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Protein

Acyl-coenzyme A synthetase ACSM2A, mitochondrial

Gene

ACSM2A

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) (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+2 Publications, Mn2+2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391Coenzyme A1 Publication
Binding sitei364 – 3641Substrate1 Publication
Binding sitei446 – 4461ATP2 Publications
Binding sitei461 – 4611ATP2 Publications
Binding sitei472 – 4721Substrate1 Publication
Binding sitei501 – 5011Coenzyme A1 Publication
Binding sitei532 – 5321Coenzyme A1 Publication
Binding sitei557 – 5571ATP2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2299ATP2 Publications
Nucleotide bindingi359 – 3646ATP2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • butyrate-CoA ligase activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • fatty acid metabolic process Source: UniProtKB-KW
  • glucose homeostasis Source: BHF-UCL
  • medium-chain fatty-acyl-CoA metabolic process Source: BHF-UCL
  • triglyceride homeostasis Source: BHF-UCL
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_6812. Conjugation of salicylate with glycine.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A synthetase ACSM2A, mitochondrial (EC:6.2.1.2)
Alternative name(s):
Acyl-CoA synthetase medium-chain family member 2A
Butyrate--CoA ligase 2A
Butyryl-coenzyme A synthetase 2A
Middle-chain acyl-CoA synthetase 2A
Gene namesi
Name:ACSM2A
Synonyms:ACSM2, MACS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:32017. ACSM2A.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162375402.

Polymorphism and mutation databases

BioMutaiACSM2A.
DMDMi257050995.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
BLAST
Chaini47 – 577531Acyl-coenzyme A synthetase ACSM2A, mitochondrialPRO_0000306093Add
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 – 5131PhosphoserineBy similarity
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

MaxQBiQ08AH3.
PaxDbiQ08AH3.
PRIDEiQ08AH3.

PTM databases

PhosphoSiteiQ08AH3.

Expressioni

Gene expression databases

BgeeiQ08AH3.
ExpressionAtlasiQ08AH3. baseline.
GenevisibleiQ08AH3. HS.

Organism-specific databases

HPAiHPA057699.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000219054.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni34 – 363Combined sources
Helixi46 – 494Combined sources
Helixi51 – 599Combined sources
Beta strandi67 – 726Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 9816Combined sources
Turni99 – 1013Combined sources
Beta strandi108 – 1125Combined sources
Helixi117 – 12913Combined sources
Beta strandi132 – 1354Combined sources
Helixi142 – 15211Combined sources
Beta strandi155 – 1606Combined sources
Turni161 – 1633Combined sources
Helixi164 – 1707Combined sources
Helixi171 – 1733Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi191 – 1933Combined sources
Helixi194 – 2007Combined sources
Beta strandi214 – 2207Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi230 – 2345Combined sources
Helixi235 – 24511Combined sources
Turni246 – 2494Combined sources
Beta strandi256 – 2594Combined sources
Helixi266 – 2716Combined sources
Helixi274 – 2785Combined sources
Beta strandi282 – 2865Combined sources
Helixi293 – 30210Combined sources
Beta strandi307 – 3104Combined sources
Helixi312 – 3198Combined sources
Turni323 – 3253Combined sources
Beta strandi333 – 3397Combined sources
Helixi343 – 35311Combined sources
Beta strandi358 – 3636Combined sources
Turni364 – 3663Combined sources
Beta strandi367 – 3715Combined sources
Beta strandi392 – 3954Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi415 – 4173Combined sources
Helixi430 – 4356Combined sources
Beta strandi441 – 45010Combined sources
Beta strandi456 – 4616Combined sources
Helixi462 – 4643Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi471 – 4733Combined sources
Helixi475 – 4839Combined sources
Beta strandi488 – 49811Combined sources
Turni499 – 5013Combined sources
Beta strandi502 – 51110Combined sources
Helixi513 – 5153Combined sources
Helixi520 – 53415Combined sources
Helixi537 – 5393Combined sources
Beta strandi542 – 5487Combined sources
Helixi560 – 5678Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VZEX-ray2.45A/B/C32-577[»]
2WD9X-ray2.60A/B/C32-576[»]
3B7WX-ray2.00A32-577[»]
3C5EX-ray1.60A32-577[»]
3DAYX-ray1.95A32-577[»]
3EQ6X-ray2.40A/B32-577[»]
3GPCX-ray1.90A/B32-577[»]
ProteinModelPortaliQ08AH3.
SMRiQ08AH3. Positions 34-569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08AH3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni469 – 4713Coenzyme A binding1 Publication
Regioni540 – 5423Coenzyme A binding1 Publication

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ08AH3.
KOiK01896.
OMAiTIQMKAK.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ08AH3.
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.

Q08AH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV
60 70 80 90 100
LDHWADMEKA GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANVLSGA
110 120 130 140 150
CGLQRGDRVA VVLPRVPEWW 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 CSLMEPWALG ACTFVHLLPK FDPLVILKTL
310 320 330 340 350
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCVTVGES LLPETLENWR
360 370 380 390 400
AQTGLDIRES YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQIIDDKGN
410 420 430 440 450
VLPPGTEGDI GIRVKPIRPI GIFSGYVDNP DKTAANIRGD FWLLGDRGIK
460 470 480 490 500
DEDGYFQFMG RANDIINSSG YRIGPSEVEN ALMEHPAVVE TAVISSPDPV
510 520 530 540 550
RGEVVKAFVV LASQFLSHDP EQLTKELQQH VKSVTAPYKY PRKIEFVLNL
560 570
PKTVTGKIQR AKLRDKEWKM SGKARAQ
Length:577
Mass (Da):64,223
Last modified:September 1, 2009 - v2
Checksum:i16167FC69562436F
GO

Sequence cautioni

The sequence AAC23497.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti463 – 4631N → D in BAG53201 (PubMed:14702039).Curated
Sequence conflicti463 – 4631N → D in AAI25177 (PubMed:15489334).Curated
Sequence conflicti463 – 4631N → D in AAC23497 (PubMed:10493829).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351V → L.
Corresponds to variant rs4643305 [ dbSNP | Ensembl ].
VAR_058692
Natural varianti336 – 3361T → A.
Corresponds to variant rs5002299 [ dbSNP | Ensembl ].
VAR_058693
Natural varianti337 – 3371V → G.
Corresponds to variant rs4586421 [ dbSNP | Ensembl ].
VAR_058694
Natural varianti513 – 5131S → L.3 Publications
Corresponds to variant rs1133607 [ dbSNP | Ensembl ].
VAR_035247
Natural varianti561 – 5611A → T.
Corresponds to variant rs1054977 [ dbSNP | Ensembl ].
VAR_035248

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096039 mRNA. Translation: BAG53201.1.
AC137056 Genomic DNA. No translation available.
BC125176 mRNA. Translation: AAI25177.1.
AC003034 Genomic DNA. Translation: AAC23497.1. Sequence problems.
CCDSiCCDS32401.1.
RefSeqiNP_001295101.1. NM_001308172.1.
UniGeneiHs.298252.
Hs.656497.

Genome annotation databases

EnsembliENST00000219054; ENSP00000219054; ENSG00000183747.
ENST00000396104; ENSP00000379411; ENSG00000183747.
ENST00000573854; ENSP00000459451; ENSG00000183747.
ENST00000575690; ENSP00000460349; ENSG00000183747.
GeneIDi123876.
KEGGihsa:123876.
UCSCiuc002dhf.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK096039 mRNA. Translation: BAG53201.1.
AC137056 Genomic DNA. No translation available.
BC125176 mRNA. Translation: AAI25177.1.
AC003034 Genomic DNA. Translation: AAC23497.1. Sequence problems.
CCDSiCCDS32401.1.
RefSeqiNP_001295101.1. NM_001308172.1.
UniGeneiHs.298252.
Hs.656497.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VZEX-ray2.45A/B/C32-577[»]
2WD9X-ray2.60A/B/C32-576[»]
3B7WX-ray2.00A32-577[»]
3C5EX-ray1.60A32-577[»]
3DAYX-ray1.95A32-577[»]
3EQ6X-ray2.40A/B32-577[»]
3GPCX-ray1.90A/B32-577[»]
ProteinModelPortaliQ08AH3.
SMRiQ08AH3. Positions 34-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000219054.

PTM databases

PhosphoSiteiQ08AH3.

Polymorphism and mutation databases

BioMutaiACSM2A.
DMDMi257050995.

Proteomic databases

MaxQBiQ08AH3.
PaxDbiQ08AH3.
PRIDEiQ08AH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219054; ENSP00000219054; ENSG00000183747.
ENST00000396104; ENSP00000379411; ENSG00000183747.
ENST00000573854; ENSP00000459451; ENSG00000183747.
ENST00000575690; ENSP00000460349; ENSG00000183747.
GeneIDi123876.
KEGGihsa:123876.
UCSCiuc002dhf.4. human.

Organism-specific databases

CTDi123876.
GeneCardsiGC16P020463.
H-InvDBHIX0012859.
HGNCiHGNC:32017. ACSM2A.
HPAiHPA057699.
MIMi614358. gene.
neXtProtiNX_Q08AH3.
PharmGKBiPA162375402.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0365.
GeneTreeiENSGT00760000119178.
HOGENOMiHOG000229982.
HOVERGENiHBG053031.
InParanoidiQ08AH3.
KOiK01896.
OMAiTIQMKAK.
OrthoDBiEOG7D85VZ.
PhylomeDBiQ08AH3.
TreeFamiTF354264.

Enzyme and pathway databases

ReactomeiREACT_6812. Conjugation of salicylate with glycine.

Miscellaneous databases

EvolutionaryTraceiQ08AH3.
GenomeRNAii123876.
NextBioi81177.
PROiQ08AH3.
SOURCEiSearch...

Gene expression databases

BgeeiQ08AH3.
ExpressionAtlasiQ08AH3. baseline.
GenevisibleiQ08AH3. HS.

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].
    Tissue: Kidney.
  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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 299-577, VARIANT LEU-513.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Crystal structure of L64P mutant of human acyl-CoA synthetase medium-chain family member 2A."
    Structural genomics consortium (SGC)
    Submitted (FEB-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH AMP AND MAGNESIUM.
  7. "Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A."
    Kochan G., Pilka E.S., von Delft F., Oppermann U., Yue W.W.
    J. Mol. Biol. 388:997-1008(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 32-577 IN COMPLEXES WITH ATP; COENZYME A; IBUPROFEN AND MAGNESIUM.
  8. "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: VARIANT LEU-513.
  9. "The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population."
    Lindner I., Rubin D., Helwig U., Nitz I., Hampe J., Schreiber S., Schrezenmeir J., Doering F.
    Mol. Nutr. Food Res. 50:270-274(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-513.

Entry informationi

Entry nameiACS2A_HUMAN
AccessioniPrimary (citable) accession number: Q08AH3
Secondary accession number(s): B3KTT9, O75202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 1, 2009
Last modified: July 22, 2015
This is version 75 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.