Reviewed, UniProtKB/Swiss-Prot Q96GR2 (ACBG1_HUMAN)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase ACSBG1
    EC=6.2.1.3
Alternative name(s):
    Acyl-CoA synthetase bubblegum family member 1
      Short name=hsBGM
      Short name=hsBG
      Short name=hBG1
    Lipodisin

Gene names

Name:	ACSBG1
Synonyms:	BGM, KIAA0631, LPD

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Subcellular location	Cytoplasm. Cytoplasmic vesicleBy similarity. MicrosomeBy similarity. Endoplasmic reticulumBy similarity.
Tissue specificity	Expressed primarily in brain. Expressed at lower level in testis and adrenal gland. Present in all regions of brain except pituitary.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Microsome
Coding sequence diversity	Polymorphism
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 724	724	Long-chain-fatty-acid--CoA ligase ACSBG1
Amino acid modifications
	Modified residue	135	1	Phosphotyrosine
	Modified residue	138	1	Phosphotyrosine
	Modified residue	139	1	Phosphotyrosine
	Modified residue	658	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	194	1	E → V: dbSNP rs12899901.
	Natural variant	633	1	V → M: dbSNP rs2304824.
	Natural variant	673	1	A → V: dbSNP rs11072735.

Sequences

	Sequence		Length	Mass (Da)
	Q96GR2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3926EA7F658F7FBC	FASTA	724	81,258
	10 20 30 40 50 60 MPRNSGAGYG CPHGDPSMLD SRETPQESRQ DMIVRTTQEK LKTSSLTDRQ PLSKESLNHA 70 80 90 100 110 120 LELSVPEKVN NAQWDAPEEA LWTTRADGRV RLRIDPSCPQ LPYTVHRMFY EALDKYGDLI 130 140 150 160 170 180 ALGFKRQDKW EHISYSQYYL LARRAAKGFL KLGLKQAHSV AILGFNSPEW FFSAVGTVFA 190 200 210 220 230 240 GGIVTGIYTT SSPEACQYIA YDCCANVIMV DTQKQLEKIL KIWKQLPHLK AVVIYKEPPP 250 260 270 280 290 300 NKMANVYTME EFMELGNEVP EEALDAIIDT QQPNQCCVLV YTSGTTGNPK GVMLSQDNIT 310 320 330 340 350 360 WTARYGSQAG DIRPAEVQQE VVVSYLPLSH IAAQIYDLWT GIQWGAQVCF AEPDALKGSL 370 380 390 400 410 420 VNTLREVEPT SHMGVPRVWE KIMERIQEVA AQSGFIRRKM LLWAMSVTLE QNLTCPGSDL 430 440 450 460 470 480 KPFTTRLADY LVLAKVRQAL GFAKCQKNFY GAAPMMAETQ HFFLGLNIRL YAGYGLSETS 490 500 510 520 530 540 GPHFMSSPYN YRLYSSGKLV PGCRVKLVNQ DAEGIGEICL WGRTIFMGYL NMEDKTCEAI 550 560 570 580 590 600 DEEGWLHTGD AGRLDADGFL YITGRLKELI ITAGGENVPP VPIEEAVKME LPIISNAMLI 610 620 630 640 650 660 GDQRKFLSML LTLKCTLDPD TSDQTDNLTE QAVEFCQRVG SRATTVSEII EKKDEAVYQA 670 680 690 700 710 720 IEEGIRRVNM NAAARPYHIQ KWAILERDFS ISGGELGPTM KLKRLTVLEK YKGIIDSFYQ EQKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Very long-chain acyl-CoA synthetases. Human 'bubblegum' represents a new family of proteins capable of activating very long-chain fatty acids." Steinberg S.J., Morgenthaler J., Heinzer A.K., Smith K.D., Watkins P.A. J. Biol. Chem. 275:35162-35169(2000) [PubMed: 10954726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT MET-633. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	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. , 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].
[6]	"The acyl-CoA synthetase 'bubblegum' (lipidosin): further characterization and role in neuronal fatty acid beta-oxidation." Pei Z., Oey N.A., Zuidervaart M.M., Jia Z., Li Y., Steinberg S.J., Smith K.D., Watkins P.A. J. Biol. Chem. 278:47070-47078(2003) [PubMed: 12975357] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135; TYR-138 AND TYR-139, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF179481 mRNA. Translation: AAG09404.1. AB014531 mRNA. Translation: BAA31606.2. Different initiation. BC009289 mRNA. Translation: AAH09289.1. CH471136 Genomic DNA. Translation: EAW99180.1.
RefSeq	NP_055977.3.
UniGene	Hs.655760
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
PTM databases
PhosphoSite	Q96GR2.
Genome annotation databases
Ensembl	ENSG00000103740. Homo sapiens. [Contig view]
GeneID	23205.
KEGG	hsa:23205.
Organism-specific databases
HGNC	HGNC:29567. ACSBG1.
PharmGKB	PA142672648.
HUGE	Search...
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q96GR2.
Gene expression databases
ArrayExpress	Q96GR2.
CleanEx	HS_ACSBG1.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PRINTS	PR00154. AMPBINDING.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProDom	Q96GR2. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ACBG1_HUMAN

Accession

Primary (citable) accession number: Q96GR2
Secondary accession number(s): O75126, Q76N27, Q9HC26

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 1, 2001
Last modified:	September 2, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)