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Q68CK6 (ACS2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A synthetase ACSM2B, mitochondrial

EC=6.2.1.2
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 2B
Butyrate--CoA ligase 2B
Butyryl-coenzyme A synthetase 2B
Middle-chain acyl-CoA synthetase 2B
Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A
Gene names
Name:ACSM2B
Synonyms:ACSM2
ORF Names:HYST1046
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 to C11 and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro). Ref.1

Catalytic activity

ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA.

Cofactor

Magnesium or manganese. Ref.4

Enzyme regulation

Activated by monovalent cations, such as potassium, rubidium or ammonium. Ref.4

Subunit structure

Monomer. Ref.1

Subcellular location

Mitochondrion matrix Ref.1 Ref.4 Ref.5.

Tissue specificity

Detected in liver. Ref.4 Ref.5

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 577531Acyl-coenzyme A synthetase ACSM2B, mitochondrial
PRO_0000306094

Regions

Nucleotide binding221 – 2299ATP By similarity
Nucleotide binding359 – 3646ATP By similarity
Region469 – 4713Coenzyme A binding By similarity
Region540 – 5423Coenzyme A binding By similarity

Sites

Binding site1391Coenzyme A By similarity
Binding site3641Substrate By similarity
Binding site4461ATP By similarity
Binding site4611ATP By similarity
Binding site4721Substrate By similarity
Binding site5011Coenzyme A By similarity
Binding site5321Coenzyme A By similarity
Binding site5571ATP By similarity

Experimental info

Sequence conflict461F → L in AAO17576. Ref.1
Sequence conflict961I → V in AAO17576. Ref.1
Sequence conflict961I → V in BAD38642. Ref.2
Sequence conflict1331F → I in AAO17576. Ref.1
Sequence conflict1361G → E in AAO17576. Ref.1
Sequence conflict1431T → A in AAO17576. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q68CK6 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 93A6F0581A47F222

FASTA57764,271
        10         20         30         40         50         60 
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA 

        70         80         90        100        110        120 
GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANILSGA CGLQRGDRVA VMLPRVPEWW 

       130        140        150        160        170        180 
LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK 

       190        200        210        220        230        240 
LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL 

       250        260        270        280        290        300 
KAKMDAGWTG LQASDIMWTI SDTGWILNIL GSLLESWTLG ACTFVHLLPK FDPLVILKTL 

       310        320        330        340        350        360 
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCLAGGES LLPETLENWR AQTGLDIREF 

       370        380        390        400        410        420 
YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQVIDDKGN VLPPGTEGDI GIRVKPIRPI 

       430        440        450        460        470        480 
GIFSGYVENP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RADDIINSSG YRIGPSEVEN 

       490        500        510        520        530        540 
ALMKHPAVVE TAVISSPDPV RGEVVKAFVI LASQFLSHDP EQLTKELQQH VKSVTAPYKY 

       550        560        570 
PRKIEFVLNL PKTVTGKIQR TKLRDKEWKM SGKARAQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria."
Vessey D.A., Lau E., Kelley M., Warren R.S.
J. Biochem. Mol. Toxicol. 17:1-6(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 152-163 AND 483-491, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
Tissue: Liver.
[2]"Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids."
Vessey D.A., Kelley M., Warren R.S.
Biochim. Biophys. Acta 1428:455-462(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, COFACTOR, TISSUE SPECIFICITY, ENZYME REGULATION.
[5]"Comparative analyses of disease risk genes belonging to the acyl-CoA synthetase medium-chain (ACSM) family in human liver and cell lines."
Boomgaarden I., Vock C., Klapper M., Doering F.
Biochem. Genet. 47:739-748(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY160217 mRNA. Translation: AAO17576.1.
AB073604 mRNA. Translation: BAD38642.1.
AC141053 Genomic DNA. No translation available.
AC141273 Genomic DNA. No translation available.
RefSeqNP_001098539.1. NM_001105069.1.
NP_872423.3. NM_182617.3.
UniGeneHs.298252.
Hs.567879.

3D structure databases

ProteinModelPortalQ68CK6.
SMRQ68CK6. Positions 34-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ68CK6. 1 interaction.

PTM databases

PhosphoSiteQ68CK6.

Polymorphism databases

DMDM296434397.

Proteomic databases

PaxDbQ68CK6.
PRIDEQ68CK6.

Protocols and materials databases

DNASU348158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329697; ENSP00000327453; ENSG00000066813.
ENST00000565232; ENSP00000454995; ENSG00000066813.
ENST00000567001; ENSP00000456378; ENSG00000066813.
GeneID348158.
KEGGhsa:348158.
UCSCuc002dhj.4. human.

Organism-specific databases

CTD348158.
GeneCardsGC16M020547.
H-InvDBHIX0026968.
HGNCHGNC:30931. ACSM2B.
MIM614359. gene.
neXtProtNX_Q68CK6.
PharmGKBPA162375437.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229982.
HOVERGENHBG053031.
InParanoidQ68CK6.
KOK01896.
OMAGQTECNF.
OrthoDBEOG7D85VZ.
PhylomeDBQ68CK6.
TreeFamTF354264.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ68CK6.
BgeeQ68CK6.
CleanExHS_ACSM2B.
GenevestigatorQ68CK6.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACSM2B.
GenomeRNAi348158.
NextBio99351.
PROQ68CK6.
SOURCESearch...

Entry information

Entry nameACS2B_HUMAN
AccessionPrimary (citable) accession number: Q68CK6
Secondary accession number(s): Q86YT1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 84 of the entry and version 2 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 chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM