UniProtKB - Q9GZR5 (ELOV4_HUMAN)
Protein
Elongation of very long chain fatty acids protein 4
Gene
ELOVL4
Organism
Homo sapiens (Human)
Status
Functioni
Catalyzes the first and rate-limiting reaction of the four reactions 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 catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids 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.UniRule annotation2 Publications
Catalytic activityi
- a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoAUniRule annotation1 PublicationEC:2.3.1.199UniRule annotation1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (19Z,22Z,25Z,28Z,31Z)-tetratriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(21Z,24Z,27Z,30Z,33Z)-hexatriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + H+ + malonyl-CoA = (9Z,12Z,15Z,18Z)-3-oxotetracosatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11Z,14Z,17Z,20Z,23Z)-hexacosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(13Z,16Z,19Z,22Z,25Z)-octacosapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (13Z,16Z,19Z,22Z,25Z)-octacosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(15Z,18Z,21Z,24Z,27Z)-triacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (15Z,18Z,21Z,24Z,27Z)-triacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(17Z,20Z,23Z,26Z,29Z)-dotriacontapentaenoyl-CoA + CO2 + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (17Z,20Z,23Z,26Z,29Z)-dotriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(19Z,22Z,25Z,28Z,31Z)-tetratriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (21Z,24Z,27Z,30Z,33Z)-hexatriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(23Z,26Z,29Z,32Z,35Z)-octatriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11Z,14Z,17Z,20Z)-hexacosatetraenoyl-CoA + H+ + malonyl-CoA = (13Z,16Z,19Z,22Z)-3-oxooctacosatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (13Z,16Z,19Z,22Z)-octacosatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(15Z,18Z,21Z,24Z)-triacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (15Z,18Z,21Z,24Z)-triacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(17Z,20Z,23Z,26Z)-dotriacontatetraenoyl-CoA + CO2 + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (17Z,20Z,23Z,26Z)-dotriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(19Z,22Z,25Z,28Z)-tetratriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (19Z,22Z,25Z,28Z)-tetratriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(21Z,24Z,27Z,30Z)-hexatriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (21Z,24Z,27Z,30Z)-hexatriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(23Z,26Z,29Z,32Z)-octatriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(8Z,11Z,14Z,17Z,20Z,23Z)-hexacosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (8Z,11Z,14Z,17Z,20Z,23Z)-hexacosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(10Z,13Z,16Z,19Z,22Z,25Z)-octacosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (10Z,13Z,16Z,19Z,22Z,25Z)-octacosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(12Z,15Z,18Z,21Z,24Z,27Z)-triacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (12Z,15Z,18Z,21Z,24Z,27Z)-triacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(14Z,17Z,20Z,23Z,26Z,29Z)-dotriacontahexaenoyl-CoA + CO2 + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14Z,17Z,20Z,23Z,26Z,29Z)-dotriacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(16Z,19Z,22Z,25Z,28Z,31Z)-tetratriacontahexaenoyl-CoA + CO2 + CoA1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (16Z,19Z,22Z,25Z,28Z,31Z)-tetratriacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(18Z,21Z,24Z,27Z,30Z,33Z)-hexatriacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(11Z,14Z,17Z,20Z,23Z)-hexacosapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation2 PublicationsView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
GO - Molecular functioni
- 3-oxo-arachidoyl-CoA synthase activity Source: UniProtKB-EC
- 3-oxo-cerotoyl-CoA synthase activity Source: UniProtKB-EC
- 3-oxo-lignoceronyl-CoA synthase activity Source: UniProtKB-EC
- fatty acid elongase activity Source: UniProtKB
- G protein-coupled photoreceptor activity Source: UniProtKB
- very-long-chain 3-ketoacyl-CoA synthase activity Source: UniProtKB-EC
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB
- fatty acid elongation, monounsaturated fatty acid Source: GO_Central
- fatty acid elongation, polyunsaturated fatty acid Source: UniProtKB
- fatty acid elongation, saturated fatty acid Source: UniProtKB
- long-chain fatty-acyl-CoA biosynthetic process Source: UniProtKB-UniRule
- sphingolipid biosynthetic process Source: GO_Central
- unsaturated fatty acid biosynthetic process Source: UniProtKB-UniRule
- very long-chain fatty acid biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000118402-MONOMER |
PathwayCommonsi | Q9GZR5 |
Reactomei | R-HSA-75876, Synthesis of very long-chain fatty acyl-CoAs |
UniPathwayi | UPA00094 |
Chemistry databases
SwissLipidsi | SLP:000000255 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation of very long chain fatty acids protein 4UniRule annotationCurated (EC:2.3.1.199UniRule annotation2 Publications)Alternative name(s): 3-keto acyl-CoA synthase ELOVL4UniRule annotation ELOVL fatty acid elongase 4UniRule annotation Short name: ELOVL FA elongase 4UniRule annotation Very long chain 3-ketoacyl-CoA synthase 4UniRule annotation Very long chain 3-oxoacyl-CoA synthase 4UniRule annotation |
Gene namesi | Name:ELOVL4UniRule annotation |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000118402.5 |
HGNCi | HGNC:14415, ELOVL4 |
MIMi | 605512, gene |
neXtProti | NX_Q9GZR5 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation2 Publications; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- integral component of endoplasmic reticulum membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 42 – 62 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 78 – 98 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 127 – 147 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 165 – 185 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 188 – 208 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 217 – 237 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 247 – 267 | HelicalUniRule annotationAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePathology & Biotechi
Involvement in diseasei
Stargardt disease 3 (STGD3)2 Publications
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.
Related information in OMIMIchthyosis, 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.
Related information in OMIMSpinocerebellar 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072565 | 168 | L → F in SCA34. 1 PublicationCorresponds to variant dbSNP:rs587777598EnsemblClinVar. | 1 |
Keywords - Diseasei
Disease mutation, Ichthyosis, Mental retardation, Neurodegeneration, Spinocerebellar ataxia, Stargardt diseaseOrganism-specific databases
DisGeNETi | 6785 |
MalaCardsi | ELOVL4 |
MIMi | 133190, phenotype 600110, phenotype 614457, phenotype |
OpenTargetsi | ENSG00000118402 |
Orphaneti | 352333, Congenital ichthyosis-intellectual disability-spastic quadriplegia syndrome 1955, Spinocerebellar ataxia type 34 827, Stargardt disease |
PharmGKBi | PA27763 |
Miscellaneous databases
Pharosi | Q9GZR5, Tbio |
Chemistry databases
DrugBanki | DB09568, Omega-3-carboxylic acids DB09328, Vayarin |
Polymorphism and mutation databases
BioMutai | ELOVL4 |
DMDMi | 20137966 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207542 | 1 – 314 | Elongation of very long chain fatty acids protein 4Add BLAST | 314 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 20 | N-linked (GlcNAc...) asparagineUniRule annotation1 Publication | 1 |
Post-translational modificationi
N-glycosylated.By similarity
Keywords - PTMi
GlycoproteinProteomic databases
EPDi | Q9GZR5 |
MassIVEi | Q9GZR5 |
PaxDbi | Q9GZR5 |
PeptideAtlasi | Q9GZR5 |
PRIDEi | Q9GZR5 |
ProteomicsDBi | 80120 |
PTM databases
GlyGeni | Q9GZR5, 1 site |
iPTMneti | Q9GZR5 |
PhosphoSitePlusi | Q9GZR5 |
SwissPalmi | Q9GZR5 |
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
Bgeei | ENSG00000118402, Expressed in mammalian vulva and 196 other tissues |
Genevisiblei | Q9GZR5, HS |
Organism-specific databases
HPAi | ENSG00000118402, Tissue enhanced (lymphoid tissue, skin) |
Interactioni
Subunit structurei
Oligomer.
UniRule annotation1 PublicationBinary interactionsi
Q9GZR5
Protein-protein interaction databases
BioGRIDi | 112661, 104 interactors |
IntActi | Q9GZR5, 94 interactors |
STRINGi | 9606.ENSP00000358831 |
Miscellaneous databases
RNActi | Q9GZR5, protein |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 310 – 314 | Di-lysine motifUniRule annotation | 5 |
Domaini
The C-terminal di-lysine motif confers endoplasmic reticulum localization.UniRule annotation
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q9GZR5 |
OMAi | SIYIDCP |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9GZR5 |
TreeFami | TF323454 |
Family and domain databases
HAMAPi | MF_03204, VLCF_elongase_4, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033678, ELOVL4 |
PANTHERi | PTHR11157, PTHR11157, 1 hit |
Pfami | View protein in Pfam PF01151, ELO, 1 hit |
PROSITEi | View protein in PROSITE PS01188, ELO, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9GZR5-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 44 | Q → R in AAH38506 (PubMed:15489334).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_072565 | 168 | L → F in SCA34. 1 PublicationCorresponds to variant dbSNP:rs587777598EnsemblClinVar. | 1 | |
Natural variantiVAR_017043 | 267 | I → T1 PublicationCorresponds to variant dbSNP:rs148594713EnsemblClinVar. | 1 | |
Natural variantiVAR_012492 | 299 | M → V2 PublicationsCorresponds to variant dbSNP:rs3812153EnsemblClinVar. | 1 |
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 Genomic DNA No translation available. AL132875 Genomic DNA No translation available. CH471051 Genomic DNA Translation: EAW48701.1 BC038506 mRNA Translation: AAH38506.1 |
CCDSi | CCDS4992.1 |
RefSeqi | NP_073563.1, NM_022726.3 |
Genome annotation databases
Ensembli | ENST00000369816; ENSP00000358831; ENSG00000118402 |
GeneIDi | 6785 |
KEGGi | hsa:6785 |
UCSCi | uc003pja.5, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
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 Genomic DNA No translation available. AL132875 Genomic DNA No translation available. CH471051 Genomic DNA Translation: EAW48701.1 BC038506 mRNA Translation: AAH38506.1 |
CCDSi | CCDS4992.1 |
RefSeqi | NP_073563.1, NM_022726.3 |
3D structure databases
SMRi | Q9GZR5 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 112661, 104 interactors |
IntActi | Q9GZR5, 94 interactors |
STRINGi | 9606.ENSP00000358831 |
Chemistry databases
DrugBanki | DB09568, Omega-3-carboxylic acids DB09328, Vayarin |
SwissLipidsi | SLP:000000255 |
PTM databases
GlyGeni | Q9GZR5, 1 site |
iPTMneti | Q9GZR5 |
PhosphoSitePlusi | Q9GZR5 |
SwissPalmi | Q9GZR5 |
Polymorphism and mutation databases
BioMutai | ELOVL4 |
DMDMi | 20137966 |
Proteomic databases
EPDi | Q9GZR5 |
MassIVEi | Q9GZR5 |
PaxDbi | Q9GZR5 |
PeptideAtlasi | Q9GZR5 |
PRIDEi | Q9GZR5 |
ProteomicsDBi | 80120 |
Protocols and materials databases
Antibodypediai | 31608, 232 antibodies |
DNASUi | 6785 |
Genome annotation databases
Ensembli | ENST00000369816; ENSP00000358831; ENSG00000118402 |
GeneIDi | 6785 |
KEGGi | hsa:6785 |
UCSCi | uc003pja.5, human |
Organism-specific databases
CTDi | 6785 |
DisGeNETi | 6785 |
EuPathDBi | HostDB:ENSG00000118402.5 |
GeneCardsi | ELOVL4 |
HGNCi | HGNC:14415, ELOVL4 |
HPAi | ENSG00000118402, Tissue enhanced (lymphoid tissue, skin) |
MalaCardsi | ELOVL4 |
MIMi | 133190, phenotype 600110, phenotype 605512, gene 614457, phenotype |
neXtProti | NX_Q9GZR5 |
OpenTargetsi | ENSG00000118402 |
Orphaneti | 352333, Congenital ichthyosis-intellectual disability-spastic quadriplegia syndrome 1955, Spinocerebellar ataxia type 34 827, Stargardt disease |
PharmGKBi | PA27763 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q9GZR5 |
OMAi | SIYIDCP |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9GZR5 |
TreeFami | TF323454 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
BioCyci | MetaCyc:ENSG00000118402-MONOMER |
PathwayCommonsi | Q9GZR5 |
Reactomei | R-HSA-75876, Synthesis of very long-chain fatty acyl-CoAs |
Miscellaneous databases
BioGRID-ORCSi | 6785, 26 hits in 841 CRISPR screens |
GeneWikii | ELOVL4 |
GenomeRNAii | 6785 |
Pharosi | Q9GZR5, Tbio |
PROi | PR:Q9GZR5 |
RNActi | Q9GZR5, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000118402, Expressed in mammalian vulva and 196 other tissues |
Genevisiblei | Q9GZR5, HS |
Family and domain databases
HAMAPi | MF_03204, VLCF_elongase_4, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033678, ELOVL4 |
PANTHERi | PTHR11157, PTHR11157, 1 hit |
Pfami | View protein in Pfam PF01151, ELO, 1 hit |
PROSITEi | View protein in PROSITE PS01188, ELO, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ELOV4_HUMAN | |
Accessioni | Q9GZR5Primary (citable) accession number: Q9GZR5 Secondary accession number(s): B2R6B5 Q9H139 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 23, 2002 |
Last sequence update: | March 1, 2001 | |
Last modified: | December 2, 2020 | |
This is version 174 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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
Reference proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations