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Protein

Neurofilament heavy polypeptide

Gene

Nefh

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • axon development Source: BHF-UCL
  • axon regeneration Source: Ensembl
  • cellular response to estradiol stimulus Source: Ensembl
  • cellular response to oxidative stress Source: Ensembl
  • cerebral cortex development Source: Ensembl
  • hippocampus development Source: Ensembl
  • intermediate filament bundle assembly Source: MGI
  • intermediate filament cytoskeleton organization Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • neurofilament bundle assembly Source: MGI
  • neurofilament cytoskeleton organization Source: MGI
  • ovarian follicle atresia Source: Ensembl
  • peripheral nervous system neuron axonogenesis Source: MGI
  • regulation of organelle transport along microtubule Source: MGI
  • response to acrylamide Source: Ensembl
  • response to cocaine Source: Ensembl
  • response to sodium arsenite Source: Ensembl
  • spinal cord development Source: Ensembl
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:Kiaa0845, Nfh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:97309. Nefh.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • neurofibrillary tangle Source: MGI
  • neurofilament Source: MGI
  • neuronal postsynaptic density Source: MGI
  • nucleus Source: Ensembl
  • perikaryon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10901090Neurofilament heavy polypeptidePRO_0000063801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineCombined sources
Modified residuei122 – 1221PhosphoserineCombined sources
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei416 – 4161PhosphoserineCombined sources
Modified residuei419 – 4191PhosphoserineCombined sources
Modified residuei508 – 5081PhosphoserineBy similarity
Modified residuei523 – 5231PhosphoserineBy similarity
Modified residuei529 – 5291PhosphoserineCombined sources
Modified residuei535 – 5351PhosphoserineCombined sources
Modified residuei541 – 5411PhosphoserineCombined sources
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei553 – 5531PhosphoserineCombined sources
Modified residuei559 – 5591PhosphoserineCombined sources
Modified residuei565 – 5651PhosphoserineCombined sources
Modified residuei571 – 5711PhosphoserineCombined sources
Modified residuei577 – 5771PhosphoserineCombined sources
Modified residuei583 – 5831PhosphoserineCombined sources
Modified residuei589 – 5891PhosphoserineCombined sources
Modified residuei595 – 5951PhosphoserineCombined sources
Modified residuei601 – 6011PhosphoserineCombined sources
Modified residuei607 – 6071PhosphoserineCombined sources
Modified residuei613 – 6131PhosphoserineCombined sources
Modified residuei619 – 6191PhosphoserineCombined sources
Modified residuei625 – 6251PhosphoserineCombined sources
Modified residuei631 – 6311PhosphoserineCombined sources
Modified residuei637 – 6371PhosphoserineCombined sources
Modified residuei643 – 6431PhosphoserineCombined sources
Modified residuei649 – 6491PhosphoserineCombined sources
Modified residuei655 – 6551PhosphoserineCombined sources
Modified residuei661 – 6611PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei673 – 6731PhosphoserineCombined sources
Modified residuei679 – 6791PhosphoserineCombined sources
Modified residuei685 – 6851PhosphoserineCombined sources
Modified residuei691 – 6911PhosphoserineCombined sources
Modified residuei697 – 6971PhosphoserineCombined sources
Modified residuei703 – 7031PhosphoserineCombined sources
Modified residuei709 – 7091PhosphoserineCombined sources
Modified residuei715 – 7151PhosphoserineCombined sources
Modified residuei721 – 7211PhosphoserineBy similarity
Modified residuei727 – 7271PhosphoserineCombined sources
Modified residuei733 – 7331PhosphoserineCombined sources
Modified residuei739 – 7391PhosphoserineCombined sources
Modified residuei745 – 7451PhosphoserineCombined sources
Modified residuei751 – 7511PhosphoserineCombined sources
Modified residuei757 – 7571PhosphoserineCombined sources
Modified residuei763 – 7631PhosphoserineCombined sources
Modified residuei769 – 7691PhosphoserineCombined sources
Modified residuei783 – 7831PhosphoserineCombined sources
Modified residuei789 – 7891PhosphoserineCombined sources
Modified residuei795 – 7951PhosphoserineCombined sources
Modified residuei809 – 8091PhosphoserineBy similarity
Modified residuei815 – 8151PhosphoserineCombined sources
Modified residuei834 – 8341PhosphoserineCombined sources
Modified residuei839 – 8391PhosphothreonineBy similarity
Modified residuei859 – 8591PhosphoserineCombined sources
Modified residuei867 – 8671PhosphoserineCombined sources
Modified residuei888 – 8881PhosphoserineCombined sources
Modified residuei947 – 9471PhosphoserineBy similarity

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

EPDiP19246.
MaxQBiP19246.
PaxDbiP19246.
PeptideAtlasiP19246.
PRIDEiP19246.

2D gel databases

UCD-2DPAGEP19246.

PTM databases

iPTMnetiP19246.
PhosphoSiteiP19246.

Expressioni

Gene expression databases

BgeeiP19246.
CleanExiMM_NEFH.
GenevisibleiP19246. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi237594. 4 interactions.
IntActiP19246. 2 interactions.
MINTiMINT-4103546.
STRINGi10090.ENSMUSP00000091061.

Structurei

3D structure databases

DisProtiDP00050.
ProteinModelPortaliP19246.
SMRiP19246. Positions 333-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati522 – 52761
Repeati528 – 53362
Repeati534 – 53963
Repeati540 – 54564
Repeati546 – 55165
Repeati552 – 55766
Repeati558 – 56367
Repeati564 – 56968
Repeati570 – 57569
Repeati576 – 581610
Repeati582 – 587611
Repeati588 – 593612
Repeati594 – 599613
Repeati600 – 605614
Repeati606 – 611615
Repeati612 – 617616
Repeati618 – 623617
Repeati624 – 629618
Repeati630 – 635619
Repeati636 – 641620
Repeati642 – 647621
Repeati648 – 653622
Repeati654 – 659623
Repeati660 – 665624
Repeati666 – 671625
Repeati672 – 677626
Repeati678 – 683627
Repeati684 – 689628
Repeati690 – 695629
Repeati696 – 701630
Repeati702 – 707631
Repeati708 – 713632
Repeati714 – 719633
Repeati720 – 725634
Repeati726 – 731635
Repeati732 – 737636
Repeati738 – 743637
Repeati744 – 749638
Repeati750 – 755639
Repeati756 – 761640
Repeati762 – 767641
Repeati768 – 773642
Repeati774 – 779643; approximate
Repeati782 – 787644
Repeati788 – 793645
Repeati794 – 799646
Repeati808 – 813647
Repeati814 – 819648
Repeati833 – 838649
Repeati858 – 863650
Repeati866 – 871651
Repeati887 – 892652

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9897HeadAdd
BLAST
Regioni99 – 411313RodAdd
BLAST
Regioni99 – 13032Coil 1AAdd
BLAST
Regioni131 – 14313Linker 1Add
BLAST
Regioni144 – 24299Coil 1BAdd
BLAST
Regioni243 – 26422Linker 12Add
BLAST
Regioni265 – 28622Coil 2AAdd
BLAST
Regioni287 – 2904Linker 2
Regioni291 – 411121Coil 2BAdd
BLAST
Regioni412 – 1090679TailAdd
BLAST
Regioni522 – 89237152 X 6 AA approximate tandem repeats of K-S-P-[AGISV]-[EATK]-[APVQ]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi439 – 52082Glu-rich (acidic)Add
BLAST
Compositional biasi890 – 1090201Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP19246.
KOiK04574.
OMAiPMKEAKS.
OrthoDBiEOG7GQXVW.
PhylomeDBiP19246.
TreeFamiTF330122.

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. 14 hits.
PF00038. Filament. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19246-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSFGSADAL LGAPFAPLHG GGSLHYSLSR KAGPGGTRSA AGSSSGFHSW
60 70 80 90 100
ARTSVSSVSA SPSRFRGAAS STDSLDTLSN GPEGCVVAAV AARSEKEQLQ
110 120 130 140 150
ALNDRFAGYI DKVRQLEAHN RSLEGEAAAL RQQQAGRAAM GELYEREVRE
160 170 180 190 200
MRGAVLRLGA ARGQLRLEQE HLLEDIAHVR QRLDEEARQR EEAEAAARAL
210 220 230 240 250
ARFAQEAEAA RVELQKKAQA LQEECGYLRR HHQEEVGELL GQIQGCGAAQ
260 270 280 290 300
AQAQAEARDA LKCDVTSALR EIRAQLEGHA VQSTLQSEEW FRVRLDRLSE
310 320 330 340 350
AAKVNTDAMR SAQEEITEYR RQLQARTTEL EALKSTKESL ERQRSELEDR
360 370 380 390 400
HQADIASYQD AIQQLDSELR NTKWEMAAQL REYQDLLNVK MALDIEIAAY
410 420 430 440 450
RKLLEGEECR IGFGPSPFSL TEGLPKIPSI STHIKVKSEE MIKVVEKSEK
460 470 480 490 500
ETVIVEGQTE EIRVTEGVTE EEDKEAQGQE GEEAEEGEEK EEEEGAAATS
510 520 530 540 550
PPAEEAASPE KETKSRVKEE AKSPGEAKSP GEAKSPAEAK SPGEAKSPGE
560 570 580 590 600
AKSPGEAKSP AEPKSPAEPK SPAEAKSPAE PKSPATVKSP GEAKSPSEAK
610 620 630 640 650
SPAEAKSPAE AKSPAEAKSP AEAKSPAEAK SPAEAKSPAT VKSPGEAKSP
660 670 680 690 700
SEAKSPAEAK SPAEAKSPAE AKSPAEVKSP GEAKSPAEPK SPAEAKSPAE
710 720 730 740 750
VKSPAEAKSP AEVKSPGEAK SPAAVKSPAE AKSPAAVKSP GEAKSPGEAK
760 770 780 790 800
SPAEAKSPAE AKSPIEVKSP EKAKTPVKEG AKSPAEAKSP EKAKSPVKED
810 820 830 840 850
IKPPAEAKSP EKAKSPVKEG AKPPEKAKPL DVKSPEAQTP VQEEAKHPTD
860 870 880 890 900
IRPPEQVKSP AKEKAKSPEK EEAKTSEKVA PKKEEVKSPV KEEVKAKEPP
910 920 930 940 950
KKVEEEKTLP TPKTEAKESK KDEAPKEAPK PKVEEKKETP TEKPKDSTAE
960 970 980 990 1000
AKKEEAGEKK KAVASEEETP AKLGVKEEAK PKEKTETTKT EAEDTKAKEP
1010 1020 1030 1040 1050
SKPTETEKPK KEEMPAAPEK KDTKEEKTTE SRKPEEKPKM EAKVKEDDKS
1060 1070 1080 1090
LSKEPSKPKT EKAEKSSSTD QKESQPPEKT TEDKATKGEK
Length:1,090
Mass (Da):116,994
Last modified:May 2, 2006 - v3
Checksum:iB2A7D7D36FF2F448
GO

Sequence cautioni

The sequence AAA39813.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA83229.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1352QA → K in AAA39813 (PubMed:3220257).Curated
Sequence conflicti202 – 2021Missing in AAA39813 (PubMed:3220257).Curated
Sequence conflicti284 – 2841T → S in AAA39813 (PubMed:3220257).Curated
Sequence conflicti495 – 4951G → L in AAA39813 (PubMed:3220257).Curated
Sequence conflicti519 – 5191E → EEAKSPG in AAA39809 (PubMed:3145094).Curated
Sequence conflicti519 – 5191E → EEAKSPG in CAA83229 (Ref. 3) Curated
Sequence conflicti549 – 5491G → R in AAA39809 (PubMed:3145094).Curated
Sequence conflicti549 – 5491G → R in CAA83229 (Ref. 3) Curated
Sequence conflicti694 – 71724Missing in AAA39809 (PubMed:3145094).CuratedAdd
BLAST
Sequence conflicti694 – 71724Missing in CAA83229 (Ref. 3) CuratedAdd
BLAST
Sequence conflicti817 – 8171V → M in AAA39809 (PubMed:3145094).Curated
Sequence conflicti817 – 8171V → M in CAA83229 (Ref. 3) Curated
Sequence conflicti817 – 8171V → M in ABK96805 (Ref. 6) Curated
Sequence conflicti846 – 8472KH → ND in AAA39809 (PubMed:3145094).Curated
Sequence conflicti846 – 8472KH → ND in CAA83229 (Ref. 3) Curated
Sequence conflicti846 – 8472KH → ND in ABK96805 (Ref. 6) Curated
Sequence conflicti846 – 8472KH → TV in AAA39813 (PubMed:3220257).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35131 mRNA. Translation: AAA39809.1.
M24496
, M23349, M24494, M24495 Genomic DNA. Translation: AAA39813.1. Different initiation.
Z31012 Genomic DNA. Translation: CAA83229.1. Different initiation.
AL645522 Genomic DNA. Translation: CAI25933.1.
EF101556 mRNA. Translation: ABK96805.1.
CCDSiCCDS36099.1.
PIRiJT0368. QFMSH.
RefSeqiNP_035034.2. NM_010904.3.
UniGeneiMm.298283.

