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Q9NYP7 (ELOV5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation of very long chain fatty acids protein 5

EC=2.3.1.199
Alternative name(s):
3-keto acyl-CoA synthase ELOVL5
ELOVL fatty acid elongase 5
Short name=ELOVL FA elongase 5
Fatty acid elongase 1
Short name=hELO1
Very-long-chain 3-oxoacyl-CoA synthase 5
Gene names
Name:ELOVL5
Synonyms:ELOVL2
ORF Names:PRO0530
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Condensing enzyme that catalyzes the synthesis of monounsaturated and of polyunsaturated very long chain fatty acids Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. Ref.1 Ref.13

Catalytic activity

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

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.13.

Tissue specificity

Ubiquitous. Highly expressed in the adrenal gland and testis. Weakly expressed in prostate, lung and brain. Ref.1 Ref.13

Sequence similarities

Belongs to the ELO family.

Sequence caution

The sequence AAF16688.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC11178.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

fatty acid elongation, monounsaturated fatty acid

Inferred from direct assay PubMed 20427700. Source: UniProtKB

fatty acid elongation, polyunsaturated fatty acid

Inferred from direct assay PubMed 20427700Ref.13. Source: UniProtKB

linoleic acid metabolic process

Traceable author statement. Source: Reactome

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

unsaturated fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

very long-chain fatty acid biosynthetic process

Inferred from direct assay PubMed 20427700Ref.13. Source: UniProtKB

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionfatty acid elongase activity

Inferred from direct assay PubMed 20427700. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYP7-1)

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: Q9NYP7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     82-82: E → ESKREQPRRSACASRTDPSTQQQLPENR
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NYP7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     20-88: DTRVKGWFLL...MFCELVTGVW → GISSSVLRMG...LATIASHAPA
     89-299: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Elongation of very long chain fatty acids protein 5
PRO_0000282838

Regions

Transmembrane26 – 4621Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane139 – 15820Helical; Potential
Transmembrane168 – 18720Helical; Potential
Transmembrane205 – 22521Helical; Potential
Transmembrane226 – 24621Helical; Potential

Amino acid modifications

Modified residue2851Phosphoserine Ref.14

Natural variations

Alternative sequence20 – 8869DTRVK…VTGVW → GISSSVLRMGPPLHTVVGWL QQLQAAHSEEEEKMFHLCGF KHKEVVSQSSLPAVIPQNSL ATIASHAPA in isoform 3.
VSP_045917
Alternative sequence821E → ESKREQPRRSACASRTDPST QQQLPENR in isoform 2.
VSP_045918
Alternative sequence89 – 299211Missing in isoform 3.
VSP_045919

Experimental info

Sequence conflict591F → L in BAG64104. Ref.4
Sequence conflict167 – 26296YFGAT…GASRR → SVCADNHPDQLRGHLAVHIP SWLVVFPDWIHDFPDCSLHK LLHSDLQQERGLPKERPPEG PPEWVHGCCEWTHQQLFTPG KQCEAKEAAEGLKSKN in BAD93035. Ref.4
Sequence conflict204 – 2063QGQ → EFH in BAC11178. Ref.9
Sequence conflict2271F → S in BAC11178. Ref.9

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: AE5150AA3432E984

FASTA29935,293
        10         20         30         40         50         60 
MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP KYMRNKQPFS 

        70         80         90        100        110        120 
CRGILVVYNL GLTLLSLYMF CELVTGVWEG KYNFFCQGTR TAGESDMKII RVLWWYYFSK 

       130        140        150        160        170        180 
LIEFMDTFFF ILRKNNHQIT VLHVYHHASM LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM 

       190        200        210        220        230        240 
YSYYGLSSVP SMRPYLWWKK YITQGQLLQF VLTIIQTSCG VIWPCTFPLG WLYFQIGYMI 

       250        260        270        280        290 
SLIALFTNFY IQTYNKKGAS RRKDHLKDHQ NGSMAAVNGH TNSFSPLENN VKPRKLRKD 

« Hide

Isoform 2 [UniParc].

Checksum: DAFA9400ACB27FB1
Show »

FASTA32638,403
Isoform 3 [UniParc].

Checksum: 449F6D2F7A7E4BF1
Show »

FASTA889,580

References

« Hide 'large scale' references
[1]"Cloning of a human cDNA encoding a novel enzyme involved in the elongation of long-chain polyunsaturated fatty acids."
Leonard A.E., Bobik E.G., Dorado J., Kroeger P.E., Chuang L.-T., Thurmond J.M., Parker-Barnes J.M., Das T., Huang Y.-S., Mukerji P.
Biochem. J. 350:765-770(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
Tissue: Liver.
[2]"Homo sapiens mRNA for elongation of very long chain fatty acids (FEN1/Elo2, SUR4/Elo3, yeast)-like 2 (ELOVL2)."
Suzuki T., Nitta A., Morita R., Sugimoto Y., Yamakawa K.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[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] (ISOFORMS 1 AND 2).
Tissue: Testis.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1 AND 3).
Tissue: Eye, Leiomyosarcoma and Skin.
[9]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-299 (ISOFORM 1).
[10]Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhang Y., Liu M., He F.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-299 (ISOFORM 1).
Tissue: Liver.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis."
Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y., Sassa T., Kihara A.
Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF231981 mRNA. Translation: AAF70631.1.
AF338241 mRNA. Translation: AAM00193.1.
AL136939 mRNA. Translation: CAB66873.1.
AK074889 mRNA. Translation: BAC11270.1.
AK302948 mRNA. Translation: BAG64104.1.
AB209798 mRNA. Translation: BAD93035.1.
AL034374 Genomic DNA. Translation: CAI21530.1.
AL034374 Genomic DNA. Translation: CAI21531.1.
CH471081 Genomic DNA. Translation: EAX04419.1.
BC017270 mRNA. Translation: AAH17270.2.
BC067123 mRNA. Translation: AAH67123.2.
BC074503 mRNA. No translation available.
AK074748 mRNA. Translation: BAC11178.1. Different initiation.
AF111849 mRNA. Translation: AAF16688.1. Different initiation.
RefSeqNP_001229757.1. NM_001242828.1.
NP_001229759.1. NM_001242830.1.
NP_001229760.1. NM_001242831.1.
NP_068586.1. NM_021814.4.
XP_005249323.1. XM_005249266.1.
XP_005249324.1. XM_005249267.1.
UniGeneHs.520189.

3D structure databases

ProteinModelPortalQ9NYP7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121914. 3 interactions.
STRING9606.ENSP00000306640.

Chemistry

BindingDBQ9NYP7.
ChEMBLCHEMBL5937.

PTM databases

PhosphoSiteQ9NYP7.

Polymorphism databases

DMDM74753072.

Proteomic databases

PaxDbQ9NYP7.
PeptideAtlasQ9NYP7.
PRIDEQ9NYP7.

Protocols and materials databases

DNASU60481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304434; ENSP00000306640; ENSG00000012660. [Q9NYP7-1]
ENST00000370913; ENSP00000359951; ENSG00000012660. [Q9NYP7-3]
ENST00000541407; ENSP00000438095; ENSG00000012660. [Q9NYP7-2]
ENST00000542638; ENSP00000440728; ENSG00000012660. [Q9NYP7-1]
GeneID60481.
KEGGhsa:60481.
UCSCuc003pbq.1. human. [Q9NYP7-1]
uc003pbu.3. human.

Organism-specific databases

CTD60481.
GeneCardsGC06M053132.
HGNCHGNC:21308. ELOVL5.
HPACAB017042.
HPA047752.
MIM611805. gene.
neXtProtNX_Q9NYP7.
PharmGKBPA128394703.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305096.
HOGENOMHOG000038120.
HOVERGENHBG051468.
KOK10244.
OMAELWPIFD.
OrthoDBEOG7Z3F4V.
PhylomeDBQ9NYP7.
TreeFamTF323454.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000012660-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00658.

Gene expression databases

ArrayExpressQ9NYP7.
BgeeQ9NYP7.
CleanExHS_ELOVL2.
HS_ELOVL5.
GenevestigatorQ9NYP7.

Family and domain databases

InterProIPR002076. GNS1_SUR4.
[Graphical view]
PANTHERPTHR11157. PTHR11157. 1 hit.
PfamPF01151. ELO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSELOVL5. human.
GeneWikiELOVL5.
GenomeRNAi60481.
NextBio65351.
PROQ9NYP7.
SOURCESearch...

Entry information

Entry nameELOV5_HUMAN
AccessionPrimary (citable) accession number: Q9NYP7
Secondary accession number(s): B4DZJ2 expand/collapse secondary AC list , F6SH78, Q59EL3, Q5TGH5, Q6NXE7, Q7L2S5, Q8NCG4, Q9UI22
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 103 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM