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Protein

Neurofilament heavy polypeptide

Gene

Nefh

Organism
Rattus norvegicus (Rat)
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. NF-H has an important function in mature axons that is not subserved by the two smaller NF proteins.

GO - Molecular functioni

  • protein binding, bridging Source: BHF-UCL
  • protein heterodimerization activity Source: RGD
  • structural constituent of cytoskeleton Source: BHF-UCL
  • toxic substance binding Source: RGD

GO - Biological processi

  • axon regeneration Source: RGD
  • brain development Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • cellular response to oxidative stress Source: RGD
  • cerebral cortex development Source: RGD
  • hippocampus development Source: RGD
  • intermediate filament bundle assembly Source: BHF-UCL
  • neuron projection development Source: RGD
  • ovarian follicle atresia Source: RGD
  • response to acrylamide Source: RGD
  • response to cocaine Source: RGD
  • response to sodium arsenite Source: RGD
  • spinal cord development Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament heavy polypeptide
Short name:
NF-H
Alternative name(s):
200 kDa neurofilament protein
Neurofilament triplet H protein
Gene namesi
Name:Nefh
Synonyms:Nfh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3159. Nefh.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cytoplasm Source: BHF-UCL
  • intermediate filament Source: BHF-UCL
  • nucleus Source: RGD
  • perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10721072Neurofilament heavy polypeptidePRO_0000063803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei414 – 4141PhosphoserineCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei501 – 5011PhosphoserineCombined sources
Modified residuei516 – 5161PhosphoserineCombined sources
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources
Modified residuei534 – 5341PhosphoserineCombined sources
Modified residuei540 – 5401PhosphoserineCombined sources
Modified residuei546 – 5461PhosphoserineCombined sources
Modified residuei552 – 5521PhosphoserineCombined sources
Modified residuei558 – 5581PhosphoserineCombined sources
Modified residuei564 – 5641PhosphoserineCombined sources
Modified residuei570 – 5701PhosphoserineCombined sources
Modified residuei576 – 5761PhosphoserineCombined sources
Modified residuei582 – 5821PhosphoserineCombined sources
Modified residuei588 – 5881PhosphoserineCombined sources
Modified residuei594 – 5941PhosphoserineCombined sources
Modified residuei600 – 6001PhosphoserineCombined sources
Modified residuei606 – 6061PhosphoserineCombined sources
Modified residuei612 – 6121PhosphoserineBy similarity
Modified residuei618 – 6181PhosphoserineCombined sources
Modified residuei624 – 6241PhosphoserineCombined sources
Modified residuei627 – 6271PhosphoserineCombined sources
Modified residuei630 – 6301PhosphoserineCombined sources
Modified residuei636 – 6361PhosphoserineCombined sources
Modified residuei642 – 6421PhosphoserineCombined sources
Modified residuei648 – 6481PhosphoserineCombined sources
Modified residuei654 – 6541PhosphoserineCombined sources
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei666 – 6661PhosphoserineCombined sources
Modified residuei672 – 6721PhosphoserineCombined sources
Modified residuei678 – 6781PhosphoserineBy similarity
Modified residuei684 – 6841PhosphoserineCombined sources
Modified residuei687 – 6871PhosphoserineCombined sources
Modified residuei690 – 6901PhosphoserineCombined sources
Modified residuei696 – 6961PhosphoserineCombined sources
Modified residuei702 – 7021PhosphoserineCombined sources
Modified residuei708 – 7081PhosphoserineCombined sources
Modified residuei714 – 7141PhosphoserineCombined sources
Modified residuei720 – 7201PhosphoserineCombined sources
Modified residuei732 – 7321PhosphoserineCombined sources
Modified residuei738 – 7381PhosphoserineCombined sources
Modified residuei744 – 7441PhosphoserineCombined sources
Modified residuei750 – 7501PhosphoserineCombined sources
Modified residuei756 – 7561PhosphoserineCombined sources
Modified residuei762 – 7621PhosphoserineCombined sources
Modified residuei776 – 7761PhosphoserineBy similarity
Modified residuei782 – 7821PhosphoserineCombined sources
Modified residuei788 – 7881PhosphoserineBy similarity
Modified residuei802 – 8021PhosphoserineCombined sources
Modified residuei808 – 8081PhosphoserineCombined sources
Modified residuei816 – 8161PhosphoserineCombined sources
Modified residuei827 – 8271PhosphoserineCombined sources
Modified residuei832 – 8321PhosphothreonineCombined sources
Modified residuei846 – 8461PhosphoserineCombined sources
Modified residuei852 – 8521PhosphoserineCombined sources
Modified residuei860 – 8601PhosphoserineCombined sources
Modified residuei880 – 8801PhosphoserineCombined sources
Modified residuei937 – 9371PhosphoserineCombined sources

Post-translational modificationi

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP16884.
PRIDEiP16884.

PTM databases

iPTMnetiP16884.
PhosphoSiteiP16884.

Interactioni

GO - Molecular functioni

  • protein binding, bridging Source: BHF-UCL
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

DIPiDIP-105N.
IntActiP16884. 3 interactions.
MINTiMINT-4582714.
STRINGi10116.ENSRNOP00000011604.

Structurei

3D structure databases

ProteinModelPortaliP16884.
SMRiP16884. Positions 92-127, 327-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati507 – 51261
Repeati515 – 52062
Repeati521 – 52663
Repeati527 – 53264
Repeati533 – 53865
Repeati539 – 54466
Repeati545 – 55067
Repeati551 – 55668
Repeati557 – 56269
Repeati563 – 568610
Repeati569 – 574611
Repeati575 – 580612
Repeati581 – 586613
Repeati587 – 592614
Repeati593 – 598615
Repeati599 – 604616
Repeati605 – 610617
Repeati611 – 616618
Repeati617 – 622619
Repeati623 – 628620
Repeati629 – 634621
Repeati635 – 640622
Repeati641 – 646623
Repeati647 – 652624
Repeati653 – 658625
Repeati659 – 664626
Repeati665 – 670627
Repeati671 – 676628
Repeati677 – 682629
Repeati683 – 688630
Repeati689 – 694631
Repeati695 – 700632
Repeati701 – 706633
Repeati707 – 712634
Repeati713 – 718635
Repeati719 – 724636
Repeati725 – 730637; approximate
Repeati731 – 736638
Repeati737 – 742639
Repeati743 – 748640
Repeati749 – 754641
Repeati755 – 760642
Repeati761 – 766643
Repeati767 – 772644
Repeati775 – 780645; approximate
Repeati781 – 786646
Repeati787 – 792647
Repeati795 – 800648; approximate
Repeati801 – 806649
Repeati807 – 812650
Repeati815 – 820651
Repeati826 – 831652
Repeati851 – 856653
Repeati859 – 864654
Repeati879 – 884655

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 64336655 X 6 AA approximate tandem repeats of K-S-P-[VAGSE]-[KEVTSGA]-[EAVK]Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili98 – 13235Sequence analysisAdd
BLAST
Coiled coili174 – 22249Sequence analysisAdd
BLAST
Coiled coili293 – 38088Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP16884.
PhylomeDBiP16884.

Family and domain databases

InterProiIPR010790. DUF1388.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR033183. NF-H.
[Graphical view]
PANTHERiPTHR23214:SF1. PTHR23214:SF1. 2 hits.
PfamiPF07142. DUF1388. 19 hits.
PF00038. Filament. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16884-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSFGSADAL LGAPFAPLHG GGSLHYALSR KAGAGGTRSA AGSSSGFHSW
60 70 80 90 100
ARTSVSSVSA SPSRFRGAAS STDSLDTLSN GPEGCVAAVA ARSEKEQLQA
110 120 130 140 150
LNDRFAGYID KVRQLEAHNR TLEGEAAALR QQKGRAAMGE LYEREVREMR
160 170 180 190 200
GAVLRLGAAR GHVRLEQEHL LEDIAHVRQR LDEEARQREE AEAAARALAR
210 220 230 240 250
FAQEAEAARV ELQKKAQALQ EECGYLRRHH QEEVGELLGQ IQGCGAAQAQ
260 270 280 290 300
AQAEARDALK CDVTSALREI RAQLEGHTVQ STLQSEEWFR VRLDRLSEAA
310 320 330 340 350
KVNTDAMRSA QEEITEYRRQ LQARTTELEA LKSTKESLER QRSELEDRHQ
360 370 380 390 400
VDMASYQDAI QQLDNELRNT KWEMAAQLRE YQDLLNVKMA LDIEIAAYRK
410 420 430 440 450
LLEGEECRIG FGPSPFSLTE GLPKIPSMST HIKVKSEEKI KVVEKSEKET
460 470 480 490 500
VIVEEQTEEI QVTEEVTEEE DKEAQGEEEE EAEEGGEEAA TTSPPAEEAA
510 520 530 540 550
SPEKETKSPV KEEAKSPAEA KSPAEAKSPA EAKSPAEVKS PAEVKSPAEA
560 570 580 590 600
KSPAEAKSPA EVKSPAEVKS PAEAKSPAEA KSPAEVKSPA TVKSPGEAKS
610 620 630 640 650
PAEAKSPAEV KSPVEAKSPA EAKSPASVKS PGEAKSPAEA KSPAEVKSPA
660 670 680 690 700
TVKSPVEAKS PAEVKSPVTV KSPAEAKSPV EVKSPASVKS PSEAKSPAGA
710 720 730 740 750
KSPAEAKSPV VAKSPAEAKS PAEAKPPAEA KSPAEAKSPA EAKSPAEAKS
760 770 780 790 800
PAEAKSPVEV KSPEKAKSPV KEGAKSLAEA KSPEKAKSPV KEEIKPPAEV
810 820 830 840 850
KSPEKAKSPM KEEAKSPEKA KTLDVKSPEA KTPAKEEAKR PADIRSPEQV
860 870 880 890 900
KSPAKEEAKS PEKEETRTEK VAPKKEEVKS PVEEVKAKEP PKKVEEEKTP
910 920 930 940 950
ATPKTEVKES KKDEAPKEAQ KPKAEEKEPL TEKPKDSPGE AKKEEAKEKK
960 970 980 990 1000
AAAPEEETPA KLGVKEEAKP KEKAEDAKAK EPSKPSEKEK PKKEEVPAAP
1010 1020 1030 1040 1050
EKKDTKEEKT TESKKPEEKP KMEAKAKEED KGLPQEPSKP KTEKAEKSSS
1060 1070
TDQKDSQPSE KAPEDKAAKG DK
Length:1,072
Mass (Da):115,378
Last modified:December 6, 2005 - v4
Checksum:i89BDFD7E2164D78B
GO

Sequence cautioni

The sequence CAA32038.1 differs from that shown. Reason: Frameshift at position 1024. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931I → L in AAA41693 (PubMed:3143606).Curated
Sequence conflicti393 – 3931I → L in CAA32038 (PubMed:3143606).Curated
Sequence conflicti414 – 4141S → I in AAA41693 (PubMed:3143606).Curated
Sequence conflicti414 – 4141S → I in CAA32038 (PubMed:3143606).Curated
Sequence conflicti422 – 4221L → T in AAA41695 (PubMed:2457365).Curated
Sequence conflicti428 – 4281M → T in AAA41695 (PubMed:2457365).Curated
Sequence conflicti555 – 5551E → V (PubMed:3143606).Curated
Sequence conflicti555 – 5551E → V (PubMed:2457365).Curated
Sequence conflicti567 – 5671E → T in AAB87068 (PubMed:2230956).Curated
Sequence conflicti587 – 5871K → N in AAA41693 (PubMed:3143606).Curated
Sequence conflicti587 – 5871K → N in CAA32038 (PubMed:3143606).Curated
Sequence conflicti614 – 6141V → A (PubMed:2457365).Curated
Sequence conflicti614 – 6141V → A (Ref. 7) Curated
Sequence conflicti723 – 7231E → G in AAA41693 (PubMed:3143606).Curated
Sequence conflicti723 – 7231E → G in CAA32038 (PubMed:3143606).Curated
Sequence conflicti726 – 7261P → S (PubMed:2457365).Curated
Sequence conflicti726 – 7261P → S (Ref. 7) Curated
Sequence conflicti811 – 8122KE → RK in AAA41693 (PubMed:3143606).Curated
Sequence conflicti811 – 8122KE → RK in CAA32038 (PubMed:3143606).Curated
Sequence conflicti832 – 8321T → P in AAA41693 (PubMed:3143606).Curated
Sequence conflicti832 – 8321T → P in CAA32038 (PubMed:3143606).Curated
Sequence conflicti968 – 9681A → V in AAA41692 (PubMed:2928342).Curated
Sequence conflicti998 – 10003AAP → GST in AAA41692 (PubMed:2928342).Curated
Sequence conflicti1010 – 10101T → L (PubMed:2457365).Curated
Sequence conflicti1010 – 10101T → L (Ref. 7) Curated
Sequence conflicti1016 – 10161P → R in AAA41693 (PubMed:3143606).Curated
Sequence conflicti1016 – 10161P → R in CAA32038 (PubMed:3143606).Curated
Sequence conflicti1023 – 10231E → Q in AAB87068 (PubMed:2230956).Curated

Polymorphismi

The number of repeats in the tandem repeat domain is shown to vary between 53 and 55.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37227 mRNA. Translation: AAA41693.1. Frameshift.
X13804 mRNA. Translation: CAA32038.1. Frameshift.
AF031879 mRNA. Translation: AAB87068.1.
M21964 mRNA. Translation: AAA41695.1.
J04517 mRNA. Translation: AAA41692.1.
AY112897 mRNA. Translation: AAM49796.1.
PIRiA37221.
S02003.
UniGeneiRn.108194.

Genome annotation databases

UCSCiRGD:3159. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37227 mRNA. Translation: AAA41693.1. Frameshift.
X13804 mRNA. Translation: CAA32038.1. Frameshift.
AF031879 mRNA. Translation: AAB87068.1.
M21964 mRNA. Translation: AAA41695.1.
J04517 mRNA. Translation: AAA41692.1.
AY112897 mRNA. Translation: AAM49796.1.
PIRiA37221.
S02003.
UniGeneiRn.108194.

3D structure databases

ProteinModelPortaliP16884.
SMRiP16884. Positions 92-127, 327-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-105N.
IntActiP16884. 3 interactions.
MINTiMINT-4582714.
STRINGi10116.ENSRNOP00000011604.

PTM databases

iPTMnetiP16884.
PhosphoSiteiP16884.

Proteomic databases

PaxDbiP16884.
PRIDEiP16884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3159. rat.

Organism-specific databases

RGDi3159. Nefh.

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP16884.
PhylomeDBiP16884.

Miscellaneous databases

PROiP16884.

Family and domain databases

InterProiIPR010790. DUF1388.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR033183. NF-H.
[Graphical view]
PANTHERiPTHR23214:SF1. PTHR23214:SF1. 2 hits.
PfamiPF07142. DUF1388. 19 hits.
PF00038. Filament. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Partial sequence of the rat heavy neurofilament polypeptide (NF-H). Identification of putative phosphorylation sites."
    Breen K.C., Robinson P.A., Wion D., Anderton B.H.
    FEBS Lett. 241:213-218(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form."
    Chin S.S., Liem R.K.
    J. Neurosci. 10:3714-3726(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Isolation of a cDNA for the rat heavy neurofilament polypeptide (NF-H)."
    Robinson P.A., Wion D., Anderton B.H.
    FEBS Lett. 209:203-205(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 230-318 AND 472-554.
  4. "The large neurofilament subunit (NF-H) of the rat: cDNA cloning and in situ detection."
    Dautigny A., Pham-Dinh D., Roussel C., Felix J.M., Nussbaum J.-L., Jolles P.
    Biochem. Biophys. Res. Commun. 154:1099-1106(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 266-1072.
  5. Lubec G., Pradeep J.J.P., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 39-52; 165-178; 229-256; 272-290; 349-368; 389-399 AND 401-424, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  6. "Cloning of a cDNA encoding the rat high molecular weight neurofilament peptide (NF-H): developmental and tissue expression in the rat, and mapping of its human homologue to chromosomes 1 and 22."
    Lieberburg I., Spinner N., Snyder S., Anderson J., Goldgaber D., Smulowitz M., Carroll Z., Emanuel B.S., Breitner J., Rubin L.
    Proc. Natl. Acad. Sci. U.S.A. 86:2463-2467(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-1072.
  7. "Rat heavy neurofilament (NF-H) polypeptide."
    Alliel P.M., Langlois C.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-1072.
    Tissue: Brain.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414; SER-417; SER-501; SER-516; SER-522; SER-528; SER-534; SER-540; SER-546; SER-552; SER-558; SER-564; SER-570; SER-576; SER-582; SER-588; SER-594; SER-600; SER-606; SER-618; SER-624; SER-627; SER-630; SER-636; SER-642; SER-648; SER-654; SER-660; SER-666; SER-672; SER-684; SER-687; SER-690; SER-696; SER-702; SER-708; SER-714; SER-720; SER-732; SER-738; SER-744; SER-750; SER-756; SER-762; SER-782; SER-802; SER-808; SER-816; SER-827; THR-832; SER-846; SER-852; SER-860; SER-880 AND SER-937, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNFH_RAT
AccessioniPrimary (citable) accession number: P16884
Secondary accession number(s): O35482, Q540Z7, Q63368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 6, 2005
Last modified: May 11, 2016
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.