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Protein

Serine/threonine-protein kinase Nek9

Gene

NEK9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Activated during mitosis by intramolecular autophosphorylation. Activity and autophosphorylation is activated by manganese >> magnesium ions. Sensitive to increasing concentration of detergents. It is not cell-cycle regulated but activity is higher in G0-arrested cells.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81ATP1
Active sitei176Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi58 – 66ATPPROSITE-ProRule annotation9

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS04314-MONOMER.
ReactomeiR-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
SignaLinkiQ8TD19.
SIGNORiQ8TD19.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Nek9 (EC:2.7.11.1)
Alternative name(s):
Nercc1 kinase
Never in mitosis A-related kinase 9
Short name:
NimA-related protein kinase 9
NimA-related kinase 8
Short name:
Nek8
Gene namesi
Name:NEK9
Synonyms:KIAA1995, NEK8, NERCC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18591. NEK9.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi81K → M: Loss of activity and autophosphorylation. 1 Publication1
Mutagenesisi210T → A: Significant reduction of autophosphorylation. 1 Publication1
Mutagenesisi214T → A: No effect on autophosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi91754.
OpenTargetsiENSG00000119638.
PharmGKBiPA38593.

Chemistry databases

ChEMBLiCHEMBL5257.
GuidetoPHARMACOLOGYi2124.

Polymorphism and mutation databases

BioMutaiNEK9.
DMDMi116242675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000864352 – 979Serine/threonine-protein kinase Nek9Add BLAST978

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei16PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei52PhosphotyrosineCombined sources1
Modified residuei76PhosphoserineCombined sources1
Modified residuei210Phosphothreonine; by autocatalysis1 Publication1
Modified residuei254PhosphothreonineCombined sources1
Modified residuei331PhosphoserineCombined sources1
Modified residuei333PhosphothreonineCombined sources1
Modified residuei741PhosphoserineCombined sources1
Modified residuei801PhosphoserineCombined sources1
Modified residuei832PhosphoserineCombined sources1
Modified residuei868PhosphoserineCombined sources1
Modified residuei869PhosphoserineCombined sources1
Modified residuei886PhosphothreonineCombined sources1
Modified residuei944PhosphoserineCombined sources1
Modified residuei978PhosphoserineCombined sources1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8TD19.
MaxQBiQ8TD19.
PaxDbiQ8TD19.
PeptideAtlasiQ8TD19.
PRIDEiQ8TD19.

PTM databases

iPTMnetiQ8TD19.
PhosphoSitePlusiQ8TD19.

Expressioni

Tissue specificityi

Most abundant in heart, liver, kidney and testis. Also expressed in smooth muscle cells and fibroblasts.

Developmental stagei

Expression varied mildly across the cell cycle, with highest expression observed in G1 and stationary-phase cells.

Gene expression databases

BgeeiENSG00000119638.
CleanExiHS_NEK8.
HS_NEK9.
ExpressionAtlasiQ8TD19. baseline and differential.
GenevisibleiQ8TD19. HS.

Organism-specific databases

HPAiHPA001405.

Interactioni

Subunit structurei

Homodimer. Binds to Ran GTPase. Has a greater affinity for Ran-GDP over Ran-GTP. Interacts with NEK6, NEK7 and BICD2. Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex. Interacts with DYNLL1; phosphorylation at Ser-944 strongly reduces DYNLL1 binding.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DYNLL1P631674EBI-1044009,EBI-349105
GABARAPO951665EBI-1044009,EBI-712001
GABARAPL1Q9H0R86EBI-1044009,EBI-746969
GABARAPL2P605207EBI-1044009,EBI-720116
HSP90AB1P082382EBI-1044009,EBI-352572
MAP1LC3BQ9GZQ82EBI-1044009,EBI-373144
MAP1LC3CQ9BXW42EBI-1044009,EBI-2603996
PLK1P533505EBI-1044009,EBI-476768

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi124876. 32 interactors.
IntActiQ8TD19. 24 interactors.
MINTiMINT-2984282.
STRINGi9606.ENSP00000238616.

Chemistry databases

BindingDBiQ8TD19.

Structurei

Secondary structure

1979
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi942 – 948Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortaliQ8TD19.
SMRiQ8TD19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 308Protein kinasePROSITE-ProRule annotationAdd BLAST257
Repeati388 – 444RCC1 1Add BLAST57
Repeati445 – 498RCC1 2Add BLAST54
Repeati499 – 550RCC1 3Add BLAST52
Repeati551 – 615RCC1 4Add BLAST65
Repeati616 – 668RCC1 5Add BLAST53
Repeati669 – 726RCC1 6Add BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni732 – 891Interaction with NEK61 PublicationAdd BLAST160

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili892 – 939Sequence analysisAdd BLAST48

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi752 – 760Poly-Gly9
Compositional biasi765 – 888Pro/Ser/Thr-richAdd BLAST124

