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Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)

 AURKA_PIG               Reviewed;         402 AA.
A5GFW1;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
25-OCT-2017, entry version 88.
RecName: Full=Aurora kinase A;
EC=2.7.11.1 {ECO:0000250|UniProtKB:P04198};
AltName: Full=Aurora 2;
AltName: Full=Aurora/IPL1-related kinase 1;
Short=ARK-1;
Short=Aurora-related kinase 1;
AltName: Full=Serine/threonine-protein kinase 15;
AltName: Full=Serine/threonine-protein kinase 6;
AltName: Full=Serine/threonine-protein kinase aurora-A;
Name=AURKA;
Synonyms=AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Porcine genome sequencing project;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Mitotic serine/threonine kinases 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 (By similarity).
Necessary for proper cilia disassembly prior to mitosis (By
similarity). Interacts with SIRT2 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:O14965}.
-!- ENZYME REGULATION: Activation of CDK1, appears to be an upstream
event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and
TPX2 act also as activators. 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 (By similarity). Activated during the early
phase of cilia disassembly in the presence of PIFO (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well
as with the protein phosphatase type 1 (PP1) isoforms PPP1CA,
PPP1CB and PPP1CC (By similarity). Interacts also with its
substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53.
Interaction with BORA promotes phosphorylation of PLK1. Interacts
with FBXL7 and PIFO. Interacts with GADD45A, competing with its
oligomerization (By similarity). Interacts (via C-terminus) with
AUNIP (via C-terminus) (By similarity). Identified in a complex
with AUNIP and NIN (By similarity). Interacts with FRY; this
interaction facilitates AURKA-mediated PLK1 phosphorylation (By
similarity). 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 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:O14965}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:O14965}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, cilium
basal body {ECO:0000250|UniProtKB:P97477}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome, centriole
{ECO:0000250|UniProtKB:P97477}. Note=Detected at the neurite
hillock in developing neurons. Localizes at the centrosome in
mitotic cells from early prophase until telophase, but also
localizes to the spindle pole MTs from prophase to anaphase. Moves
to the midbody during both telophase and cytokinesis. Associates
with both the pericentriolar material (PCM) and centrioles.
Colocalized with SIRT2 at centrosome.
{ECO:0000250|UniProtKB:O14965, ECO:0000250|UniProtKB:P97477}.
-!- PTM: 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.
-!- PTM: Ubiquitinated by CHFR, leading to its degradation by the
proteasome. Ubiquitinated by the anaphase-promoting complex (APC),
leading to its degradation by the proteasome. Ubiquitinated by the
E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis,
leading to its degradation by the proteasome (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; CR956640; CAN13135.1; -; Genomic_DNA.
RefSeq; XP_005673091.1; XM_005673034.2.
RefSeq; XP_005673092.1; XM_005673035.2.
UniGene; Ssc.1466; -.
ProteinModelPortal; A5GFW1; -.
SMR; A5GFW1; -.
STRING; 9823.ENSSSCP00000028760; -.
iPTMnet; A5GFW1; -.
PaxDb; A5GFW1; -.
PRIDE; A5GFW1; -.
Ensembl; ENSSSCT00000036639; ENSSSCP00000028760; ENSSSCG00000007493.
GeneID; 574063; -.
CTD; 6790; -.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
GeneTree; ENSGT00870000136439; -.
HOVERGEN; HBG108519; -.
InParanoid; A5GFW1; -.
OMA; QATSVPH; -.
OrthoDB; EOG091G0EU2; -.
TreeFam; TF105331; -.
Proteomes; UP000008227; Chromosome 17.
Bgee; ENSSSCG00000007493; -.
Genevisible; A5GFW1; SS.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IBA:GO_Central.
GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
GO; GO:0031616; C:spindle pole centrosome; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0000212; P:meiotic spindle organization; IEA:InterPro.
GO; GO:0007100; P:mitotic centrosome separation; IEA:InterPro.
GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:1904146; P:positive regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
GO; GO:0045727; P:positive regulation of translation; IMP:AgBase.
GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
CDD; cd14116; STKc_Aurora-A; 1.
InterPro; IPR030616; Aur.
InterPro; IPR030611; AURKA.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR24350; PTHR24350; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell projection; Cilium;
Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Kinase; Microtubule; Mitosis;
Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 402 Aurora kinase A.
/FTId=PRO_0000296392.
DOMAIN 133 383 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 210 213 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 260 261 ATP. {ECO:0000250|UniProtKB:O14965}.
REGION 280 293 Activation segment. {ECO:0000250}.
ACT_SITE 256 256 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 143 143 ATP; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
BINDING 162 162 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 274 274 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 287 287 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 288 288 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 342 342 Phosphoserine; by PKA and PAK.
{ECO:0000250|UniProtKB:O14965}.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O14965}.
SEQUENCE 402 AA; 45516 MW; 0A27B84699873BDE CRC64;
MDKCKENCIS GLKTTVPPGD GPKRVPVTQH FPAQHLPSAN SGQAQRVLCP SNSSQRLPSH
TQKLVSSHKP VQNLKQKQSQ ATSGPRPVSR PLSNTQQSEQ PQPAAPGNNP EKEAASKQKN
EESKKRQWAL EDFEIGRPLG KGKFGNVYLA REKQSKFILA LKVLFKTQLE KAGVEHQLRR
EVEIQSHLRH PNILRLYGYF HDATRVYLIL EYAPLGAVYR ELQKLSKFDE QRTATYITEL
ANALSYCHSK RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD FVPEGARDLI
SRLLKHNPSH RPTLKEVLEH PWITANSKPA SSHKKESTSK QP


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