Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongation of very long chain fatty acids protein 5

Gene

ELOVL5

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 acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.2 Publications

Catalytic activityi

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

Pathway: polyunsaturated fatty acid biosynthesis

This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway polyunsaturated fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • fatty acid elongase activity Source: UniProtKB

GO - Biological processi

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:ENSG00000012660-MONOMER.
BRENDAi2.3.1.119. 2681.
ReactomeiREACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_380. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00658.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 5Curated (EC:2.3.1.1991 Publication)
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 namesi
Name:ELOVL5
Synonyms:ELOVL2
ORF Names:PRO0530
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21308. ELOVL5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 4621HelicalSequence AnalysisAdd
BLAST
Transmembranei64 – 8421HelicalSequence AnalysisAdd
BLAST
Transmembranei112 – 13221HelicalSequence AnalysisAdd
BLAST
Transmembranei139 – 15820HelicalSequence AnalysisAdd
BLAST
Transmembranei168 – 18720HelicalSequence AnalysisAdd
BLAST
Transmembranei205 – 22521HelicalSequence AnalysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • dendrite Source: UniProtKB-SubCell
  • dendritic tree Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • neuronal cell body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 38 (SCA38)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. SCA38 is an autosomal dominant form characterized by adult-onset of slowly progressive gait ataxia accompanied by nystagmus. Brain MRI shows cerebellar atrophy.

See also OMIM:615957
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721L → V in SCA38. 1 Publication
VAR_072361
Natural varianti230 – 2301G → V in SCA38. 1 Publication
VAR_072362

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MIMi615957. phenotype.
PharmGKBiPA128394703.

Polymorphism and mutation databases

BioMutaiELOVL5.
DMDMi74753072.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Elongation of very long chain fatty acids protein 5PRO_0000282838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei285 – 2851Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYP7.
PaxDbiQ9NYP7.
PeptideAtlasiQ9NYP7.
PRIDEiQ9NYP7.

PTM databases

PhosphoSiteiQ9NYP7.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in the adrenal gland and testis. Weakly expressed in prostate, lung and brain. Expressed in the cerebellum.3 Publications

Gene expression databases

BgeeiQ9NYP7.
CleanExiHS_ELOVL2.
HS_ELOVL5.
ExpressionAtlasiQ9NYP7. baseline and differential.
GenevisibleiQ9NYP7. HS.

Organism-specific databases

HPAiCAB017042.
HPA047752.

Interactioni

Protein-protein interaction databases

BioGridi121914. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9NYP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ELO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000139716.
HOVERGENiHBG051468.
InParanoidiQ9NYP7.
KOiK10244.
OMAiAICHYNG.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9NYP7.
TreeFamiTF323454.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NYP7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEHFDASLST YFKALLGPRD TRVKGWFLLD NYIPTFICSV IYLLIVWLGP
60 70 80 90 100
KYMRNKQPFS CRGILVVYNL GLTLLSLYMF CELVTGVWEG KYNFFCQGTR
110 120 130 140 150
TAGESDMKII RVLWWYYFSK LIEFMDTFFF ILRKNNHQIT VLHVYHHASM
160 170 180 190 200
LNIWWFVMNW VPCGHSYFGA TLNSFIHVLM YSYYGLSSVP SMRPYLWWKK
210 220 230 240 250
YITQGQLLQF VLTIIQTSCG VIWPCTFPLG WLYFQIGYMI SLIALFTNFY
260 270 280 290
IQTYNKKGAS RRKDHLKDHQ NGSMAAVNGH TNSFSPLENN VKPRKLRKD
Length:299
Mass (Da):35,293
Last modified:October 1, 2000 - v1
Checksum:iAE5150AA3432E984
GO
Isoform 2 (identifier: Q9NYP7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-82: E → ESKREQPRRSACASRTDPSTQQQLPENR

Note: No experimental confirmation available.
Show »
Length:326
Mass (Da):38,403
Checksum:iDAFA9400ACB27FB1
GO
Isoform 3 (identifier: Q9NYP7-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:88
Mass (Da):9,580
Checksum:i449F6D2F7A7E4BF1
GO

Sequence cautioni

The sequence AAF16688.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11178.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591F → L in BAG64104 (PubMed:14702039).Curated
Sequence conflicti167 – 26296YFGAT…GASRR → SVCADNHPDQLRGHLAVHIP SWLVVFPDWIHDFPDCSLHK LLHSDLQQERGLPKERPPEG PPEWVHGCCEWTHQQLFTPG KQCEAKEAAEGLKSKN in BAD93035 (PubMed:14702039).CuratedAdd
BLAST
Sequence conflicti204 – 2063QGQ → EFH in BAC11178 (PubMed:16303743).Curated
Sequence conflicti227 – 2271F → S in BAC11178 (PubMed:16303743).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721L → V in SCA38. 1 Publication
VAR_072361
Natural varianti230 – 2301G → V in SCA38. 1 Publication
VAR_072362

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 8869DTRVK…VTGVW → GISSSVLRMGPPLHTVVGWL QQLQAAHSEEEEKMFHLCGF KHKEVVSQSSLPAVIPQNSL ATIASHAPA in isoform 3. 1 PublicationVSP_045917Add
BLAST
Alternative sequencei82 – 821E → ESKREQPRRSACASRTDPST QQQLPENR in isoform 2. 1 PublicationVSP_045918
Alternative sequencei89 – 299211Missing in isoform 3. 1 PublicationVSP_045919Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4951.1. [Q9NYP7-1]
CCDS56433.1. [Q9NYP7-2]
CCDS56434.1. [Q9NYP7-3]
RefSeqiNP_001229757.1. NM_001242828.1. [Q9NYP7-2]
NP_001229759.1. NM_001242830.1.
NP_001229760.1. NM_001242831.1. [Q9NYP7-3]
NP_001288785.1. NM_001301856.1. [Q9NYP7-1]
NP_068586.1. NM_021814.4. [Q9NYP7-1]
UniGeneiHs.520189.

Genome annotation databases

EnsembliENST00000304434; ENSP00000306640; ENSG00000012660. [Q9NYP7-1]
ENST00000370913; ENSP00000359951; ENSG00000012660. [Q9NYP7-3]
ENST00000370918; ENSP00000359956; ENSG00000012660. [Q9NYP7-2]
GeneIDi60481.
KEGGihsa:60481.
UCSCiuc003pbq.1. human. [Q9NYP7-1]
uc003pbu.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4951.1. [Q9NYP7-1]
CCDS56433.1. [Q9NYP7-2]
CCDS56434.1. [Q9NYP7-3]
RefSeqiNP_001229757.1. NM_001242828.1. [Q9NYP7-2]
NP_001229759.1. NM_001242830.1.
NP_001229760.1. NM_001242831.1. [Q9NYP7-3]
NP_001288785.1. NM_001301856.1. [Q9NYP7-1]
NP_068586.1. NM_021814.4. [Q9NYP7-1]
UniGeneiHs.520189.

3D structure databases

ProteinModelPortaliQ9NYP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121914. 4 interactions.

Chemistry

BindingDBiQ9NYP7.
ChEMBLiCHEMBL5937.

PTM databases

PhosphoSiteiQ9NYP7.

Polymorphism and mutation databases

BioMutaiELOVL5.
DMDMi74753072.

Proteomic databases

MaxQBiQ9NYP7.
PaxDbiQ9NYP7.
PeptideAtlasiQ9NYP7.
PRIDEiQ9NYP7.

Protocols and materials databases

DNASUi60481.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304434; ENSP00000306640; ENSG00000012660. [Q9NYP7-1]
ENST00000370913; ENSP00000359951; ENSG00000012660. [Q9NYP7-3]
ENST00000370918; ENSP00000359956; ENSG00000012660. [Q9NYP7-2]
GeneIDi60481.
KEGGihsa:60481.
UCSCiuc003pbq.1. human. [Q9NYP7-1]
uc003pbu.3. human.

Organism-specific databases

CTDi60481.
GeneCardsiGC06M053132.
HGNCiHGNC:21308. ELOVL5.
HPAiCAB017042.
HPA047752.
MIMi611805. gene.
615957. phenotype.
neXtProtiNX_Q9NYP7.
PharmGKBiPA128394703.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000139716.
HOVERGENiHBG051468.
InParanoidiQ9NYP7.
KOiK10244.
OMAiAICHYNG.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9NYP7.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00658.
BioCyciMetaCyc:ENSG00000012660-MONOMER.
BRENDAi2.3.1.119. 2681.
ReactomeiREACT_121100. Linoleic acid (LA) metabolism.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiELOVL5. human.
GeneWikiiELOVL5.
GenomeRNAii60481.
NextBioi65351.
PROiQ9NYP7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYP7.
CleanExiHS_ELOVL2.
HS_ELOVL5.
ExpressionAtlasiQ9NYP7. baseline and differential.
GenevisibleiQ9NYP7. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, 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].
  16. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN SCA38, VARIANTS SCA38 VAL-72 AND VAL-230.

Entry informationi

Entry nameiELOV5_HUMAN
AccessioniPrimary (citable) accession number: Q9NYP7
Secondary accession number(s): B4DZJ2
, F6SH78, Q59EL3, Q5TGH5, Q6NXE7, Q7L2S5, Q8NCG4, Q9UI22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 117 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.