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Acyl-coenzyme A synthetase ACSM2B, mitochondrial (EC 6.2.1.2) (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)

 ACS2B_HUMAN             Reviewed;         577 AA.
Q68CK6; Q86YT1;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
30-AUG-2017, entry version 110.
RecName: Full=Acyl-coenzyme A synthetase ACSM2B, mitochondrial;
EC=6.2.1.2;
AltName: Full=Acyl-CoA synthetase medium-chain family member 2B;
AltName: Full=Butyrate--CoA ligase 2B;
AltName: Full=Butyryl-coenzyme A synthetase 2B;
AltName: Full=Middle-chain acyl-CoA synthetase 2B;
AltName: Full=Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A;
Flags: Precursor;
Name=ACSM2B; Synonyms=ACSM2; ORFNames=HYST1046;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 152-163 AND 483-491,
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
TISSUE=Liver;
PubMed=12616642; DOI=10.1002/jbt.10056;
Vessey D.A., Lau E., Kelley M., Warren R.S.;
"Isolation, sequencing, and expression of a cDNA for the HXM-A form of
xenobiotic/medium-chain fatty acid:CoA ligase from human liver
mitochondria.";
J. Biochem. Mol. Toxicol. 17:1-6(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15221005; DOI=10.1038/sj.onc.1207782;
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.;
"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.";
Oncogene 23:5901-5911(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
SUBCELLULAR LOCATION, COFACTOR, TISSUE SPECIFICITY, AND ENZYME
REGULATION.
PubMed=10434065; DOI=10.1016/S0304-4165(99)00088-4;
Vessey D.A., Kelley M., Warren R.S.;
"Characterization of the CoA ligases of human liver mitochondria
catalyzing the activation of short- and medium-chain fatty acids and
xenobiotic carboxylic acids.";
Biochim. Biophys. Acta 1428:455-462(1999).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19634011; DOI=10.1007/s10528-009-9273-z;
Boomgaarden I., Vock C., Klapper M., Doering F.;
"Comparative analyses of disease risk genes belonging to the acyl-CoA
synthetase medium-chain (ACSM) family in human liver and cell lines.";
Biochem. Genet. 47:739-748(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Has medium-chain fatty acid:CoA ligase activity with
broad substrate specificity (in vitro). Acts on acids from C(4) to
C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-
unsaturated acids (in vitro). {ECO:0000269|PubMed:12616642}.
-!- CATALYTIC ACTIVITY: ATP + a carboxylate + CoA = AMP + diphosphate
+ an acyl-CoA.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10434065};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:10434065};
-!- ENZYME REGULATION: Activated by monovalent cations, such as
potassium, rubidium or ammonium. {ECO:0000269|PubMed:10434065}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12616642}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:10434065, ECO:0000269|PubMed:12616642,
ECO:0000269|PubMed:19634011}.
-!- TISSUE SPECIFICITY: Detected in liver.
{ECO:0000269|PubMed:10434065, ECO:0000269|PubMed:19634011}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
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EMBL; AY160217; AAO17576.1; -; mRNA.
EMBL; AB073604; BAD38642.1; -; mRNA.
EMBL; AC141053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC141273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS10586.1; -.
RefSeq; NP_001098539.1; NM_001105069.1.
RefSeq; NP_872423.3; NM_182617.3.
UniGene; Hs.298252; -.
UniGene; Hs.567879; -.
ProteinModelPortal; Q68CK6; -.
SMR; Q68CK6; -.
IntAct; Q68CK6; 2.
STRING; 9606.ENSP00000327453; -.
iPTMnet; Q68CK6; -.
PhosphoSitePlus; Q68CK6; -.
BioMuta; ACSM2B; -.
DMDM; 296434397; -.
MaxQB; Q68CK6; -.
PaxDb; Q68CK6; -.
PeptideAtlas; Q68CK6; -.
PRIDE; Q68CK6; -.
DNASU; 348158; -.
Ensembl; ENST00000329697; ENSP00000327453; ENSG00000066813.
Ensembl; ENST00000414188; ENSP00000390378; ENSG00000066813.
Ensembl; ENST00000565232; ENSP00000454995; ENSG00000066813.
Ensembl; ENST00000567001; ENSP00000456378; ENSG00000066813.
GeneID; 348158; -.
KEGG; hsa:348158; -.
UCSC; uc002dhj.5; human.
CTD; 348158; -.
DisGeNET; 348158; -.
GeneCards; ACSM2B; -.
H-InvDB; HIX0026968; -.
HGNC; HGNC:30931; ACSM2B.
HPA; HPA057699; -.
MIM; 614359; gene.
neXtProt; NX_Q68CK6; -.
OpenTargets; ENSG00000066813; -.
PharmGKB; PA162375437; -.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
GeneTree; ENSGT00760000119178; -.
HOGENOM; HOG000229982; -.
HOVERGEN; HBG053031; -.
InParanoid; Q68CK6; -.
KO; K01896; -.
OMA; NAGACIF; -.
OrthoDB; EOG091G03NW; -.
PhylomeDB; Q68CK6; -.
TreeFam; TF354264; -.
Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
Reactome; R-HSA-177162; Conjugation of phenylacetate with glutamine.
SABIO-RK; Q68CK6; -.
ChiTaRS; ACSM2B; human.
GeneWiki; ACSM2B; -.
GenomeRNAi; 348158; -.
PRO; PR:Q68CK6; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000066813; -.
CleanEx; HS_ACSM2B; -.
ExpressionAtlas; Q68CK6; baseline and differential.
Genevisible; Q68CK6; HS.
GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; NAS:BHF-UCL.
GO; GO:0003996; F:acyl-CoA ligase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0016405; F:CoA-ligase activity; TAS:Reactome.
GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Fatty acid metabolism; Ligase;
Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Transit peptide.
TRANSIT 1 46 Mitochondrion. {ECO:0000255}.
CHAIN 47 577 Acyl-coenzyme A synthetase ACSM2B,
mitochondrial.
/FTId=PRO_0000306094.
NP_BIND 221 229 ATP. {ECO:0000250}.
NP_BIND 359 364 ATP. {ECO:0000250}.
REGION 469 471 Coenzyme A binding. {ECO:0000250}.
REGION 540 542 Coenzyme A binding. {ECO:0000250}.
BINDING 139 139 Coenzyme A. {ECO:0000250}.
BINDING 364 364 Substrate. {ECO:0000250}.
BINDING 446 446 ATP. {ECO:0000250}.
BINDING 461 461 ATP. {ECO:0000250}.
BINDING 472 472 Substrate. {ECO:0000250}.
BINDING 501 501 Coenzyme A. {ECO:0000250}.
BINDING 532 532 Coenzyme A. {ECO:0000250}.
BINDING 557 557 ATP. {ECO:0000250}.
MOD_RES 327 327 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BGA8}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CONFLICT 46 46 F -> L (in Ref. 1; AAO17576).
{ECO:0000305}.
CONFLICT 96 96 I -> V (in Ref. 1; AAO17576 and 2;
BAD38642). {ECO:0000305}.
CONFLICT 133 133 F -> I (in Ref. 1; AAO17576).
{ECO:0000305}.
CONFLICT 136 136 G -> E (in Ref. 1; AAO17576).
{ECO:0000305}.
CONFLICT 143 143 T -> A (in Ref. 1; AAO17576).
{ECO:0000305}.
SEQUENCE 577 AA; 64271 MW; 93A6F0581A47F222 CRC64;
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA
GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANILSGA CGLQRGDRVA VMLPRVPEWW
LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK
LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL
KAKMDAGWTG LQASDIMWTI SDTGWILNIL GSLLESWTLG ACTFVHLLPK FDPLVILKTL
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCLAGGES LLPETLENWR AQTGLDIREF
YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQVIDDKGN VLPPGTEGDI GIRVKPIRPI
GIFSGYVENP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RADDIINSSG YRIGPSEVEN
ALMKHPAVVE TAVISSPDPV RGEVVKAFVI LASQFLSHDP EQLTKELQQH VKSVTAPYKY
PRKIEFVLNL PKTVTGKIQR TKLRDKEWKM SGKARAQ


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