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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

  • Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000638031 – 1072Neurofilament heavy polypeptideAdd BLAST1072

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74PhosphoserineBy similarity1
Modified residuei343PhosphoserineCombined sources1
Modified residuei414PhosphoserineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei501PhosphoserineCombined sources1
Modified residuei516PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Modified residuei528PhosphoserineCombined sources1
Modified residuei534PhosphoserineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei546PhosphoserineCombined sources1
Modified residuei552PhosphoserineCombined sources1
Modified residuei558PhosphoserineCombined sources1
Modified residuei564PhosphoserineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei576PhosphoserineCombined sources1
Modified residuei582PhosphoserineCombined sources1
Modified residuei588PhosphoserineCombined sources1
Modified residuei594PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei606PhosphoserineCombined sources1
Modified residuei612PhosphoserineBy similarity1
Modified residuei618PhosphoserineCombined sources1
Modified residuei624PhosphoserineCombined sources1
Modified residuei627PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei636PhosphoserineCombined sources1
Modified residuei642PhosphoserineCombined sources1
Modified residuei648PhosphoserineCombined sources1
Modified residuei654PhosphoserineCombined sources1
Modified residuei660PhosphoserineCombined sources1
Modified residuei666PhosphoserineCombined sources1
Modified residuei672PhosphoserineCombined sources1
Modified residuei678PhosphoserineBy similarity1
Modified residuei684PhosphoserineCombined sources1
Modified residuei687PhosphoserineCombined sources1
Modified residuei690PhosphoserineCombined sources1
Modified residuei696PhosphoserineCombined sources1
Modified residuei702PhosphoserineCombined sources1
Modified residuei708PhosphoserineCombined sources1
Modified residuei714PhosphoserineCombined sources1
Modified residuei720PhosphoserineCombined sources1
Modified residuei732PhosphoserineCombined sources1
Modified residuei738PhosphoserineCombined sources1
Modified residuei744PhosphoserineCombined sources1
Modified residuei750PhosphoserineCombined sources1
Modified residuei756PhosphoserineCombined sources1
Modified residuei762PhosphoserineCombined sources1
Modified residuei776PhosphoserineBy similarity1
Modified residuei782PhosphoserineCombined sources1
Modified residuei788PhosphoserineBy similarity1
Modified residuei802PhosphoserineCombined sources1
Modified residuei808PhosphoserineCombined sources1
Modified residuei816PhosphoserineCombined sources1
Modified residuei827PhosphoserineCombined sources1
Modified residuei832PhosphothreonineCombined sources1
Modified residuei846PhosphoserineCombined sources1
Modified residuei852PhosphoserineCombined sources1
Modified residuei860PhosphoserineCombined sources1
Modified residuei880PhosphoserineCombined sources1
Modified residuei937PhosphoserineCombined sources1

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.
PhosphoSitePlusiP16884.

Interactioni

GO - Molecular functioni

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP16884.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati507 – 51216
Repeati515 – 52026
Repeati521 – 52636
Repeati527 – 53246
Repeati533 – 53856
Repeati539 – 54466
Repeati545 – 55076
Repeati551 – 55686
Repeati557 – 56296
Repeati563 – 568106
Repeati569 – 574116
Repeati575 – 580126
Repeati581 – 586136
Repeati587 – 592146
Repeati593 – 598156
Repeati599 – 604166
Repeati605 – 610176
Repeati611 – 616186
Repeati617 – 622196
Repeati623 – 628206
Repeati629 – 634216
Repeati635 – 640226
Repeati641 – 646236
Repeati647 – 652246
Repeati653 – 658256
Repeati659 – 664266
Repeati665 – 670276
Repeati671 – 676286
Repeati677 – 682296
Repeati683 – 688306
Repeati689 – 694316
Repeati695 – 700326
Repeati701 – 706336
Repeati707 – 712346
Repeati713 – 718356
Repeati719 – 724366
Repeati725 – 73037; approximate6
Repeati731 – 736386
Repeati737 – 742396
Repeati743 – 748406
Repeati749 – 754416
Repeati755 – 760426
Repeati761 – 766436
Repeati767 – 772446
Repeati775 – 78045; approximate6
Repeati781 – 786466
Repeati787 – 792476
Repeati795 – 80048; approximate6
Repeati801 – 806496
Repeati807 – 812506
Repeati815 – 820516
Repeati826 – 831526
Repeati851 – 856536
Repeati859 – 864546
Repeati879 – 884556

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 64355 X 6 AA approximate tandem repeats of K-S-P-[VAGSE]-[KEVTSGA]-[EAVK]Add BLAST366

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili98 – 132Sequence analysisAdd BLAST35
Coiled coili174 – 222Sequence analysisAdd BLAST49
Coiled coili293 – 380Sequence analysisAdd BLAST88

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 differs from that shown. Reason: Frameshift at position 1024.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti393I → L in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti393I → L in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti414S → I in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti414S → I in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti422L → T in AAA41695 (PubMed:2457365).Curated1
Sequence conflicti428M → T in AAA41695 (PubMed:2457365).Curated1
Sequence conflicti555E → V (PubMed:3143606).Curated1
Sequence conflicti555E → V (PubMed:2457365).Curated1
Sequence conflicti567E → T in AAB87068 (PubMed:2230956).Curated1
Sequence conflicti587K → N in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti587K → N in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti614V → A (PubMed:2457365).Curated1
Sequence conflicti614V → A (Ref. 7) Curated1
Sequence conflicti723E → G in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti723E → G in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti726P → S (PubMed:2457365).Curated1
Sequence conflicti726P → S (Ref. 7) Curated1
Sequence conflicti811 – 812KE → RK in AAA41693 (PubMed:3143606).Curated2
Sequence conflicti811 – 812KE → RK in CAA32038 (PubMed:3143606).Curated2
Sequence conflicti832T → P in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti832T → P in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti968A → V in AAA41692 (PubMed:2928342).Curated1
Sequence conflicti998 – 1000AAP → GST in AAA41692 (PubMed:2928342).Curated3
Sequence conflicti1010T → L (PubMed:2457365).Curated1
Sequence conflicti1010T → L (Ref. 7) Curated1
Sequence conflicti1016P → R in AAA41693 (PubMed:3143606).Curated1
Sequence conflicti1016P → R in CAA32038 (PubMed:3143606).Curated1
Sequence conflicti1023E → Q in AAB87068 (PubMed:2230956).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP16884.
PhosphoSitePlusiP16884.

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...

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: November 2, 2016
This is version 137 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.