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Q9NZJ6 (COQ3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hexaprenyldihydroxybenzoate methyltransferase, mitochondrial

EC=2.1.1.114
Alternative name(s):
2-polyprenyl-6-hydroxyphenol methylase
EC=2.1.1.222
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
Short name=DHHB methyltransferase
Short name=DHHB-MT
Short name=DHHB-MTase
3-demethylubiquinone-10 3-methyltransferase
EC=2.1.1.64
Dihydroxyhexaprenylbenzoate methyltransferase
Gene names
Name:COQ3
ORF Names:UG0215E05
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate. Ref.6

S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n. Ref.6

S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol. Ref.6

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis.

Subcellular location

Mitochondrion matrix Probable.

Sequence similarities

Belongs to the methyltransferase superfamily. UbiG/COQ3 family.

Sequence caution

The sequence AAF66826.1 differs from that shown. Reason: Frameshift at positions 16, 18, 22, 26, 44, 49, 60, 363 and 364.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 369Hexaprenyldihydroxybenzoate methyltransferase, mitochondrialPRO_0000035926

Amino acid modifications

Modified residue1431N6-acetyllysine By similarity
Modified residue1491N6-acetyllysine By similarity
Modified residue1961N6-acetyllysine By similarity

Natural variations

Natural variant1341K → E. Ref.1 Ref.5
Corresponds to variant rs11548336 [ dbSNP | Ensembl ].
VAR_061925
Natural variant2721S → G. Ref.1 Ref.3 Ref.5 Ref.6
Corresponds to variant rs6925344 [ dbSNP | Ensembl ].
VAR_020789
Natural variant3291Y → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs4144164 [ dbSNP | Ensembl ].
VAR_020790

Experimental info

Sequence conflict211G → V in CAB66660. Ref.2
Sequence conflict1801N → D in CAB66660. Ref.2
Sequence conflict287 – 2893PET → LEP in AAN76515. Ref.1
Sequence conflict3211N → D in AAN76515. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NZJ6 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: B257A099D6C06A2D

FASTA36941,054
        10         20         30         40         50         60 
MWSGRKLGSS GGWFLRVLGP GGCNTKAARP LISSAVYVKN QLSGTLQIKP GVFNEYRTIW 

        70         80         90        100        110        120 
FKSYRTIFSC LNRIKSFRYP WARLYSTSQT TVDSGEVKTF LALAHKWWDE QGVYAPLHSM 

       130        140        150        160        170        180 
NDLRVPFIRD NLLKTIPNHQ PGKPLLGMKI LDVGCGGGLL TEPLGRLGAS VIGIDPVDEN 

       190        200        210        220        230        240 
IKTAQCHKSF DPVLDKRIEY RVCSLEEIVE ETAETFDAVV ASEVVEHVID LETFLQCCCQ 

       250        260        270        280        290        300 
VLKPGGSLFI TTINKTQLSY ALGIVFSEQI ASIVPKGTHT WEKFVSPETL ESILESNGLS 

       310        320        330        340        350        360 
VQTVVGMLYN PFSGYWHWSE NTSLNYAAYA VKSRVQEHPA SAEFVLKGET EELQANACTN 


PAVHEKLKK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of full-length cDNA clones from human fetal brain cDNA library."
Xie Y., Mao Y.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-134; GLY-272 AND HIS-329.
Tissue: Fetal brain.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-329.
Tissue: Kidney.
[3]"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], VARIANTS GLY-272 AND HIS-329.
Tissue: Skeletal muscle.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANTS GLU-134; GLY-272 AND HIS-329.
Tissue: Brain and Skin.
[6]"Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis."
Jonassen T., Clarke C.F.
J. Biol. Chem. 275:12381-12387(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-369, CATALYTIC ACTIVITY, VARIANTS GLY-272 AND HIS-329.
[7]"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
AF351615 mRNA. Translation: AAN76515.1.
AL136726 mRNA. Translation: CAB66660.1.
AK056955 mRNA. Translation: BAG51832.1.
AL513550 Genomic DNA. Translation: CAI17193.1.
BC015634 mRNA. Translation: AAH15634.2.
BC063463 mRNA. Translation: AAH63463.1.
AF193016 mRNA. Translation: AAF66826.1. Frameshift.
CCDSCCDS5042.1.
RefSeqNP_059117.3. NM_017421.3.
UniGeneHs.713623.

3D structure databases

ProteinModelPortalQ9NZJ6.
SMRQ9NZJ6. Positions 149-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119731. 1 interaction.
STRING9606.ENSP00000254759.

PTM databases

PhosphoSiteQ9NZJ6.

Polymorphism databases

DMDM313104241.

Proteomic databases

MaxQBQ9NZJ6.
PaxDbQ9NZJ6.
PRIDEQ9NZJ6.

Protocols and materials databases

DNASU51805.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254759; ENSP00000254759; ENSG00000132423.
GeneID51805.
KEGGhsa:51805.
UCSCuc003ppk.3. human.

Organism-specific databases

CTD51805.
GeneCardsGC06M099817.
H-InvDBHIX0200854.
HGNCHGNC:18175. COQ3.
HPAHPA031273.
HPA031274.
MIM605196. gene.
neXtProtNX_Q9NZJ6.
PharmGKBPA134934287.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2227.
HOVERGENHBG051078.
InParanoidQ9NZJ6.
KOK00591.
OMANYMVHTH.
OrthoDBEOG7FJH1X.
PhylomeDBQ9NZJ6.
TreeFamTF314553.

Enzyme and pathway databases

BioCycMetaCyc:HS05632-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00232.

Gene expression databases

ArrayExpressQ9NZJ6.
BgeeQ9NZJ6.
CleanExHS_COQ3.
GenevestigatorQ9NZJ6.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR013216. Methyltransf_11.
IPR029063. SAM-dependent_MTases-like.
IPR010233. UbiG_MeTrfase.
[Graphical view]
PANTHERPTHR23134. PTHR23134. 1 hit.
PfamPF08241. Methyltransf_11. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR01983. UbiG. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi51805.
NextBio55924.
PROQ9NZJ6.
SOURCESearch...

Entry information

Entry nameCOQ3_HUMAN
AccessionPrimary (citable) accession number: Q9NZJ6
Secondary accession number(s): B3KPX0 expand/collapse secondary AC list , Q5T061, Q6P4F0, Q8IXG6, Q96BG1, Q9H0N1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 128 of the entry and version 3 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 6

Human chromosome 6: entries, gene names and cross-references to MIM