Q68CK6 (ACS2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW small molecule metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW butyrate-CoA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Mitochondrion Potential
	Chain	47 – 577	531	Acyl-coenzyme A synthetase ACSM2B, mitochondrial		PRO_0000306094
Regions
	Nucleotide binding	221 – 229	9	ATP By similarity
	Nucleotide binding	359 – 364	6	ATP By similarity
	Region	469 – 471	3	Coenzyme A binding By similarity
	Region	540 – 542	3	Coenzyme A binding By similarity
Sites
	Binding site	139	1	Coenzyme A By similarity
	Binding site	364	1	Substrate By similarity
	Binding site	446	1	ATP By similarity
	Binding site	461	1	ATP By similarity
	Binding site	472	1	Substrate By similarity
	Binding site	501	1	Coenzyme A By similarity
	Binding site	532	1	Coenzyme A By similarity
	Binding site	557	1	ATP By similarity
Experimental info
	Sequence conflict	46	1	F → L in AAO17576. Ref.1
	Sequence conflict	96	1	I → V in AAO17576. Ref.1
	Sequence conflict	96	1	I → V in BAD38642. Ref.2
	Sequence conflict	133	1	F → I in AAO17576. Ref.1
	Sequence conflict	136	1	G → E in AAO17576. Ref.1
	Sequence conflict	143	1	T → A in AAO17576. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q68CK6 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 93A6F0581A47F222	FASTA	577	64,271
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00329444.
RefSeq	NP_001098539.1. NM_001105069.1. NP_872423.3. NM_182617.3.
UniGene	Hs.298252. Hs.567879.
3D structure databases
ProteinModelPortal	Q68CK6.
SMR	Q68CK6. Positions 34-569.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q68CK6. 1 interaction.
PTM databases
PhosphoSite	Q68CK6.
Polymorphism databases
DMDM	296434397.
Proteomic databases
PaxDb	Q68CK6.
PRIDE	Q68CK6.
Protocols and materials databases
DNASU	348158.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000329697; ENSP00000327453; ENSG00000066813. ENST00000565232; ENSP00000454995; ENSG00000066813. ENST00000567001; ENSP00000456378; ENSG00000066813.
GeneID	348158.
KEGG	hsa:348158.
UCSC	uc002dhj.4. human.
Organism-specific databases
CTD	348158.
GeneCards	GC16M020547.
H-InvDB	HIX0026968.
HGNC	HGNC:30931. ACSM2B.
MIM	614359. gene.
neXtProt	NX_Q68CK6.
PharmGKB	PA162375437.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000229982.
HOVERGEN	HBG053031.
InParanoid	Q68CK6.
KO	K01896.
OMA	EESEWIL.
OrthoDB	EOG40ZQXB.
PhylomeDB	Q68CK6.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q68CK6.
Bgee	Q68CK6.
CleanEx	HS_ACSM2B.
Genevestigator	Q68CK6.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	348158.
NextBio	99351.
SOURCE	Search...

Entry information

Entry name

ACS2B_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.