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Protein

Atypical kinase COQ8A, mitochondrial

Gene

COQ8A

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

Functioni

Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:25498144, PubMed:21296186, PubMed:25540914, PubMed:27499294). Its substrate specificity is unclear: does not show any protein kinase activity (PubMed:25498144, PubMed:27499294). Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (PubMed:25498144, PubMed:27499294). Shows an unusual selectivity for binding ADP over ATP (PubMed:25498144).2 Publications2 Publications

Enzyme regulationi

Autoinhibited by the N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket. Nucleotide-binding relieves inhibition (PubMed:27499294).2 Publications

Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei340ATP1 Publication1 PublicationImported1
Binding sitei358ATP1 PublicationImported1
Active sitei488Proton acceptor1 Publication1
Binding sitei493ATP1 PublicationImported1
Binding sitei507ATP1 PublicationImported1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi445 – 448ATP1 PublicationImported4

GO - Molecular functioni

  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB

GO - Biological processi

  • phosphorylation Source: UniProtKB
  • ubiquinone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163050-MONOMER.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
Atypical kinase COQ8A, mitochondrialCurated (EC:2.7.-.-1 Publication)
Alternative name(s):
Chaperone activity of bc1 complex-like1 Publication
Short name:
Chaperone-ABC1-like1 Publication
Coenzyme Q protein 8ACurated
aarF domain-containing protein kinase 3Imported
Gene namesi
Name:COQ8A1 PublicationImported
Synonyms:ADCK3Imported, CABC11 Publication
ORF Names:PP265
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16812. COQ8A.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei214 – 230HelicalSequence analysis1 PublicationAdd BLAST17

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Coenzyme Q10 deficiency, primary, 4 (COQ10D4)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by childhood-onset of cerebellar ataxia and exercise intolerance. Patient manifest gait ataxia and cerebellar atrophy with slow progression. Additional features include brisk tendon reflexes and Hoffmann sign, variable psychomotor retardation and variable seizures.
See also OMIM:612016
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_044402213R → W in COQ10D4. 2 PublicationsCorresponds to variant rs119468005dbSNPEnsembl.1
Natural variantiVAR_072622271R → C in COQ10D4. 1 PublicationCorresponds to variant rs145034527dbSNPEnsembl.1
Natural variantiVAR_044403272G → D in COQ10D4. 2 PublicationsCorresponds to variant rs119468006dbSNPEnsembl.1
Natural variantiVAR_044404272G → V in COQ10D4. 2 PublicationsCorresponds to variant rs119468006dbSNPEnsembl.1
Natural variantiVAR_072623299R → W in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs201908721dbSNPEnsembl.1
Natural variantiVAR_072624304A → T in COQ10D4. 1 PublicationCorresponds to variant rs778798354dbSNPEnsembl.1
Natural variantiVAR_072625304A → V in COQ10D4. 1 PublicationCorresponds to variant rs748118737dbSNPEnsembl.1
Natural variantiVAR_072626429Y → C in COQ10D4; decreased stability. 2 PublicationsCorresponds to variant rs144147839dbSNPEnsembl.1
Natural variantiVAR_044405514Y → C in COQ10D4. 1 PublicationCorresponds to variant rs119468008dbSNPEnsembl.1
Natural variantiVAR_044406549G → S in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs119468009dbSNPEnsembl.1
Natural variantiVAR_044407551E → K in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs119468004dbSNPEnsembl.1
Natural variantiVAR_076860578F → V in COQ10D4; unknown pathological significance. 1 Publication1
Natural variantiVAR_044408584Missing in COQ10D4. 1 Publication1
Natural variantiVAR_072627602P → R in COQ10D4; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 PublicationCorresponds to variant rs61995958dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi214L → A, I, L or F: Strongly impairs homodimerization. 1 Publication1
Mutagenesisi214L → I, F, G or V: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi215A → I, L or G: Does not impair homodimerization. 1 Publication1
Mutagenesisi216N → A, L, F or M: Does not impair homodimerization. 1 Publication1
Mutagenesisi217F → A: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi218G → I, L or F: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi219G → A or F: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi219G → I: Strongly impairs homodimerization. 1 Publication1
Mutagenesisi220L → G: Impaired homodimerization. 1 Publication1
Mutagenesisi221A → L: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi222V → A: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi223G → A, I, L or F: Strongly impairs homodimerization. 1 Publication1
Mutagenesisi224L → V: Impaired homodimerization. 1 Publication1
Mutagenesisi225G → L: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi226F → A: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi227G → V, F, L or I: Strongly impairs homodimerization. 1 Publication1
Mutagenesisi228A → I, L or F: Does not impair homodimerization. 1 Publication1
Mutagenesisi229L → A: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi230A → I: Slightly impaired homodimerization. 1 Publication1
Mutagenesisi276K → R or H: Does not affect selectivity for binding ADP or ATP. Impaired multi-subunit COQ enzyme complex. 2 Publications1
Mutagenesisi279Q → R or H: Does not affect selectivity for binding ADP or ATP. 1 Publication1
Mutagenesisi339A → G: Enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo. 1 Publication1
Mutagenesisi358K → R: Abolishes binding ADP or ATP. 1 Publication1
Mutagenesisi405E → A or Q: Slightly affects selectivity for binding ADP or ATP. 1 Publication1
Mutagenesisi411E → Q: Impaired binding ADP or ATP. 1 Publication1
Mutagenesisi488D → N: Impaired binding ADP or ATP. 1 Publication1
Mutagenesisi493N → A: Impaired binding ADP or ATP. 1 Publication1
Mutagenesisi507D → N: Strongly impairs binding ADP or ATP. Impaired multi-subunit COQ enzyme complex. 2 Publications1
Mutagenesisi611R → A or Q: Does not affect selectivity for binding ADP or ATP. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi56997.
MalaCardsiADCK3.
MIMi612016. phenotype.
OpenTargetsiENSG00000163050.
Orphaneti139485. Autosomal recessive ataxia due to ubiquinone deficiency.
PharmGKBiPA25999.

Chemistry databases

ChEMBLiCHEMBL5550.
GuidetoPHARMACOLOGYi1927.

Polymorphism and mutation databases

BioMutaiADCK3.
DMDMi27923741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 162Mitochondrion1 PublicationAdd BLAST162
ChainiPRO_0000000262163 – 647Atypical kinase COQ8A, mitochondrialAdd BLAST485

Proteomic databases

EPDiQ8NI60.
MaxQBiQ8NI60.
PaxDbiQ8NI60.
PeptideAtlasiQ8NI60.
PRIDEiQ8NI60.

PTM databases

iPTMnetiQ8NI60.
PhosphoSitePlusiQ8NI60.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in adrenal gland, heart, pancreas, nasal mucosa, stomach, uterus and skeletal muscle.1 Publication

Inductioni

By p53/TP53.1 Publication

Gene expression databases

BgeeiENSG00000163050.
CleanExiHS_CABC1.
ExpressionAtlasiQ8NI60. baseline and differential.
GenevisibleiQ8NI60. HS.

Organism-specific databases

HPAiHPA061662.

Interactioni

Subunit structurei

Homodimer; homodimerizes via its transmembrane region (PubMed:25216398). Interacts with the multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (PubMed:27499294, PubMed:27499296).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-745535,EBI-741181
RABAC1Q9UI148EBI-745535,EBI-712367
REEP6Q96HR97EBI-745535,EBI-750345
TFIP11Q9UBB97EBI-745535,EBI-1105213
TMEM159Q96B965EBI-745535,EBI-7055862
TMEM239Q8WW345EBI-745535,EBI-9675724

Protein-protein interaction databases

BioGridi121312. 39 interactors.
IntActiQ8NI60. 17 interactors.
MINTiMINT-1479202.
STRINGi9606.ENSP00000355739.

Chemistry databases

BindingDBiQ8NI60.

Structurei

Secondary structure

1647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi260 – 269Combined sources10
Helixi271 – 281Combined sources11
Beta strandi284 – 289Combined sources6
Helixi291 – 302Combined sources12
Helixi303 – 306Combined sources4
Helixi309 – 320Combined sources12
Helixi325 – 327Combined sources3
Beta strandi328 – 331Combined sources4
Beta strandi336 – 339Combined sources4
Beta strandi342 – 349Combined sources8
Beta strandi354 – 360Combined sources7
Turni362 – 364Combined sources3
Helixi365 – 367Combined sources3
Helixi368 – 382Combined sources15
Beta strandi387 – 389Combined sources3
Helixi391 – 393Combined sources3
Helixi395 – 405Combined sources11
Helixi408 – 421Combined sources14
Turni422 – 424Combined sources3
Beta strandi426 – 429Combined sources4
Helixi435 – 437Combined sources3
Beta strandi442 – 446Combined sources5
Beta strandi450 – 452Combined sources3
Helixi453 – 455Combined sources3
Helixi461 – 480Combined sources20
Beta strandi484 – 488Combined sources5
Helixi491 – 493Combined sources3
Beta strandi494 – 497Combined sources4
Turni498 – 501Combined sources4
Beta strandi502 – 505Combined sources4
Helixi508 – 510Combined sources3
Beta strandi511 – 513Combined sources3
Helixi516 – 530Combined sources15
Helixi534 – 543Combined sources10
Helixi553 – 571Combined sources19
Helixi581 – 588Combined sources8
Helixi589 – 594Combined sources6
Beta strandi596 – 600Combined sources5
Helixi604 – 622Combined sources19
Helixi630 – 643Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PEDX-ray1.64A256-647[»]
5I35X-ray2.30A256-647[»]
ProteinModelPortaliQ8NI60.
SMRiQ8NI60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini329 – 518Protein kinaseAdd BLAST190

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi276 – 279KxGQ motif1 Publication4
Motifi337 – 340AAAS motif1 Publication4

Domaini

Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains, a number of features are positioned to inhibit the kinase activity: (1) an atypical AAAS motif in an alanine-rich (A-rich) loop that replaces the canonical glycine-rich (G-rich) nucleotide-binding loop and limits ATP binding by establishing an unusual selectivity for ADP and (2) an N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket (PubMed:25498144). Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture (PubMed:27499294).2 Publications

Sequence similaritiesi

Contains 1 protein kinase domain.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1234. Eukaryota.
COG0661. LUCA.
GeneTreeiENSGT00550000074739.
HOGENOMiHOG000201140.
HOVERGENiHBG061318.
InParanoidiQ8NI60.
KOiK08869.
OMAiYEVKVME.
OrthoDBiEOG091G02P9.
PhylomeDBiQ8NI60.
TreeFamiTF300630.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR004147. UbiB_dom.
[Graphical view]
PfamiPF03109. ABC1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NI60-1) [UniParc]FASTAAdd to basket

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
MAAILGDTIM VAKGLVKLTQ AAVETHLQHL GIGGELIMAA RALQSTAVEQ
60 70 80 90 100
IGMFLGKVQG QDKHEEYFAE NFGGPEGEFH FSVPHAAGAS TDFSSASAPD
110 120 130 140 150
QSAPPSLGHA HSEGPAPAYV ASGPFREAGF PGQASSPLGR ANGRLFANPR
160 170 180 190 200
DSFSAMGFQR RFFHQDQSPV GGLTAEDIEK ARQAKARPEN KQHKQTLSEH
210 220 230 240 250
ARERKVPVTR IGRLANFGGL AVGLGFGALA EVAKKSLRSE DPSGKKAVLG
260 270 280 290 300
SSPFLSEANA ERIVRTLCKV RGAALKLGQM LSIQDDAFIN PHLAKIFERV
310 320 330 340 350
RQSADFMPLK QMMKTLNNDL GPNWRDKLEY FEERPFAAAS IGQVHLARMK
360 370 380 390 400
GGREVAMKIQ YPGVAQSINS DVNNLMAVLN MSNMLPEGLF PEHLIDVLRR
410 420 430 440 450
ELALECDYQR EAACARKFRD LLKGHPFFYV PEIVDELCSP HVLTTELVSG
460 470 480 490 500
FPLDQAEGLS QEIRNEICYN ILVLCLRELF EFHFMQTDPN WSNFFYDPQQ
510 520 530 540 550
HKVALLDFGA TREYDRSFTD LYIQIIRAAA DRDRETVRAK SIEMKFLTGY
560 570 580 590 600
EVKVMEDAHL DAILILGEAF ASDEPFDFGT QSTTEKIHNL IPVMLRHRLV
610 620 630 640
PPPEETYSLH RKMGGSFLIC SKLKARFPCK AMFEEAYSNY CKRQAQQ
Length:647
Mass (Da):71,950
Last modified:October 1, 2002 - v1
Checksum:iDEF8F022027BF6CC
GO
Isoform 2 (identifier: Q8NI60-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-484: Missing.

Note: No experimental confirmation available.
Show »
Length:163
Mass (Da):18,937
Checksum:iA309AB9DDBE67C56
GO
Isoform 3 (identifier: Q8NI60-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Note: No experimental confirmation available.
Show »
Length:595
Mass (Da):66,627
Checksum:i83F12FA56BCB190E
GO
Isoform 4 (identifier: Q8NI60-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-279: Missing.

Note: No experimental confirmation available.
Show »
Length:368
Mass (Da):42,537
Checksum:i8522AEA0D7547110
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti283 – 284IQ → VR in BAC11143 (PubMed:14702039).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02031985H → Q.Corresponds to variant rs2297411dbSNPEnsembl.1
Natural variantiVAR_044402213R → W in COQ10D4. 2 PublicationsCorresponds to variant rs119468005dbSNPEnsembl.1
Natural variantiVAR_072622271R → C in COQ10D4. 1 PublicationCorresponds to variant rs145034527dbSNPEnsembl.1
Natural variantiVAR_044403272G → D in COQ10D4. 2 PublicationsCorresponds to variant rs119468006dbSNPEnsembl.1
Natural variantiVAR_044404272G → V in COQ10D4. 2 PublicationsCorresponds to variant rs119468006dbSNPEnsembl.1
Natural variantiVAR_072623299R → W in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs201908721dbSNPEnsembl.1
Natural variantiVAR_072624304A → T in COQ10D4. 1 PublicationCorresponds to variant rs778798354dbSNPEnsembl.1
Natural variantiVAR_072625304A → V in COQ10D4. 1 PublicationCorresponds to variant rs748118737dbSNPEnsembl.1
Natural variantiVAR_045576341I → T.1 PublicationCorresponds to variant rs55798516dbSNPEnsembl.1
Natural variantiVAR_072626429Y → C in COQ10D4; decreased stability. 2 PublicationsCorresponds to variant rs144147839dbSNPEnsembl.1
Natural variantiVAR_044405514Y → C in COQ10D4. 1 PublicationCorresponds to variant rs119468008dbSNPEnsembl.1
Natural variantiVAR_044406549G → S in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs119468009dbSNPEnsembl.1
Natural variantiVAR_044407551E → K in COQ10D4; decreased stability. 3 PublicationsCorresponds to variant rs119468004dbSNPEnsembl.1
Natural variantiVAR_076860578F → V in COQ10D4; unknown pathological significance. 1 Publication1
Natural variantiVAR_044408584Missing in COQ10D4. 1 Publication1
Natural variantiVAR_072627602P → R in COQ10D4; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 PublicationCorresponds to variant rs61995958dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0223511 – 484Missing in isoform 2. 1 PublicationAdd BLAST484
Alternative sequenceiVSP_0223521 – 279Missing in isoform 4. 1 PublicationAdd BLAST279
Alternative sequenceiVSP_0223531 – 52Missing in isoform 3. 1 PublicationAdd BLAST52

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073905 mRNA. Translation: BAB91363.1.
AJ278126 mRNA. Translation: CAC00482.1.
AF218003 mRNA. Translation: AAG17245.1.
AK074693 mRNA. Translation: BAC11143.1.
BX648860 mRNA. Translation: CAH56132.1.
AL353689 Genomic DNA. Translation: CAI19103.1.
AL353689 Genomic DNA. Translation: CAI19105.1.
BC005171 mRNA. Translation: AAH05171.2.
CCDSiCCDS1557.1. [Q8NI60-1]
RefSeqiNP_064632.2. NM_020247.4. [Q8NI60-1]
XP_005273258.1. XM_005273201.1. [Q8NI60-1]
XP_011542540.1. XM_011544238.1. [Q8NI60-1]
XP_011542541.1. XM_011544239.2. [Q8NI60-1]
XP_011542542.1. XM_011544240.2. [Q8NI60-1]
XP_011542543.1. XM_011544241.2. [Q8NI60-1]
XP_016857341.1. XM_017001852.1. [Q8NI60-1]
UniGeneiHs.118241.

Genome annotation databases

EnsembliENST00000366777; ENSP00000355739; ENSG00000163050. [Q8NI60-1]
ENST00000366778; ENSP00000355740; ENSG00000163050. [Q8NI60-3]
ENST00000366779; ENSP00000355741; ENSG00000163050. [Q8NI60-1]
GeneIDi56997.
KEGGihsa:56997.
UCSCiuc001hqm.2. human. [Q8NI60-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073905 mRNA. Translation: BAB91363.1.
AJ278126 mRNA. Translation: CAC00482.1.
AF218003 mRNA. Translation: AAG17245.1.
AK074693 mRNA. Translation: BAC11143.1.
BX648860 mRNA. Translation: CAH56132.1.
AL353689 Genomic DNA. Translation: CAI19103.1.
AL353689 Genomic DNA. Translation: CAI19105.1.
BC005171 mRNA. Translation: AAH05171.2.
CCDSiCCDS1557.1. [Q8NI60-1]
RefSeqiNP_064632.2. NM_020247.4. [Q8NI60-1]
XP_005273258.1. XM_005273201.1. [Q8NI60-1]
XP_011542540.1. XM_011544238.1. [Q8NI60-1]
XP_011542541.1. XM_011544239.2. [Q8NI60-1]
XP_011542542.1. XM_011544240.2. [Q8NI60-1]
XP_011542543.1. XM_011544241.2. [Q8NI60-1]
XP_016857341.1. XM_017001852.1. [Q8NI60-1]
UniGeneiHs.118241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PEDX-ray1.64A256-647[»]
5I35X-ray2.30A256-647[»]
ProteinModelPortaliQ8NI60.
SMRiQ8NI60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121312. 39 interactors.
IntActiQ8NI60. 17 interactors.
MINTiMINT-1479202.
STRINGi9606.ENSP00000355739.

Chemistry databases

BindingDBiQ8NI60.
ChEMBLiCHEMBL5550.
GuidetoPHARMACOLOGYi1927.

PTM databases

iPTMnetiQ8NI60.
PhosphoSitePlusiQ8NI60.

Polymorphism and mutation databases

BioMutaiADCK3.
DMDMi27923741.

Proteomic databases

EPDiQ8NI60.
MaxQBiQ8NI60.
PaxDbiQ8NI60.
PeptideAtlasiQ8NI60.
PRIDEiQ8NI60.

Protocols and materials databases

DNASUi56997.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366777; ENSP00000355739; ENSG00000163050. [Q8NI60-1]
ENST00000366778; ENSP00000355740; ENSG00000163050. [Q8NI60-3]
ENST00000366779; ENSP00000355741; ENSG00000163050. [Q8NI60-1]
GeneIDi56997.
KEGGihsa:56997.
UCSCiuc001hqm.2. human. [Q8NI60-1]

Organism-specific databases

CTDi56997.
DisGeNETi56997.
GeneCardsiADCK3.
H-InvDBHIX0001648.
HGNCiHGNC:16812. COQ8A.
HPAiHPA061662.
MalaCardsiADCK3.
MIMi606980. gene.
612016. phenotype.
neXtProtiNX_Q8NI60.
OpenTargetsiENSG00000163050.
Orphaneti139485. Autosomal recessive ataxia due to ubiquinone deficiency.
PharmGKBiPA25999.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1234. Eukaryota.
COG0661. LUCA.
GeneTreeiENSGT00550000074739.
HOGENOMiHOG000201140.
HOVERGENiHBG061318.
InParanoidiQ8NI60.
KOiK08869.
OMAiYEVKVME.
OrthoDBiEOG091G02P9.
PhylomeDBiQ8NI60.
TreeFamiTF300630.

Enzyme and pathway databases

UniPathwayiUPA00232.
BioCyciZFISH:ENSG00000163050-MONOMER.

Miscellaneous databases

ChiTaRSiADCK3. human.
GeneWikiiCABC1.
GenomeRNAii56997.
PROiQ8NI60.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163050.
CleanExiHS_CABC1.
ExpressionAtlasiQ8NI60. baseline and differential.
GenevisibleiQ8NI60. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR004147. UbiB_dom.
[Graphical view]
PfamiPF03109. ABC1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCOQ8A_HUMAN
AccessioniPrimary (citable) accession number: Q8NI60
Secondary accession number(s): Q5T7A5
, Q63HK0, Q8NCJ6, Q9HBQ1, Q9NQ67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 131 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

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 one 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.