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Q96CM8 (ACSF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-CoA synthetase family member 2, mitochondrial

EC=6.2.1.-
Gene names
Name:ACSF2
ORF Names:UNQ493/PRO1009
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation. Ref.5 Ref.6

Subcellular location

Mitochondrion Potential.

Induction

By PPARG. Ref.5

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Mitochondrion Potential
Chain42 – 615574Acyl-CoA synthetase family member 2, mitochondrial
PRO_0000315793

Regions

Nucleotide binding263 – 2719ATP By similarity

Sites

Binding site4931ATP By similarity
Binding site5081ATP By similarity
Binding site5991ATP By similarity

Amino acid modifications

Modified residue1791N6-acetyllysine By similarity
Modified residue1821N6-acetyllysine; alternate By similarity
Modified residue1821N6-succinyllysine; alternate By similarity
Modified residue3401N6-acetyllysine By similarity
Modified residue3981N6-acetyllysine By similarity
Modified residue4781N6-succinyllysine By similarity
Modified residue5101N6-acetyllysine By similarity
Modified residue5441N6-acetyllysine; alternate By similarity
Modified residue5441N6-succinyllysine; alternate By similarity
Modified residue5701N6-acetyllysine; alternate By similarity
Modified residue5701N6-succinyllysine; alternate By similarity
Modified residue5991N6-succinyllysine By similarity

Natural variations

Natural variant751G → V. Ref.4
Corresponds to variant rs17856448 [ dbSNP | Ensembl ].
VAR_038304
Natural variant3161V → M.
Corresponds to variant rs3744523 [ dbSNP | Ensembl ].
VAR_038305

Sequences

Sequence LengthMass (Da)Tools
Q96CM8 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: A3356EEA7C14730B

FASTA61568,125
        10         20         30         40         50         60 
MAVYVGMLRL GRLCAGSSGV LGARAALSRS WQEARLQGVR FLSSREVDRM VSTPIGGLSY 

        70         80         90        100        110        120 
VQGCTKKHLN SKTVGQCLET TAQRVPEREA LVVLHEDVRL TFAQLKEEVD KAASGLLSIG 

       130        140        150        160        170        180 
LCKGDRLGMW GPNSYAWVLM QLATAQAGII LVSVNPAYQA MELEYVLKKV GCKALVFPKQ 

       190        200        210        220        230        240 
FKTQQYYNVL KQICPEVENA QPGALKSQRL PDLTTVISVD APLPGTLLLD EVVAAGSTRQ 

       250        260        270        280        290        300 
HLDQLQYNQQ FLSCHDPINI QFTSGTTGSP KGATLSHYNI VNNSNILGER LKLHEKTPEQ 

       310        320        330        340        350        360 
LRMILPNPLY HCLGSVAGTM MCLMYGATLI LASPIFNGKK ALEAISRERG TFLYGTPTMF 

       370        380        390        400        410        420 
VDILNQPDFS SYDISTMCGG VIAGSPAPPE LIRAIINKIN MKDLVVAYGT TENSPVTFAH 

       430        440        450        460        470        480 
FPEDTVEQKA ESVGRIMPHT EARIMNMEAG TLAKLNTPGE LCIRGYCVML GYWGEPQKTE 

       490        500        510        520        530        540 
EAVDQDKWYW TGDVATMNEQ GFCKIVGRSK DMIIRGGENI YPAELEDFFH THPKVQEVQV 

       550        560        570        580        590        600 
VGVKDDRMGE EICACIRLKD GEETTVEEIK AFCKGKISHF KIPKYIVFVT NYPLTISGKI 

       610 
QKFKLREQME RHLNL 

« Hide

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"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. expand/collapse author list , 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].
Tissue: Adipose tissue.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT VAL-75.
Tissue: Kidney and Skin.
[5]"Identification of novel PPARgamma target genes in primary human adipocytes."
Perera R.J., Marcusson E.G., Koo S., Kang X., Kim Y., White N., Dean N.M.
Gene 369:90-99(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[6]"Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome."
Watkins P.A., Maiguel D., Jia Z., Pevsner J.
J. Lipid Res. 48:2736-2750(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358660 mRNA. Translation: AAQ89023.1.
AK024573 mRNA. Translation: BAB14930.1.
CH471109 Genomic DNA. Translation: EAW94612.1.
BC012053 mRNA. Translation: AAH12053.1.
BC014123 mRNA. Translation: AAH14123.1.
RefSeqNP_001275901.1. NM_001288972.1.
NP_079425.3. NM_025149.5.
UniGeneHs.288959.

3D structure databases

ProteinModelPortalQ96CM8.
SMRQ96CM8. Positions 78-609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123187. 1 interaction.
IntActQ96CM8. 4 interactions.
STRING9606.ENSP00000300441.

Polymorphism databases

DMDM166198367.

Proteomic databases

PaxDbQ96CM8.
PeptideAtlasQ96CM8.
PRIDEQ96CM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300441; ENSP00000300441; ENSG00000167107.
GeneID80221.
KEGGhsa:80221.
UCSCuc002iqu.2. human.

Organism-specific databases

CTD80221.
GeneCardsGC17P048503.
HGNCHGNC:26101. ACSF2.
HPAHPA024693.
MIM610465. gene.
neXtProtNX_Q96CM8.
PharmGKBPA162375338.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000229999.
HOVERGENHBG103408.
InParanoidQ96CM8.
KOK00666.
PhylomeDBQ96CM8.
TreeFamTF313466.

Gene expression databases

ArrayExpressQ96CM8.
BgeeQ96CM8.
CleanExHS_ACSF2.
GenevestigatorQ96CM8.

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

ChiTaRSACSF2. human.
GenomeRNAi80221.
NextBio70634.
PROQ96CM8.
SOURCESearch...

Entry information

Entry nameACSF2_HUMAN
AccessionPrimary (citable) accession number: Q96CM8
Secondary accession number(s): Q9H7G2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: March 19, 2014
This is version 88 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM