P51955 · NEK2_HUMAN
- ProteinSerine/threonine-protein kinase Nek2
- GeneNEK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids445 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143).
Involved in the regulation of centrosome disjunction (PubMed:26220856).
Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835).
Isoform 1
Isoform 2
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Activity regulation
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 Nek2
- 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 accessionP51955
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Isoform 4
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinitis pigmentosa 67 (RP67)
- Note
- DescriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
- See alsoMIM:615565
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 37 | Loss of kinase activity and of ability to activate NEK11. Loss of phosphorylation of CCDC102B. | ||||
Sequence: K → R | ||||||
Mutagenesis | 141 | Loss of autophosphorylation. | ||||
Sequence: D → A | ||||||
Mutagenesis | 170 | No effect on kinase activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 170 | Kinase activity increased by two fold. | ||||
Sequence: T → E | ||||||
Mutagenesis | 171 | No effect on kinase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 171 | Kinase activity increased by two fold. | ||||
Sequence: S → D | ||||||
Mutagenesis | 175 | Kinase activity decreased by two fold. | ||||
Sequence: T → A | ||||||
Mutagenesis | 175 | Kinase activity increased by two fold. | ||||
Sequence: T → E | ||||||
Mutagenesis | 179 | Loss of kinase activity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 179 | Loss of kinase activity. | ||||
Sequence: T → E | ||||||
Mutagenesis | 241 | Loss of kinase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 241 | Loss of kinase activity. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_019990 | 354 | in dbSNP:rs2230489 | |||
Sequence: N → S | ||||||
Natural variant | VAR_040907 | 410 | in dbSNP:rs56102977 | |||
Sequence: C → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 434 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000086421 | 1-445 | UniProt | Serine/threonine-protein kinase Nek2 | |||
Sequence: MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR | |||||||
Modified residue | 170 | UniProt | Phosphothreonine; by autocatalysis | ||||
Sequence: T | |||||||
Modified residue | 171 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S | |||||||
Modified residue | 175 | UniProt | Phosphothreonine; by autocatalysis | ||||
Sequence: T | |||||||
Modified residue | 179 | UniProt | Phosphothreonine; by autocatalysis | ||||
Sequence: T | |||||||
Modified residue | 184 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 241 | UniProt | Phosphoserine; by autocatalysis | ||||
Sequence: S | |||||||
Modified residue | 296 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 300 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 356 | UniProt | Phosphoserine; by STK3/MST2 | ||||
Sequence: S | |||||||
Modified residue | 365 | UniProt | Phosphoserine; by STK3/MST2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 387 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 397 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 402 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Phosphoserine; by STK3/MST2 | ||||
Sequence: S | |||||||
Modified residue | 428 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 438 | UniProt | Phosphoserine; by STK3/MST2 | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Isoform 1 interacts with CDC20, CTNB1, MAD1L1, MAPK, NEK11, NPM1, NDC80, PCNT and SGO1 (PubMed:14978040, PubMed:15161910, PubMed:15358203, PubMed:15388344, PubMed:17621308, PubMed:18086858, PubMed:18297113, PubMed:20034488, PubMed:20599736).
Isoform 1 interacts with STK3/MST2 (via SARAH domain) and SAV1 (via SARAH domain) (PubMed:21076410).
Isoform 1 and isoform 2 interact with MAD2L1 (PubMed:20034488).
Isoform 1 and isoform 4 interact with PPP1CA and PPP1CC (PubMed:15659832, PubMed:17283141).
Interacts with CEP68; the interaction leads to phosphorylation of CEP68. Interacts with CNTLN; the interaction leads to phosphorylation of CNTLN (PubMed:24554434).
Isoform 1 interacts with CEP85 (PubMed:26220856).
Interacts with CCDC102B; the interaction leads to phosphorylation of CCDC102B (PubMed:30404835).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P51955 | ANAPC4 Q9UJX5 | 7 | EBI-633182, EBI-2554854 | |
BINARY | P51955 | CDC27 P30260 | 3 | EBI-633182, EBI-994813 | |
BINARY | P51955 | KIF24 Q5T7B8 | 7 | EBI-633182, EBI-2556811 | |
BINARY | P51955 | MCC P23508 | 3 | EBI-633182, EBI-307531 | |
XENO | P51955 | MGC80529 Q6GQ04 | 2 | EBI-633182, EBI-995003 | |
BINARY | P51955 | NEK11 Q8NG66 | 5 | EBI-633182, EBI-633195 | |
BINARY | P51955 | PPP1CC P36873-1 | 2 | EBI-633182, EBI-356289 | |
BINARY | P51955-1 | NEK11 Q8NG66 | 2 | EBI-687792, EBI-633195 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-271 | Protein kinase | ||||
Sequence: YEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLI | ||||||
Region | 264-445 | Interaction with PCNT | ||||
Sequence: EILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR | ||||||
Region | 301-445 | Interaction with CEP85 | ||||
Sequence: PVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR | ||||||
Coiled coil | 303-362 | |||||
Sequence: LSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERK | ||||||
Region | 306-334 | Leucine-zipper | ||||
Sequence: LKLKEIQLQERERALKAREERLEQKEQEL | ||||||
Region | 329-445 | Necessary for interaction with MAD1L1 | ||||
Sequence: QKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR | ||||||
Region | 333-370 | Required for microtubule binding and for localization to the centrosomes | ||||
Sequence: ELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNP | ||||||
Region | 403-439 | Interaction with SAV1 and STK3/MST2 | ||||
Sequence: QLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSR | ||||||
Coiled coil | 406-430 | |||||
Sequence: SKSKCKDLKKRLHAAQLRAQALSDI |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
P51955-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsNek2A
- Length445
- Mass (Da)51,763
- Last updated1996-10-01 v1
- ChecksumD33A37778ABB6D9E
P51955-2
- Name2
- SynonymsNek2B
P51955-3
- Name3
P51955-4
- Name4
- SynonymsNek2C, Nek2A-T
- Differences from canonical
- 371-378: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6U4U2 | F6U4U2_HUMAN | NEK2 | 388 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 84-85 | in Ref. 8; CAA80912 | ||||
Sequence: IV → LY | ||||||
Alternative sequence | VSP_015576 | 323-326 | in isoform 3 | |||
Sequence: REER → KKKK | ||||||
Sequence conflict | 325 | in Ref. 5; BAD97073 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_015577 | 327-445 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_041758 | 371-378 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015578 | 371-384 | in isoform 2 | |||
Sequence: ELLNLPSSVIKKKV → GMRINLVNRSWCYK | ||||||
Alternative sequence | VSP_015579 | 385-445 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z29066 EMBL· GenBank· DDBJ | CAA82309.1 EMBL· GenBank· DDBJ | mRNA | ||
AY045701 EMBL· GenBank· DDBJ | AAK92212.1 EMBL· GenBank· DDBJ | mRNA | ||
U11050 EMBL· GenBank· DDBJ | AAA19558.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019729 EMBL· GenBank· DDBJ | AAV38534.1 EMBL· GenBank· DDBJ | mRNA | ||
AK223353 EMBL· GenBank· DDBJ | BAD97073.1 EMBL· GenBank· DDBJ | mRNA | ||
AC096637 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL356310 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC043502 EMBL· GenBank· DDBJ | AAH43502.2 EMBL· GenBank· DDBJ | mRNA | ||
BC052807 EMBL· GenBank· DDBJ | AAH52807.1 EMBL· GenBank· DDBJ | mRNA | ||
BC065932 EMBL· GenBank· DDBJ | AAH65932.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
Z25425 EMBL· GenBank· DDBJ | CAA80912.1 EMBL· GenBank· DDBJ | mRNA | ||
AY863109 EMBL· GenBank· DDBJ | AAW56418.1 EMBL· GenBank· DDBJ | mRNA |