Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12036 (NFH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurofilament heavy polypeptide

Short name=NF-H
Alternative name(s):
200 kDa neurofilament protein
Neurofilament triplet H protein
Gene names
Name:NEFH
Synonyms:KIAA0845, NFH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1026 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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. Ref.7

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. Ref.7

Polymorphism

The number of repeats is shown to vary between 29 and 30.

Involvement in disease

Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence BAA74868.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAG63896.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentIntermediate filament
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon development

Inferred from mutant phenotype PubMed 7536898. Source: BHF-UCL

axonogenesis

Traceable author statement PubMed 17498690. Source: BHF-UCL

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell projection assembly

Traceable author statement PubMed 17498690. Source: BHF-UCL

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neurofilament bundle assembly

Inferred from mutant phenotype PubMed 7536898. Source: BHF-UCL

peripheral nervous system neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of organelle transport along microtubule

Inferred from mutant phenotype PubMed 7536898. Source: BHF-UCL

   Cellular_componentaxon

Traceable author statement PubMed 14662745. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neurofibrillary tangle

Inferred from direct assay PubMed 21828286. Source: BHF-UCL

neurofilament

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functiondynein binding

Traceable author statement PubMed 17498690. Source: BHF-UCL

kinesin binding

Traceable author statement PubMed 17498690. Source: BHF-UCL

microtubule binding

Traceable author statement PubMed 17498690. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction PubMed 9313898. Source: BHF-UCL

structural constituent of cytoskeleton

Traceable author statement. Source: BHF-UCL

structural molecule activity

Inferred from mutant phenotype PubMed 7536898. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12036-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P12036-2)

The sequence of this isoform differs from the canonical sequence as follows:
     750-812: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10261026Neurofilament heavy polypeptide
PRO_0000063800

Regions

Repeat525 – 53061
Repeat531 – 53662
Repeat539 – 54463
Repeat545 – 55064
Repeat559 – 56465
Repeat573 – 57866
Repeat579 – 58467
Repeat593 – 59868
Repeat599 – 60469
Repeat613 – 618610
Repeat627 – 632611
Repeat633 – 638612
Repeat647 – 652613
Repeat653 – 658614
Repeat667 – 672615
Repeat673 – 678616
Repeat681 – 686617
Repeat687 – 692618
Repeat695 – 700619
Repeat701 – 706620
Repeat709 – 714621
Repeat715 – 720622
Repeat723 – 728623
Repeat729 – 734624
Repeat743 – 748625
Repeat751 – 756626
Repeat768 – 773627
Repeat792 – 797628
Repeat800 – 805629
Repeat827 – 832630
Region1 – 100100Head
Region101 – 413313Rod
Region101 – 13232Coil 1A
Region133 – 14513Linker 1
Region146 – 24499Coil 1B
Region245 – 26622Linker 12
Region267 – 28822Coil 2A
Region289 – 2924Linker 2
Region293 – 413121Coil 2B
Region414 – 1026613Tail
Region525 – 83230830 X 6 AA repeats of K-S-P-[AEPV]-[EAK]-[AEVK]

Amino acid modifications

Modified residue5321Phosphoserine By similarity
Modified residue5461Phosphoserine By similarity
Modified residue5601Phosphoserine By similarity
Modified residue5661Phosphoserine By similarity
Modified residue5801Phosphoserine By similarity
Modified residue5941Phosphoserine By similarity
Modified residue6001Phosphoserine By similarity
Modified residue6061Phosphoserine By similarity
Modified residue6141Phosphoserine By similarity
Modified residue6201Phosphoserine By similarity
Modified residue6281Phosphoserine By similarity
Modified residue6341Phosphoserine By similarity
Modified residue6401Phosphoserine By similarity
Modified residue6481Phosphoserine By similarity
Modified residue6541Phosphoserine By similarity
Modified residue6601Phosphoserine By similarity
Modified residue6741Phosphoserine By similarity
Modified residue6821Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity
Modified residue6961Phosphoserine By similarity
Modified residue7021Phosphoserine By similarity
Modified residue7101Phosphoserine By similarity
Modified residue7241Phosphoserine By similarity
Modified residue7691Phosphoserine By similarity
Modified residue8011Phosphoserine By similarity
Modified residue8281Phosphoserine By similarity

Natural variations

Alternative sequence750 – 81263Missing in isoform 2.
VSP_036706
Natural variant5751P → S.
Corresponds to variant rs6006164 [ dbSNP | Ensembl ].
VAR_054787
Natural variant6151P → L.
Corresponds to variant rs5763269 [ dbSNP | Ensembl ].
VAR_056025
Natural variant7961Missing in ALS. Ref.8
VAR_023063
Natural variant8111E → A. Ref.1
Corresponds to variant rs165602 [ dbSNP | Ensembl ].
VAR_026163

Experimental info

Sequence conflict647 – 6526Missing in CAA33366. Ref.1
Sequence conflict647 – 6526Missing in AC000035. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 24, 2009. Version 4.
Checksum: 0879B6A08D208C17

FASTA1,026112,479
        10         20         30         40         50         60 
MMSFGGADAL LGAPFAPLHG GGSLHYALAR KGGAGGTRSA AGSSSGFHSW TRTSVSSVSA 

        70         80         90        100        110        120 
SPSRFRGAGA ASSTDSLDTL SNGPEGCMVA VATSRSEKEQ LQALNDRFAG YIDKVRQLEA 

       130        140        150        160        170        180 
HNRSLEGEAA ALRQQQAGRS AMGELYEREV REMRGAVLRL GAARGQLRLE QEHLLEDIAH 

       190        200        210        220        230        240 
VRQRLDDEAR QREEAEAAAR ALARFAQEAE AARVDLQKKA QALQEECGYL RRHHQEEVGE 

       250        260        270        280        290        300 
LLGQIQGSGA AQAQMQAETR DALKCDVTSA LREIRAQLEG HAVQSTLQSE EWFRVRLDRL 

       310        320        330        340        350        360 
SEAAKVNTDA MRSAQEEITE YRRQLQARTT ELEALKSTKD SLERQRSELE DRHQADIASY 

       370        380        390        400        410        420 
QEAIQQLDAE LRNTKWEMAA QLREYQDLLN VKMALDIEIA AYRKLLEGEE CRIGFGPIPF 

       430        440        450        460        470        480 
SLPEGLPKIP SVSTHIKVKS EEKIKVVEKS EKETVIVEEQ TEETQVTEEV TEEEEKEAKE 

       490        500        510        520        530        540 
EEGKEEEGGE EEEAEGGEEE TKSPPAEEAA SPEKEAKSPV KEEAKSPAEA KSPEKEEAKS 

       550        560        570        580        590        600 
PAEVKSPEKA KSPAKEEAKS PPEAKSPEKE EAKSPAEVKS PEKAKSPAKE EAKSPAEAKS 

       610        620        630        640        650        660 
PEKAKSPVKE EAKSPAEAKS PVKEEAKSPA EVKSPEKAKS PTKEEAKSPE KAKSPEKAKS 

       670        680        690        700        710        720 
PEKEEAKSPE KAKSPVKAEA KSPEKAKSPV KAEAKSPEKA KSPVKEEAKS PEKAKSPVKE 

       730        740        750        760        770        780 
EAKSPEKAKS PVKEEAKTPE KAKSPVKEEA KSPEKAKSPE KAKTLDVKSP EAKTPAKEEA 

       790        800        810        820        830        840 
RSPADKFPEK AKSPVKEEVK SPEKAKSPLK EDAKAPEKEI PKKEEVKSPV KEEEKPQEVK 

       850        860        870        880        890        900 
VKEPPKKAEE EKAPATPKTE EKKDSKKEEA PKKEAPKPKV EEKKEPAVEK PKESKVEAKK 

       910        920        930        940        950        960 
EEAEDKKKVP TPEKEAPAKV EVKEDAKPKE KTEVAKKEPD DAKAKEPSKP AEKKEAAPEK 

       970        980        990       1000       1010       1020 
KDTKEEKAKK PEEKPKTEAK AKEDDKTLSK EPSKPKAEKA EKSSSTDQKD SKPPEKATED 


KAAKGK 

« Hide

Isoform 2 [UniParc].

Checksum: 6E272AB8F3FBF5EA
Show »

FASTA963105,639

References

« Hide 'large scale' references
[1]"The structure and organization of the human heavy neurofilament subunit (NF-H) and the gene encoding it."
Lees J.F., Shneidman P.S., Skuntz S.F., Carden M.J., Lazzarini R.A.
EMBO J. 7:1947-1955(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-811.
[2]"Molecular Cloning of human hSTE cDNA."
Zhu Y., Han Y.
Beijing Yi Ke Da Xue Xue Bao 31:531-531(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 606-1026 (ISOFORM 2).
Tissue: Eye.
[7]"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(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PKN1.
[8]"Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis."
Figlewicz D.A., Krizus A., Martinoli M.G., Meininger V., Dib M., Rouleau G.A., Julien J.-P.
Hum. Mol. Genet. 3:1757-1761(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALS LYS-796 DEL.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15306 expand/collapse EMBL AC list , X15307, X15308, X15309 Genomic DNA. Translation: CAA33366.1.
AF203032 mRNA. Translation: AAF13722.1.
AB020652 mRNA. Translation: BAA74868.2. Different initiation.
AK302660 mRNA. Translation: BAG63896.1. Different initiation.
AC000035 Genomic DNA. No translation available.
BC008648 mRNA. Translation: AAH08648.1.
BC073969 mRNA. Translation: AAH73969.1.
PIRQFHUH. S00979.
RefSeqNP_066554.2. NM_021076.3.
UniGeneHs.198760.

3D structure databases

ProteinModelPortalP12036.
SMRP12036. Positions 93-245, 266-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110819. 28 interactions.
IntActP12036. 14 interactions.
STRING9606.ENSP00000311997.

PTM databases

PhosphoSiteP12036.

Polymorphism databases

DMDM226726294.

2D gel databases

UCD-2DPAGEP12036.

Proteomic databases

PaxDbP12036.
PRIDEP12036.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310624; ENSP00000311997; ENSG00000100285.
GeneID4744.
KEGGhsa:4744.
UCSCuc003afo.3. human. [P12036-2]

Organism-specific databases

CTD4744.
GeneCardsGC22P029876.
H-InvDBHIX0016351.
HGNCHGNC:7737. NEFH.
HPACAB007786.
MIM105400. phenotype.
162230. gene.
neXtProtNX_P12036.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA31540.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP12036.
KOK04574.
OrthoDBEOG7GQXVW.
PhylomeDBP12036.
TreeFamTF330122.

Gene expression databases

BgeeP12036.
CleanExHS_NEFH.
GenevestigatorP12036.

Family and domain databases

InterProIPR010790. DUF1388.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PfamPF07142. DUF1388. 3 hits.
PF00038. Filament. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi4744.
NextBio18288.
PROP12036.
SOURCESearch...

Entry information

Entry nameNFH_HUMAN
AccessionPrimary (citable) accession number: P12036
Secondary accession number(s): B4DYY4 expand/collapse secondary AC list , Q96HF8, Q9UJS7, Q9UQ14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM