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Q9ULC5 (ACSL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
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 names
Name:ACSL5
Synonyms:ACS5, FACL5
ORF Names:UNQ633/PRO1250
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.11

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subcellular location

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 Ref.1 Ref.11.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Biophysicochemical properties

Kinetic parameters:

KM=0.11 µM for palmitic acid (isoform 1 at pH 7.5) Ref.1

KM=0.38 µM for palmitic acid (isoform 1 at pH 9.5)

KM=0.04 µM for palmitic acid (isoform 3 at pH 7.5)

KM=0.15 µM for palmitic acid (isoform 3 at pH 8.5)

pH dependence:

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

Sequence caution

The sequence BAA85979.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

long-chain fatty acid metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ULC5-1)

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.
Note: Localize in mitochondrion and endoplasmic reticulum.
Isoform 2 (identifier: Q9ULC5-3)

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.
Isoform 3 (identifier: Q9ULC5-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Long-chain-fatty-acid--CoA ligase 5
PRO_0000193112

Regions

Transmembrane12 – 3221Helical; Signal-anchor for type III membrane protein; Potential
Topological domain33 – 683651Cytoplasmic Potential

Amino acid modifications

Modified residue3611N6-acetyllysine By similarity

Natural variations

Alternative sequence11M → MDALKPPCLWRNHERGKKDR DSCGRKNSEPGSPHSLEALR DAAPSQGLNFLLLFTKM in isoform 2.
VSP_037947
Alternative sequence614 – 63724Missing in isoform 3.
VSP_038233
Natural variant1821M → V.
Corresponds to variant rs3736946 [ dbSNP | Ensembl ].
VAR_022117
Natural variant3881K → R in a colorectal cancer sample; somatic mutation. Ref.13
VAR_036377
Natural variant4661G → D in a colorectal cancer sample; somatic mutation. Ref.13
VAR_036378
Natural variant4861T → A.
Corresponds to variant rs12254915 [ dbSNP | Ensembl ].
VAR_048240

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ACSL5b) (ACSL5-fl) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 781AFE1A7A78C286

FASTA68375,991
        10         20         30         40         50         60 
MLFIFNFLFS PLPTPALICI LTFGAAIFLW LITRPQPVLP LLDLNNQSVG IEGGARKGVS 

        70         80         90        100        110        120 
QKNNDLTSCC FSDAKTMYEV FQRGLAVSDN GPCLGYRKPN QPYRWLSYKQ VSDRAEYLGS 

       130        140        150        160        170        180 
CLLHKGYKSS PDQFVGIFAQ NRPEWIISEL ACYTYSMVAV PLYDTLGPEA IVHIVNKADI 

       190        200        210        220        230        240 
AMVICDTPQK ALVLIGNVEK GFTPSLKVII LMDPFDDDLK QRGEKSGIEI LSLYDAENLG 

       250        260        270        280        290        300 
KEHFRKPVPP SPEDLSVICF TSGTTGDPKG AMITHQNIVS NAAAFLKCVE HAYEPTPDDV 

       310        320        330        340        350        360 
AISYLPLAHM FERIVQAVVY SCGARVGFFQ GDIRLLADDM KTLKPTLFPA VPRLLNRIYD 

       370        380        390        400        410        420 
KVQNEAKTPL KKFLLKLAVS SKFKELQKGI IRHDSFWDKL IFAKIQDSLG GRVRVIVTGA 

       430        440        450        460        470        480 
APMSTSVMTF FRAAMGCQVY EAYGQTECTG GCTFTLPGDW TSGHVGVPLA CNYVKLEDVA 

       490        500        510        520        530        540 
DMNYFTVNNE GEVCIKGTNV FKGYLKDPEK TQEALDSDGW LHTGDIGRWL PNGTLKIIDR 

       550        560        570        580        590        600 
KKNIFKLAQG EYIAPEKIEN IYNRSQPVLQ IFVHGESLRS SLVGVVVPDT DVLPSFAAKL 

       610        620        630        640        650        660 
GVKGSFEELC QNQVVREAIL EDLQKIGKES GLKTFEQVKA IFLHPEPFSI ENGLLTPTLK 

       670        680 
AKRGELSKYF RTQIDSLYEH IQD 

« Hide

Isoform 2 (ACSL5a) [UniParc].

Checksum: C3A1ABCA53717BCE
Show »

FASTA73982,263
Isoform 3 (ACSL5delta20) [UniParc].

Checksum: 8FA678B997F35EF7
Show »

FASTA65973,278

References

« Hide 'large scale' references
[1]"Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing."
Gassler N., Roth W., Funke B., Schneider A., Herzog F., Ehemann V., Sykora J., Haas T.L., Walczak H., Ganten T., Zentgraf H., Erb P., Alonso A., Autschbach F., Schirmacher P., Knuechel R., Kopitz J.
Gastroenterology 133:587-598(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Small intestine mucosa.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. 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] (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. expand/collapse author list , 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]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].
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-388 AND ASP-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7572.1. [Q9ULC5-3]
CCDS7573.1. [Q9ULC5-1]
RefSeqNP_057318.2. NM_016234.3. [Q9ULC5-3]
NP_976313.1. NM_203379.1. [Q9ULC5-1]
NP_976314.1. NM_203380.1. [Q9ULC5-1]
UniGeneHs.11638.

3D structure databases

ProteinModelPortalQ9ULC5.
SMRQ9ULC5. Positions 104-620.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119687. 1 interaction.
IntActQ9ULC5. 2 interactions.
STRING9606.ENSP00000348429.

PTM databases

PhosphoSiteQ9ULC5.

Polymorphism databases

DMDM13431659.

Proteomic databases

MaxQBQ9ULC5.
PaxDbQ9ULC5.
PRIDEQ9ULC5.

Protocols and materials databases

DNASU51703.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354273; ENSP00000346223; ENSG00000197142. [Q9ULC5-1]
ENST00000354655; ENSP00000346680; ENSG00000197142. [Q9ULC5-1]
ENST00000356116; ENSP00000348429; ENSG00000197142. [Q9ULC5-3]
ENST00000393081; ENSP00000376796; ENSG00000197142. [Q9ULC5-1]
ENST00000433418; ENSP00000403647; ENSG00000197142. [Q9ULC5-4]
GeneID51703.
KEGGhsa:51703.
UCSCuc001kzs.3. human. [Q9ULC5-1]
uc001kzu.3. human. [Q9ULC5-3]

Organism-specific databases

CTD51703.
GeneCardsGC10P114123.
HGNCHGNC:16526. ACSL5.
HPACAB062546.
HPA007162.
MIM605677. gene.
neXtProtNX_Q9ULC5.
PharmGKBPA27969.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1022.
HOGENOMHOG000159459.
HOVERGENHBG050452.
InParanoidQ9ULC5.
KOK01897.
OMAIFVHPEP.
OrthoDBEOG71CFKN.
PhylomeDBQ9ULC5.
TreeFamTF313877.

Enzyme and pathway databases

BioCycMetaCyc:HS01349-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9ULC5.
BgeeQ9ULC5.
CleanExHS_ACSL5.
GenevestigatorQ9ULC5.

Family and domain databases

InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACSL5. human.
GeneWikiACSL5.
GenomeRNAi51703.
NextBio35462376.
PROQ9ULC5.
SOURCESearch...

Entry information

Entry nameACSL5_HUMAN
AccessionPrimary (citable) accession number: Q9ULC5
Secondary accession number(s): A6GV77 expand/collapse secondary AC list , D3DRB3, Q6UX44, Q9UIU4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 134 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM