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Protein

Acyl-coenzyme A synthetase ACSM5, mitochondrial

Gene

ACSM5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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) (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei455 – 4551ATPBy similarity
Binding sitei470 – 4701ATPBy similarity
Binding sitei566 – 5661ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi230 – 2389ATPBy similarity
Nucleotide bindingi368 – 3736ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_6812. Conjugation of salicylate with glycine.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A synthetase ACSM5, mitochondrial (EC:6.2.1.2)
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 5
Gene namesi
Name:ACSM5
Synonyms:MACS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:26060. ACSM5.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162375501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 579553Acyl-coenzyme A synthetase ACSM5, mitochondrialPRO_0000306101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-acetyllysine; alternateBy similarity
Modified residuei97 – 971N6-succinyllysine; alternateBy similarity
Modified residuei152 – 1521N6-acetyllysineBy similarity
Modified residuei303 – 3031N6-acetyllysine; alternateBy similarity
Modified residuei303 – 3031N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ6NUN0.
PRIDEiQ6NUN0.

PTM databases

PhosphoSiteiQ6NUN0.

Expressioni

Tissue specificityi

Detected in kidney and liver.1 Publication

Gene expression databases

BgeeiQ6NUN0.
CleanExiHS_ACSM5.
ExpressionAtlasiQ6NUN0. baseline and differential.
GenevestigatoriQ6NUN0.

Organism-specific databases

HPAiHPA041435.

Interactioni

Protein-protein interaction databases

BioGridi120323. 1 interaction.
IntActiQ6NUN0. 1 interaction.
STRINGi9606.ENSP00000327916.

Structurei

3D structure databases

ProteinModelPortaliQ6NUN0.
SMRiQ6NUN0. Positions 11-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ6NUN0.
KOiK01896.
OMAiLTRYQFQ.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ6NUN0.
TreeFamiTF354287.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6NUN0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRPWLRHLVL QALRNSRAFC GSHGKPAPLP VPQKIVATWE AISLGRQLVP
60 70 80 90 100
EYFNFAHDVL DVWSRLEEAG HRPPNPAFWW VNGTGAEIKW SFEELGKQSR
110 120 130 140 150
KAANVLGGAC GLQPGDRMML VLPRLPEWWL VSVACMRTGT VMIPGVTQLT
160 170 180 190 200
EKDLKYRLQA SRAKSIITSD SLAPRVDAIS AECPSLQTKL LVSDSSRPGW
210 220 230 240 250
LNFRELLREA STEHNCMRTK SRDPLAIYFT SGTTGAPKMV EHSQSSYGLG
260 270 280 290 300
FVASGRRWVA LTESDIFWNT TDTGWVKAAW TLFSAWPNGS CIFVHELPRV
310 320 330 340 350
DAKVILNTLS KFPITTLCCV PTIFRLLVQE DLTRYQFQSL RHCLTGGEAL
360 370 380 390 400
NPDVREKWKH QTGVELYEGY GQSETVVICA NPKGMKIKSG SMGKASPPYD
410 420 430 440 450
VQIVDDEGNV LPPGEEGNVA VRIRPTRPFC FFNCYLDNPE KTAASEQGDF
460 470 480 490 500
YITGDRARMD KDGYFWFMGR NDDVINSSSY RIGPVEVESA LAEHPAVLES
510 520 530 540 550
AVVSSPDPIR GEVVKAFIVL TPAYSSHDPE ALTRELQEHV KRVTAPYKYP
560 570
RKVAFVSELP KTVSGKIQRS KLRSQEWGK
Length:579
Mass (Da):64,760
Last modified:November 24, 2009 - v2
Checksum:i9493CB853CE29CB1
GO
Isoform 2 (identifier: Q6NUN0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-579: Missing.

Note: No experimental confirmation available.

Show »
Length:208
Mass (Da):23,320
Checksum:i5C29746BE07D3E30
GO

Sequence cautioni

The sequence BAA91273.1 differs from that shown. Reason: Frameshift at position 560. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421M → V in AAH16703. (PubMed:15489334)Curated
Sequence conflicti231 – 2344SGTT → KREPP in BAA91273. (PubMed:14702039)Curated
Sequence conflicti502 – 5021V → A in AAH68516. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651R → Q.
Corresponds to variant rs9928053 [ dbSNP | Ensembl ].
VAR_055495
Natural varianti159 – 1591Q → H.1 Publication
VAR_035252
Natural varianti182 – 1821E → K.
Corresponds to variant rs7192210 [ dbSNP | Ensembl ].
VAR_055496
Natural varianti217 – 2171M → V.
Corresponds to variant rs59025904 [ dbSNP | Ensembl ].
VAR_061011
Natural varianti352 – 3521P → R.1 Publication
Corresponds to variant rs8062344 [ dbSNP | Ensembl ].
VAR_035253
Natural varianti360 – 3601H → R.1 Publication
Corresponds to variant rs12931877 [ dbSNP | Ensembl ].
VAR_035254
Natural varianti533 – 5331T → M.1 Publication
Corresponds to variant rs56308819 [ dbSNP | Ensembl ].
VAR_035255

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 579371Missing in isoform 2. 1 PublicationVSP_028398Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000588 mRNA. Translation: BAA91273.1. Frameshift.
AC137056 Genomic DNA. No translation available.
BC013753 mRNA. Translation: AAH13753.1.
BC016703 mRNA. Translation: AAH16703.1.
BC068516 mRNA. Translation: AAH68516.1.
CCDSiCCDS10585.1. [Q6NUN0-1]
RefSeqiNP_060358.2. NM_017888.2. [Q6NUN0-1]
UniGeneiHs.659606.

Genome annotation databases

EnsembliENST00000331849; ENSP00000327916; ENSG00000183549. [Q6NUN0-1]
ENST00000575584; ENSP00000460112; ENSG00000183549. [Q6NUN0-2]
GeneIDi54988.
KEGGihsa:54988.
UCSCiuc002dhd.1. human. [Q6NUN0-2]
uc002dhe.3. human. [Q6NUN0-1]

Polymorphism databases

DMDMi269849538.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000588 mRNA. Translation: BAA91273.1. Frameshift.
AC137056 Genomic DNA. No translation available.
BC013753 mRNA. Translation: AAH13753.1.
BC016703 mRNA. Translation: AAH16703.1.
BC068516 mRNA. Translation: AAH68516.1.
CCDSiCCDS10585.1. [Q6NUN0-1]
RefSeqiNP_060358.2. NM_017888.2. [Q6NUN0-1]
UniGeneiHs.659606.

3D structure databases

ProteinModelPortaliQ6NUN0.
SMRiQ6NUN0. Positions 11-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120323. 1 interaction.
IntActiQ6NUN0. 1 interaction.
STRINGi9606.ENSP00000327916.

PTM databases

PhosphoSiteiQ6NUN0.

Polymorphism databases

DMDMi269849538.

Proteomic databases

PaxDbiQ6NUN0.
PRIDEiQ6NUN0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331849; ENSP00000327916; ENSG00000183549. [Q6NUN0-1]
ENST00000575584; ENSP00000460112; ENSG00000183549. [Q6NUN0-2]
GeneIDi54988.
KEGGihsa:54988.
UCSCiuc002dhd.1. human. [Q6NUN0-2]
uc002dhe.3. human. [Q6NUN0-1]

Organism-specific databases

CTDi54988.
GeneCardsiGC16P020420.
H-InvDBHIX0023110.
HGNCiHGNC:26060. ACSM5.
HPAiHPA041435.
MIMi614361. gene.
neXtProtiNX_Q6NUN0.
PharmGKBiPA162375501.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ6NUN0.
KOiK01896.
OMAiLTRYQFQ.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ6NUN0.
TreeFamiTF354287.

Enzyme and pathway databases

ReactomeiREACT_6812. Conjugation of salicylate with glycine.

Miscellaneous databases

GenomeRNAii54988.
NextBioi58283.
PROiQ6NUN0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NUN0.
CleanExiHS_ACSM5.
ExpressionAtlasiQ6NUN0. baseline and differential.
GenevestigatoriQ6NUN0.

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. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  2. "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].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Kidney.
  4. "An acyl-CoA synthetase gene family in chromosome 16p12 may contribute to multiple risk factors."
    Iwai N., Mannami T., Tomoike H., Ono K., Iwanaga Y.
    Hypertension 41:1041-1046(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-159; ARG-352; ARG-360 AND MET-533, TISSUE SPECIFICITY.

Entry informationi

Entry nameiACSM5_HUMAN
AccessioniPrimary (citable) accession number: Q6NUN0
Secondary accession number(s): Q96AV1, Q96CX8, Q9NWV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 24, 2009
Last modified: January 7, 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.