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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 6) (Serine/threonine-protein kinase aurora-A) (ratAurA)

 AURKA_RAT               Reviewed;         397 AA.
P59241;
27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
27-JAN-2003, sequence version 1.
23-MAY-2018, entry version 128.
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 6;
AltName: Full=Serine/threonine-protein kinase aurora-A;
Short=ratAurA;
Name=Aurka;
Synonyms=Aik, Airk, Ark1, Aura, Ayk1, Btak, Iak1, Stk15, Stk6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar Furth; TISSUE=Mammary gland;
PubMed=12124350;
Goepfert T.M., Adigun Y.E., Zhong L., Gay J., Medina D.,
Brinkley W.R.;
"Centrosome amplification and overexpression of aurora A are early
events in rat mammary carcinogenesis.";
Cancer Res. 62:4115-4122(2002).
[2]
FUNCTION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=19812038; DOI=10.1074/jbc.M109.055897;
Khazaei M.R., Puschel A.W.;
"Phosphorylation of the par polarity complex protein Par3 at serine
962 is mediated by aurora A and regulates its function in neuronal
polarity.";
J. Biol. Chem. 284:33571-33579(2009).
-!- 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 stabilizating 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,
ECO:0000269|PubMed:19812038}.
-!- 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). Interacts with HNRNPU (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=Localizes on centrosomes in
interphase cells and at each spindle pole in mitosis. Associates
with both the pericentriolar material (PCM) and centrioles.
Detected at the neurite hillock in developing neurons. Colocalized
with SIRT2 at centrosome. {ECO:0000250|UniProtKB:O14965,
ECO:0000250|UniProtKB:P97477}.
-!- TISSUE SPECIFICITY: Detected in neurons in brain cortex and
hippocampus (at protein level). Expressed in mammary gland and
tumor. {ECO:0000269|PubMed:19812038}.
-!- INDUCTION: Activated by progesterone.
-!- PTM: Activated by phosphorylation at Thr-281; this brings about a
change in the conformation of the activation segment.
Phosphorylation at Thr-281 varies during the cell cycle and is
highest during M phase. Autophosphorylated at Thr-281 upon TPX2
binding. Thr-281 can be phosphorylated by several kinases,
including PAK and PKA. Protein phosphatase type 1 (PP1) binds
AURKA and inhibits its activity by dephosphorylating Thr-281
during mitosis. Phosphorylation at Ser-335 decreases the kinase
activity. PPP2CA controls degradation by dephosphorylating Ser-52
at the end of mitosis (By similarity). Phosphorylated in embryonic
brain neurons. {ECO:0000250, ECO:0000269|PubMed:19812038}.
-!- PTM: Ubiquitinated by the anaphase-promoting complex (APC),
leading to its degradation by the proteasome (By similarity).
Ubiquitinated by CHFR, 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; AF537333; AAN06823.1; -; mRNA.
UniGene; Rn.161874; -.
ProteinModelPortal; P59241; -.
SMR; P59241; -.
STRING; 10116.ENSRNOP00000051977; -.
iPTMnet; P59241; -.
PhosphoSitePlus; P59241; -.
PaxDb; P59241; -.
PRIDE; P59241; -.
RGD; 628895; Aurka.
eggNOG; KOG0580; Eukaryota.
eggNOG; ENOG410XNRB; LUCA.
HOVERGEN; HBG108519; -.
InParanoid; P59241; -.
PhylomeDB; P59241; -.
PRO; PR:P59241; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:RGD.
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:0005819; C:spindle; IDA:RGD.
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:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
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:0007052; P:mitotic spindle organization; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
InterPro; IPR030616; Aur.
InterPro; IPR011009; Kinase-like_dom_sf.
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.
1: Evidence at protein level;
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 1 397 Aurora kinase A.
/FTId=PRO_0000086694.
DOMAIN 126 376 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 203 206 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 253 254 ATP. {ECO:0000250|UniProtKB:O14965}.
REGION 273 286 Activation segment. {ECO:0000250}.
ACT_SITE 249 249 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 136 136 ATP; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
BINDING 155 155 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 267 267 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 280 280 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 281 281 Phosphothreonine.
{ECO:0000250|UniProtKB:O14965}.
MOD_RES 335 335 Phosphoserine; by PKA and PAK.
{ECO:0000250|UniProtKB:O14965}.
CROSSLNK 251 251 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O14965}.
SEQUENCE 397 AA; 44874 MW; 95DECA2198DCED85 CRC64;
MDRCKENCVS RPVKSTVPFG PKRVLVTEQI PSQHPGSASS GQAQRVLCPS NSQRVPPQAQ
KPVAGQKPVL KQLPAASGPR PASRLSNPQK SEQPQPAASG NNSEKEQTSI QKTEDSKKRQ
WTLEDFDIGR PLGKGKFGNV YLAREKQSKF ILALKVLFKV QLEKAGVEHQ LRREVEIQSH
LRHPNILRLY GYFHDATRVY LILEYAPLGT VYRELQKLSK FDEQRTATYI TELANALSYC
HSKRVIHRDI KPENLLLGSN GELKIADFGW SVHAPSSRRT TLCGTLDYQP PEMIEGRMHD
EKVDLWSLGV LCYEFLVGMP PFEAHTYQET YRRISRVEFT FPDFVTEGAR DLISRLLKHN
SSQRLTLAEV LEHPWIKANS SKPPTGHNSK EATSKSS


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