Descriptions

Polo-like kinase 4 (or serine/threonine-protein kinase) is a master regulator of centriole duplication. The linker region between kinase domain and PB1 domain is involved in autoinhibition by blocking the active site of the kinase domain. Phosphorylation of residues within the linker region relieves autoinhibition.

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
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole
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