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Protein

Atypical kinase ADCK3, mitochondrial

Gene

ADCK3

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). Its substrate specificity is unclear: either acts as protein kinase that phosphorylates other proteins in the CoQ complex to stabilize their interactions or acts as a small molecule kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway (PubMed:25498144). Shows an unusual selectivity for binding ADP over ATP (PubMed:25498144).2 Publications1 Publication

Enzyme regulationi

Autoinhibited by the N-terminal domain, containing the KxGQ motif, that completely occludes the typical substrate binding pocket.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei358 – 3581ATPBy similarity
Active sitei488 – 4881Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi336 – 3449ATP1 Publication

GO - Molecular functioni

  1. ADP binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. kinase activity Source: UniProtKB

GO - Biological processi

  1. phosphorylation Source: UniProtKB
  2. ubiquinone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Ubiquinone biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended name:
Atypical kinase ADCK3, mitochondrialCurated (EC:2.7.-.-1 Publication)
Alternative name(s):
Chaperone activity of bc1 complex-like1 Publication
Short name:
Chaperone-ABC1-like1 Publication
aarF domain-containing protein kinase 3Imported
Gene namesi
Name:ADCK3Imported
Synonyms:CABC11 Publication
ORF Names:PP265
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16812. ADCK3.

Subcellular locationi

  1. Mitochondrion 2 Publications
  2. Membrane Sequence Analysis; Single-pass membrane protein Sequence Analysis1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei214 – 23017HelicalSequence Analysis1 PublicationAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Coenzyme Q10 deficiency, primary, 4 (COQ10D4)6 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131R → W in COQ10D4. 2 Publications
VAR_044402
Natural varianti271 – 2711R → C in COQ10D4. 1 Publication
VAR_072622
Natural varianti272 – 2721G → D in COQ10D4. 2 Publications
VAR_044403
Natural varianti272 – 2721G → V in COQ10D4. 2 Publications
VAR_044404
Natural varianti299 – 2991R → W in COQ10D4; decreased stability. 2 Publications
VAR_072623
Natural varianti304 – 3041A → T in COQ10D4. 1 Publication
VAR_072624
Natural varianti304 – 3041A → V in COQ10D4. 1 Publication
VAR_072625
Natural varianti429 – 4291Y → C in COQ10D4; decreased stability. 2 Publications
VAR_072626
Natural varianti514 – 5141Y → C in COQ10D4. 1 Publication
VAR_044405
Natural varianti549 – 5491G → S in COQ10D4; decreased stability. 3 Publications
VAR_044406
Natural varianti551 – 5511E → K in COQ10D4; decreased stability. 3 Publications
VAR_044407
Natural varianti584 – 5841Missing in COQ10D4. 1 Publication
VAR_044408
Natural varianti602 – 6021P → R in COQ10D4; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 Publication
VAR_072627

