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Protein

Aurora kinase A

Gene

AURKA

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

Functioni

Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis.21 Publications

Miscellaneous

Centrosome amplification can occur when the cycles are uncoupled, and this amplification is associated with cancer and with an increase in the levels of chromosomal instability.

Caution

Authors initially considered AURKA/STK6 and STK15 as 2 different proteins (PubMed:9771714). It is clear that they are the same protein.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.5 Publications

Enzyme regulationi

Activation of CDK1, appears to be an upstream event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Inactivated by the G2 checkpoint. Inhibited by GADD45A and p53/TP53, and through dephosphorylation by protein phosphatase type 1 (PP1). MLN8054 is also a potent and selective inhibitor. Activated during the early phase of cilia disassembly in the presence of PIFO.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei143ATP; via amide nitrogenCombined sources1 Publication1
Binding sitei162ATPCombined sources1 Publication1
Active sitei256Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei274ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi211 – 213ATPCombined sources1 Publication3
Nucleotide bindingi260 – 261ATPCombined sources1 Publication2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone serine kinase activity Source: GO_Central
  • protein heterodimerization activity Source: CAFA
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome
  • ubiquitin protein ligase binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Cilium biogenesis/degradation, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8854521 Interaction between PHLDA1 and AURKA
SignaLinkiO14965
SIGNORiO14965

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase A (EC:2.7.11.11 Publication)
Alternative name(s):
Aurora 2
Aurora/IPL1-related kinase 1
Short name:
ARK-1
Short name:
Aurora-related kinase 1
Short name:
hARK1
Breast tumor-amplified kinase
Serine/threonine-protein kinase 15
Serine/threonine-protein kinase 6
Serine/threonine-protein kinase aurora-A
Gene namesi
Name:AURKA
Synonyms:AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000087586.17
HGNCiHGNC:11393 AURKA
MIMi603072 gene
neXtProtiNX_O14965

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi162K → R: Loss of kinase activity. 2 Publications1
Mutagenesisi165F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1
Mutagenesisi198G → N: Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. 1 Publication1
Mutagenesisi205R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication1
Mutagenesisi274D → N: Abolishes autophosphorylation. 1 Publication1
Mutagenesisi287T → A: No direct effect on catalytic activity. 1 Publication1
Mutagenesisi287T → E: Enhances interaction with TPX2. 1 Publication1
Mutagenesisi288T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication1
Mutagenesisi290C → A: Enhances stability; when associated with A-393. 1 Publication1
Mutagenesisi334Y → A: Reduces binding to MYCN. 1 Publication1
Mutagenesisi335Q → A: Reduces binding to MYCN. 1 Publication1
Mutagenesisi346F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1
Mutagenesisi393C → A: Enhances stability; when associated with A-290. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi6790
MalaCardsiAURKA
PharmGKBiPA36201

Chemistry databases

ChEMBLiCHEMBL4722
DrugBankiDB08065 2-(1H-pyrazol-3-yl)-1H-benzimidazole
DB05169 AT9283
DB05198 CYC116
DB05220 MLN8237
DB08066 N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE
DB07801 N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide
DB07545 N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE
DB02482 Phosphonothreonine
GuidetoPHARMACOLOGYi1936

Polymorphism and mutation databases

BioMutaiAURKA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866921 – 403Aurora kinase AAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41PhosphoserineCombined sources1
Modified residuei51Phosphoserine1 Publication1
Cross-linki258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei287Phosphothreonine2 Publications1
Modified residuei288Phosphothreonine7 Publications1
Modified residuei342Phosphoserine; by PKA and PAK1 Publication1

Post-translational modificationi

Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.10 Publications
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome.By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO14965
MaxQBiO14965
PaxDbiO14965
PeptideAtlasiO14965
PRIDEiO14965

PTM databases

iPTMnetiO14965
PhosphoSitePlusiO14965

Expressioni

Tissue specificityi

Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.

Inductioni

Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after.5 Publications

Gene expression databases

BgeeiENSG00000087586
CleanExiHS_AURKA
ExpressionAtlasiO14965 baseline and differential
GenevisibleiO14965 HS

Organism-specific databases

HPAiCAB001454
HPA002636

Interactioni

Subunit structurei

Interacts with FBXL7 (By similarity). Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts with GADD45A, competing with its oligomerization. Interacts (via C-terminus) with AUNIP (via C-terminus). Identified in a complex with AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with SIRT2. Interacts with MYCN; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (PubMed:27837025). Interacts with HNRNPU (PubMed:21242313, PubMed:25986610).By similarity29 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein heterodimerization activity Source: CAFA
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: Ensembl

Protein-protein interaction databases

BioGridi112666, 330 interactors
CORUMiO14965
DIPiDIP-33068N
ELMiO14965
IntActiO14965, 127 interactors
MINTiO14965
STRINGi9606.ENSP00000216911

Chemistry databases

BindingDBiO14965

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi130 – 132Combined sources3
Beta strandi133 – 141Combined sources9
Beta strandi143 – 152Combined sources10
Turni153 – 155Combined sources3
Beta strandi158 – 165Combined sources8
Helixi166 – 171Combined sources6
Turni172 – 174Combined sources3
Helixi175 – 185Combined sources11
Beta strandi191 – 193Combined sources3
Beta strandi196 – 201Combined sources6
Beta strandi203 – 210Combined sources8
Beta strandi214 – 217Combined sources4
Helixi218 – 225Combined sources8
Helixi230 – 249Combined sources20
Helixi259 – 261Combined sources3
Beta strandi262 – 264Combined sources3
Beta strandi266 – 268Combined sources3
Beta strandi270 – 272Combined sources3
Helixi275 – 277Combined sources3
Beta strandi280 – 283Combined sources4
Beta strandi287 – 289Combined sources3
Helixi290 – 292Combined sources3
Helixi293 – 295Combined sources3
Helixi298 – 302Combined sources5
Helixi307 – 309Combined sources3
Helixi310 – 324Combined sources15
Helixi334 – 342Combined sources9
Beta strandi350 – 352Combined sources3
Helixi354 – 363Combined sources10
Helixi368 – 370Combined sources3
Helixi374 – 378Combined sources5
Helixi381 – 386Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4C3PX-ray2.69A/D122-403[»]
4C3RX-ray2.79A122-403[»]
4CEGX-ray2.10A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4J8MX-ray1.85A123-401[»]
4J8NX-ray3.14A/B/C/D123-401[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
4O0SX-ray2.50A122-403[»]
4O0UX-ray2.60A122-403[»]
4O0WX-ray2.60A122-403[»]
4PRJX-ray2.80A124-391[»]
4UTDX-ray2.36A122-403[»]
4UYNX-ray1.90A125-399[»]
4UZDX-ray3.20A/B125-399[»]
4UZHX-ray2.00A125-399[»]
4ZS0X-ray3.00A122-403[»]
4ZTQX-ray2.80A122-403[»]
4ZTRX-ray2.85A122-403[»]
4ZTSX-ray2.90A122-403[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5DN3X-ray2.05A125-391[»]
5DNRX-ray1.95A125-391[»]
5DOSX-ray2.98A126-390[»]
5DPVX-ray2.29A126-390[»]
5DR2X-ray2.46A128-390[»]
5DR6X-ray2.53A126-390[»]
5DR9X-ray2.47A126-390[»]
5DRDX-ray2.13A126-390[»]
5DT0X-ray2.15A126-390[»]
5DT3X-ray2.33A126-390[»]
5DT4X-ray2.86A126-390[»]
5EW9X-ray2.18A123-390[»]
5G15X-ray2.06A122-403[»]
5G1XX-ray1.72A122-403[»]
5L8JX-ray1.68A122-403[»]
5L8KX-ray1.79A122-403[»]
5L8LX-ray1.67A122-403[»]
5LXMX-ray2.08A122-403[»]
5OBJX-ray2.90A125-391[»]
5OBRX-ray2.62A125-391[»]
5ODTX-ray2.02A122-403[»]
5ONEX-ray2.60A122-403[»]
5ORLX-ray1.69A127-391[»]
5ORNX-ray2.19A127-391[»]
5OROX-ray2.12A127-391[»]
5ORPX-ray2.19A127-391[»]
5ORRX-ray2.09A127-391[»]
5ORSX-ray1.98A127-391[»]
5ORTX-ray2.56A127-391[»]
5ORVX-ray1.88A127-391[»]
5ORWX-ray2.00A127-391[»]
5ORXX-ray1.88A127-391[»]
5ORYX-ray1.99A127-391[»]
5ORZX-ray1.92A127-391[»]
5OS0X-ray1.74A127-391[»]
5OS1X-ray1.90A127-391[»]
5OS2X-ray1.92A127-391[»]
5OS3X-ray1.81A127-391[»]
5OS4X-ray1.88A127-391[»]
5OS5X-ray1.74A125-392[»]
5OS6X-ray2.20A127-391[»]
5OSDX-ray1.99A125-391[»]
5OSEX-ray1.90A127-391[»]
5OSFX-ray1.89A127-391[»]
ProteinModelPortaliO14965
SMRiO14965
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14965

