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Protein

Serine/threonine-protein kinase Nek6

Gene

Nek6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741ATPPROSITE-ProRule annotation
Sitei108 – 1081AutoinhibitoryBy similarity
Active sitei172 – 1721Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi51 – 599ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: UniProtKB
  5. signal transducer activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. chromosome segregation Source: UniProtKB
  4. G2 DNA damage checkpoint Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB-KW
  6. peptidyl-serine phosphorylation Source: Ensembl
  7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  8. protein autophosphorylation Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. regulation of mitotic metaphase/anaphase transition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198320. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_198363. Nuclear Pore Complex (NPC) Disassembly.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Nek6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi727779. Nek6.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nuclear speck Source: UniProtKB-SubCell
  4. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Serine/threonine-protein kinase Nek6PRO_0000086429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei202 – 2021PhosphothreonineBy similarity
Modified residuei206 – 2061Phosphoserine; by NEK9By similarity
Modified residuei210 – 2101PhosphothreonineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

Highly expressed in the liver.1 Publication

Gene expression databases

ExpressionAtlasiP59895. baseline.
GenevestigatoriP59895.

Interactioni

Subunit structurei

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.By similarity

Structurei

3D structure databases

ProteinModelPortaliP59895.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 310266Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4444Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4By similarityAdd
BLAST
Regioni267 – 2704Interaction with APBB1By similarity

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118997.
HOGENOMiHOG000233029.
HOVERGENiHBG105886.
InParanoidiP59895.
KOiK08857.
OMAiHQIAKQM.
OrthoDBiEOG74J983.
PhylomeDBiP59895.
TreeFamiTF105135.

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59895-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGQPSHMPH GGSPNHLCHV LGPAHPPDPQ RHPNTLSFRC SLADFQIEKK
60 70 80 90 100
IGRGQFSEVY KATCLLDRKT VALKKVQIFE MMDAKARQDC VKEIGLLKQL
110 120 130 140 150
NHPNIIKYLD SFIEDNELNI VLELADAGDL SQMIKYFKKQ KRLIPERTVW
160 170 180 190 200
KYFVQLCSAV EHMHSRRVMH RDIKPANVFI TATGIVKLGD LGLGRFFSSE
210 220 230 240 250
TTAAHSLVGT PYYMSPERIH ENGYNFKSDI WSLGCLLYEM AALQSPFYGD
260 270 280 290 300
KMNLFSLCQK IEQCDYPPLP GEHYSEKLRE LVSMCIYPDP NHRPDIEYVH
310
QVAKQMHVWT SST
Length:313
Mass (Da):35,835
Last modified:October 3, 2003 - v1
Checksum:i4CC398D70916021F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY334013 mRNA. Translation: AAP97428.1.
RefSeqiNP_001264161.1. NM_001277232.1.
NP_891998.1. NM_182953.2.
XP_006234162.1. XM_006234100.1.
UniGeneiRn.18744.

Genome annotation databases

EnsembliENSRNOT00000014630; ENSRNOP00000014631; ENSRNOG00000010897.
GeneIDi360161.
KEGGirno:360161.
UCSCiRGD:727779. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY334013 mRNA. Translation: AAP97428.1.
RefSeqiNP_001264161.1. NM_001277232.1.
NP_891998.1. NM_182953.2.
XP_006234162.1. XM_006234100.1.
UniGeneiRn.18744.

3D structure databases

ProteinModelPortaliP59895.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014630; ENSRNOP00000014631; ENSRNOG00000010897.
GeneIDi360161.
KEGGirno:360161.
UCSCiRGD:727779. rat.

Organism-specific databases

CTDi10783.
RGDi727779. Nek6.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118997.
HOGENOMiHOG000233029.
HOVERGENiHBG105886.
InParanoidiP59895.
KOiK08857.
OMAiHQIAKQM.
OrthoDBiEOG74J983.
PhylomeDBiP59895.
TreeFamiTF105135.

Enzyme and pathway databases

ReactomeiREACT_198320. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_198363. Nuclear Pore Complex (NPC) Disassembly.

Miscellaneous databases

NextBioi672720.
PROiP59895.

Gene expression databases

ExpressionAtlasiP59895. baseline.
GenevestigatoriP59895.

Family and domain databases

InterProiIPR011009. 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.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiNEK6_RAT
AccessioniPrimary (citable) accession number: P59895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: February 4, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.