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Reviewed, UniProtKB/Swiss-Prot Q96GR2 (ACBG1_HUMAN)

Last modified October 13, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. Ref.1 Ref.7

Catalytic activity

ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1

Subcellular location

Cytoplasm. Cytoplasmic vesicle By similarity. Microsome By similarity. Endoplasmic reticulum By similarity.

Tissue specificity

Expressed primarily in brain. Expressed at lower level in testis and adrenal gland. Present in all regions of brain except pituitary. Ref.1 Ref.7

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Long-chain-fatty-acid--CoA ligase ACSBG1
PRO_0000315808

Regions

Nucleotide binding282 – 2909ATP By similarity
Nucleotide binding472 – 4776ATP By similarity

Sites

Binding site5501ATP By similarity
Binding site5651ATP By similarity
Binding site7011ATP By similarity

Amino acid modifications

Modified residue1351Phosphotyrosine Ref.8
Modified residue1381Phosphotyrosine Ref.8
Modified residue1391Phosphotyrosine Ref.8
Modified residue6581Phosphotyrosine By similarity

Natural variations

Natural variant1941E → V: dbSNP rs12899901.
VAR_038314
Natural variant6331V → M: dbSNP rs2304824. Ref.1
VAR_038315
Natural variant6731A → V: dbSNP rs11072735. Ref.4
VAR_038316

Sequences

Sequence LengthMass (Da)Tools
Q96GR2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 3926EA7F658F7FBC

FASTA72481,258
        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 

« Hide

References

« Hide '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]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-673.
Tissue: Testis.
[5]"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.
[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 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.
[8]"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. expand/collapse author list , 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

AF179481 mRNA. Translation: AAG09404.1.
AB014531 mRNA. Translation: BAA31606.2. Different initiation.
AK314508 mRNA. Translation: BAG37108.1.
BC009289 mRNA. Translation: AAH09289.1.
CH471136 Genomic DNA. Translation: EAW99180.1.
IPIIPI00550128.
RefSeqNP_055977.3.
UniGeneHs.655760

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96GR2.

PTM databases

PhosphoSiteQ96GR2.

Proteomic databases

PRIDEQ96GR2.

Genome annotation databases

EnsemblENST00000258873; ENSP00000258873; ENSG00000103740; Homo sapiens. [Genome view]
GeneID23205.
KEGGhsa:23205.
UCSCuc002bdh.1. human.

Organism-specific databases

CTD23205.
GeneCardsGC15M076247.
HGNCHGNC:29567. ACSBG1.
PharmGKBPA142672648.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ96GR2.

Enzyme and pathway databases

BRENDA6.2.1.3. 247.

Gene expression databases

ArrayExpressQ96GR2.
BgeeQ96GR2.
CleanExHS_ACSBG1.
GenevestigatorQ96GR2.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio44731.

Entry information

Entry nameACBG1_HUMAN
AccessionPrimary (citable) accession number: Q96GR2
Secondary accession number(s): B2RB61 expand/collapse secondary AC list , O75126, Q76N27, Q9HC26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 1, 2001
Last modified: October 13, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Human chromosome 15: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents