Q8K1R7 · NEK9_MOUSE
- ProteinSerine/threonine-protein kinase Nek9
- GeneNek9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids984 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
Cofactor
Activity regulation
Activated during mitosis by intramolecular autophosphorylation. Activity and autophosphorylation is activated by manganese >> magnesium ions. It is not cell-cycle regulated but activity is higher in G0-arrested cells.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein kinase activator activity | |
Molecular Function | protein kinase binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cell division | |
Biological Process | mitotic cell cycle | |
Biological Process | regulation of mitotic cell cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase Nek9
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8K1R7
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000086436 | 2-984 | Serine/threonine-protein kinase Nek9 | |||
Sequence: SVLGEYERHCDSINSDFGSESGGGGDSGPGPSAVPGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQLVHACLDQDPEQRPAADALLDLPLLRTRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIHQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVSGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQRVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVVQSSSPGGGIGGGGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAVGNSCGASSSCPGWLRKELENAEFIPMPDSPAPLSAAFSQSEKDTLPYEELQGLKVASEVPPEPQRAAGAWPPRLDPAVPCVGKALTSAACACSALQVEVDRLQALVLKCLEEQQKLQQENLQMFTQLQKLNKKLEGGQQVGMHSRGTQTAKEEMEMDPKPDLDSESWCLLGTDSCRPSL | ||||||
Modified residue | 13 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 16 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 52 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 76 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 210 | Phosphothreonine; by autocatalysis | ||||
Sequence: T | ||||||
Modified residue | 254 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 331 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 333 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 741 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 808 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 839 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 891 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 949 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 983 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated on serine and threonine residues. When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr-210. Phosphorylated by CDK1 in vitro.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer; homodimerization is required to activate NEK7. Binds to Ran GTPase. Has a greater affinity for Ran-GDP over Ran-GTP. Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex. Interacts with DYNLL1; phosphorylation at Ser-949 strongly reduces DYNLL1 binding.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, repeat, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 14-43 | Disordered | ||||
Sequence: INSDFGSESGGGGDSGPGPSAVPGPRAGGG | ||||||
Domain | 52-308 | Protein kinase | ||||
Sequence: YIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQLVHACLDQDPEQRPAADALLDLPLL | ||||||
Repeat | 388-444 | RCC1 1 | ||||
Sequence: KELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIHQVSCGDDFTVCVTDE | ||||||
Repeat | 445-498 | RCC1 2 | ||||
Sequence: GQLYAFGSDYYGCMGVDKVSGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRN | ||||||
Repeat | 499-550 | RCC1 3 | ||||
Sequence: KEVYSWGCGEYGRLGLDSEEDYYTPQRVDVPKALIIVAVQCGCDGTFLLTQS | ||||||
Repeat | 551-615 | RCC1 4 | ||||
Sequence: GKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDER | ||||||
Repeat | 616-668 | RCC1 5 | ||||
Sequence: GRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDD | ||||||
Repeat | 669-726 | RCC1 6 | ||||
Sequence: NHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEK | ||||||
Region | 732-896 | Interaction with NEK6 | ||||
Sequence: TIRSNSSGLSIGTVVQSSSPGGGIGGGGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAVGNSCGASSSCPGWLRKELENAEFIPMPDSPAPLSAAFSQSEKDTLPYEELQGLKVASEVPPEPQRAAGAWPPRLDPAVPCVGKALTSAACA | ||||||
Region | 744-790 | Disordered | ||||
Sequence: TVVQSSSPGGGIGGGGGGGGGGGGEEEDSQQESETPDPSGGFRGTME | ||||||
Coiled coil | 896-945 | |||||
Sequence: ACSALQVEVDRLQALVLKCLEEQQKLQQENLQMFTQLQKLNKKLEGGQQV | ||||||
Region | 940-984 | Disordered | ||||
Sequence: EGGQQVGMHSRGTQTAKEEMEMDPKPDLDSESWCLLGTDSCRPSL | ||||||
Compositional bias | 953-967 | Basic and acidic residues | ||||
Sequence: QTAKEEMEMDPKPDL |
Domain
Dimerizes through its coiled-coil domain.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length984
- Mass (Da)107,143
- Last updated2011-07-27 v2
- Checksum034A33BF04667487
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 929 | in Ref. 1; CAD34025 | ||||
Sequence: F → S | ||||||
Compositional bias | 953-967 | Basic and acidic residues | ||||
Sequence: QTAKEEMEMDPKPDL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ489828 EMBL· GenBank· DDBJ | CAD34025.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466590 EMBL· GenBank· DDBJ | EDL02865.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC024926 EMBL· GenBank· DDBJ | AAH24926.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC117971 EMBL· GenBank· DDBJ | AAI17972.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117972 EMBL· GenBank· DDBJ | AAI17973.1 EMBL· GenBank· DDBJ | mRNA |