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 383Protein kinasePROSITE-ProRule annotationAdd BLAST251

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni280 – 293Activation segmentAdd BLAST14

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0580 Eukaryota
ENOG410XNRB LUCA
HOVERGENiHBG108519
InParanoidiO14965
KOiK11481
OrthoDBiEOG091G0EU2
PhylomeDBiO14965
TreeFamiTF105331

Family and domain databases

CDDicd14116 STKc_Aurora-A, 1 hit
InterProiView protein in InterPro
IPR030616 Aur
IPR030611 AURKA
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24350 PTHR24350, 1 hit
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

O14965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP
60 70 80 90 100
SNSSQRVPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ
110 120 130 140 150
PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA
160 170 180 190 200
REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHLRH PNILRLYGYF
210 220 230 240 250
HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL ANALSYCHSK
260 270 280 290 300
RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM
310 320 330 340 350
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD
360 370 380 390 400
FVTEGARDLI SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS

KQS
Length:403
Mass (Da):45,809
Last modified:January 27, 2003 - v2
Checksum:i125F3594834CD157
GO

Sequence cautioni

The sequence BAA23592 differs from that shown. Reason: Frameshift at positions 105, 125, 129, 235 and 241.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03084011G → R. Corresponds to variant dbSNP:rs6069717Ensembl.1
Natural variantiVAR_03084131F → I5 PublicationsCorresponds to variant dbSNP:rs2273535Ensembl.1
Natural variantiVAR_04112750P → L1 PublicationCorresponds to variant dbSNP:rs34572020Ensembl.1
Natural variantiVAR_03084257V → I4 PublicationsCorresponds to variant dbSNP:rs1047972Ensembl.1
Natural variantiVAR_061745104S → L. Corresponds to variant dbSNP:rs2230743Ensembl.1
Natural variantiVAR_041128155S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 2 Publications1
Natural variantiVAR_041129174V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 2 Publications1
Natural variantiVAR_041130373M → V1 PublicationCorresponds to variant dbSNP:rs33923703Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84212 mRNA Translation: BAA23592.1 Frameshift.
AF008551 mRNA Translation: AAC12708.1
AF011467 Genomic DNA Translation: AAC23448.1
AF011468 mRNA Translation: AAC63902.1
AF195947
, AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA Translation: AAF29508.1
AL121914 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75550.1
CH471077 Genomic DNA Translation: EAW75551.1
CH471077 Genomic DNA Translation: EAW75552.1
CH471077 Genomic DNA Translation: EAW75553.1
CH471077 Genomic DNA Translation: EAW75554.1
CH471077 Genomic DNA Translation: EAW75555.1
CH471077 Genomic DNA Translation: EAW75556.1
CH471077 Genomic DNA Translation: EAW75557.1
CH471077 Genomic DNA Translation: EAW75558.1
CH471077 Genomic DNA Translation: EAW75559.1
CH471077 Genomic DNA Translation: EAW75561.1
CH471077 Genomic DNA Translation: EAW75562.1
BC001280 mRNA Translation: AAH01280.1
BC002499 mRNA Translation: AAH02499.1
BC006423 mRNA Translation: AAH06423.1
BC027464 mRNA Translation: AAH27464.1
CCDSiCCDS13451.1
PIRiJC5974
RefSeqiNP_001310232.1, NM_001323303.1
NP_001310233.1, NM_001323304.1
NP_001310234.1, NM_001323305.1
NP_003591.2, NM_003600.3
NP_940835.1, NM_198433.2
NP_940836.1, NM_198434.2
NP_940837.1, NM_198435.2
NP_940838.1, NM_198436.2
NP_940839.1, NM_198437.2
XP_016883524.1, XM_017028035.1
UniGeneiHs.250822

Genome annotation databases

EnsembliENST00000312783; ENSP00000321591; ENSG00000087586
ENST00000347343; ENSP00000216911; ENSG00000087586
ENST00000371356; ENSP00000360407; ENSG00000087586
ENST00000395911; ENSP00000379247; ENSG00000087586
ENST00000395913; ENSP00000379249; ENSG00000087586
ENST00000395914; ENSP00000379250; ENSG00000087586
ENST00000395915; ENSP00000379251; ENSG00000087586
GeneIDi6790
KEGGihsa:6790
UCSCiuc002xxe.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAURKA_HUMAN
AccessioniPrimary (citable) accession number: O14965
Secondary accession number(s): E1P5F9
, O60445, O75873, Q9BQD6, Q9UPG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: April 25, 2018
This is version 207 of the entry and version 2 of the sequence. See 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, Reference proteome
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