Q9H4B4 · PLK3_HUMAN
- ProteinSerine/threonine-protein kinase PLK3
- GenePLK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids646 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase PLK3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H4B4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocates to the nucleus upon cisplatin treatment. Localizes to the Golgi apparatus during interphase. According to a report, PLK3 localizes only in the nucleolus and not in the centrosome, or in any other location in the cytoplasm (PubMed:17264206).
The discrepancies in results may be explained by the PLK3 antibody specificity, by cell line-specific expression or post-translational modifications
The discrepancies in results may be explained by the PLK3 antibody specificity, by cell line-specific expression or post-translational modifications
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_021091 | 61 | in dbSNP:rs17884581 | |||
Sequence: T → S | ||||||
Natural variant | VAR_021092 | 68 | in dbSNP:rs17884316 | |||
Sequence: L → F | ||||||
Mutagenesis | 91 | Kinase defective mutant, abolishes activity. | ||||
Sequence: K → R | ||||||
Mutagenesis | 203 | Kinase defective mutant, abolishes activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 219 | Kinase-defective mutant. | ||||
Sequence: T → E | ||||||
Natural variant | VAR_021093 | 283 | in dbSNP:rs17880471 | |||
Sequence: L → F | ||||||
Mutagenesis | 467-468 | Abolishes localization to the centrosome and ability to induce the G2/M arrest. | ||||
Sequence: WV → FA | ||||||
Natural variant | VAR_021094 | 483 | in dbSNP:rs17884653 | |||
Sequence: R → C | ||||||
Natural variant | VAR_062384 | 491 | in dbSNP:rs17855444 | |||
Sequence: D → N | ||||||
Natural variant | VAR_021095 | 498 | in dbSNP:rs17880829 | |||
Sequence: S → L | ||||||
Natural variant | VAR_021096 | 618 | in dbSNP:rs17881786 | |||
Sequence: S → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 705 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086564 | 1-646 | Serine/threonine-protein kinase PLK3 | |||
Sequence: MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRGPELEMLAGLPTSDPGRLITDPRSGRTYLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFFTKGYTPDRLPISSCVTVPDLTPPNPARSLFAKVTKSLFGRKKKSKNHAQERDEVSGLVSGLMRTSVGHQDARPEAPAASGPAPVSLVETAPEDSSPRGTLASSGDGFEEGLTVATVVESALCALRNCIAFMPPAEQNPAPLAQPEPLVWVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGAVPRALQPQLGILRYFASYMEQHLMKGGDLPSVEEVEVPAPPLLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSPA |
Post-translational modification
Phosphorylated in an ATM-dependent manner following DNA damage. Phosphorylated as cells enter mitosis and dephosphorylated as cells exit mitosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Transcripts are highly detected in placenta, lung, followed by skeletal muscle, heart, pancreas, ovaries and kidney and weakly detected in liver and brain. May have a short half-live. In cells of hematopoietic origin, strongly and exclusively detected in terminally differentiated macrophages. Transcript expression appears to be down-regulated in primary lung tumor.
Induction
Cytokine and cellular adhesion trigger induction. Down-regulated in a majority of lung carcinoma samples.
Developmental stage
Expression is cell cycle regulated with a peak in G1 phase.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via the POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity. Interacts with GOLGB1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H4B4 | LSM5 Q9Y4Y9 | 3 | EBI-751877, EBI-373007 | |
BINARY | Q9H4B4 | MFF Q9GZY8-5 | 3 | EBI-751877, EBI-11956541 | |
BINARY | Q9H4B4 | POU2F1 P14859 | 3 | EBI-751877, EBI-624770 | |
BINARY | Q9H4B4 | PRNP P04156 | 4 | EBI-751877, EBI-977302 | |
BINARY | Q9H4B4 | RAD52 P43351 | 3 | EBI-751877, EBI-706448 | |
BINARY | Q9H4B4 | RNF141 Q8WVD5 | 3 | EBI-751877, EBI-4308142 | |
BINARY | Q9H4B4 | VRK1 Q99986 | 12 | EBI-751877, EBI-1769146 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Disordered | ||||
Sequence: MEPAAGFLSPRPFQRAAAAPAPPAGPGPPPSALRG | ||||||
Compositional bias | 16-33 | Pro residues | ||||
Sequence: AAAAPAPPAGPGPPPSAL | ||||||
Domain | 62-314 | Protein kinase | ||||
Sequence: YLKGRLLGKGGFARCYEATDTETGSAYAVKVIPQSRVAKPHQREKILNEIELHRDLQHRHIVRFSHHFEDADNIYIFLELCSRKSLAHIWKARHTLLEPEVRYYLRQILSGLKYLHQRGILHRDLKLGNFFITENMELKVGDFGLAARLEPPEQRKKTICGTPNYVAPEVLLRQGHGPEADVWSLGCVMYTLLCGSPPFETADLKETYRCIKQVHYTLPASLSLPARQLLAAILRASPRDRPSIDQILRHDFF | ||||||
Region | 381-417 | Disordered | ||||
Sequence: GHQDARPEAPAASGPAPVSLVETAPEDSSPRGTLASS | ||||||
Domain | 463-541 | POLO box 1 | ||||
Sequence: WVSKWVDYSNKFGFGYQLSSRRVAVLFNDGTHMALSANRKTVHYNPTSTKHFSFSVGAVPRALQPQLGILRYFASYMEQ | ||||||
Domain | 562-645 | POLO box 2 | ||||
Sequence: LLLQWVKTDQALLMLFSDGTVQVNFYGDHTKLILSGWEPLLVTFVARNRSACTYLASHLRQLGCSPDLRQRLRYALRLLRDRSP |
Domain
The POLO box domains act as phosphopeptide-binding module that recognizes and binds serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK3 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).
The POLO box domains mediate localization to the centrosome
The POLO box domains mediate localization to the centrosome
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length646
- Mass (Da)71,629
- Last updated2004-08-16 v2
- Checksum324CA3E9DE482514
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 16 | in Ref. 1; CAC10659 | ||||
Sequence: A → T | ||||||
Compositional bias | 16-33 | Pro residues | ||||
Sequence: AAAAPAPPAGPGPPPSAL | ||||||
Sequence conflict | 20 | in Ref. 1; CAC10659 | ||||
Sequence: P → T | ||||||
Sequence conflict | 99 | in Ref. 1; CAC10659 | ||||
Sequence: A → V | ||||||
Sequence conflict | 353 | in Ref. 1; CAC10659 | ||||
Sequence: G → V | ||||||
Sequence conflict | 419 | in Ref. 1; CAC10659 | ||||
Sequence: D → H | ||||||
Sequence conflict | 464-470 | in Ref. 1; CAC10659 | ||||
Sequence: VSKWVDY → FSEWVGF | ||||||
Sequence conflict | 522 | in Ref. 1; CAC10659 | ||||
Sequence: P → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ293866 EMBL· GenBank· DDBJ | CAC10659.1 EMBL· GenBank· DDBJ | mRNA | ||
AY764184 EMBL· GenBank· DDBJ | AAU88146.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL592166 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07021.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC013899 EMBL· GenBank· DDBJ | AAH13899.1 EMBL· GenBank· DDBJ | mRNA | ||
U56998 EMBL· GenBank· DDBJ | AAC50637.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |