P19246 · NFH_MOUSE
- ProteinNeurofilament heavy polypeptide
- GeneNefh
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1090 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Names & Taxonomy
Protein names
- Recommended nameNeurofilament heavy polypeptide
- Short namesNF-H
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP19246
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000063801 | 1-1090 | Neurofilament heavy polypeptide | |||
Sequence: MMSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQQAGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEEGAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK | ||||||
Modified residue | 74 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 122 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 416 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 419 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 508 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 523 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 529 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 541 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 547 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 553 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 559 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 565 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 571 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 577 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 583 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 589 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 595 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 601 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 607 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 613 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 619 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 625 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 631 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 637 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 643 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 649 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 655 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 661 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 667 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 673 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 679 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 685 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 691 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 697 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 703 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 709 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 715 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 721 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 727 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 733 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 739 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 745 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 751 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 757 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 763 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 769 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 783 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 789 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 795 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 809 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 815 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 834 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 839 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 859 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 867 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 888 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 947 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-98 | Head | ||||
Sequence: MSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQ | ||||||
Domain | 95-411 | IF rod | ||||
Sequence: EKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQQAGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRI | ||||||
Region | 99-130 | Coil 1A | ||||
Sequence: LQALNDRFAGYIDKVRQLEAHNRSLEGEAAAL | ||||||
Region | 131-143 | Linker 1 | ||||
Sequence: RQQQAGRAAMGEL | ||||||
Region | 144-242 | Coil 1B | ||||
Sequence: YEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQ | ||||||
Region | 243-264 | Linker 12 | ||||
Sequence: IQGCGAAQAQAQAEARDALKCD | ||||||
Region | 265-286 | Coil 2A | ||||
Sequence: VTSALREIRAQLEGHAVQSTLQ | ||||||
Region | 287-290 | Linker 2 | ||||
Sequence: SEEW | ||||||
Region | 291-411 | Coil 2B | ||||
Sequence: FRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRI | ||||||
Region | 412-1090 | Tail | ||||
Sequence: GFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEEGAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK | ||||||
Compositional bias | 456-474 | Basic and acidic residues | ||||
Sequence: EGQTEEIRVTEGVTEEEDK | ||||||
Region | 456-1090 | Disordered | ||||
Sequence: EGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEEGAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK | ||||||
Compositional bias | 475-493 | Acidic residues | ||||
Sequence: EAQGQEGEEAEEGEEKEEE | ||||||
Compositional bias | 507-527 | Basic and acidic residues | ||||
Sequence: ASPEKETKSRVKEEAKSPGEA | ||||||
Repeat | 522-527 | 1 | ||||
Sequence: KSPGEA | ||||||
Region | 522-892 | 52 X 6 AA approximate tandem repeats of K-S-P-[AGISV]-[EATK]-[APVQ] | ||||
Sequence: KSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKE | ||||||
Repeat | 528-533 | 2 | ||||
Sequence: KSPGEA | ||||||
Repeat | 534-539 | 3 | ||||
Sequence: KSPAEA | ||||||
Repeat | 540-545 | 4 | ||||
Sequence: KSPGEA | ||||||
Repeat | 546-551 | 5 | ||||
Sequence: KSPGEA | ||||||
Repeat | 552-557 | 6 | ||||
Sequence: KSPGEA | ||||||
Repeat | 558-563 | 7 | ||||
Sequence: KSPAEP | ||||||
Repeat | 564-569 | 8 | ||||
Sequence: KSPAEP | ||||||
Repeat | 570-575 | 9 | ||||
Sequence: KSPAEA | ||||||
Repeat | 576-581 | 10 | ||||
Sequence: KSPAEP | ||||||
Repeat | 582-587 | 11 | ||||
Sequence: KSPATV | ||||||
Repeat | 588-593 | 12 | ||||
Sequence: KSPGEA | ||||||
Repeat | 594-599 | 13 | ||||
Sequence: KSPSEA | ||||||
Repeat | 600-605 | 14 | ||||
Sequence: KSPAEA | ||||||
Repeat | 606-611 | 15 | ||||
Sequence: KSPAEA | ||||||
Repeat | 612-617 | 16 | ||||
Sequence: KSPAEA | ||||||
Repeat | 618-623 | 17 | ||||
Sequence: KSPAEA | ||||||
Repeat | 624-629 | 18 | ||||
Sequence: KSPAEA | ||||||
Repeat | 630-635 | 19 | ||||
Sequence: KSPAEA | ||||||
Repeat | 636-641 | 20 | ||||
Sequence: KSPATV | ||||||
Repeat | 642-647 | 21 | ||||
Sequence: KSPGEA | ||||||
Repeat | 648-653 | 22 | ||||
Sequence: KSPSEA | ||||||
Repeat | 654-659 | 23 | ||||
Sequence: KSPAEA | ||||||
Repeat | 660-665 | 24 | ||||
Sequence: KSPAEA | ||||||
Repeat | 666-671 | 25 | ||||
Sequence: KSPAEA | ||||||
Repeat | 672-677 | 26 | ||||
Sequence: KSPAEV | ||||||
Repeat | 678-683 | 27 | ||||
Sequence: KSPGEA | ||||||
Repeat | 684-689 | 28 | ||||
Sequence: KSPAEP | ||||||
Repeat | 690-695 | 29 | ||||
Sequence: KSPAEA | ||||||
Repeat | 696-701 | 30 | ||||
Sequence: KSPAEV | ||||||
Repeat | 702-707 | 31 | ||||
Sequence: KSPAEA | ||||||
Repeat | 708-713 | 32 | ||||
Sequence: KSPAEV | ||||||
Repeat | 714-719 | 33 | ||||
Sequence: KSPGEA | ||||||
Repeat | 720-725 | 34 | ||||
Sequence: KSPAAV | ||||||
Repeat | 726-731 | 35 | ||||
Sequence: KSPAEA | ||||||
Repeat | 732-737 | 36 | ||||
Sequence: KSPAAV | ||||||
Repeat | 738-743 | 37 | ||||
Sequence: KSPGEA | ||||||
Repeat | 744-749 | 38 | ||||
Sequence: KSPGEA | ||||||
Repeat | 750-755 | 39 | ||||
Sequence: KSPAEA | ||||||
Repeat | 756-761 | 40 | ||||
Sequence: KSPAEA | ||||||
Repeat | 762-767 | 41 | ||||
Sequence: KSPIEV | ||||||
Compositional bias | 765-832 | Basic and acidic residues | ||||
Sequence: IEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDV | ||||||
Repeat | 768-773 | 42 | ||||
Sequence: KSPEKA | ||||||
Repeat | 774-779 | 43; approximate | ||||
Sequence: KTPVKE | ||||||
Repeat | 782-787 | 44 | ||||
Sequence: KSPAEA | ||||||
Repeat | 788-793 | 45 | ||||
Sequence: KSPEKA | ||||||
Repeat | 794-799 | 46 | ||||
Sequence: KSPVKE | ||||||
Repeat | 808-813 | 47 | ||||
Sequence: KSPEKA | ||||||
Repeat | 814-819 | 48 | ||||
Sequence: KSPVKE | ||||||
Repeat | 833-838 | 49 | ||||
Sequence: KSPEAQ | ||||||
Compositional bias | 843-1090 | Basic and acidic residues | ||||
Sequence: EEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK | ||||||
Repeat | 858-863 | 50 | ||||
Sequence: KSPAKE | ||||||
Repeat | 866-871 | 51 | ||||
Sequence: KSPEKE | ||||||
Repeat | 887-892 | 52 | ||||
Sequence: KSPVKE |
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,090
- Mass (Da)116,994
- Last updated2006-05-02 v3
- ChecksumB2A7D7D36FF2F448
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 134-135 | in Ref. 2; AAA39813 | ||||
Sequence: QA → K | ||||||
Sequence conflict | 202 | in Ref. 2; AAA39813 | ||||
Sequence: Missing | ||||||
Sequence conflict | 284 | in Ref. 2; AAA39813 | ||||
Sequence: T → S | ||||||
Compositional bias | 456-474 | Basic and acidic residues | ||||
Sequence: EGQTEEIRVTEGVTEEEDK | ||||||
Compositional bias | 475-493 | Acidic residues | ||||
Sequence: EAQGQEGEEAEEGEEKEEE | ||||||
Sequence conflict | 495 | in Ref. 2; AAA39813 | ||||
Sequence: G → L | ||||||
Compositional bias | 507-527 | Basic and acidic residues | ||||
Sequence: ASPEKETKSRVKEEAKSPGEA | ||||||
Sequence conflict | 519 | in Ref. 1; AAA39809 and 3; CAA83229 | ||||
Sequence: E → EEAKSPG | ||||||
Sequence conflict | 549 | in Ref. 1; AAA39809 and 3; CAA83229 | ||||
Sequence: G → R | ||||||
Sequence conflict | 694-717 | in Ref. 1; AAA39809 and 3; CAA83229 | ||||
Sequence: Missing | ||||||
Compositional bias | 765-832 | Basic and acidic residues | ||||
Sequence: IEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDV | ||||||
Sequence conflict | 817 | in Ref. 1; AAA39809, 3; CAA83229 and 6; ABK96805 | ||||
Sequence: V → M | ||||||
Compositional bias | 843-1090 | Basic and acidic residues | ||||
Sequence: EEAKHPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK | ||||||
Sequence conflict | 846-847 | in Ref. 1; AAA39809, 3; CAA83229 and 6; ABK96805 | ||||
Sequence: KH → ND | ||||||
Sequence conflict | 846-847 | in Ref. 2; AAA39813 | ||||
Sequence: KH → TV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |