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Protein

Bifunctional coenzyme A synthase

Gene

COASY

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

Functioni

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.1 Publication

Catalytic activityi

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.
ATP + 3'-dephospho-CoA = ADP + CoA.

Kineticsi

  1. KM=7.6 mM for 4'-phoshopantetheine
  2. KM=145 mM for ATP (in the PPAT reaction)
  3. KM=16.7 mM for dephospho-CoA
  4. KM=34.4 mM for ATP (in the DPCK reaction)

    Pathway:icoenzyme A biosynthesis

    This protein is involved in step 4 and 5 of the subpathway that synthesizes CoA from (R)-pantothenate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Pantothenate kinase 4 (PANK4), Pantothenate kinase 3 (PANK3), Pantothenate kinase 1 (PANK1), Pantothenate kinase 2, mitochondrial (PANK2)
    2. Phosphopantothenate--cysteine ligase (PPCS)
    3. Phosphopantothenoylcysteine decarboxylase (PPCDC)
    4. Bifunctional coenzyme A synthase (COASY)
    5. Bifunctional coenzyme A synthase (COASY)
    This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi365 – 3728ATPSequence Analysis

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • dephospho-CoA kinase activity Source: UniProtKB
    • pantetheine-phosphate adenylyltransferase activity Source: UniProtKB

    GO - Biological processi

    Keywords - Molecular functioni

    Kinase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Coenzyme A biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.24. 2681.
    2.7.7.3. 2681.
    ReactomeiREACT_11218. Coenzyme A biosynthesis.
    SABIO-RKQ13057.
    UniPathwayiUPA00241; UER00355.
    UPA00241; UER00356.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional coenzyme A synthase
    Short name:
    CoA synthase
    Alternative name(s):
    NBP
    POV-2
    Including the following 2 domains:
    Phosphopantetheine adenylyltransferase (EC:2.7.7.3)
    Alternative name(s):
    Dephospho-CoA pyrophosphorylase
    Pantetheine-phosphate adenylyltransferase
    Short name:
    PPAT
    Dephospho-CoA kinase (EC:2.7.1.24)
    Short name:
    DPCK
    Alternative name(s):
    Dephosphocoenzyme A kinase
    Short name:
    DPCOAK
    Gene namesi
    Name:COASY
    ORF Names:PSEC0106
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:29932. COASY.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • extracellular exosome Source: UniProtKB
    • mitochondrial matrix Source: UniProtKB
    • mitochondrial outer membrane Source: Reactome
    • nucleoplasm Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Neurodegeneration with brain iron accumulation 6 (NBIA6)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by progressive motor and cognitive dysfunction beginning in childhood or young adulthood. Patients show extrapyramidal motor signs, such as spasticity, dystonia, and parkinsonism.

    See also OMIM:615643
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti499 – 4991R → C in NBIA6. 1 Publication
    VAR_070975

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi615643. phenotype.
    Orphaneti397725. COASY protein-associated neurodegeneration.
    PharmGKBiPA134867942.

    Polymorphism and mutation databases

    BioMutaiCOASY.
    DMDMi32363505.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 564564Bifunctional coenzyme A synthasePRO_0000173039Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei178 – 1781Phosphoserine4 Publications
    Modified residuei183 – 1831Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13057.
    PaxDbiQ13057.
    PRIDEiQ13057.

    PTM databases

    PhosphoSiteiQ13057.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    BgeeiQ13057.
    CleanExiHS_COASY.
    ExpressionAtlasiQ13057. baseline and differential.
    GenevisibleiQ13057. HS.

    Organism-specific databases

    HPAiHPA022875.
    HPA022912.
    HPA023273.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CNTROBQ8N1373EBI-10227704,EBI-947360
    EDC4Q6P2E93EBI-745967,EBI-1006038
    KIAA1958Q8N8K93EBI-10227704,EBI-10181113

    Protein-protein interaction databases

    BioGridi123254. 21 interactions.
    IntActiQ13057. 5 interactions.
    MINTiMINT-1212728.
    STRINGi9606.ENSP00000464814.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13057.
    SMRiQ13057. Positions 195-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini360 – 563204DPCKAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni180 – 358179Phosphopantetheine adenylyltransferaseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0237.
    GeneTreeiENSGT00550000075078.
    HOVERGENiHBG051059.
    InParanoidiQ13057.
    KOiK02318.
    OMAiSRVFGNK.
    OrthoDBiEOG7NKKKK.
    PhylomeDBiQ13057.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00376. Dephospho_CoA_kinase.
    InterProiIPR004821. Cyt_trans-like.
    IPR001977. Depp_CoAkinase.
    IPR027417. P-loop_NTPase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF01121. CoaE. 1 hit.
    PF01467. CTP_transf_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00152. TIGR00152. 1 hit.
    PROSITEiPS51219. DPCK. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q13057-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP
    60 70 80 90 100
    AQPQSSPVQA TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL
    110 120 130 140 150
    PTSVQNLAHP PEVVLTDFQT LDGSQYNPVK QQLVRYATSC YSCCPRLASV
    160 170 180 190 200
    LLYSDYGIGE VPVEPLDVPL PSTIRPASPV AGSPKQPVRG YYRGAVGGTF
    210 220 230 240 250
    DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL LQPYTERVEH
    260 270 280 290 300
    LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
    310 320 330 340 350
    FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE
    360 370 380 390 400
    RPELPTCLYV IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG
    410 420 430 440 450
    PAYQPVVEAF GTDILHKDGI INRKVLGSRV FGNKKQLKIL TDIMWPIIAK
    460 470 480 490 500
    LAREEMDRAV AEGKRVCVID AAVLLEAGWQ NLVHEVWTAV IPETEAVRRI
    510 520 530 540 550
    VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI TQRQVEKAWA
    560
    LLQKRIPKTH QALD
    Length:564
    Mass (Da):62,329
    Last modified:June 27, 2003 - v4
    Checksum:i7DC9E93B356C5DB7
    GO
    Isoform 2 (identifier: Q13057-2) [UniParc]FASTAAdd to basket

    Also known as: CoASy beta

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

    Show »
    Length:593
    Mass (Da):65,339
    Checksum:iBE77FF6197170615
    GO

    Sequence cautioni

    The sequence AAA69699.1 differs from that shown. Reason: Frameshift at position 535. Curated
    The sequence AAF87955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH06354.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH20985.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AK075415 differs from that shown. Reason: Frameshift at position 315. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411L → P in BAG36775 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551S → Y.4 Publications
    Corresponds to variant rs615942 [ dbSNP | Ensembl ].
    VAR_030299
    Natural varianti499 – 4991R → C in NBIA6. 1 Publication
    VAR_070975

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRTPRLRAQPRGAVYQAPSP PPAPVGLGSM in isoform 2. 1 PublicationVSP_036404

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS11429.1. [Q13057-1]
    CCDS45685.1. [Q13057-2]
    RefSeqiNP_001035994.1. NM_001042529.2. [Q13057-1]
    NP_001035997.2. NM_001042532.3. [Q13057-2]
    NP_079509.5. NM_025233.6. [Q13057-1]
    XP_006722179.1. XM_006722116.2. [Q13057-2]
    XP_011523602.1. XM_011525300.1. [Q13057-1]
    UniGeneiHs.296422.
    Hs.742262.

    Genome annotation databases

    EnsembliENST00000393818; ENSP00000377406; ENSG00000068120.
    ENST00000421097; ENSP00000393564; ENSG00000068120.
    ENST00000590958; ENSP00000464814; ENSG00000068120. [Q13057-2]
    GeneIDi80347.
    KEGGihsa:80347.
    UCSCiuc002hzz.4. human. [Q13057-1]
    uc010cyj.4. human. [Q13057-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS11429.1. [Q13057-1]
    CCDS45685.1. [Q13057-2]
    RefSeqiNP_001035994.1. NM_001042529.2. [Q13057-1]
    NP_001035997.2. NM_001042532.3. [Q13057-2]
    NP_079509.5. NM_025233.6. [Q13057-1]
    XP_006722179.1. XM_006722116.2. [Q13057-2]
    XP_011523602.1. XM_011525300.1. [Q13057-1]
    UniGeneiHs.296422.
    Hs.742262.

    3D structure databases

    ProteinModelPortaliQ13057.
    SMRiQ13057. Positions 195-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi123254. 21 interactions.
    IntActiQ13057. 5 interactions.
    MINTiMINT-1212728.
    STRINGi9606.ENSP00000464814.

    PTM databases

    PhosphoSiteiQ13057.

    Polymorphism and mutation databases

    BioMutaiCOASY.
    DMDMi32363505.

    Proteomic databases

    MaxQBiQ13057.
    PaxDbiQ13057.
    PRIDEiQ13057.

    Protocols and materials databases

    DNASUi80347.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000393818; ENSP00000377406; ENSG00000068120.
    ENST00000421097; ENSP00000393564; ENSG00000068120.
    ENST00000590958; ENSP00000464814; ENSG00000068120. [Q13057-2]
    GeneIDi80347.
    KEGGihsa:80347.
    UCSCiuc002hzz.4. human. [Q13057-1]
    uc010cyj.4. human. [Q13057-2]

    Organism-specific databases

    CTDi80347.
    GeneCardsiGC17P040714.
    HGNCiHGNC:29932. COASY.
    HPAiHPA022875.
    HPA022912.
    HPA023273.
    MIMi609855. gene.
    615643. phenotype.
    neXtProtiNX_Q13057.
    Orphaneti397725. COASY protein-associated neurodegeneration.
    PharmGKBiPA134867942.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0237.
    GeneTreeiENSGT00550000075078.
    HOVERGENiHBG051059.
    InParanoidiQ13057.
    KOiK02318.
    OMAiSRVFGNK.
    OrthoDBiEOG7NKKKK.
    PhylomeDBiQ13057.

    Enzyme and pathway databases

    UniPathwayiUPA00241; UER00355.
    UPA00241; UER00356.
    BRENDAi2.7.1.24. 2681.
    2.7.7.3. 2681.
    ReactomeiREACT_11218. Coenzyme A biosynthesis.
    SABIO-RKQ13057.

    Miscellaneous databases

    ChiTaRSiCOASY. human.
    GeneWikiiCOASY.
    GenomeRNAii80347.
    NextBioi70944.
    PROiQ13057.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ13057.
    CleanExiHS_COASY.
    ExpressionAtlasiQ13057. baseline and differential.
    GenevisibleiQ13057. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00376. Dephospho_CoA_kinase.
    InterProiIPR004821. Cyt_trans-like.
    IPR001977. Depp_CoAkinase.
    IPR027417. P-loop_NTPase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF01121. CoaE. 1 hit.
    PF01467. CTP_transf_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00152. TIGR00152. 1 hit.
    PROSITEiPS51219. DPCK. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: SUBCELLULAR LOCATION, VARIANT NBIA6 CYS-499.
    17. "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-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiCOASY_HUMAN
    AccessioniPrimary (citable) accession number: Q13057
    Secondary accession number(s): B2RA78
    , B4DLU0, Q6GS23, Q8NBM7, Q8NEW1, Q8WXD4, Q9NRM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 27, 2003
    Last modified: July 22, 2015
    This is version 156 of the entry and version 4 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.