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Q9ULC5

- ACSL5_HUMAN

UniProt

Q9ULC5 - ACSL5_HUMAN

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Protein
Long-chain-fatty-acid--CoA ligase 5
Gene
ACSL5, ACS5, FACL5, UNQ633/PRO1250
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acyl-CoA synthetases (ACSL) activate long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage By similarity. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids By similarity. It was suggested that it may also stimulate fatty acid oxidation By similarity. At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL. May have a role in the survival of glioma cells.3 Publications

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Magnesium By similarity.

Kineticsi

  1. KM=0.11 µM for palmitic acid (isoform 1 at pH 7.5)1 Publication
  2. KM=0.38 µM for palmitic acid (isoform 1 at pH 9.5)
  3. KM=0.04 µM for palmitic acid (isoform 3 at pH 7.5)
  4. KM=0.15 µM for palmitic acid (isoform 3 at pH 8.5)

pH dependencei

Optimum pH is 9.5 (isoform 1), 7.5-8.5 (isoform 3).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. long-chain fatty acid metabolic process Source: UniProtKB
  3. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  4. regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. triglyceride biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01349-MONOMER.
ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 5 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 5
Short name:
LACS 5
Gene namesi
Name:ACSL5
Synonyms:ACS5, FACL5
ORF Names:UNQ633/PRO1250
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:16526. ACSL5.

Subcellular locationi

Mitochondrion. Endoplasmic reticulum. Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221Helical; Signal-anchor for type III membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – 683651Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. mitochondrial inner membrane Source: Ensembl
  5. mitochondrial outer membrane Source: UniProtKB-SubCell
  6. mitochondrion Source: HPA
  7. nucleolus Source: HPA
  8. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27969.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Long-chain-fatty-acid--CoA ligase 5
PRO_0000193112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei361 – 3611N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ULC5.
PaxDbiQ9ULC5.
PRIDEiQ9ULC5.

PTM databases

PhosphoSiteiQ9ULC5.

Expressioni

Gene expression databases

ArrayExpressiQ9ULC5.
BgeeiQ9ULC5.
CleanExiHS_ACSL5.
GenevestigatoriQ9ULC5.

Organism-specific databases

HPAiCAB062546.
HPA007162.

Interactioni

Protein-protein interaction databases

BioGridi119687. 1 interaction.
IntActiQ9ULC5. 3 interactions.
STRINGi9606.ENSP00000348429.

Structurei

3D structure databases

ProteinModelPortaliQ9ULC5.
SMRiQ9ULC5. Positions 104-620.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ9ULC5.
KOiK01897.
OMAiIFVHPEP.
OrthoDBiEOG71CFKN.
PhylomeDBiQ9ULC5.
TreeFamiTF313877.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ULC5-1) [UniParc]FASTAAdd to Basket

Also known as: ACSL5b, ACSL5-fl

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

MLFIFNFLFS PLPTPALICI LTFGAAIFLW LITRPQPVLP LLDLNNQSVG    50
IEGGARKGVS QKNNDLTSCC FSDAKTMYEV FQRGLAVSDN GPCLGYRKPN 100
QPYRWLSYKQ VSDRAEYLGS CLLHKGYKSS PDQFVGIFAQ NRPEWIISEL 150
ACYTYSMVAV PLYDTLGPEA IVHIVNKADI AMVICDTPQK ALVLIGNVEK 200
GFTPSLKVII LMDPFDDDLK QRGEKSGIEI LSLYDAENLG KEHFRKPVPP 250
SPEDLSVICF TSGTTGDPKG AMITHQNIVS NAAAFLKCVE HAYEPTPDDV 300
AISYLPLAHM FERIVQAVVY SCGARVGFFQ GDIRLLADDM KTLKPTLFPA 350
VPRLLNRIYD KVQNEAKTPL KKFLLKLAVS SKFKELQKGI IRHDSFWDKL 400
IFAKIQDSLG GRVRVIVTGA APMSTSVMTF FRAAMGCQVY EAYGQTECTG 450
GCTFTLPGDW TSGHVGVPLA CNYVKLEDVA DMNYFTVNNE GEVCIKGTNV 500
FKGYLKDPEK TQEALDSDGW LHTGDIGRWL PNGTLKIIDR KKNIFKLAQG 550
EYIAPEKIEN IYNRSQPVLQ IFVHGESLRS SLVGVVVPDT DVLPSFAAKL 600
GVKGSFEELC QNQVVREAIL EDLQKIGKES GLKTFEQVKA IFLHPEPFSI 650
ENGLLTPTLK AKRGELSKYF RTQIDSLYEH IQD 683

Note: Localize in mitochondrion and endoplasmic reticulum.

Length:683
Mass (Da):75,991
Last modified:May 1, 2000 - v1
Checksum:i781AFE1A7A78C286
GO
Isoform 2 (identifier: Q9ULC5-3) [UniParc]FASTAAdd to Basket

Also known as: ACSL5a

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDALKPPCLWRNHERGKKDRDSCGRKNSEPGSPHSLEALRDAAPSQGLNFLLLFTKM

Note: Contains a phosphoserine at position 32.

Show »
Length:739
Mass (Da):82,263
Checksum:iC3A1ABCA53717BCE
GO
Isoform 3 (identifier: Q9ULC5-4) [UniParc]FASTAAdd to Basket

Also known as: ACSL5delta20

The sequence of this isoform differs from the canonical sequence as follows:
     614-637: Missing.

Note: Localize in mitochondrion and endoplasmic reticulum.

Show »
Length:659
Mass (Da):73,278
Checksum:i8FA678B997F35EF7
GO

Sequence cautioni

The sequence BAA85979.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA86054.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821M → V.
Corresponds to variant rs3736946 [ dbSNP | Ensembl ].
VAR_022117
Natural varianti388 – 3881K → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036377
Natural varianti466 – 4661G → D in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036378
Natural varianti486 – 4861T → A.
Corresponds to variant rs12254915 [ dbSNP | Ensembl ].
VAR_048240

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDALKPPCLWRNHERGKKDR DSCGRKNSEPGSPHSLEALR DAAPSQGLNFLLLFTKM in isoform 2.
VSP_037947
Alternative sequencei614 – 63724Missing in isoform 3.
VSP_038233Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM262166 mRNA. Translation: CAK18174.1.
AY358520 mRNA. Translation: AAQ88884.1.
AK000339 mRNA. No translation available.
AK222782 mRNA. No translation available.
AL157786 Genomic DNA. Translation: CAH72510.1.
CH471066 Genomic DNA. Translation: EAW49532.1.
CH471066 Genomic DNA. Translation: EAW49535.1.
CH471066 Genomic DNA. Translation: EAW49536.1.
CH471066 Genomic DNA. Translation: EAW49539.1.
BC007985 mRNA. Translation: AAH07985.2.
AB033899 mRNA. Translation: BAA85979.1. Different initiation.
AB033920 Genomic DNA. Translation: BAA86054.1. Sequence problems.
CCDSiCCDS7572.1. [Q9ULC5-3]
CCDS7573.1. [Q9ULC5-1]
RefSeqiNP_057318.2. NM_016234.3. [Q9ULC5-3]
NP_976313.1. NM_203379.1. [Q9ULC5-1]
NP_976314.1. NM_203380.1. [Q9ULC5-1]
UniGeneiHs.11638.

Genome annotation databases

EnsembliENST00000354273; ENSP00000346223; ENSG00000197142. [Q9ULC5-1]
ENST00000354655; ENSP00000346680; ENSG00000197142. [Q9ULC5-1]
ENST00000356116; ENSP00000348429; ENSG00000197142. [Q9ULC5-3]
ENST00000393081; ENSP00000376796; ENSG00000197142. [Q9ULC5-1]
ENST00000433418; ENSP00000403647; ENSG00000197142. [Q9ULC5-4]
GeneIDi51703.
KEGGihsa:51703.
UCSCiuc001kzs.3. human. [Q9ULC5-1]
uc001kzu.3. human. [Q9ULC5-3]

