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Protein

Acyl-coenzyme A synthetase ACSM2B, mitochondrial

Gene

ACSM2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 Publication

Enzyme regulationi

Activated by monovalent cations, such as potassium, rubidium or ammonium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Coenzyme ABy similarity
Binding sitei364 – 3641SubstrateBy similarity
Binding sitei446 – 4461ATPBy similarity
Binding sitei461 – 4611ATPBy similarity
Binding sitei472 – 4721SubstrateBy similarity
Binding sitei501 – 5011Coenzyme ABy similarity
Binding sitei532 – 5321Coenzyme ABy similarity
Binding sitei557 – 5571ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2299ATPBy similarity
Nucleotide bindingi359 – 3646ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. butyrate-CoA ligase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB-KW
  2. small molecule metabolic process Source: Reactome
  3. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_6800. Conjugation of phenylacetate with glutamine.
REACT_6812. Conjugation of salicylate with glycine.
REACT_6933. Conjugation of benzoate with glycine.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ACSM2B
Synonyms:ACSM2
ORF Names:HYST1046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:30931. ACSM2B.

Subcellular locationi

Mitochondrion matrix 3 Publications

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162375437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
BLAST
Chaini47 – 577531Acyl-coenzyme A synthetase ACSM2B, mitochondrialPRO_0000306094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411N6-acetyllysine; alternateBy similarity
Modified residuei141 – 1411N6-succinyllysine; alternateBy similarity
Modified residuei327 – 3271N6-acetyllysineBy similarity
Modified residuei513 – 5131Phosphoserine1 Publication
Modified residuei525 – 5251N6-acetyllysineBy similarity
Modified residuei532 – 5321N6-acetyllysine; alternateBy similarity
Modified residuei532 – 5321N6-succinyllysine; alternateBy similarity
Modified residuei543 – 5431N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ68CK6.
PaxDbiQ68CK6.
PRIDEiQ68CK6.

PTM databases

PhosphoSiteiQ68CK6.

Expressioni

Tissue specificityi

Detected in liver.2 Publications

Gene expression databases

BgeeiQ68CK6.
CleanExiHS_ACSM2B.
ExpressionAtlasiQ68CK6. baseline and differential.
GenevestigatoriQ68CK6.

Organism-specific databases

HPAiHPA057699.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiQ68CK6. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ68CK6.
SMRiQ68CK6. Positions 34-569.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni469 – 4713Coenzyme A bindingBy similarity
Regioni540 – 5423Coenzyme A bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ68CK6.
KOiK01896.
OMAiECNFVLS.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ68CK6.
TreeFamiTF354264.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q68CK6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV
60 70 80 90 100
LDHWADMEKA GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANILSGA
110 120 130 140 150
CGLQRGDRVA VMLPRVPEWW LVILGCIRAG LIFMPGTIQM KSTDILYRLQ
160 170 180 190 200
MSKAKAIVAG DEVIQEVDTV ASECPSLRIK LLVSEKSCDG WLNFKKLLNE
210 220 230 240 250
ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL KAKMDAGWTG
260 270 280 290 300
LQASDIMWTI SDTGWILNIL GSLLESWTLG ACTFVHLLPK FDPLVILKTL
310 320 330 340 350
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCLAGGES LLPETLENWR
360 370 380 390 400
AQTGLDIREF YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQVIDDKGN
410 420 430 440 450
VLPPGTEGDI GIRVKPIRPI GIFSGYVENP DKTAANIRGD FWLLGDRGIK
460 470 480 490 500
DEDGYFQFMG RADDIINSSG YRIGPSEVEN ALMKHPAVVE TAVISSPDPV
510 520 530 540 550
RGEVVKAFVI LASQFLSHDP EQLTKELQQH VKSVTAPYKY PRKIEFVLNL
560 570
PKTVTGKIQR TKLRDKEWKM SGKARAQ
Length:577
Mass (Da):64,271
Last modified:May 18, 2010 - v2
Checksum:i93A6F0581A47F222
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461F → L in AAO17576 (PubMed:12616642).Curated
Sequence conflicti96 – 961I → V in AAO17576 (PubMed:12616642).Curated
Sequence conflicti96 – 961I → V in BAD38642 (PubMed:15221005).Curated
Sequence conflicti133 – 1331F → I in AAO17576 (PubMed:12616642).Curated
Sequence conflicti136 – 1361G → E in AAO17576 (PubMed:12616642).Curated
Sequence conflicti143 – 1431T → A in AAO17576 (PubMed:12616642).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY160217 mRNA. Translation: AAO17576.1.
AB073604 mRNA. Translation: BAD38642.1.
AC141053 Genomic DNA. No translation available.
AC141273 Genomic DNA. No translation available.
CCDSiCCDS10586.1.
RefSeqiNP_001098539.1. NM_001105069.1.
NP_872423.3. NM_182617.3.
UniGeneiHs.298252.
Hs.567879.

Genome annotation databases

EnsembliENST00000329697; ENSP00000327453; ENSG00000066813.
ENST00000414188; ENSP00000390378; ENSG00000066813.
ENST00000565232; ENSP00000454995; ENSG00000066813.
ENST00000567001; ENSP00000456378; ENSG00000066813.
GeneIDi348158.
KEGGihsa:348158.
UCSCiuc002dhj.4. human.

Polymorphism databases

DMDMi296434397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY160217 mRNA. Translation: AAO17576.1.
AB073604 mRNA. Translation: BAD38642.1.
AC141053 Genomic DNA. No translation available.
AC141273 Genomic DNA. No translation available.
CCDSiCCDS10586.1.
RefSeqiNP_001098539.1. NM_001105069.1.
NP_872423.3. NM_182617.3.
UniGeneiHs.298252.
Hs.567879.

3D structure databases

ProteinModelPortaliQ68CK6.
SMRiQ68CK6. Positions 34-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ68CK6. 1 interaction.

PTM databases

PhosphoSiteiQ68CK6.

Polymorphism databases

DMDMi296434397.

Proteomic databases

MaxQBiQ68CK6.
PaxDbiQ68CK6.
PRIDEiQ68CK6.

Protocols and materials databases

DNASUi348158.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329697; ENSP00000327453; ENSG00000066813.
ENST00000414188; ENSP00000390378; ENSG00000066813.
ENST00000565232; ENSP00000454995; ENSG00000066813.
ENST00000567001; ENSP00000456378; ENSG00000066813.
GeneIDi348158.
KEGGihsa:348158.
UCSCiuc002dhj.4. human.

Organism-specific databases

CTDi348158.
GeneCardsiGC16M020547.
H-InvDBHIX0026968.
HGNCiHGNC:30931. ACSM2B.
HPAiHPA057699.
MIMi614359. gene.
neXtProtiNX_Q68CK6.
PharmGKBiPA162375437.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ68CK6.
KOiK01896.
OMAiECNFVLS.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ68CK6.
TreeFamiTF354264.

Enzyme and pathway databases

ReactomeiREACT_6800. Conjugation of phenylacetate with glutamine.
REACT_6812. Conjugation of salicylate with glycine.
REACT_6933. Conjugation of benzoate with glycine.

Miscellaneous databases

ChiTaRSiACSM2B. human.
GeneWikiiACSM2B.
GenomeRNAii348158.
NextBioi99351.
PROiQ68CK6.
SOURCEiSearch...

Gene expression databases

BgeeiQ68CK6.
CleanExiHS_ACSM2B.
ExpressionAtlasiQ68CK6. baseline and differential.
GenevestigatoriQ68CK6.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACS2B_HUMAN
AccessioniPrimary (citable) accession number: Q68CK6
Secondary accession number(s): Q86YT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 18, 2010
Last modified: March 4, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.