SLC27A2 | ENSG00000140284 | NCBI 11001

Details for: SLC27A2

Gene ID: 11001

Symbol: SLC27A2

Ensembl ID: ENSG00000140284

Description: solute carrier family 27 member 2

Associated with

Alpha-oxidation of phytanate
(R-HSA-389599)
Bile acid and bile salt metabolism
(R-HSA-194068)
Fatty acid metabolism
(R-HSA-8978868)
Fatty acyl-coa biosynthesis
(R-HSA-75105)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of steroids
(R-HSA-8957322)
Neutrophil degranulation
(R-HSA-6798695)
Peroxisomal lipid metabolism
(R-HSA-390918)
Peroxisomal protein import
(R-HSA-9033241)
Protein localization
(R-HSA-9609507)
Synthesis of bile acids and bile salts
(R-HSA-192105)
Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
(R-HSA-193368)
Synthesis of bile acids and bile salts via 24-hydroxycholesterol
(R-HSA-193775)
Arachidonate-coa ligase activity
(GO:0047676)
Atp binding
(GO:0005524)
Bile acid biosynthetic process
(GO:0006699)
Bile acid metabolic process
(GO:0008206)
Cholate-coa ligase activity
(GO:0047747)
Cytosol
(GO:0005829)
Endoplasmic reticulum lumen
(GO:0005788)
Endoplasmic reticulum membrane
(GO:0005789)
Enzyme binding
(GO:0019899)
Extracellular exosome
(GO:0070062)
Fatty-acyl-coa biosynthetic process
(GO:0046949)
Fatty acid alpha-oxidation
(GO:0001561)
Fatty acid beta-oxidation
(GO:0006635)
Fatty acid transmembrane transporter activity
(GO:0015245)
Long-chain fatty acid-coa ligase activity
(GO:0004467)
Long-chain fatty acid import into cell
(GO:0044539)
Long-chain fatty acid metabolic process
(GO:0001676)
Long-chain fatty acid transporter activity
(GO:0005324)
Methyl-branched fatty acid metabolic process
(GO:0097089)
Oleate transmembrane transporter activity
(GO:1901480)
Peroxisomal membrane
(GO:0005778)
Phytanate-coa ligase activity
(GO:0050197)
Plasma membrane
(GO:0005886)
Pristanate-coa ligase activity
(GO:0070251)
Specific granule membrane
(GO:0035579)
Very long-chain fatty acid-coa ligase activity
(GO:0031957)

Other Information

Proteins

Arachidonate--CoA ligase

Genular Protein ID: 1721208352

Symbol: S27A2_HUMAN

Name: Arachidonate--CoA ligase

UniProtKB Accession Codes:

O14975 A8K2J7 Q53FY6 Q6PF09

Database IDs:

Citations:

PubMed ID: 10198260

Title: Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism.

PubMed ID: 10198260

DOI: 10.1006/bbrc.1999.0510

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10640429

Title: Intraperoxisomal localization of very-long-chain fatty acyl-CoA synthetase: implication in X-adrenoleukodystrophy.

PubMed ID: 10640429

DOI: 10.1006/excr.1999.4757

PubMed ID: 10749848

Title: The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase.

PubMed ID: 10749848

DOI: 10.1074/jbc.c000015200

PubMed ID: 11980911

Title: Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling.

PubMed ID: 11980911

DOI: 10.1074/jbc.m203295200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 20530735

Title: FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase.

PubMed ID: 20530735

DOI: 10.1152/ajpendo.00226.2010

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 22022213

Title: Overexpression of CD36 and acyl-CoA synthetases FATP2, FATP4 and ACSL1 increases fatty acid uptake in human hepatoma cells.

PubMed ID: 22022213

DOI: 10.7150/ijms.8.599

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21768100

Title: Human fatty acid transport protein 2a/very long chain acyl-CoA synthetase 1 (FATP2a/Acsvl1) has a preference in mediating the channeling of exogenous n-3 fatty acids into phosphatidylinositol.

PubMed ID: 21768100

DOI: 10.1074/jbc.m111.226316

PubMed ID: 24269233

Title: Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway.

PubMed ID: 24269233

DOI: 10.1016/j.bbrc.2013.11.036

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

Sequence Information:

Length: 620
Mass: 70312
Checksum: 752E2FFBB2E47C26
Sequence:

MLSAIYTVLA GLLFLPLLVN LCCPYFFQDI GYFLKVAAVG RRVRSYGKRR PARTILRAFL 
EKARQTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG LRQGDCVALL MGNEPAYVWL 
WLGLVKLGCA MACLNYNIRA KSLLHCFQCC GAKVLLVSPE LQAAVEEILP SLKKDDVSIY 
YVSRTSNTDG IDSFLDKVDE VSTEPIPESW RSEVTFSTPA LYIYTSGTTG LPKAAMITHQ 
RIWYGTGLTF VSGLKADDVI YITLPFYHSA ALLIGIHGCI VAGATLALRT KFSASQFWDD 
CRKYNVTVIQ YIGELLRYLC NSPQKPNDRD HKVRLALGNG LRGDVWRQFV KRFGDICIYE 
FYAATEGNIG FMNYARKVGA VGRVNYLQKK IITYDLIKYD VEKDEPVRDE NGYCVRVPKG 
EVGLLVCKIT QLTPFNGYAG AKAQTEKKKL RDVFKKGDLY FNSGDLLMVD HENFIYFHDR 
VGDTFRWKGE NVATTEVADT VGLVDFVQEV NVYGVHVPDH EGRIGMASIK MKENHEFDGK 
KLFQHIADYL PSYARPRFLR IQDTIEITGT FKHRKMTLVE EGFNPAVIKD ALYFLDDTAK 
MYVPMTEDIY NAISAKTLKL

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: SLC27A2

Associated with

Other Information

Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. PubMed ID: 10198260

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Analysis of the DNA sequence and duplication history of human chromosome 15. PubMed ID: 16572171

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Intraperoxisomal localization of very-long-chain fatty acyl-CoA synthetase: implication in X-adrenoleukodystrophy. PubMed ID: 10640429

The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase. PubMed ID: 10749848

Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. PubMed ID: 11980911

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain acyl-CoA synthetase. PubMed ID: 20530735

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Overexpression of CD36 and acyl-CoA synthetases FATP2, FATP4 and ACSL1 increases fatty acid uptake in human hepatoma cells. PubMed ID: 22022213

Initial characterization of the human central proteome. PubMed ID: 21269460

Human fatty acid transport protein 2a/very long chain acyl-CoA synthetase 1 (FATP2a/Acsvl1) has a preference in mediating the channeling of exogenous n-3 fatty acids into phosphatidylinositol. PubMed ID: 21768100

Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. PubMed ID: 24269233

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569