B3NE99
Gene name |
SAK (GG13228) |
Protein name |
Serine/threonine-protein kinase PLK4 |
Names |
Polo-like kinase 4, PLK-4, Serine/threonine-protein kinase SAK |
Species |
Drosophila erecta (Fruit fly) |
KEGG Pathway |
der:6543822 |
EC number |
2.7.11.21: Protein-serine/threonine kinases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
14-267 (Protein kinase domain) |
Relief mechanism |
Partner binding, PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for B3NE99
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-B3NE99-F1 | Predicted | AlphaFoldDB |
No variants for B3NE99
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for B3NE99 |
No associated diseases with B3NE99
7 regional properties for B3NE99
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Protein kinase domain | 14 - 267 | IPR000719 |
domain | POLO box domain | 668 - 711 | IPR000959 |
active_site | Tyrosine-protein kinase, active site | 134 - 146 | IPR008266 |
binding_site | Protein kinase, ATP binding site | 20 - 43 | IPR017441 |
domain | Plk4, C-terminal polo-box domain | 655 - 736 | IPR033696 |
domain | Plk4, second cryptic polo-box domain | 496 - 600 | IPR033698 |
domain | Plk4, first cryptic polo-box domain | 379 - 496 | IPR033699 |
Functions
Description | ||
---|---|---|
EC Number | 2.7.11.21 | Protein-serine/threonine kinases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
2 GO annotations of cellular component
Name | Definition |
---|---|
centriole | A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
5 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
identical protein binding | Binding to an identical protein or proteins. |
protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
8 GO annotations of biological process
Name | Definition |
---|---|
centriole replication | The cell cycle process in which a daughter centriole is formed perpendicular to an existing centriole. An immature centriole contains a ninefold radially symmetric array of single microtubules; mature centrioles consist of a radial array of nine microtubule triplets, doublets, or singlets depending upon the species and cell type. Duplicated centrioles also become the ciliary basal body in cells that form cilia during G0. |
male meiotic nuclear division | A cell cycle process by which the cell nucleus divides as part of a meiotic cell cycle in the male germline. |
positive regulation of protein catabolic process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
regulation of centriole replication | Any process that modulates the frequency, rate or extent of the formation of a daughter centriole of an existing centriole. |
regulation of protein stability | Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation. |
sperm axoneme assembly | The assembly and organization of the sperm flagellar axoneme, the bundle of microtubules and associated proteins that forms the core of the eukaryotic sperm flagellum, and is responsible for movement. |
syncytial blastoderm mitotic cell cycle | Mitotic division cycles 10 to 13 of the insect embryo. This is the second phase of the syncytial period where nuclei divide in a common cytoplasm without cytokinesis. The majority of migrating nuclei reach the embryo surface during cycle 10, after which they divide less synchronously than before, and the syncytial blastoderm cycles lengthen progressively. |
No homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
No homologous proteins |
10 | 20 | 30 | 40 | 50 | 60 |
MLSNRAFGET | IEDYEVQHLL | GKGGFAIVYK | ARCLHTHQDV | AIKMIDKKLI | QGTGLTNRVR |
70 | 80 | 90 | 100 | 110 | 120 |
QEVEIHSRLK | HPSVLQLYTF | FQDANYVYLV | LELAHNGELH | RYMNHIARPF | TETEAASILK |
130 | 140 | 150 | 160 | 170 | 180 |
QVVAGLLYLH | SHNIMHRDIS | LSNLLLSKEM | HVKIADFGLA | TQLKRPDERH | MTMCGTPNYI |
190 | 200 | 210 | 220 | 230 | 240 |
SPEVVSRSSH | GLPADVWSVG | CMLYTLLVGR | PPFETDAVQS | TLNKVVMSEY | IMPAHLSYEA |
250 | 260 | 270 | 280 | 290 | 300 |
QDLINKLLKK | LPHERITLEA | VLCHPFMLKC | SNGGHSTPGA | LNMFSQSMES | GDSGIITFAS |
310 | 320 | 330 | 340 | 350 | 360 |
SDSRNSQQIR | SVENSGPQQV | LPQIQEEFKH | HKLTYEQPGL | FRQTSTGLAE | PNWPGATKAS |
370 | 380 | 390 | 400 | 410 | 420 |
SFRMEMGMVQ | NSKPAPVKED | RISVPPLNTK | RLLPTRYKTK | NAIMSILRNG | EVVLEFFRFR |
430 | 440 | 450 | 460 | 470 | 480 |
PTYNEDRITD | ICRISDDGQR | IIIYQPDPGR | GLPVREQPPD | LQIPSGDCVY | NYENLPSKHW |
490 | 500 | 510 | 520 | 530 | 540 |
KKYIYGARFV | GLVKSKTPKV | TYFSTLGKCQ | LMETMTDFEI | RFYSGAKLLK | TPSEGLKVYD |
550 | 560 | 570 | 580 | 590 | 600 |
RNGMFLSDHS | CSESRSLIEH | GNECFTHCVN | ISNALEVAQT | KENSCFPVTI | GRRPLTDVQP |
610 | 620 | 630 | 640 | 650 | 660 |
AQRLDGLRDT | TNIAFSTPKS | NQGSINFSVS | TISSTRNTTG | FETNCSRSNM | LAAHQNIPIK |
670 | 680 | 690 | 700 | 710 | 720 |
RISVPDVGIA | TELSHGVVQV | QFYDGSVVSV | IPSMQGGGIT | YTQPNGTSTH | FGKDDDLPFP |
730 | 740 | 750 | 760 | ||
VRDRVGQIPN | IQLKLKTAPL | LESGRKIDYN | AMTPKTTTPC | YNRMLL |