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Q13057 (COASY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional coenzyme A synthase

Short name=CoA synthase
Alternative name(s):
NBP
POV-2

Including the following 2 domains:

  1. Phosphopantetheine adenylyltransferase
    EC=2.7.7.3
    Alternative name(s):
    Dephospho-CoA pyrophosphorylase
    Pantetheine-phosphate adenylyltransferase
    Short name=PPAT
  2. Dephospho-CoA kinase
    Short name=DPCK
    EC=2.7.1.24
    Alternative name(s):
    Dephosphocoenzyme A kinase
    Short name=DPCOAK
Gene names
Name:COASY
ORF Names:PSEC0106
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. Ref.1

Catalytic activity

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. HAMAP-Rule MF_00376

ATP + 3'-dephospho-CoA = ADP + CoA. HAMAP-Rule MF_00376

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. HAMAP-Rule MF_00376

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.

Subunit structure

Monomer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00376.

Tissue specificity

Expressed in all tissues examined including brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta, lung and peripheral blood leukocyte. Lowest expression in peripheral blood leukocytes and highest in kidney and liver. Isoform 2 is expressed mainly in the brain. Ref.1

Sequence similarities

In the central section; belongs to the eukaryotic CoaD family.

Contains 1 DPCK (dephospho-CoA kinase) domain.

Biophysicochemical properties

Kinetic parameters:

KM=7.6 mM for 4'-phoshopantetheine

KM=145 mM for ATP (in the PPAT reaction)

KM=16.7 mM for dephospho-CoA

KM=34.4 mM for ATP (in the DPCK reaction)

Sequence caution

The sequence AAA69699.1 differs from that shown. Reason: Frameshift at position 535.

The sequence AAF87955.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH06354.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH20985.1 differs from that shown. Reason: Erroneous initiation.

The sequence AK075415 differs from that shown. Reason: Frameshift at position 315.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EDC4Q6P2E93EBI-745967,EBI-1006038

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13057-1)

Also known as: CoASy alpha;

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.
Isoform 2 (identifier: Q13057-2)

Also known as: CoASy beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564Bifunctional coenzyme A synthase HAMAP-Rule MF_00376
PRO_0000173039

Regions

Domain360 – 563204DPCK
Nucleotide binding365 – 3728ATP Potential
Region180 – 358179Phosphopantetheine adenylyltransferase HAMAP-Rule MF_00376

Amino acid modifications

Modified residue1781Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue1831Phosphoserine Ref.14

Natural variations

Alternative sequence11M → MRTPRLRAQPRGAVYQAPSP PPAPVGLGSM in isoform 2.
VSP_036404
Natural variant551S → Y. Ref.1 Ref.4 Ref.6 Ref.7
Corresponds to variant rs615942 [ dbSNP | Ensembl ].
VAR_030299

Experimental info

Sequence conflict411L → P in BAG36775. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CoASy alpha) [UniParc].

Last modified June 27, 2003. Version 4.
Checksum: 7DC9E93B356C5DB7

FASTA56462,329
        10         20         30         40         50         60 
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA 

        70         80         90        100        110        120 
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT 

       130        140        150        160        170        180 
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV 

       190        200        210        220        230        240 
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL 

       250        260        270        280        290        300 
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR 

       310        320        330        340        350        360 
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV 

       370        380        390        400        410        420 
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI 

       430        440        450        460        470        480 
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ 

       490        500        510        520        530        540 
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI 

       550        560 
TQRQVEKAWA LLQKRIPKTH QALD 

« Hide

Isoform 2 (CoASy beta) [UniParc].

Checksum: BE77FF6197170615
Show »

FASTA59365,339

References

« Hide 'large scale' references
[1]"Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics."
Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A., de Crecy-Lagard V., Osterman A.
J. Biol. Chem. 277:21431-21439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT TYR-55.
[2]"Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)."
Aghajanian S., Worrall D.M.
Biochem. J. 365:13-18(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
[3]"HRI human cDNA sequencing project."
Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[4]"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] (ISOFORMS 1 AND 2), VARIANT TYR-55.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-55.
[7]"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] (ISOFORM 1), VARIANT TYR-55.
Tissue: Colon, Muscle and Uterus.
[8]"Molecular cloning of a NBP gene cDNA."
Zhu Y.-B., Han Y.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
[9]"A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase."
Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.
Hum. Genet. 96:532-538(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2).
Tissue: Ovary.
[10]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
[11]"Identification of a novel CoA synthase isoform, which is primarily expressed in the brain."
Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V., Gout I.T.
Biochem. Biophys. Res. Commun. 341:995-1000(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[12]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF453478 mRNA. Translation: AAL50813.1.
AY094602 mRNA. Translation: AAM19996.1.
AK075415 mRNA. No translation available.
AK297153 mRNA. Translation: BAG59652.1.
AK314076 mRNA. Translation: BAG36775.1.
AC067852 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60840.1.
BC006354 mRNA. Translation: AAH06354.1. Different initiation.
BC020985 mRNA. Translation: AAH20985.1. Different initiation.
BC067254 mRNA. Translation: AAH67254.1.
AF208536 mRNA. Translation: AAF87955.1. Different initiation.
U18919 mRNA. Translation: AAA69699.1. Frameshift.
BT007168 mRNA. Translation: AAP35832.1.
RefSeqNP_001035994.1. NM_001042529.2.
NP_001035997.2. NM_001042532.3.
NP_079509.5. NM_025233.6.
UniGeneHs.296422.
Hs.742262.

3D structure databases

ProteinModelPortalQ13057.
SMRQ13057. Positions 192-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123254. 12 interactions.
IntActQ13057. 3 interactions.
MINTMINT-1212728.
STRING9606.ENSP00000377404.

PTM databases

PhosphoSiteQ13057.

Polymorphism databases

DMDM32363505.

Proteomic databases

PaxDbQ13057.
PRIDEQ13057.

Protocols and materials databases

DNASU80347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393818; ENSP00000377406; ENSG00000068120. [Q13057-1]
ENST00000420359; ENSP00000413338; ENSG00000068120. [Q13057-1]
ENST00000421097; ENSP00000393564; ENSG00000068120. [Q13057-1]
ENST00000449624; ENSP00000407740; ENSG00000068120.
ENST00000590958; ENSP00000464814; ENSG00000068120. [Q13057-2]
GeneID80347.
KEGGhsa:80347.
UCSCuc002hzz.4. human. [Q13057-1]
uc010cyj.4. human. [Q13057-2]

Organism-specific databases

CTD80347.
GeneCardsGC17P040714.
HGNCHGNC:29932. COASY.
HPAHPA022875.
HPA022912.
HPA023273.
MIM609855. gene.
neXtProtNX_Q13057.
PharmGKBPA134867942.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0237.
HOVERGENHBG051059.
InParanoidQ13057.
KOK02318.
OMAMSGQQLV.
OrthoDBEOG7NKKKK.
PhylomeDBQ13057.

Enzyme and pathway databases

BRENDA2.7.1.24. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ13057.
UniPathwayUPA00241; UER00355.
UPA00241; UER00356.

Gene expression databases

ArrayExpressQ13057.
BgeeQ13057.
CleanExHS_COASY.
GenevestigatorQ13057.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00376. Dephospho_CoA_kinase.
InterProIPR004821. Cyt_trans-like.
IPR001977. Depp_CoAkinase.
IPR027417. P-loop_NTPase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01121. CoaE. 1 hit.
PF01467. CTP_transf_2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00152. TIGR00152. 1 hit.
PROSITEPS51219. DPCK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOASY. human.
GeneWikiCOASY.
GenomeRNAi80347.
NextBio70944.
PROQ13057.
SOURCESearch...

Entry information

Entry nameCOASY_HUMAN
AccessionPrimary (citable) accession number: Q13057
Secondary accession number(s): B2RA78 expand/collapse secondary AC list , B4DLU0, Q6GS23, Q8NBM7, Q8NEW1, Q8WXD4, Q9NRM3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 27, 2003
Last modified: April 16, 2014
This is version 142 of the entry and version 4 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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