication
Corresponds to variant rs58332872 [ dbSNP | Ensembl ].
VAR_016022
Natural varianti98 – 981N → S in CMT1F. 1 Publication
Corresponds to variant rs58982919 [ dbSNP | Ensembl ].
VAR_016023
Natural varianti332 – 3321Q → P in CMT2E. 1 Publication
Corresponds to variant rs59443585 [ dbSNP | Ensembl ].
VAR_009703
Natural varianti336 – 3361L → P in CMT2E. 1 Publication
VAR_021613
Natural varianti396 – 3961E → K in CMT1F and CMT2E. 3 Publications
VAR_021614
Natural varianti468 – 4681D → N.1 Publication
Corresponds to variant rs57153321 [ dbSNP | Ensembl ].
VAR_016024
Natural varianti527 – 5271Missing in CMT1F. 1 Publication
VAR_016025

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05608 Genomic DNA. Translation: CAA29097.1.
AY156690 mRNA. Translation: AAN74826.1.
AC107373 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63598.1.
CH471080 Genomic DNA. Translation: EAW63599.1.
CH471080 Genomic DNA. Translation: EAW63600.1.
BC039237 mRNA. Translation: AAH39237.1.
S70309 Genomic DNA. Translation: AAD14057.1.
CCDSiCCDS75712.1.
PIRiS07144.
RefSeqiNP_006149.2. NM_006158.4.
UniGeneiHs.521461.

Genome annotation databases

EnsembliENST00000610854; ENSP00000482169; ENSG00000277586.
GeneIDi4747.
KEGGihsa:4747.
UCSCiuc003xee.4. human.

Polymorphism databases

DMDMi62511894.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db
Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05608 Genomic DNA. Translation: CAA29097.1.
AY156690 mRNA. Translation: AAN74826.1.
AC107373 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63598.1.
CH471080 Genomic DNA. Translation: EAW63599.1.
CH471080 Genomic DNA. Translation: EAW63600.1.
BC039237 mRNA. Translation: AAH39237.1.
S70309 Genomic DNA. Translation: AAD14057.1.
CCDSiCCDS75712.1.
PIRiS07144.
RefSeqiNP_006149.2. NM_006158.4.
UniGeneiHs.521461.

3D structure databases

ProteinModelPortaliP07196.
SMRiP07196. Positions 133-238, 252-321, 326-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110822. 39 interactions.
IntActiP07196. 15 interactions.
MINTiMINT-1370620.
STRINGi9606.ENSP00000221169.

PTM databases

PhosphoSiteiP07196.

Polymorphism databases

DMDMi62511894.

2D gel databases

UCD-2DPAGEP07196.

Proteomic databases

MaxQBiP07196.
PaxDbiP07196.
PRIDEiP07196.

Protocols and materials databases

DNASUi4747.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000610854; ENSP00000482169; ENSG00000277586.
GeneIDi4747.
KEGGihsa:4747.
UCSCiuc003xee.4. human.

Organism-specific databases

CTDi4747.
GeneCardsiGC08M024808.
GeneReviewsiNEFL.
HGNCiHGNC:7739. NEFL.
MIMi162280. gene.
607684. phenotype.
607734. phenotype.
neXtProtiNX_P07196.
Orphaneti99939. Autosomal dominant Charcot-Marie-Tooth disease type 2E.
101085. Charcot-Marie-Tooth disease type 1F.
228374. Severe early-onset axonal neuropathy due to NEFL deficiency.
PharmGKBiPA31542.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145720.
GeneTreeiENSGT00760000118905.
HOVERGENiHBG013015.
InParanoidiP07196.
KOiK04572.
PhylomeDBiP07196.

Enzyme and pathway databases

ReactomeiREACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
REACT_20642. CREB phosphorylation through the activation of CaMKII.

Miscellaneous databases

ChiTaRSiNEFL. human.
GeneWikiiNEFL.
GenomeRNAii4747.
NextBioi18298.
PROiP07196.
SOURCEiSearch...

Gene expression databases

CleanExiHS_NEFL.
ExpressionAtlasiP07196. baseline and differential.
GenevestigatoriP07196.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027692. NF-L.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF22. PTHR23239:SF22. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of a human neurofilament gene (NF-L): a unique exon-intron organization in the intermediate filament gene family."
    Julien J.-P., Grosveld F., Yazdanbaksh K., Flavell D., Meijer D., Mushynski W.
    Biochim. Biophys. Acta 909:10-20(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Effects of Charcot-Marie-Tooth-linked mutations of the neurofilament light subunit on intermediate filament formation."
    Perez-Olle R., Leung C.L., Liem R.K.
    J. Cell Sci. 115:4937-4946(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "AP-1 and Krox-24 transcription factors activate the neurofilament light gene promoter in P19 embryonal carcinoma cells."
    Pospelov V.A., Pospelova T.V., Julien J.-P.
    Cell Growth Differ. 5:187-196(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-54; 213-224; 340-353; 380-390 AND 422-437, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "Highly acidic proteins from human brain: purification and properties of Glu-50 protein."
    Nomata Y., Watanabe T., Wada H.
    J. Biochem. 93:825-831(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 468-473.
    Tissue: Brain.
  9. "PKN associates and phosphorylates the head-rod domain of neurofilament protein."
    Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M., Sunakawa H., Ono Y.
    J. Biol. Chem. 271:9816-9822(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKN1.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene."
    Mersiyanova I.V., Perepelov A.V., Polyakov A.V., Sitnikov V.F., Dadali E.L., Oparin R.B., Petrin A.N., Evgrafov O.V.
    Am. J. Hum. Genet. 67:37-46(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2E PRO-332.
  13. "Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E."
    De Jonghe P., Mersivanova I., Nelis E., Del Favero J., Martin J.-J., Van Broeckhoven C., Evgrafov O., Timmerman V.
    Ann. Neurol. 49:245-249(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2E ARG-8.
  14. "A novel NF-L mutation Pro22Ser is associated with CMT2 in a large Slovenian family."
    Georgiou D.-M., Zidar J., Korosec M., Middleton L.T., Kyriakides T., Christodoulou K.
    Neurogenetics 4:93-96(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2E SER-22.
  15. Cited for: VARIANTS CMT1F ARG-8; LEU-8; GLN-8; LYS-90; SER-98 AND GLU-527 DEL, VARIANTS LYS-7 AND ASN-468.
  16. "Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean Charcot-Marie-Tooth neuropathy patients."
    Choi B.-O., Lee M.S., Shin S.H., Hwang J.H., Choi K.-G., Kim W.-K., Sunwoo I.N., Kim N.K., Chung K.W.
    Hum. Mutat. 24:185-186(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2E PRO-336, VARIANT CMT1F LYS-396.
  17. "The novel neurofilament light (NEFL) mutation Glu397Lys is associated with a clinically and morphologically heterogeneous type of Charcot-Marie-Tooth neuropathy."
    Zuechner S., Vorgerd M., Sindern E., Schroeder J.M.
    Neuromuscul. Disord. 14:147-157(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT1F LYS-396.
  18. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
    Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
    PLoS ONE 6:E29393-E29393(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CMT2E ARG-8; SER-22 AND LYS-396.

Entry informationi

Entry nameiNFL_HUMAN
AccessioniPrimary (citable) accession number: P07196
Secondary accession number(s): B9ZVN2, Q16154, Q8IU72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

NF-L is the most abundant of the three neurofilament proteins and, like the other nonepithelial intermediate filament proteins, it can form homopolymeric 10-nm filaments.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.