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Protein

Serine/threonine-protein kinase Nek7

Gene

Nek7

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

Functioni

Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1. releasing the autoinhibitory function of Tyr-97 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-97.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATPPROSITE-ProRule annotation
Sitei97 – 971AutoinhibitoryBy similarity
Active sitei161 – 1611Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Nek7 (EC:2.7.11.1)
Alternative name(s):
Never in mitosis A-related kinase 7
Short name:
NimA-related protein kinase 7
Gene namesi
Name:Nek7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1311160. Nek7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Serine/threonine-protein kinase Nek7PRO_0000412823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei191 – 1911PhosphothreonineBy similarity
Modified residuei195 – 1951Phosphoserine; by NEK9By similarity
Modified residuei199 – 1991PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylation at Ser-195 required for its activation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiD3ZBE5.

Expressioni

Tissue specificityi

Highly expressed in the liver.1 Publication

Gene expression databases

GenevisibleiD3ZBE5. RN.

Interactioni

Subunit structurei

Monomer. Interacts with NEK9 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000817.

Structurei

3D structure databases

ProteinModelPortaliD3ZBE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 299266Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 3314NTE motifBy similarityAdd
BLAST

Domaini

Displays an autoinhibited conformation: Tyr-97 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
The NTE (N-terminal extension) motif is a structural component of the catalytic domain and thus contributes to activity.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000118997.
InParanoidiD3ZBE5.
KOiK08857.
OMAiQLVNICI.
OrthoDBiEOG74J983.
PhylomeDBiD3ZBE5.
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.

D3ZBE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEQPQGMQG PPVPQFQPQK ALRPDMGYNT LANFRIEKKI GRGQFSEVYR
60 70 80 90 100
ASCLLDGVPV ALKKVQIFDL MDAKARADCI KEIDLLKQLN HPNVIKYYAS
110 120 130 140 150
FIEDNELNIV LELADAGDLS RMIKHFKKQK RLIPERTVWK YFVQLCSALD
160 170 180 190 200
HMHSRRVMHR DIKPANVFIT ATGVVKLGDL GLGRFFSSKT TAAHSLVGTP
210 220 230 240 250
YYMSPERIHE NGYNFKSDIW SLGCLLYEMA ALQSPFYGDK MNLYSLCKKI
260 270 280 290 300
EQCDYPPLPS DHYSEELRQL VNICINPDPE KRPDIAYVYD VAKRMHACTA

SS
Length:302
Mass (Da):34,529
Last modified:April 20, 2010 - v1
Checksum:i1773BB6E19DFBEDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473958 Genomic DNA. Translation: EDM09639.1.
RefSeqiNP_001101816.1. NM_001108346.2.
XP_006249988.1. XM_006249926.2.
XP_006249989.1. XM_006249927.2.
UniGeneiRn.211490.

Genome annotation databases

EnsembliENSRNOT00000000817; ENSRNOP00000000817; ENSRNOG00000000657.
GeneIDi360850.
KEGGirno:360850.
UCSCiRGD:1311160. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473958 Genomic DNA. Translation: EDM09639.1.
RefSeqiNP_001101816.1. NM_001108346.2.
XP_006249988.1. XM_006249926.2.
XP_006249989.1. XM_006249927.2.
UniGeneiRn.211490.

3D structure databases

ProteinModelPortaliD3ZBE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000817.

Proteomic databases

PRIDEiD3ZBE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000817; ENSRNOP00000000817; ENSRNOG00000000657.
GeneIDi360850.
KEGGirno:360850.
UCSCiRGD:1311160. rat.

Organism-specific databases

CTDi140609.
RGDi1311160. Nek7.

Phylogenomic databases

GeneTreeiENSGT00760000118997.
InParanoidiD3ZBE5.
KOiK08857.
OMAiQLVNICI.
OrthoDBiEOG74J983.
PhylomeDBiD3ZBE5.
TreeFamiTF105135.

Miscellaneous databases

NextBioi674364.
PROiD3ZBE5.

Gene expression databases

GenevisibleiD3ZBE5. RN.

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

« Hide 'large scale' publications
  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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, TISSUE SPECIFICITY.

Entry informationi

Entry nameiNEK7_RAT
AccessioniPrimary (citable) accession number: D3ZBE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: April 20, 2010
Last modified: June 24, 2015
This is version 43 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.