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141L → A, I, L or F: Strongly impairs homodimerization. 1 Publication
Mutagenesisi214 – 2141L → I, F, G or V: Slightly impaired homodimerization. 1 Publication
Mutagenesisi215 – 2151A → I, L or G: Does not impair homodimerization. 1 Publication
Mutagenesisi216 – 2161N → A, L, F or M: Does not impair homodimerization. 1 Publication
Mutagenesisi217 – 2171F → A: Slightly impaired homodimerization. 1 Publication
Mutagenesisi218 – 2181G → I, L or F: Slightly impaired homodimerization. 1 Publication
Mutagenesisi219 – 2191G → A or F: Slightly impaired homodimerization. 1 Publication
Mutagenesisi219 – 2191G → I: Strongly impairs homodimerization. 1 Publication
Mutagenesisi220 – 2201L → G: Impaired homodimerization. 1 Publication
Mutagenesisi221 – 2211A → L: Slightly impaired homodimerization. 1 Publication
Mutagenesisi222 – 2221V → A: Slightly impaired homodimerization. 1 Publication
Mutagenesisi223 – 2231G → A, I, L or F: Strongly impairs homodimerization. 1 Publication
Mutagenesisi224 – 2241L → V: Impaired homodimerization. 1 Publication
Mutagenesisi225 – 2251G → L: Slightly impaired homodimerization. 1 Publication
Mutagenesisi226 – 2261F → A: Slightly impaired homodimerization. 1 Publication
Mutagenesisi227 – 2271G → V, F, L or I: Strongly impairs homodimerization. 1 Publication
Mutagenesisi228 – 2281A → I, L or F: Does not impair homodimerization. 1 Publication
Mutagenesisi229 – 2291L → A: Slightly impaired homodimerization. 1 Publication
Mutagenesisi230 – 2301A → I: Slightly impaired homodimerization. 1 Publication
Mutagenesisi276 – 2761K → R or H: Does not affect selectivity for binding ADP or ATP. 1 Publication
Mutagenesisi279 – 2791Q → R or H: Does not affect selectivity for binding ADP or ATP. 1 Publication
Mutagenesisi339 – 3391A → G: Enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo. 1 Publication
Mutagenesisi358 – 3581K → R: Abolishes binding ADP or ATP. 1 Publication
Mutagenesisi405 – 4051E → A or Q: Slightly affects selectivity for binding ADP or ATP. 1 Publication
Mutagenesisi411 – 4111E → Q: Impaired binding ADP or ATP. 1 Publication
Mutagenesisi488 – 4881D → N: Impaired binding ADP or ATP. 1 Publication
Mutagenesisi493 – 4931N → A: Impaired binding ADP or ATP. 1 Publication
Mutagenesisi507 – 5071D → N: Strongly impairs binding ADP or ATP. 1 Publication
Mutagenesisi611 – 6111R → A or Q: Does not affect selectivity for binding ADP or ATP. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiADCK3.
DMDMi27923741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 162162Mitochondrion1 PublicationAdd
BLAST
Chaini163 – 647485Atypical kinase ADCK3, mitochondrialPRO_0000000262Add
BLAST

Proteomic databases

MaxQBiQ8NI60.
PaxDbiQ8NI60.
PRIDEiQ8NI60.

PTM databases

PhosphoSiteiQ8NI60.

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.

Gene expression databases

BgeeiQ8NI60.
CleanExiHS_CABC1.
ExpressionAtlasiQ8NI60. baseline and differential.
GenevestigatoriQ8NI60.

Organism-specific databases

HPAiHPA018217.

Interactioni

Subunit structurei

Homodimer; homodimerizes via its transmembrane region.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-745535,EBI-741181
RABAC1Q9UI146EBI-745535,EBI-712367
REEP6Q96HR95EBI-745535,EBI-750345
TFIP11Q9UBB95EBI-745535,EBI-1105213
TMEM159Q96B965EBI-745535,EBI-7055862
TMEM239Q8WW345EBI-745535,EBI-9675724

Protein-protein interaction databases

BioGridi121312. 13 interactions.
IntActiQ8NI60. 12 interactions.
MINTiMINT-1479202.

Structurei

Secondary structure

1
647
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi260 – 26910Combined sources
Helixi271 – 28111Combined sources
Beta strandi284 – 2896Combined sources
Helixi291 – 30212Combined sources
Helixi303 – 3064Combined sources
Helixi309 – 32012Combined sources
Helixi325 – 3273Combined sources
Beta strandi328 – 3314Combined sources
Beta strandi336 – 3394Combined sources
Beta strandi342 – 3498Combined sources
Beta strandi354 – 3607Combined sources
Turni362 – 3643Combined sources
Helixi365 – 3673Combined sources
Helixi368 – 38215Combined sources
Helixi391 – 3933Combined sources
Helixi395 – 40511Combined sources
Helixi408 – 42114Combined sources
Turni422 – 4243Combined sources
Beta strandi426 – 4294Combined sources
Helixi435 – 4373Combined sources
Beta strandi442 – 4465Combined sources
Beta strandi450 – 4523Combined sources
Helixi453 – 4553Combined sources
Helixi461 – 48020Combined sources
Beta strandi484 – 4885Combined sources
Helixi491 – 4933Combined sources
Beta strandi494 – 4974Combined sources
Turni498 – 5014Combined sources
Beta strandi502 – 5054Combined sources
Beta strandi511 – 5133Combined sources
Helixi516 – 53015Combined sources
Helixi534 – 54310Combined sources
Helixi553 – 57119Combined sources
Helixi581 – 5888Combined sources
Helixi589 – 5946Combined sources
Helixi604 – 62219Combined sources
Helixi630 – 64314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PEDX-ray1.64A256-647[»]
ProteinModelPortaliQ8NI60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini329 – 518190Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi276 – 2794KxGQ motif1 Publication
Motifi337 – 3404AAAS motif1 Publication

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.1 Publication

Sequence similaritiesi

Contains 1 protein kinase domain.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0661.
GeneTreeiENSGT00550000074739.
HOGENOMiHOG000201140.
HOVERGENiHBG061318.
InParanoidiQ8NI60.
KOiK08869.
OMAiKVQGQDK.
OrthoDBiEOG7X9G6H.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2842IQ → VR in BAC11143 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti85 – 851H → Q.
Corresponds to variant rs2297411 [ dbSNP | Ensembl ].
VAR_020319
Natural varianti213 – 2131R → W in COQ10D4. 2 Publications
VAR_044402
Natural varianti271 – 2711R → C in COQ10D4. 1 Publication
VAR_072622
Natural varianti272 – 2721G → D in COQ10D4. 2 Publications
VAR_044403
Natural varianti272 – 2721G → V in COQ10D4. 2 Publications
VAR_044404
Natural varianti299 – 2991R → W in COQ10D4; decreased stability. 2 Publications
VAR_072623
Natural varianti304 – 3041A → T in COQ10D4. 1 Publication
VAR_072624
Natural varianti304 – 3041A → V in COQ10D4. 1 Publication
VAR_072625
Natural varianti341 – 3411I → T.1 Publication
Corresponds to variant rs55798516 [ dbSNP | Ensembl ].
VAR_045576
Natural varianti429 – 4291Y → C in COQ10D4; decreased stability. 2 Publications
VAR_072626
Natural varianti514 – 5141Y → C in COQ10D4. 1 Publication
VAR_044405
Natural varianti549 – 5491G → S in COQ10D4; decreased stability. 3 Publications
VAR_044406
Natural varianti551 – 5511E → K in COQ10D4; decreased stability. 3 Publications
VAR_044407
Natural varianti584 – 5841Missing in COQ10D4. 1 Publication
VAR_044408
Natural varianti602 – 6021P → R in COQ10D4; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 Publication
VAR_072627

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 484484Missing in isoform 2. 1 PublicationVSP_022351Add
BLAST
Alternative sequencei1 – 279279Missing in isoform 4. 1 PublicationVSP_022352Add
BLAST
Alternative sequencei1 – 5252Missing in isoform 3. 1 PublicationVSP_022353Add
BLAST

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]
UniGeneiHs.118241.

Genome annotation databases

EnsembliENST00000366777; ENSP00000355739; ENSG00000163050. [Q8NI60-1]
ENST00000366778; ENSP00000355740; ENSG00000163050. [Q8NI60-3]
ENST00000366779; ENSP00000355741; ENSG00000163050. [Q8NI60-1]
GeneIDi56997.
KEGGihsa:56997.
UCSCiuc001hqm.1. human. [Q8NI60-1]
uc009xer.1. human. [Q8NI60-2]

Polymorphism and mutation databases

BioMutaiADCK3.

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]
UniGeneiHs.118241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PEDX-ray1.64A256-647[»]
ProteinModelPortaliQ8NI60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121312. 13 interactions.
IntActiQ8NI60. 12 interactions.
MINTiMINT-1479202.

Chemistry

BindingDBiQ8NI60.
ChEMBLiCHEMBL5550.
GuidetoPHARMACOLOGYi1927.

PTM databases

PhosphoSiteiQ8NI60.

Polymorphism and mutation databases

BioMutaiADCK3.
DMDMi27923741.

Proteomic databases

MaxQBiQ8NI60.
PaxDbiQ8NI60.
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.1. human. [Q8NI60-1]
uc009xer.1. human. [Q8NI60-2]

Organism-specific databases

CTDi56997.
GeneCardsiGC01P227087.
H-InvDBHIX0001648.
HGNCiHGNC:16812. ADCK3.
HPAiHPA018217.
MIMi606980. gene.
612016. phenotype.
neXtProtiNX_Q8NI60.
Orphaneti139485. Autosomal recessive ataxia due to ubiquinone deficiency.
PharmGKBiPA25999.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0661.
GeneTreeiENSGT00550000074739.
HOGENOMiHOG000201140.
HOVERGENiHBG061318.
InParanoidiQ8NI60.
KOiK08869.
OMAiKVQGQDK.
OrthoDBiEOG7X9G6H.
PhylomeDBiQ8NI60.
TreeFamiTF300630.

