PLK1_BOVIN
ID PLK1_BOVIN Reviewed; 602 AA.
AC Q2TA25; F1N225;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein kinase PLK1;
DE EC=2.7.11.21;
DE AltName: Full=Polo-like kinase 1;
DE Short=PLK-1;
GN Name=PLK1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine-protein kinase that performs several
CC important functions throughout M phase of the cell cycle, including the
CC regulation of centrosome maturation and spindle assembly, the removal
CC of cohesins from chromosome arms, the inactivation of anaphase-
CC promoting complex/cyclosome (APC/C) inhibitors, and the regulation of
CC mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding
CC and phosphorylating proteins are that already phosphorylated on a
CC specific motif recognized by the POLO box domains. Phosphorylates BORA,
CC BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1,
CC KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ,
CC PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS,
CC p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome
CC functions and the assembly of bipolar spindles by phosphorylating KIZ,
CC NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of
CC the gamma-tubulin ring complex (gTuRC) to the centrosome, an important
CC step for spindle formation. Phosphorylation of NINL component of the
CC centrosome leads to NINL dissociation from other centrosomal proteins.
CC Involved in mitosis exit and cytokinesis by phosphorylating CEP55,
CC ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central
CC spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates
CC its own docking sites on PRC1 and KIF20A/MKLP2 by mediating
CC phosphorylation of sites subsequently recognized by the POLO box
CC domains. Phosphorylates RACGAP1, thereby creating a docking site for
CC the Rho GTP exchange factor ECT2 that is essential for the cleavage
CC furrow formation. Promotes the central spindle recruitment of ECT2.
CC Plays a central role in G2/M transition of mitotic cell cycle by
CC phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1,
CC PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the
CC activation of CDK1 by phosphorylating the positive regulator CDC25C and
CC inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by
CC mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in
CC prophase. Phosphorylates FOXM1, a key mitotic transcription regulator,
CC leading to enhance FOXM1 transcriptional activity. Involved in
CC kinetochore functions and sister chromatid cohesion by phosphorylating
CC BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached
CC kinetochores suggesting a role of PLK1 in kinetochore attachment or in
CC spindle assembly checkpoint (SAC) regulation. Required for kinetochore
CC localization of BUB1B. Regulates the dissociation of cohesin from
CC chromosomes by phosphorylating cohesin subunits such as STAG2/SA2.
CC Phosphorylates SGO1: required for spindle pole localization of isoform
CC 3 of SGO1 and plays a role in regulating its centriole cohesion
CC function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator
CC of the APC/C complex during prophase, leading to FBXO5/EMI1
CC ubiquitination and degradation by the proteasome. Acts as a negative
CC regulator of p53 family members: phosphorylates TOPORS, leading to
CC inhibit the sumoylation of p53/TP53 and simultaneously enhance the
CC ubiquitination and subsequent degradation of p53/TP53. Phosphorylates
CC the transactivation domain of the transcription factor p73/TP73,
CC leading to inhibit p73/TP73-mediated transcriptional activation and
CC pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the
CC degradation of BORA. Contributes to the regulation of AURKA function.
CC Also required for recovery after DNA damage checkpoint and entry into
CC mitosis.Phosphorylates MISP, leading to stabilization of cortical and
CC astral microtubule attachments required for proper spindle positioning.
CC Together with MEIKIN, acts as a regulator of kinetochore function
CC during meiosis I: required both for mono-orientation of kinetochores on
CC sister chromosomes and protection of centromeric cohesin from separase-
CC mediated cleavage. Phosphorylates CEP68 and is required for its
CC degradation. Regulates nuclear envelope breakdown during prophase by
CC phosphorylating DCTN1 resulting in its localization in the nuclear
CC envelope. Phosphorylates the heat shock transcription factor HSF1,
CC promoting HSF1 nuclear translocation upon heat shock. Phosphorylates
CC HSF1 also in the early mitotic period; this phosphorylation regulates
CC HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC)
CC ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic
CC progression. Regulates mitotic progression by phosphorylating RIOK2 (By
CC similarity). Through the phosphorylation of DZIP1 regulates the
CC localization during mitosis of the BBSome, a ciliary protein complex
CC involved in cilium biogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P53350, ECO:0000250|UniProtKB:Q07832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21;
CC Evidence={ECO:0000250|UniProtKB:P53350};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000250|UniProtKB:P53350};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-208 by AURKA;
CC phosphorylation by AURKA is enhanced by BORA. Once activated, activity
CC is stimulated by binding target proteins. Binding of target proteins
CC has no effect on the non-activated kinase. Several inhibitors targeting
CC PLKs are currently in development and are under investigation in a
CC growing number of clinical trials, such as BI 2536, an ATP-competitive
CC PLK1 inhibitor or BI 6727, a dihydropteridinone that specifically
CC inhibits the catalytic activity of PLK1 (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- SUBUNIT: Interacts with CEP170 and EVI5. Interacts and phosphorylates
CC ERCC6L. Interacts with FAM29A. Interacts with SLX4/BTBD12 and TTDN1.
CC Interacts with BUB1B. Interacts (via POLO-box domain) with the
CC phosphorylated form of BUB1, CENPU and CDC25C. Interacts with isoform 3
CC of SGO1. Interacts with BORA, KIF2A and AURKA. Interacts with TOPORS
CC and CYLD. Interacts with ECT2; the interaction is stimulated upon
CC phosphorylation of ECT2 on 'Thr-444'. Interacts with PRC1. Interacts
CC with KIF20A/MKLP2 (when phosphorylated), leading to the recruitment at
CC the central spindle. Interacts (via POLO box domains) with
CC PPP1R12A/MYPT1 (when previously phosphorylated by CDK1). Part of an
CC astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1,
CC DYNLL1 and SGO2. Interacts with BIRC6/bruce. Interacts with CDK1-
CC phosphorylated FRY; this interaction occurs in mitotic cells, but not
CC in interphase cells. FRY interaction facilitates AURKA-mediated PLK1
CC phosphorylation. Interacts with CDK1-phosphorylated DCTN6 during
CC mitotic prometaphase; the interaction facilitates recruitment to
CC kinetochores. Interacts with CEP68; the interaction phosphorylates
CC CEP68. Interacts (via POLO-box domain) with DCTN1. Interacts with CEP20
CC in later G1, S, G2 and M phases of the cell cycle; this interaction
CC recruits PLK1 to centrosomes, a step required for S phase progression.
CC Interacts with HSF1; this interaction increases upon heat shock but
CC does not modulate neither HSF1 homotrimerization nor DNA-binding
CC activities. Interacts with HNRNPU; this interaction induces
CC phosphorylation of HNRNPU in mitosis. Interacts (via its N-terminus) to
CC RIOK2 (By similarity). {ECO:0000250|UniProtKB:P53350}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53350}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P53350}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P53350}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P53350}. Midbody {ECO:0000250|UniProtKB:P53350}.
CC Note=localization at the centrosome starts at the G1/S transition (By
CC similarity). During early stages of mitosis, the phosphorylated form is
CC detected on centrosomes and kinetochores. Localizes to the outer
CC kinetochore. Presence of SGO1 and interaction with the phosphorylated
CC form of BUB1 is required for the kinetochore localization. Localizes
CC onto the central spindle by phosphorylating and docking at midzone
CC proteins KIF20A/MKLP2 and PRC1 (By similarity). Colocalizes with FRY to
CC separating centrosomes and spindle poles from prophase to metaphase in
CC mitosis, but not in other stages of the cell cycle (By similarity).
CC Localization to the centrosome is required for S phase progression (By
CC similarity). Colocalizes with HSF1 at the spindle poles during
CC prometaphase (By similarity). {ECO:0000250|UniProtKB:P53350}.
CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that
CC recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X)
CC motifs. PLK1 recognizes and binds docking proteins that are already
CC phosphorylated on these motifs, and then phosphorylates them. PLK1 can
CC also create its own docking sites by mediating phosphorylation of
CC serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently
CC recognized by the POLO box domains (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-208.
CC Phosphorylation at Thr-208 is first detected on centrosomes in the G2
CC phase of the cell cycle, peaks in prometaphase and gradually disappears
CC from centrosomes during anaphase. Dephosphorylation at Thr-208 at
CC centrosomes is probably mediated by protein phosphatase 1C (PP1C), via
CC interaction with PPP1R12A/MYPT1. Autophosphorylation and
CC phosphorylation of Ser-135 may not be significant for the activation of
CC PLK1 during mitosis, but may enhance catalytic activity during recovery
CC after DNA damage checkpoint. Phosphorylated in vitro by STK10 (By
CC similarity). {ECO:0000250|UniProtKB:P53350}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C)
CC in anaphase and following DNA damage, leading to its degradation by the
CC proteasome. Ubiquitination is mediated via its interaction with
CC FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry
CC into mitosis and is essential to maintain an efficient G2 DNA damage
CC checkpoint. Monoubiquitination at Lys-490 by the BCR(KLHL22) ubiquitin
CC ligase complex does not lead to degradation: it promotes PLK1
CC dissociation from phosphoreceptor proteins and subsequent removal from
CC kinetochores, allowing silencing of the spindle assembly checkpoint
CC (SAC) and chromosome segregation (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AAFC03124496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111149; AAI11150.1; -; mRNA.
DR RefSeq; NP_001033262.1; NM_001038173.2.
DR AlphaFoldDB; Q2TA25; -.
DR SMR; Q2TA25; -.
DR STRING; 9913.ENSBTAP00000019217; -.
DR PaxDb; Q2TA25; -.
DR PRIDE; Q2TA25; -.
DR Ensembl; ENSBTAT00000019217; ENSBTAP00000019217; ENSBTAG00000014453.
DR GeneID; 538238; -.
DR KEGG; bta:538238; -.
DR CTD; 5347; -.
DR VEuPathDB; HostDB:ENSBTAG00000014453; -.
DR VGNC; VGNC:33033; PLK1.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000157752; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q2TA25; -.
DR OMA; LKHFERY; -.
DR OrthoDB; 507604at2759; -.
DR TreeFam; TF101089; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000014453; Expressed in saliva-secreting gland and 107 other tissues.
DR ExpressionAtlas; Q2TA25; baseline and differential.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; IEA:Ensembl.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
DR GO; GO:1904776; P:regulation of protein localization to cell cortex; IEA:Ensembl.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IEA:Ensembl.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase; Kinetochore;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CHAIN 2..602
FT /note="Serine/threonine-protein kinase PLK1"
FT /id="PRO_0000284066"
FT DOMAIN 51..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 415..478
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 513..582
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..219
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 336..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..505
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 536..538
FT /note="Important for interaction with phosphorylated
FT proteins"
FT /evidence="ECO:0000250"
FT MOTIF 335..338
FT /note="D-box that targets the protein for proteasomal
FT degradation in anaphase"
FT /evidence="ECO:0000250"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 57..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 208
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 267
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 336
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 490
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CONFLICT 528
FT /note="V -> E (in Ref. 2; AAI11150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 68000 MW; 03C27EB8B216E5DD CRC64;
MSAAATAGKL GRAPADPGKA PGVAAPGAST AAPPAKEIPE VLVDPRSRRR YLRGRFLGKG
GFAKCFEISD ADTKEVFAGK IVPKSLLLKP HQKEKMSMEI SIHRSLAHQH VVGFHGFFED
NDFVFVVLEL CRRRSLLELH KRRKALTEPE ARYYLRQIVL GCQYLHGNRV IHRDLKLGNL
FLNEDLEVKI GDFGLATKVE YDGERKKTLC GTPNYIAPEV LSKKGHSFEV DVWSIGCIMY
TLLVGKPPFE TSCLKETYLR IKNNEYSIPK HINPVASSLI KKMLQPDPTA RPTIHELLND
EFFTSGYIPA RLPITCLTIP PRFSIAPSSL DPSNRKPLTV LNKGMENPMP ERPREKEEPV
VREASEPVDC HLSDMLQQLH SVNASKPSER GLVRQEEAED PACIPIFWVS KWVDYSDKYG
LGYQLCDNSV GVLFNDSTRL ILYSDGDSLQ YIERDGSESY LTVSSHPNSL IKKITLLKYF
RNYMSEHLLK AGANITPREG DELARLPYLR TWFRTRSAII LHLSNGCVQI NFFQDHTKLI
LCPLMAAVTY IDEKRDFRTY RLSLLEEYGC SKELASRLRY ARAMVDKLLS SRSAANRLKA
SS
