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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)

Pathwayi

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. dephospho-CoA kinase activity Source: UniProtKB
  3. pantetheine-phosphate adenylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. coenzyme A biosynthetic process Source: UniProtKB
  2. coenzyme biosynthetic process Source: Reactome
  3. pantothenate metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

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.
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: Chromosome 17

Organism-specific databases

HGNCiHGNC:29932. COASY.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion matrix 1 Publication
Note: The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrial outer membrane Source: Reactome
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Neurodegeneration with brain iron accumulation 61 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.

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.
GenevestigatoriQ13057.

Organism-specific databases

HPAiHPA022875.
HPA022912.
HPA023273.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EDC4Q6P2E93EBI-745967,EBI-1006038

Protein-protein interaction databases

BioGridi123254. 24 interactions.
IntActiQ13057. 3 interactions.
MINTiMINT-1212728.
STRINGi9606.ENSP00000377404.

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.
OMAiPGMSLEG.
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_006722116.1. [Q13057-2]
UniGeneiHs.296422.
Hs.742262.

Genome annotation databases

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

Polymorphism databases

DMDMi32363505.

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_006722116.1. [Q13057-2]
UniGeneiHs.296422.
Hs.742262.

3D structure databases

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

Protein-protein interaction databases

BioGridi123254. 24 interactions.
IntActiQ13057. 3 interactions.
MINTiMINT-1212728.
STRINGi9606.ENSP00000377404.

PTM databases

PhosphoSiteiQ13057.

Polymorphism databases

DMDMi32363505.

Proteomic databases

MaxQBiQ13057.
PaxDbiQ13057.
PRIDEiQ13057.

Protocols and materials databases

DNASUi80347.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393818; ENSP00000377406; ENSG00000068120. [Q13057-1]
ENST00000421097; ENSP00000393564; ENSG00000068120. [Q13057-1]
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.
OMAiPGMSLEG.
OrthoDBiEOG7NKKKK.
PhylomeDBiQ13057.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00355.
UPA00241; UER00356.
BRENDAi2.7.1.24. 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.
GenevestigatoriQ13057.

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

« Hide 'large scale' publications
  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: March 4, 2015
This is version 151 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.