Genome annotation databases

EnsembliENSMUST00000093369; ENSMUSP00000091061; ENSMUSG00000020396.
GeneIDi380684.
KEGGimmu:380684.
UCSCiuc007hvm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35131 mRNA. Translation: AAA39809.1.
M24496
, M23349, M24494, M24495 Genomic DNA. Translation: AAA39813.1. Different initiation.
Z31012 Genomic DNA. Translation: CAA83229.1. Different initiation.
AL645522 Genomic DNA. Translation: CAI25933.1.
EF101556 mRNA. Translation: ABK96805.1.
CCDSiCCDS36099.1.
PIRiJT0368. QFMSH.
RefSeqiNP_035034.2. NM_010904.3.
UniGeneiMm.298283.

3D structure databases

DisProtiDP00050.
ProteinModelPortaliP19246.
SMRiP19246. Positions 333-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237594. 4 interactions.
IntActiP19246. 2 interactions.
MINTiMINT-4103546.
STRINGi10090.ENSMUSP00000091061.

PTM databases

iPTMnetiP19246.
PhosphoSiteiP19246.

2D gel databases

UCD-2DPAGEP19246.

Proteomic databases

EPDiP19246.
MaxQBiP19246.
PaxDbiP19246.
PeptideAtlasiP19246.
PRIDEiP19246.

Protocols and materials databases

DNASUi380684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000093369; ENSMUSP00000091061; ENSMUSG00000020396.
GeneIDi380684.
KEGGimmu:380684.
UCSCiuc007hvm.1. mouse.

Organism-specific databases

CTDi4744.
MGIiMGI:97309. Nefh.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
GeneTreeiENSGT00830000128228.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP19246.
KOiK04574.
OMAiPMKEAKS.
OrthoDBiEOG7GQXVW.
PhylomeDBiP19246.
TreeFamiTF330122.

Miscellaneous databases

PROiP19246.
SOURCEiSearch...

Gene expression databases

BgeeiP19246.
CleanExiMM_NEFH.
GenevisibleiP19246. MM.

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. 14 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. "The structure of the largest murine neurofilament protein (NF-H) as revealed by cDNA and genomic sequences."
    Shneidman P.S., Carden M.J., Lees J.F., Lazzarini R.A.
    Brain Res. 464:217-231(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster.
    Tissue: Brain.
  2. "Sequence and structure of the mouse gene coding for the largest neurofilament subunit."
    Julien J.-P., Cote F., Beaudet L., Sidky M., Flavell D., Grosveld F., Mushynski W.
    Gene 68:307-314(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Carden M.J.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Swiss Webster.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Lubec G., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 167-180; 351-370; 382-401 AND 903-917, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Novel metastatic mouse tumor cells express multiple properties of macrophages."
    Huysentruyt L.C., Banerjee D., Seyfried T.N.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 814-961.
    Strain: VM.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-529; SER-535; SER-547; SER-559; SER-565; SER-571; SER-577; SER-589; SER-601; SER-607; SER-613; SER-619; SER-625; SER-631; SER-637; SER-655; SER-661; SER-667; SER-673; SER-679; SER-685; SER-697; SER-703; SER-709; SER-715; SER-727; SER-733; SER-739; SER-745; SER-751; SER-757; SER-763; SER-769; SER-783; SER-789; SER-815; SER-834; SER-867 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-122; SER-416; SER-419; SER-535; SER-541; SER-547; SER-553; SER-559; SER-565; SER-571; SER-583; SER-589; SER-595; SER-601; SER-607; SER-619; SER-631; SER-637; SER-643; SER-649; SER-655; SER-661; SER-667; SER-673; SER-679; SER-685; SER-691; SER-697; SER-703; SER-709; SER-727; SER-733; SER-739; SER-745; SER-751; SER-757; SER-763; SER-769; SER-795; SER-834 AND SER-859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiNFH_MOUSE
AccessioniPrimary (citable) accession number: P19246
Secondary accession number(s): A1E2H9, Q5SVF6, Q61959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 2, 2006
Last modified: July 6, 2016
This is version 154 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.