Polymorphism databases

DMDMi13431659.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM262166 mRNA. Translation: CAK18174.1 .
AY358520 mRNA. Translation: AAQ88884.1 .
AK000339 mRNA. No translation available.
AK222782 mRNA. No translation available.
AL157786 Genomic DNA. Translation: CAH72510.1 .
CH471066 Genomic DNA. Translation: EAW49532.1 .
CH471066 Genomic DNA. Translation: EAW49535.1 .
CH471066 Genomic DNA. Translation: EAW49536.1 .
CH471066 Genomic DNA. Translation: EAW49539.1 .
BC007985 mRNA. Translation: AAH07985.2 .
AB033899 mRNA. Translation: BAA85979.1 . Different initiation.
AB033920 Genomic DNA. Translation: BAA86054.1 . Sequence problems.
CCDSi CCDS7572.1. [Q9ULC5-3 ]
CCDS7573.1. [Q9ULC5-1 ]
RefSeqi NP_057318.2. NM_016234.3. [Q9ULC5-3 ]
NP_976313.1. NM_203379.1. [Q9ULC5-1 ]
NP_976314.1. NM_203380.1. [Q9ULC5-1 ]
UniGenei Hs.11638.

3D structure databases

ProteinModelPortali Q9ULC5.
SMRi Q9ULC5. Positions 104-620.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119687. 1 interaction.
IntActi Q9ULC5. 3 interactions.
STRINGi 9606.ENSP00000348429.

PTM databases

PhosphoSitei Q9ULC5.

Polymorphism databases

DMDMi 13431659.

Proteomic databases

MaxQBi Q9ULC5.
PaxDbi Q9ULC5.
PRIDEi Q9ULC5.

Protocols and materials databases

DNASUi 51703.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354273 ; ENSP00000346223 ; ENSG00000197142 . [Q9ULC5-1 ]
ENST00000354655 ; ENSP00000346680 ; ENSG00000197142 . [Q9ULC5-1 ]
ENST00000356116 ; ENSP00000348429 ; ENSG00000197142 . [Q9ULC5-3 ]
ENST00000393081 ; ENSP00000376796 ; ENSG00000197142 . [Q9ULC5-1 ]
ENST00000433418 ; ENSP00000403647 ; ENSG00000197142 . [Q9ULC5-4 ]
GeneIDi 51703.
KEGGi hsa:51703.
UCSCi uc001kzs.3. human. [Q9ULC5-1 ]
uc001kzu.3. human. [Q9ULC5-3 ]

Organism-specific databases

CTDi 51703.
GeneCardsi GC10P114123.
HGNCi HGNC:16526. ACSL5.
HPAi CAB062546.
HPA007162.
MIMi 605677. gene.
neXtProti NX_Q9ULC5.
PharmGKBi PA27969.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1022.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi Q9ULC5.
KOi K01897.
OMAi IFVHPEP.
OrthoDBi EOG71CFKN.
PhylomeDBi Q9ULC5.
TreeFami TF313877.

Enzyme and pathway databases

BioCyci MetaCyc:HS01349-MONOMER.
Reactomei REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSi ACSL5. human.
GeneWikii ACSL5.
GenomeRNAii 51703.
NextBioi 35462376.
PROi Q9ULC5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULC5.
Bgeei Q9ULC5.
CleanExi HS_ACSL5.
Genevestigatori Q9ULC5.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Small intestine mucosa.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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] (ISOFORM 1).
    Tissue: Hepatoma.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 2).
    Tissue: Colon.
  8. "Human FACL5 (or ACS5)."
    Yamashita Y.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Acyl-CoA synthetase as a cancer survival factor: its inhibition enhances the efficacy of etoposide."
    Mashima T., Sato S., Okabe S., Miyata S., Matsuura M., Sugimoto Y., Tsuruo T., Seimiya H.
    Cancer Sci. 100:1556-1562(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Promotion of glioma cell survival by acyl-CoA synthetase 5 under extracellular acidosis conditions."
    Mashima T., Sato S., Sugimoto Y., Tsuruo T., Seimiya H.
    Oncogene 28:9-19(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-388 AND ASP-466.

Entry informationi

Entry nameiACSL5_HUMAN
AccessioniPrimary (citable) accession number: Q9ULC5
Secondary accession number(s): A6GV77
, D3DRB3, Q6UX44, Q9UIU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 135 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 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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