Q9NYP7 (ELOV5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alpha-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 very long-chain fatty acid biosynthetic process Inferred from direct assay PubMed 20427700Ref.13. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	fatty 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 299	299	Elongation of very long chain fatty acids protein 5		PRO_0000282838
Regions
	Transmembrane	26 – 46	21	Helical; Potential
	Transmembrane	64 – 84	21	Helical; Potential
	Transmembrane	112 – 132	21	Helical; Potential
	Transmembrane	139 – 158	20	Helical; Potential
	Transmembrane	168 – 187	20	Helical; Potential
	Transmembrane	205 – 225	21	Helical; Potential
	Transmembrane	226 – 246	21	Helical; Potential
Amino acid modifications
	Modified residue	273	1	Phosphoserine By similarity
	Modified residue	281	1	Phosphothreonine By similarity
	Modified residue	283	1	Phosphoserine By similarity
	Modified residue	285	1	Phosphoserine Ref.14
Natural variations
	Alternative sequence	20 – 88	69	DTRVK…VTGVW → GISSSVLRMGPPLHTVVGWL QQLQAAHSEEEEKMFHLCGF KHKEVVSQSSLPAVIPQNSL ATIASHAPA in isoform 3.		VSP_045917
	Alternative sequence	82	1	E → ESKREQPRRSACASRTDPST QQQLPENR in isoform 2.		VSP_045918
	Alternative sequence	89 – 299	211	Missing in isoform 3.		VSP_045919
Experimental info
	Sequence conflict	59	1	F → L in BAG64104. Ref.4
	Sequence conflict	167 – 262	96	YFGAT…GASRR → SVCADNHPDQLRGHLAVHIP SWLVVFPDWIHDFPDCSLHK LLHSDLQQERGLPKERPPEG PPEWVHGCCEWTHQQLFTPG KQCEAKEAAEGLKSKN in BAD93035. Ref.4
	Sequence conflict	204 – 206	3	QGQ → EFH in BAC11178. Ref.9
	Sequence conflict	227	1	F → S in BAC11178. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: AE5150AA3432E984	FASTA	299	35,293
	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
	Isoform 2 [UniParc]. Checksum: DAFA9400ACB27FB1	FASTA	326	38,403
	10 20 30 40 50 60 MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP KYMRNKQPFS 70 80 90 100 110 120 CRGILVVYNL GLTLLSLYMF CESKREQPRR SACASRTDPS TQQQLPENRL VTGVWEGKYN 130 140 150 160 170 180 FFCQGTRTAG ESDMKIIRVL WWYYFSKLIE FMDTFFFILR KNNHQITVLH VYHHASMLNI 190 200 210 220 230 240 WWFVMNWVPC GHSYFGATLN SFIHVLMYSY YGLSSVPSMR PYLWWKKYIT QGQLLQFVLT 250 260 270 280 290 300 IIQTSCGVIW PCTFPLGWLY FQIGYMISLI ALFTNFYIQT YNKKGASRRK DHLKDHQNGS 310 320 MAAVNGHTNS FSPLENNVKP RKLRKD
	Isoform 3 [UniParc]. Checksum: 449F6D2F7A7E4BF1	FASTA	88	9,580
	10 20 30 40 50 60 MEHFDASLST YFKALLGPRG ISSSVLRMGP PLHTVVGWLQ QLQAAHSEEE EKMFHLCGFK 70 80 HKEVVSQSSL PAVIPQNSLA TIASHAPA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00328307. IPI00513972. IPI00910962.
RefSeq	NP_001229757.1. NM_001242828.1. NP_001229759.1. NM_001242830.1. NP_001229760.1. NM_001242831.1. NP_068586.1. NM_021814.4.
UniGene	Hs.520189.
3D structure databases
ProteinModelPortal	Q9NYP7.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000306640.
PTM databases
PhosphoSite	Q9NYP7.
Polymorphism databases
DMDM	74753072.
Proteomic databases
PaxDb	Q9NYP7.
PeptideAtlas	Q9NYP7.
PRIDE	Q9NYP7.
Protocols and materials databases
DNASU	60481.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304434; ENSP00000306640; ENSG00000012660. ENST00000370913; ENSP00000359951; ENSG00000012660. ENST00000541407; ENSP00000438095; ENSG00000012660. ENST00000542638; ENSP00000440728; ENSG00000012660.
GeneID	60481.
KEGG	hsa:60481.
UCSC	uc003pbq.1. human.
Organism-specific databases
CTD	60481.
GeneCards	GC06M053132.
HGNC	HGNC:21308. ELOVL5.
HPA	CAB017042.
MIM	611805. gene.
neXtProt	NX_Q9NYP7.
PharmGKB	PA128394703.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG305096.
HOGENOM	HOG000038120.
HOVERGEN	HBG051468.
KO	K10244.
OrthoDB	EOG4J118X.
PhylomeDB	Q9NYP7.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000012660-MONOMER.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9NYP7.
Bgee	Q9NYP7.
CleanEx	HS_ELOVL2. HS_ELOVL5.
Genevestigator	Q9NYP7.
Family and domain databases
InterPro	IPR002076. GNS1_SUR4. [Graphical view]
PANTHER	PTHR11157. PTHR11157. 1 hit.
Pfam	PF01151. ELO. 1 hit. [Graphical view]
PROSITE	PS01188. ELO. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9NYP7.
ChEMBL	CHEMBL5937.
ChiTaRS	ELOVL5. human.
GenomeRNAi	60481.
NextBio	65351.
SOURCE	Search...

Entry information

Entry name

ELOV5_HUMAN

Accession

Primary (citable) accession number: Q9NYP7
Secondary accession number(s): B4DZJ2 , 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:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.