Enzyme and pathway databases

UniPathwayiUPA00232.

Miscellaneous databases

ChiTaRSiADCK3. human.
GeneWikiiCABC1.
GenomeRNAii56997.
NextBioi62711.
PROiQ8NI60.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NI60.
CleanExiHS_CABC1.
ExpressionAtlasiQ8NI60. baseline and differential.
GenevestigatoriQ8NI60.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel gene, CABC1, encoding a mitochondrial protein that is highly homologous to yeast activity of bc1 complex."
    Iiizumi M., Arakawa H., Mori T., Ando A., Nakamura Y.
    Cancer Res. 62:1246-1250(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "Full length sequencing of some human and murine muscular transcript (Telethon Italy project B41)."
    Ievolella C., Stanchi F., Bertocco E., Millino C., Faulkner G., Valle G., Lanfranchi G.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Skeletal muscle.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  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] (ISOFORM 1).
    Tissue: Mammary gland.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Small intestine.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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).
    Tissue: Uterus.
  8. Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 256-647, FUNCTION, SUBCELLULAR LOCATION, PATHWAY, DOMAIN, ENZYME REGULATION, MUTAGENESIS OF LYS-276; GLN-279; ALA-339; LYS-358; GLU-405; GLU-411; ASP-488; ASN-493; ASP-507 AND ARG-611, CHARACTERIZATION OF VARIANTS COQ10D4 TRP-299; CYS-429; SER-549 AND LYS-551.
  9. "Nonsense mutations in CABC1/ADCK3 cause progressive cerebellar ataxia and atrophy."
    Gerards M., van den Bosch B., Calis C., Schoonderwoerd K., van Engelen K., Tijssen M., de Coo R., van der Kooi A., Smeets H.
    Mitochondrion 10:510-515(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN COQ10D4.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Expression of the human atypical kinase ADCK3 rescues coenzyme Q biosynthesis and phosphorylation of Coq polypeptides in yeast coq8 mutants."
    Xie L.X., Hsieh E.J., Watanabe S., Allan C.M., Chen J.Y., Tran U.C., Clarke C.F.
    Biochim. Biophys. Acta 1811:348-360(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: TISSUE SPECIFICITY.
  13. "A Gly-zipper motif mediates homodimerization of the transmembrane domain of the mitochondrial kinase ADCK3."
    Khadria A.S., Mueller B.K., Stefely J.A., Tan C.H., Pagliarini D.J., Senes A.
    J. Am. Chem. Soc. 136:14068-14077(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-214; ALA-215; ASN-216; PHE-217; GLY-218; GLY-219; LEU-220; ALA-221; VAL-222; GLY-223; LEU-224; GLY-225; PHE-226; GLY-227; ALA-228; LEU-229 AND ALA-230.
  14. "Autosomal-recessive cerebellar ataxia caused by a novel ADCK3 mutation that elongates the protein: clinical, genetic and biochemical characterisation."
    Liu Y.T., Hersheson J., Plagnol V., Fawcett K., Duberley K.E., Preza E., Hargreaves I.P., Chalasani A., Laura M., Wood N.W., Reilly M.M., Houlden H.
    J. Neurol. Neurosurg. Psych. 85:493-498(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN COQ10D4.
  15. "Preparation and characterization of human ADCK3, a putative atypical kinase."
    Wheeler B., Jia Z.
    Protein Expr. Purif. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-341.
  17. Cited for: VARIANTS COQ10D4 TRP-213; VAL-272; ASP-272 AND LYS-551.
  18. Cited for: VARIANTS COQ10D4 CYS-514; SER-549 AND THR-584 DEL.
  19. Cited for: VARIANTS COQ10D4 TRP-213; CYS-271; ASP-272; VAL-272; TRP-299; THR-304; VAL-304; CYS-429; SER-549 AND LYS-551.
  20. "Heterozygous mutations in the ADCK3 gene in siblings with cerebellar atrophy and extreme phenotypic variability."
    Blumkin L., Leshinsky-Silver E., Zerem A., Yosovich K., Lerman-Sagie T., Lev D.
    JIMD Rep. 12:103-107(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COQ10D4 ARG-602.

Entry informationi

Entry nameiADCK3_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: April 29, 2015
This is version 114 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

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.