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Protein

Elongation of very long chain fatty acids protein 4

Gene

ELOVL4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that specifically elongates C24:0 and C26:0 acyl-CoAs. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development.1 Publication

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.1 Publication

Pathwayi

GO - Molecular functioni

  • G-protein coupled photoreceptor activity Source: UniProtKB
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • cellular lipid metabolic process Source: Reactome
  • detection of visible light Source: GOC
  • fatty acid biosynthetic process Source: UniProtKB
  • fatty acid elongation, saturated fatty acid Source: UniProtKB
  • long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  • small molecule metabolic process Source: Reactome
  • triglyceride biosynthetic process Source: Reactome
  • very long-chain fatty acid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000118402-MONOMER.
ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 4Curated (EC:2.3.1.1991 Publication)
Alternative name(s):
3-keto acyl-CoA synthase ELOVL4
ELOVL fatty acid elongase 4
Short name:
ELOVL FA elongase 4
Very-long-chain 3-oxoacyl-CoA synthase 4
Gene namesi
Name:ELOVL4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14415. ELOVL4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei42 – 6221HelicalSequence AnalysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence AnalysisAdd
BLAST
Transmembranei188 – 20821HelicalSequence AnalysisAdd
BLAST
Transmembranei247 – 26721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Stargardt disease 3 (STGD3)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina.

See also OMIM:600110
Ichthyosis, spastic quadriplegia, and mental retardation (ISQMR)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA severe autosomal recessive disorder characterized by ichthyosis apparent from birth, profound psychomotor retardation with essentially no development, spastic quadriplegia, and seizures.

See also OMIM:614457
Spinocerebellar ataxia 34 (SCA34)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA34 is an autosomal dominant form characterized by the association of progressive cerebellar ataxia with erythrokeratodermia variabilis.

See also OMIM:133190
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681L → F in SCA34. 1 Publication
VAR_072565

Keywords - Diseasei

Disease mutation, Ichthyosis, Mental retardation, Neurodegeneration, Spinocerebellar ataxia, Stargardt disease

Organism-specific databases

MIMi133190. phenotype.
600110. phenotype.
614457. phenotype.
Orphaneti352333. Congenital ichthyosis - intellectual disability - spastic quadriplegia.
1955. Spinocerebellar ataxia type 34.
827. Stargardt disease.
PharmGKBiPA27763.

Chemistry

DrugBankiDB00132. Alpha-Linolenic Acid.

Polymorphism and mutation databases

BioMutaiELOVL4.
DMDMi20137966.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Elongation of very long chain fatty acids protein 4PRO_0000207542Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi20 – 201N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9GZR5.
PRIDEiQ9GZR5.

PTM databases

PhosphoSiteiQ9GZR5.

Expressioni

Tissue specificityi

Expressed in the retina and at much lower level in the brain. Ubiquitous, highest expression in thymus, followed by testis, small intestine, ovary, and prostate. Little or no expression in heart, lung, liver, or leukocates.1 Publication

Gene expression databases

BgeeiQ9GZR5.
CleanExiHS_ELOVL4.
GenevestigatoriQ9GZR5.

Interactioni

Subunit structurei

Oligomer.1 Publication

Protein-protein interaction databases

BioGridi112661. 8 interactions.
STRINGi9606.ENSP00000358831.

Structurei

3D structure databases

ProteinModelPortaliQ9GZR5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi310 – 3145Di-lysine motifSequence Analysis

Domaini

The di-lysine motif may confer endoplasmic reticulum localization.By similarity

Sequence similaritiesi

Belongs to the ELO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9GZR5.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9GZR5.
TreeFamiTF323454.

Family and domain databases

InterProiIPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GZR5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL
60 70 80 90 100
SISTLYLLFV WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG
110 120 130 140 150
SYNAGYSYIC QSVDYSNNVH EVRIAAALWW YFVSKGVEYL DTVFFILRKK
160 170 180 190 200
NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ AFFGAQLNSF IHVIMYSYYG
210 220 230 240 250
LTAFGPWIQK YLWWKRYLTM LQLIQFHVTI GHTALSLYTD CPFPKWMHWA
260 270 280 290 300
LIAYAISFIF LFLNFYIRTY KEPKKPKAGK TAMNGISANG VSKSEKQLMI
310
ENGKKQKNGK AKGD
Length:314
Mass (Da):36,829
Last modified:March 1, 2001 - v1
Checksum:iB2EBCE54D868E96E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441Q → R in AAH38506 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681L → F in SCA34. 1 Publication
VAR_072565
Natural varianti267 – 2671I → T.1 Publication
Corresponds to variant rs148594713 [ dbSNP | Ensembl ].
VAR_017043
Natural varianti299 – 2991M → V.2 Publications
Corresponds to variant rs3812153 [ dbSNP | Ensembl ].
VAR_012492

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279654
, AF279649, AF279650, AF279651, AF279652, AF279653 Genomic DNA. Translation: AAG47669.1.
AF277094 mRNA. Translation: AAG47668.1.
AY037298 mRNA. Translation: AAK68639.1.
AK055277 mRNA. Translation: BAB70895.1.
AK312511 mRNA. Translation: BAG35412.1.
AL133475, AL132875 Genomic DNA. Translation: CAI20320.1.
AL132875, AL133475 Genomic DNA. Translation: CAI23374.1.
CH471051 Genomic DNA. Translation: EAW48701.1.
BC038506 mRNA. Translation: AAH38506.1.
CCDSiCCDS4992.1.
RefSeqiNP_073563.1. NM_022726.3.
UniGeneiHs.101915.

Genome annotation databases

EnsembliENST00000369816; ENSP00000358831; ENSG00000118402.
GeneIDi6785.
KEGGihsa:6785.
UCSCiuc003pja.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the ELOVL4 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279654
, AF279649, AF279650, AF279651, AF279652, AF279653 Genomic DNA. Translation: AAG47669.1.
AF277094 mRNA. Translation: AAG47668.1.
AY037298 mRNA. Translation: AAK68639.1.
AK055277 mRNA. Translation: BAB70895.1.
AK312511 mRNA. Translation: BAG35412.1.
AL133475, AL132875 Genomic DNA. Translation: CAI20320.1.
AL132875, AL133475 Genomic DNA. Translation: CAI23374.1.
CH471051 Genomic DNA. Translation: EAW48701.1.
BC038506 mRNA. Translation: AAH38506.1.
CCDSiCCDS4992.1.
RefSeqiNP_073563.1. NM_022726.3.
UniGeneiHs.101915.

3D structure databases

ProteinModelPortaliQ9GZR5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112661. 8 interactions.
STRINGi9606.ENSP00000358831.

Chemistry

DrugBankiDB00132. Alpha-Linolenic Acid.

PTM databases

PhosphoSiteiQ9GZR5.

Polymorphism and mutation databases

BioMutaiELOVL4.
DMDMi20137966.

Proteomic databases

PaxDbiQ9GZR5.
PRIDEiQ9GZR5.

Protocols and materials databases

DNASUi6785.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369816; ENSP00000358831; ENSG00000118402.
GeneIDi6785.
KEGGihsa:6785.
UCSCiuc003pja.4. human.

Organism-specific databases

CTDi6785.
GeneCardsiGC06M080624.
HGNCiHGNC:14415. ELOVL4.
MIMi133190. phenotype.
600110. phenotype.
605512. gene.
614457. phenotype.
neXtProtiNX_Q9GZR5.
Orphaneti352333. Congenital ichthyosis - intellectual disability - spastic quadriplegia.
1955. Spinocerebellar ataxia type 34.
827. Stargardt disease.
PharmGKBiPA27763.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9GZR5.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9GZR5.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:ENSG00000118402-MONOMER.
ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

GeneWikiiELOVL4.
GenomeRNAii6785.
NextBioi26492.
PROiQ9GZR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZR5.
CleanExiHS_ELOVL4.
GenevestigatoriQ9GZR5.

Family and domain databases

InterProiIPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT VAL-299, DISEASE.
    Tissue: Retina.
  2. "A novel gene for autosomal dominant Stargardt-like macular dystrophy with homology to the SUR4 protein family."
    Edwards A.O., Donoso L.A., Ritter R. III
    Invest. Ophthalmol. Vis. Sci. 42:2652-2663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
    , 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].
    Tissue: Brain and Thalamus.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Brain.
  7. "Dominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4."
    Grayson C., Molday R.S.
    J. Biol. Chem. 280:32521-32530(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, OLIGOMERIZATION, GLYCOSYLATION AT ASN-20.
  8. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Recessive mutations in ELOVL4 cause ichthyosis, intellectual disability, and spastic quadriplegia."
    Aldahmesh M.A., Mohamed J.Y., Alkuraya H.S., Verma I.C., Puri R.D., Alaiya A.A., Rizzo W.B., Alkuraya F.S.
    Am. J. Hum. Genet. 89:745-750(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE ROLE IN BRAIN AND SKIN DEVELOPMENT, INVOLVEMENT IN ISQMR.
  10. "Evaluation of the ELOVL4 gene in patients with autosomal recessive retinitis pigmentosa and Leber congenital amaurosis."
    Rivolta C., Ayyagari R., Sieving P.A., Berson E.L., Dryja T.P.
    Mol. Vis. 9:49-51(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-267 AND VAL-299.
  11. "Expanding the clinical phenotype associated with ELOVL4 mutation: study of a large French-Canadian family with autosomal dominant spinocerebellar ataxia and erythrokeratodermia."
    Cadieux-Dion M., Turcotte-Gauthier M., Noreau A., Martin C., Meloche C., Gravel M., Drouin C.A., Rouleau G.A., Nguyen D.K., Cossette P.
    JAMA Neurol. 71:470-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SCA34, VARIANT SCA34 PHE-168.

Entry informationi

Entry nameiELOV4_HUMAN
AccessioniPrimary (citable) accession number: Q9GZR5
Secondary accession number(s): B2R6B5
, Q5TCS2, Q86YJ1, Q9H139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.