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Protein

Aurora kinase C

Gene

AURKC

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

Functioni

Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Okadaic acid, an inhibitor of protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 5 (PP5), increases AURKC activity. AURKC is also stabilized through its interaction with INCENP, which acts also as an activator.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATPPROSITE-ProRule annotation
Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone serine kinase activity Source: GO_Central
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cytokinesis Source: ProtInc
  • histone modification Source: UniProtKB
  • histone-serine phosphorylation Source: GOC
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic spindle midzone assembly Source: UniProtKB
  • oocyte development Source: InterPro
  • positive regulation of cytokinesis Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of signal transduction Source: InterPro
  • spermatogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9UQB9.

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase C (EC:2.7.11.1)
Alternative name(s):
Aurora 3
Aurora/IPL1-related kinase 3
Short name:
ARK-3
Short name:
Aurora-related kinase 3
Aurora/IPL1/Eg2 protein 2
Serine/threonine-protein kinase 13
Serine/threonine-protein kinase aurora-C
Gene namesi
Name:AURKC
Synonyms:AIE2, AIK3, AIRK3, ARK3, STK13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11391. AURKC.

Subcellular locationi

  • Nucleus
  • Chromosome
  • Chromosomecentromere
  • Cytoplasmcytoskeletonspindle

  • Note: Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis.

GO - Cellular componenti

  • chromosome passenger complex Source: UniProtKB
  • condensed chromosome Source: UniProtKB
  • condensed nuclear chromosome, centromeric region Source: GO_Central
  • cytoplasm Source: UniProtKB-KW
  • midbody Source: UniProtKB
  • spindle Source: UniProtKB
  • spindle microtubule Source: GO_Central
  • spindle midzone Source: UniProtKB
  • spindle pole centrosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spermatogenic failure 5 (SPGF5)2 Publications

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

Disease descriptionAn infertility disorder caused by spermatogenesis defects. Semen from affected men show close to 100% morphologically abnormal multiflagellar spermatozoa with low motility, oversized irregular heads, and abnormal midpiece and acrosome.

See also OMIM:243060

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721K → R: Impairs kinase activity. 2 Publications
Mutagenesisi166 – 1661D → Y: Impairs kinase activity, and keeps AURKC with the chromosomes until the end of mitosis. 1 Publication
Mutagenesisi198 – 1981T → A: Impairs kinase activity. 2 Publications

Organism-specific databases

MIMi243060. phenotype.
Orphaneti137893. Male infertility due to large-headed multiflagellar polyploid spermatozoa.
PharmGKBiPA36200.

Polymorphism and mutation databases

BioMutaiAURKC.
DMDMi27805738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Aurora kinase CPRO_0000085660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphothreonine; by PKABy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQB9.
PaxDbiQ9UQB9.
PRIDEiQ9UQB9.

PTM databases

PhosphoSiteiQ9UQB9.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in testis. Elevated expression levels were seen only in a subset of cancer cell lines such as Hep-G2, Huh-7 and HeLa. Expression is maximum at M phase.1 Publication

Inductioni

Expression is cell cycle-regulated, with an increase during G2 and M phases.2 Publications

Gene expression databases

BgeeiQ9UQB9.
CleanExiHS_AURKC.
ExpressionAtlasiQ9UQB9. baseline and differential.
GenevestigatoriQ9UQB9.

Organism-specific databases

HPAiHPA034859.

Interactioni

Subunit structurei

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts directly with BIRC5/survivin and INCENP. Interacts with TACC1.4 Publications

Protein-protein interaction databases

BioGridi112671. 28 interactions.
IntActiQ9UQB9. 4 interactions.
STRINGi9606.ENSP00000302898.

Structurei

3D structure databases

ProteinModelPortaliQ9UQB9.
SMRiQ9UQB9. Positions 36-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 293251Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120530.
HOGENOMiHOG000233016.
HOVERGENiHBG108519.
InParanoidiQ9UQB9.
KOiK11480.
OMAiRFPLSMP.
OrthoDBiEOG74FF1F.
PhylomeDBiQ9UQB9.
TreeFamiTF105331.

Family and domain databases

InterProiIPR030616. Aur.
IPR030613. AURKC.
IPR016253. Integrin-linked_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PTHR24350:SF3. PTHR24350:SF3. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000654. Integrin-linked_kinase. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UQB9-1) [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
MSSPRAVVQL GKAQPAGEEL ATANQTAQQP SSPAMRRLTV DDFEIGRPLG
60 70 80 90 100
KGKFGNVYLA RLKESHFIVA LKVLFKSQIE KEGLEHQLRR EIEIQAHLQH
110 120 130 140 150
PNILRLYNYF HDARRVYLIL EYAPRGELYK ELQKSEKLDE QRTATIIEEL
160 170 180 190 200
ADALTYCHDK KVIHRDIKPE NLLLGFRGEV KIADFGWSVH TPSLRRKTMC
210 220 230 240 250
GTLDYLPPEM IEGRTYDEKV DLWCIGVLCY ELLVGYPPFE SASHSETYRR
260 270 280 290 300
ILKVDVRFPL SMPLGARDLI SRLLRYQPLE RLPLAQILKH PWVQAHSRRV

LPPCAQMAS
Length:309
Mass (Da):35,591
Last modified:May 1, 2000 - v1
Checksum:i41B7DFCA91704201
GO
Isoform 2 (identifier: Q9UQB9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Show »
Length:275
Mass (Da):32,187
Checksum:i8DF2BDC1F436E266
GO
Isoform 3 (identifier: Q9UQB9-3) [UniParc]FASTAAdd to basket

Also known as: Aurora C-SV

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MSSPRAVVQLGKAQPAGEEL → M

Show »
Length:290
Mass (Da):33,672
Checksum:iD07FD6988B208140
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091Y → H in AAC25955 (PubMed:9809744).Curated
Sequence conflicti150 – 1501L → V in AAC77369 (PubMed:9799611).Curated
Sequence conflicti193 – 1953SLR → LPE in AAC77369 (PubMed:9799611).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521G → E in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040385
Natural varianti148 – 1481E → Q in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
VAR_040386
Natural varianti244 – 2441H → Q in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040387

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 2. 2 PublicationsVSP_004872Add
BLAST
Alternative sequencei1 – 2020MSSPR…AGEEL → M in isoform 3. 1 PublicationVSP_041095Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054621 mRNA. Translation: AAC25955.1.
AF059681 mRNA. Translation: AAC77369.1.
AB017332 mRNA. Translation: BAA76292.1.
AY661554 mRNA. Translation: AAT64422.1.
AC005261 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72485.1.
BC075064 mRNA. Translation: AAH75064.2.
CCDSiCCDS33128.1. [Q9UQB9-1]
CCDS46205.1. [Q9UQB9-3]
CCDS46206.1. [Q9UQB9-2]
RefSeqiNP_001015878.1. NM_001015878.1. [Q9UQB9-1]
NP_001015879.1. NM_001015879.1. [Q9UQB9-3]
NP_003151.2. NM_003160.2. [Q9UQB9-2]
UniGeneiHs.98338.

Genome annotation databases

EnsembliENST00000302804; ENSP00000302898; ENSG00000105146. [Q9UQB9-1]
ENST00000415300; ENSP00000407162; ENSG00000105146. [Q9UQB9-3]
ENST00000598785; ENSP00000471830; ENSG00000105146. [Q9UQB9-2]
GeneIDi6795.
KEGGihsa:6795.
UCSCiuc002qoc.3. human. [Q9UQB9-3]
uc002qod.3. human. [Q9UQB9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054621 mRNA. Translation: AAC25955.1.
AF059681 mRNA. Translation: AAC77369.1.
AB017332 mRNA. Translation: BAA76292.1.
AY661554 mRNA. Translation: AAT64422.1.
AC005261 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72485.1.
BC075064 mRNA. Translation: AAH75064.2.
CCDSiCCDS33128.1. [Q9UQB9-1]
CCDS46205.1. [Q9UQB9-3]
CCDS46206.1. [Q9UQB9-2]
RefSeqiNP_001015878.1. NM_001015878.1. [Q9UQB9-1]
NP_001015879.1. NM_001015879.1. [Q9UQB9-3]
NP_003151.2. NM_003160.2. [Q9UQB9-2]
UniGeneiHs.98338.

3D structure databases

ProteinModelPortaliQ9UQB9.
SMRiQ9UQB9. Positions 36-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112671. 28 interactions.
IntActiQ9UQB9. 4 interactions.
STRINGi9606.ENSP00000302898.

Chemistry

BindingDBiQ9UQB9.
ChEMBLiCHEMBL3935.
GuidetoPHARMACOLOGYi1938.

PTM databases

PhosphoSiteiQ9UQB9.

Polymorphism and mutation databases

BioMutaiAURKC.
DMDMi27805738.

Proteomic databases

MaxQBiQ9UQB9.
PaxDbiQ9UQB9.
PRIDEiQ9UQB9.

