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P59895 (NEK6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase Nek6

EC=2.7.11.1
Alternative name(s):
Never in mitosis A-related kinase 6
Short name=NimA-related protein kinase 6
Gene names
Name:Nek6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence By similarity. Phosphorylates RPS6KB1. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-108 By similarity.

Subunit structure

Interacts with NEK9, predominantly in mitosis. Interacts with KIF11 (via C-terminus). Interacts with APBB1 (via WW domain). Interacts with ANKRA2, ATF4, ARHGAP33, CDC42, CIR1, PRAM1, PTN, PRDX3, PIN1, RAD26L, RBBP6, RPS7, STAT3 and TRIP4 By similarity. Interacts with RPS6KB1.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Nucleus speckle By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Note: Colocalizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis By similarity.

Tissue specificity

Highly expressed in the liver. Ref.2

Domain

Displays an autoinhibited conformation: Tyr-108 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9 By similarity.

Post-translational modification

Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210 By similarity. Ref.2

Sequence similarities

Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Chromosome partition
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitotic metaphase/anaphase transition

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Serine/threonine-protein kinase Nek6
PRO_0000086429

Regions

Domain45 – 310266Protein kinase
Nucleotide binding51 – 599ATP By similarity
Region1 – 4444Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4 By similarity
Region267 – 2704Interaction with APBB1 By similarity

Sites

Active site1721Proton acceptor By similarity
Binding site741ATP By similarity
Site1081Autoinhibitory By similarity

Amino acid modifications

Modified residue371Phosphoserine By similarity
Modified residue2021Phosphothreonine By similarity
Modified residue2061Phosphoserine; by NEK9 By similarity
Modified residue2101Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P59895 [UniParc].

Last modified October 3, 2003. Version 1.
Checksum: 4CC398D70916021F

FASTA31335,835
        10         20         30         40         50         60 
MAGQPSHMPH GGSPNHLCHV LGPAHPPDPQ RHPNTLSFRC SLADFQIEKK IGRGQFSEVY 

        70         80         90        100        110        120 
KATCLLDRKT VALKKVQIFE MMDAKARQDC VKEIGLLKQL NHPNIIKYLD SFIEDNELNI 

       130        140        150        160        170        180 
VLELADAGDL SQMIKYFKKQ KRLIPERTVW KYFVQLCSAV EHMHSRRVMH RDIKPANVFI 

       190        200        210        220        230        240 
TATGIVKLGD LGLGRFFSSE TTAAHSLVGT PYYMSPERIH ENGYNFKSDI WSLGCLLYEM 

       250        260        270        280        290        300 
AALQSPFYGD KMNLFSLCQK IEQCDYPPLP GEHYSEKLRE LVSMCIYPDP NHRPDIEYVH 

       310 
QVAKQMHVWT SST 

« Hide

References

[1]"Cloning of Rattus norvegicus NIMA (never in mitosis gene a)-related expressed kinase 6 (Nek6)."
Zhou G., Zhang Y., Ni J.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase."
Belham C., Comb M.J., Avruch J.
Curr. Biol. 11:1155-1167(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY334013 mRNA. Translation: AAP97428.1.
RefSeqNP_001264161.1. NM_001277232.1.
NP_891998.1. NM_182953.2.
XP_006234162.1. XM_006234100.1.
UniGeneRn.18744.

3D structure databases

ProteinModelPortalP59895.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014630; ENSRNOP00000014631; ENSRNOG00000010897.
GeneID360161.
KEGGrno:360161.
UCSCRGD:727779. rat.

Organism-specific databases

CTD10783.
RGD727779. Nek6.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108402.
HOGENOMHOG000233029.
HOVERGENHBG105886.
InParanoidP59895.
KOK08857.
OMATLADFQI.
OrthoDBEOG74J983.
PhylomeDBP59895.
TreeFamTF105135.

Gene expression databases

GenevestigatorP59895.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio672720.
PROP59895.

Entry information

Entry nameNEK6_RAT
AccessionPrimary (citable) accession number: P59895
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families