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Q9UKU0

- ACSL6_HUMAN

UniProt

Q9UKU0 - ACSL6_HUMAN

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Protein

Long-chain-fatty-acid--CoA ligase 6

Gene

ACSL6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid.

Catalytic activityi

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

Cofactori

Magnesium.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. long-chain fatty acid-CoA ligase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. acyl-CoA metabolic process Source: UniProtKB
  2. cellular lipid metabolic process Source: Reactome
  3. cellular response to insulin stimulus Source: Ensembl
  4. fatty acid transport Source: Ensembl
  5. long-chain fatty acid metabolic process Source: UniProtKB
  6. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  7. neuroblast proliferation Source: Ensembl
  8. neuron development Source: Ensembl
  9. phospholipid biosynthetic process Source: Ensembl
  10. positive regulation of neuron projection development Source: Ensembl
  11. positive regulation of plasma membrane long-chain fatty acid transport Source: Ensembl
  12. positive regulation of triglyceride biosynthetic process Source: Ensembl
  13. response to gravity Source: Ensembl
  14. response to hypoxia Source: Ensembl
  15. response to nutrient Source: Ensembl
  16. response to steroid hormone Source: Ensembl
  17. small molecule metabolic process Source: Reactome
  18. 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:HS15193-MONOMER.
BRENDAi6.2.1.3. 2681.
ReactomeiREACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 6 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 6
Short name:
LACS 6
Gene namesi
Name:ACSL6
Synonyms:ACS2, FACL6, KIAA0837, LACS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:16496. ACSL6.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. mitochondrial outer membrane Source: UniProtKB-KW
  5. nucleus Source: Ensembl
  6. peroxisome Source: UniProtKB-KW
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving ACSL6 may be a cause of myelodysplastic syndrome with basophilia. Translocation t(5;12)(q31;p13) with ETV6.
A chromosomal aberration involving ACSL6 may be a cause of acute myelogenous leukemia with eosinophilia. Translocation t(5;12)(q31;p13) with ETV6.
A chromosomal aberration involving ACSL6 may be a cause of acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ETV6.

Organism-specific databases

PharmGKBiPA27970.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 697697Long-chain-fatty-acid--CoA ligase 6PRO_0000193115Add
BLAST

Proteomic databases

MaxQBiQ9UKU0.
PaxDbiQ9UKU0.
PRIDEiQ9UKU0.

PTM databases

PhosphoSiteiQ9UKU0.

Expressioni

Tissue specificityi

Expressed predominantly in erythrocyte precursors, in particular in reticulocytes, fetal blood cells derived from fetal liver, hemopoietic stem cells from cord blood, bone marrow and brain.1 Publication

Developmental stagei

Expression is low at earlier stages of erythroid development but is very high in reticulocytes.

Gene expression databases

BgeeiQ9UKU0.
CleanExiHS_ACSL6.
ExpressionAtlasiQ9UKU0. baseline and differential.
GenevestigatoriQ9UKU0.

Organism-specific databases

HPAiHPA040470.

Interactioni

Protein-protein interaction databases

BioGridi116897. 1 interaction.
IntActiQ9UKU0. 1 interaction.
STRINGi9606.ENSP00000296869.

Structurei

3D structure databases

ProteinModelPortaliQ9UKU0.
SMRiQ9UKU0. Positions 222-605.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini46 – 697652CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 4521Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ9UKU0.
KOiK01897.
OMAiMFERMVQ.
OrthoDBiEOG71CFKN.
PhylomeDBiQ9UKU0.
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 (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 4 (identifier: Q9UKU0-4) [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
MQTQEILRIL RLPELGDLGQ FFRSLSATTL VSMGALAAIL AYWFTHRPKA
60 70 80 90 100
LQPPCNLLMQ SEEVEDSGGA RRSVIGSGPQ LLTHYYDDAR TMYQVFRRGL
110 120 130 140 150
SISGNGPCLG FRKPKQPYQW LSYQEVADRA EFLGSGLLQH NCKACTDQFI
160 170 180 190 200
GVFAQNRPEW IIVELACYTY SMVVVPLYDT LGPGAIRYII NTADISTVIV
210 220 230 240 250
DKPQKAVLLL EHVERKETPG LKLIILMDPF EEALKERGQK CGVVIKSMQA
260 270 280 290 300
VEDCGQENHQ APVPPQPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF
310 320 330 340 350
LKVTEKVIFP RQDDVLISFL PLAHMFERVI QSVVYCHGGR VGFFQGDIRL
360 370 380 390 400
LSDDMKALCP TIFPVVPRLL NRMYDKIFSQ ANTPLKRWLL EFAAKRKQAE
410 420 430 440 450
VRSGIIRNDS IWDELFFNKI QASLGGCVRM IVTGAAPASP TVLGFLRAAL
460 470 480 490 500
GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV GAPLPCNHIK LVDVEELNYW
510 520 530 540 550
ACKGEGEICV RGPNVFKGYL KDPDRTKEAL DSDGWLHTGD IGKWLPAGTL
560 570 580 590 600
KIIDRKKHIF KLAQGEYVAP EKIENIYIRS QPVAQIYVHG DSLKAFLVGI
610 620 630 640 650
VVPDPEVMPS WAQKRGIEGT YADLCTNKDL KKAILEDMVR LGKESGLHSF
660 670 680 690
EQVKAIHIHS DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM
Length:697
Mass (Da):77,752
Last modified:March 6, 2007 - v4
Checksum:iAC566177B47D0975
GO
Isoform 1 (identifier: Q9UKU0-1) [UniParc]FASTAAdd to Basket

Also known as: Long, v2

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

Show »
Length:722
Mass (Da):80,610
Checksum:i2B7D408F2F77C1FB
GO
Isoform 2 (identifier: Q9UKU0-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     306-330: KVIFPRQDDVLISFLPLAHMFERVI → SQWAPTCADVHISYLPLAHMFERMV
     653-697: VKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM → DLPQCLIQIKVFSKY

Note: No experimental confirmation available.

Show »
Length:667
Mass (Da):74,175
Checksum:iE57CDD86836E7D64
GO
Isoform 3 (identifier: Q9UKU0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     306-330: KVIFPRQDDVLISFLPLAHMFERVI → SQWAPTCADVHISYLPLAHMFERMV

Note: No experimental confirmation available.

Show »
Length:697
Mass (Da):77,671
Checksum:iF70642502C212FA7
GO
Isoform 5 (identifier: Q9UKU0-5) [UniParc]FASTAAdd to Basket

Also known as: v4

The sequence of this isoform differs from the canonical sequence as follows:
     306-312: Missing.

Show »
Length:690
Mass (Da):76,883
Checksum:i3D96A1B1433CF6F9
GO
Isoform 6 (identifier: Q9UKU0-6) [UniParc]FASTAAdd to Basket

Also known as: v5

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: T → TGLSCQEGASATASTQ

Show »
Length:712
Mass (Da):79,144
Checksum:i1BC1636243762146
GO
Isoform 7 (identifier: Q9UKU0-7) [UniParc]FASTAAdd to Basket

Also known as: v3

The sequence of this isoform differs from the canonical sequence as follows:
     31-65: Missing.
     306-345: Missing.

Show »
Length:622
Mass (Da):69,222
Checksum:iE5BE0D13E92599ED
GO
Isoform 8 (identifier: Q9UKU0-8) [UniParc]FASTAAdd to Basket

Also known as: v1

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLTFFLVSGGSLWLFVEFVLSLLEKM
     306-330: KVIFPRQDDVLISFLPLAHMFERVI → SQWAPTCADVHISYLPLAHMFERMV

Note: No experimental confirmation available.

Show »
Length:722
Mass (Da):80,529
Checksum:i702D63A8B72BE729
GO
Isoform 9 (identifier: Q9UKU0-9) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:708
Mass (Da):79,040
Checksum:iDD0FE6A5EDA476D0
GO

Sequence cautioni

The sequence BAA74860.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH26161.1 differs from that shown. Reason: Erroneous termination at position 72. Translated as Arg.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → E in AAD47199. (PubMed:10548543)Curated
Sequence conflicti46 – 461H → Q in AAD47199. (PubMed:10548543)Curated
Sequence conflicti257 – 2571E → A in AAH47453. (PubMed:15489334)Curated
Sequence conflicti260 – 2601Q → L in AAH26161. (PubMed:15489334)Curated
Sequence conflicti356 – 3561K → R in AAZ30714. (PubMed:16834775)Curated
Sequence conflicti696 – 6961S → P in AAD47199. (PubMed:10548543)Curated
Sequence conflicti696 – 6961S → P in AAZ30714. (PubMed:16834775)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLTFFLVSGGSLWLFVEFVL SLLEKM in isoform 1 and isoform 8. 1 PublicationVSP_037819
Alternative sequencei1 – 11M → MPEFVLSLLEKM in isoform 9. 1 PublicationVSP_046954
Alternative sequencei31 – 6535Missing in isoform 7. 1 PublicationVSP_037820Add
BLAST
Alternative sequencei192 – 1921T → TGLSCQEGASATASTQ in isoform 6. 1 PublicationVSP_037821
Alternative sequencei306 – 34540Missing in isoform 7. 1 PublicationVSP_037822Add
BLAST
Alternative sequencei306 – 33025KVIFP…FERVI → SQWAPTCADVHISYLPLAHM FERMV in isoform 3, isoform 2 and isoform 8. 2 PublicationsVSP_021024Add
BLAST
Alternative sequencei306 – 3127Missing in isoform 5. 1 PublicationVSP_037823
Alternative sequencei653 – 69745VKAIH…YSISM → DLPQCLIQIKVFSKY in isoform 2. 1 PublicationVSP_000241Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129166 mRNA. Translation: AAD47199.1.
AF099740 mRNA. Translation: AAD17853.1.
DQ083030 mRNA. Translation: AAZ30713.1.
DQ083031 mRNA. Translation: AAZ30714.1.
AB020644 mRNA. Translation: BAA74860.1. Different initiation.
CR606980 mRNA. No translation available.
AC025772 Genomic DNA. No translation available.
AC026398 Genomic DNA. No translation available.
AC034228 Genomic DNA. No translation available.
BC026161 mRNA. Translation: AAH26161.1. Sequence problems.
BC047453 mRNA. Translation: AAH47453.1.
CCDSiCCDS34228.1. [Q9UKU0-8]
CCDS34229.1. [Q9UKU0-1]
CCDS56381.1. [Q9UKU0-3]
CCDS56382.1. [Q9UKU0-7]
CCDS56383.1. [Q9UKU0-9]
RefSeqiNP_001009185.1. NM_001009185.2. [Q9UKU0-1]
NP_001192176.1. NM_001205247.1.
NP_001192177.1. NM_001205248.1. [Q9UKU0-3]
NP_001192179.1. NM_001205250.1. [Q9UKU0-9]
NP_001192180.1. NM_001205251.1. [Q9UKU0-7]
NP_056071.2. NM_015256.3. [Q9UKU0-8]
XP_006714642.1. XM_006714579.1. [Q9UKU0-4]
XP_006714643.1. XM_006714580.1. [Q9UKU0-4]
UniGeneiHs.14945.

Genome annotation databases

EnsembliENST00000296869; ENSP00000296869; ENSG00000164398. [Q9UKU0-8]
ENST00000357096; ENSP00000349608; ENSG00000164398. [Q9UKU0-7]
ENST00000379240; ENSP00000368542; ENSG00000164398. [Q9UKU0-4]
ENST00000379244; ENSP00000368546; ENSG00000164398. [Q9UKU0-3]
ENST00000379246; ENSP00000368548; ENSG00000164398. [Q9UKU0-9]
ENST00000379255; ENSP00000368557; ENSG00000164398. [Q9UKU0-7]
ENST00000379264; ENSP00000368566; ENSG00000164398. [Q9UKU0-1]
ENST00000413683; ENSP00000415140; ENSG00000164398. [Q9UKU0-2]
ENST00000543479; ENSP00000442124; ENSG00000164398. [Q9UKU0-6]
GeneIDi23305.
KEGGihsa:23305.
UCSCiuc003kvx.2. human. [Q9UKU0-8]
uc003kvy.2. human. [Q9UKU0-1]
uc003kvz.2. human. [Q9UKU0-7]
uc010jdn.2. human. [Q9UKU0-6]
uc010jdo.2. human. [Q9UKU0-3]

Polymorphism databases

DMDMi146322303.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129166 mRNA. Translation: AAD47199.1 .
AF099740 mRNA. Translation: AAD17853.1 .
DQ083030 mRNA. Translation: AAZ30713.1 .
DQ083031 mRNA. Translation: AAZ30714.1 .
AB020644 mRNA. Translation: BAA74860.1 . Different initiation.
CR606980 mRNA. No translation available.
AC025772 Genomic DNA. No translation available.
AC026398 Genomic DNA. No translation available.
AC034228 Genomic DNA. No translation available.
BC026161 mRNA. Translation: AAH26161.1 . Sequence problems.
BC047453 mRNA. Translation: AAH47453.1 .
CCDSi CCDS34228.1. [Q9UKU0-8 ]
CCDS34229.1. [Q9UKU0-1 ]
CCDS56381.1. [Q9UKU0-3 ]
CCDS56382.1. [Q9UKU0-7 ]
CCDS56383.1. [Q9UKU0-9 ]
RefSeqi NP_001009185.1. NM_001009185.2. [Q9UKU0-1 ]
NP_001192176.1. NM_001205247.1.
NP_001192177.1. NM_001205248.1. [Q9UKU0-3 ]
NP_001192179.1. NM_001205250.1. [Q9UKU0-9 ]
NP_001192180.1. NM_001205251.1. [Q9UKU0-7 ]
NP_056071.2. NM_015256.3. [Q9UKU0-8 ]
XP_006714642.1. XM_006714579.1. [Q9UKU0-4 ]
XP_006714643.1. XM_006714580.1. [Q9UKU0-4 ]
UniGenei Hs.14945.

3D structure databases

ProteinModelPortali Q9UKU0.
SMRi Q9UKU0. Positions 222-605.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116897. 1 interaction.
IntActi Q9UKU0. 1 interaction.
STRINGi 9606.ENSP00000296869.

PTM databases

PhosphoSitei Q9UKU0.

Polymorphism databases

DMDMi 146322303.

Proteomic databases

MaxQBi Q9UKU0.
PaxDbi Q9UKU0.
PRIDEi Q9UKU0.

Protocols and materials databases

DNASUi 23305.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296869 ; ENSP00000296869 ; ENSG00000164398 . [Q9UKU0-8 ]
ENST00000357096 ; ENSP00000349608 ; ENSG00000164398 . [Q9UKU0-7 ]
ENST00000379240 ; ENSP00000368542 ; ENSG00000164398 . [Q9UKU0-4 ]
ENST00000379244 ; ENSP00000368546 ; ENSG00000164398 . [Q9UKU0-3 ]
ENST00000379246 ; ENSP00000368548 ; ENSG00000164398 . [Q9UKU0-9 ]
ENST00000379255 ; ENSP00000368557 ; ENSG00000164398 . [Q9UKU0-7 ]
ENST00000379264 ; ENSP00000368566 ; ENSG00000164398 . [Q9UKU0-1 ]
ENST00000413683 ; ENSP00000415140 ; ENSG00000164398 . [Q9UKU0-2 ]
ENST00000543479 ; ENSP00000442124 ; ENSG00000164398 . [Q9UKU0-6 ]
GeneIDi 23305.
KEGGi hsa:23305.
UCSCi uc003kvx.2. human. [Q9UKU0-8 ]
uc003kvy.2. human. [Q9UKU0-1 ]
uc003kvz.2. human. [Q9UKU0-7 ]
uc010jdn.2. human. [Q9UKU0-6 ]
uc010jdo.2. human. [Q9UKU0-3 ]

Organism-specific databases

CTDi 23305.
GeneCardsi GC05M131147.
HGNCi HGNC:16496. ACSL6.
HPAi HPA040470.
MIMi 604443. gene.
neXtProti NX_Q9UKU0.
PharmGKBi PA27970.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000101725.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi Q9UKU0.
KOi K01897.
OMAi MFERMVQ.
OrthoDBi EOG71CFKN.
PhylomeDBi Q9UKU0.
TreeFami TF313877.

Enzyme and pathway databases

BioCyci MetaCyc:HS15193-MONOMER.
BRENDAi 6.2.1.3. 2681.
Reactomei REACT_380. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

GeneWikii ACSL6.
GenomeRNAii 23305.
NextBioi 13615790.
PROi Q9UKU0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKU0.
CleanExi HS_ACSL6.
ExpressionAtlasi Q9UKU0. baseline and differential.
Genevestigatori Q9UKU0.

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. "Identification and molecular characterization of acyl-CoA synthetase in human red cells and erythroid precursor."
    Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.
    Biochem. J. 344:135-143(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
  2. "Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13)."
    Yagasaki F., Jinnai I., Yoshida S., Yokoyama Y., Matsuda A., Kusumoto S., Kobayashi H., Terasaki H., Ohyashiki K., Asou N., Murohashi I., Bessho M., Hirashima K.
    Genes Chromosomes Cancer 26:192-202(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH ETV6.
    Tissue: Bone marrow.
  3. "Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains."
    Soupene E., Kuypers F.A.
    BMC Mol. Biol. 7:21-21(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF 253-374 (ISOFORM 5), ALTERNATIVE SPLICING (ISOFORM 8).
  4. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  6. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 8).
  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] (ISOFORMS 7 AND 9).
    Tissue: Testis.

Entry informationi

Entry nameiACSL6_HUMAN
AccessioniPrimary (citable) accession number: Q9UKU0
Secondary accession number(s): J3KPG3
, O94924, O95829, Q108M9, Q108N0, Q4G191, Q86TN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 138 of the entry and version 4 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3