Protocols and materials databases

DNASUi6795.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302804; ENSP00000302898; ENSG00000105146. [Q9UQB9-1]
ENST00000415300; ENSP00000407162; ENSG00000105146. [Q9UQB9-3]
ENST00000598785; ENSP00000471830; ENSG00000105146. [Q9UQB9-2]
GeneIDi6795.
KEGGihsa:6795.
UCSCiuc002qoc.3. human. [Q9UQB9-3]
uc002qod.3. human. [Q9UQB9-1]

Organism-specific databases

CTDi6795.
GeneCardsiGC19P057743.
HGNCiHGNC:11391. AURKC.
HPAiHPA034859.
MIMi243060. phenotype.
603495. gene.
neXtProtiNX_Q9UQB9.
Orphaneti137893. Male infertility due to large-headed multiflagellar polyploid spermatozoa.
PharmGKBiPA36200.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120530.
HOGENOMiHOG000233016.
HOVERGENiHBG108519.
InParanoidiQ9UQB9.
KOiK11480.
OMAiRFPLSMP.
OrthoDBiEOG74FF1F.
PhylomeDBiQ9UQB9.
TreeFamiTF105331.

Enzyme and pathway databases

SignaLinkiQ9UQB9.

Miscellaneous databases

GeneWikiiAURKC.
GenomeRNAii6795.
NextBioi26545.
PROiQ9UQB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UQB9.
CleanExiHS_AURKC.
ExpressionAtlasiQ9UQB9. baseline and differential.
GenevestigatoriQ9UQB9.

Family and domain databases

InterProiIPR030616. Aur.
IPR030613. AURKC.
IPR016253. Integrin-linked_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350. PTHR24350. 1 hit.
PTHR24350:SF3. PTHR24350:SF3. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000654. Integrin-linked_kinase. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein kinase profile of sperm and eggs: cloning and characterization of two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and fly chromosome segregation regulators."
    Tseng T.-C., Chen S.-H., Hsu Y.-P.P., Tang T.K.
    DNA Cell Biol. 17:823-833(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Testis.
  2. "Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter."
    Bernard M., Sanseau P., Henry C., Couturier A., Prigent C.
    Genomics 53:406-409(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Placenta.
  3. "Cell cycle-dependent expression and centrosome localization of a third human Aurora/Ipl1-related protein kinase, AIK3."
    Kimura M., Matsuda Y., Yoshioka T., Okano Y.
    J. Biol. Chem. 274:7334-7340(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION.
    Tissue: Testis.
  4. "Cloning and characterization of a novel human Aurora C splicing variant."
    Yan X., Wu Y., Li Q., Cao L., Liu X., Saiyin H., Yu L.
    Biochem. Biophys. Res. Commun. 328:353-361(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF THR-198, SUBCELLULAR LOCATION.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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 2).
    Tissue: Brain.
  8. "Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells."
    Sasai K., Katayama H., Stenoien D.L., Fujii S., Honda R., Kimura M., Okano Y., Tatsuka M., Suzuki F., Nigg E.A., Earnshaw W.C., Brinkley W.R., Sen S.
    Cell Motil. Cytoskeleton 59:249-263(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INCENP, MUTAGENESIS OF LYS-72.
  9. "Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C."
    Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., Taniguchi H., Furukawa K., Urano T.
    J. Biol. Chem. 279:47201-47211(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CDC COMPLEX, SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION, MUTAGENESIS OF LYS-72 AND THR-198.
  10. "Aurora C is directly associated with Survivin and required for cytokinesis."
    Yan X., Cao L., Li Q., Wu Y., Zhang H., Saiyin H., Liu X., Zhang X., Shi Q., Yu L.
    Genes Cells 10:617-626(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CDC COMPLEX, INTERACTION WITH BIRC5, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF ASP-166.
  11. "Homozygous mutation of AURKC yields large-headed polyploid spermatozoa and causes male infertility."
    Dieterich K., Soto Rifo R., Faure A.K., Hennebicq S., Ben Amar B., Zahi M., Perrin J., Martinez D., Sele B., Jouk P.-S., Ohlmann T., Rousseaux S., Lunardi J., Ray P.F.
    Nat. Genet. 39:661-665(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SPGF5.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TACC1.
  13. "A role for Aurora C in the chromosomal passenger complex during human preimplantation embryo development."
    Avo Santos M., van de Werken C., de Vries M., Jahr H., Vromans M.J., Laven J.S., Fauser B.C., Kops G.J., Lens S.M., Baart E.B.
    Hum. Reprod. 26:1868-1881(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "A new AURKC mutation causing macrozoospermia: implications for human spermatogenesis and clinical diagnosis."
    Ben Khelifa M., Zouari R., Harbuz R., Halouani L., Arnoult C., Lunardi J., Ray P.F.
    Mol. Hum. Reprod. 17:762-768(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SPGF5.
  15. "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: VARIANTS [LARGE SCALE ANALYSIS] GLU-52; GLN-148 AND GLN-244.

Entry informationi

Entry nameiAURKC_HUMAN
AccessioniPrimary (citable) accession number: Q9UQB9
Secondary accession number(s): O60681
, O75442, Q6AZY8, Q6DLZ0, Q9UPK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 146 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  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.