Domaini

Dimerizes through its coiled-coil domain.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 6 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0589. Eukaryota.
KOG1426. Eukaryota.
ENOG410Y7JF. LUCA.
GeneTreeiENSGT00760000118997.
HOVERGENiHBG039572.
InParanoidiQ8TD19.
KOiK08857.
OMAiPTEAMGN.
OrthoDBiEOG091G0181.
PhylomeDBiQ8TD19.
TreeFamiTF106472.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00415. RCC1. 4 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50985. SSF50985. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50012. RCC1_3. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8TD19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL
60 70 80 90 100
HYIPIRVLGR GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI
110 120 130 140 150
VILALLQHDN IIAYYNHFMD NTTLLIELEY CNGGNLYDKI LRQKDKLFEE
160 170 180 190 200
EMVVWYLFQI VSAVSCIHKA GILHRDIKTL NIFLTKANLI KLGDYGLAKK
210 220 230 240 250
LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV IFELLTLKRT
260 270 280 290 300
FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD
310 320 330 340 350
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY
360 370 380 390 400
VWGGGKSTPQ KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT
410 420 430 440 450
KLHGQLGHGD KASYRQPKHV EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF
460 470 480 490 500
GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN PVEQVSCGDN HVVVLTRNKE
510 520 530 540 550
VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG CDGTFLLTQS
560 570 580 590 600
GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR
610 620 630 640 650
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK
660 670 680 690 700
QVIRVSCGDE FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP
710 720 730 740 750
RPIFGSLHHV PDLSCRGWHT ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS
760 770 780 790 800
PGGGGGGGGG EEEDSQQESE TPDPSGGFRG TMEADRGMEG LISPTEAMGN
810 820 830 840 850
SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK DTLPYEELQG
860 870 880 890 900
LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE
910 920 930 940 950
RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA
960 970
KEEMEMDPKP DLDSDSWCLL GTDSCRPSL
Length:979
Mass (Da):107,168
Last modified:October 17, 2006 - v2
Checksum:i8583FDDE599324A2
GO

Sequence cautioni

The sequence AAD31936 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAC02704 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti351V → I in AAL87410 (PubMed:12101123).Curated1
Sequence conflicti967W → G in AAL87410 (PubMed:12101123).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027900429R → H.3 PublicationsCorresponds to variant rs10146482dbSNPEnsembl.1
Natural variantiVAR_040926828P → T.1 PublicationCorresponds to variant rs36014869dbSNPEnsembl.1
Natural variantiVAR_040927870P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048580 mRNA. Translation: AAL05428.1.
AY080896 mRNA. Translation: AAL87410.1.
AB082526 mRNA. Translation: BAC02704.1. Different initiation.
AC007055 Genomic DNA. Translation: AAD31936.1. Sequence problems.
AC007055 Genomic DNA. Translation: AAD31938.1.
AC007055 Genomic DNA. Translation: AAD31939.1.
AC007055 Genomic DNA. Translation: AAD31940.1.
BC009336 mRNA. Translation: AAH09336.2.
BC093881 mRNA. Translation: AAH93881.1.
BC112101 mRNA. Translation: AAI12102.1.
CCDSiCCDS9839.1.
RefSeqiNP_001316166.1. NM_001329237.1.
NP_001316167.1. NM_001329238.1.
NP_149107.4. NM_033116.5.
UniGeneiHs.624721.
Hs.7200.

Genome annotation databases

EnsembliENST00000238616; ENSP00000238616; ENSG00000119638.
GeneIDi91754.
KEGGihsa:91754.
UCSCiuc001xrl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048580 mRNA. Translation: AAL05428.1.
AY080896 mRNA. Translation: AAL87410.1.
AB082526 mRNA. Translation: BAC02704.1. Different initiation.
AC007055 Genomic DNA. Translation: AAD31936.1. Sequence problems.
AC007055 Genomic DNA. Translation: AAD31938.1.
AC007055 Genomic DNA. Translation: AAD31939.1.
AC007055 Genomic DNA. Translation: AAD31940.1.
BC009336 mRNA. Translation: AAH09336.2.
BC093881 mRNA. Translation: AAH93881.1.
BC112101 mRNA. Translation: AAI12102.1.
CCDSiCCDS9839.1.
RefSeqiNP_001316166.1. NM_001329237.1.
NP_001316167.1. NM_001329238.1.
NP_149107.4. NM_033116.5.
UniGeneiHs.624721.
Hs.7200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortaliQ8TD19.
SMRiQ8TD19.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124876. 32 interactors.
IntActiQ8TD19. 24 interactors.
MINTiMINT-2984282.
STRINGi9606.ENSP00000238616.

Chemistry databases

BindingDBiQ8TD19.
ChEMBLiCHEMBL5257.
GuidetoPHARMACOLOGYi2124.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiQ8TD19.
PhosphoSitePlusiQ8TD19.

Polymorphism and mutation databases

BioMutaiNEK9.
DMDMi116242675.

Proteomic databases

EPDiQ8TD19.
MaxQBiQ8TD19.
PaxDbiQ8TD19.
PeptideAtlasiQ8TD19.
PRIDEiQ8TD19.

Protocols and materials databases

DNASUi91754.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238616; ENSP00000238616; ENSG00000119638.
GeneIDi91754.
KEGGihsa:91754.
UCSCiuc001xrl.4. human.

Organism-specific databases

CTDi91754.
DisGeNETi91754.
GeneCardsiNEK9.
HGNCiHGNC:18591. NEK9.
HPAiHPA001405.
MIMi609798. gene.
neXtProtiNX_Q8TD19.
OpenTargetsiENSG00000119638.
PharmGKBiPA38593.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0589. Eukaryota.
KOG1426. Eukaryota.
ENOG410Y7JF. LUCA.
GeneTreeiENSGT00760000118997.
HOVERGENiHBG039572.
InParanoidiQ8TD19.
KOiK08857.
OMAiPTEAMGN.
OrthoDBiEOG091G0181.
PhylomeDBiQ8TD19.
TreeFamiTF106472.

Enzyme and pathway databases

BioCyciZFISH:HS04314-MONOMER.
ReactomeiR-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
SignaLinkiQ8TD19.
SIGNORiQ8TD19.

Miscellaneous databases

ChiTaRSiNEK9. human.
GeneWikiiNEK9.
GenomeRNAii91754.
PROiQ8TD19.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119638.
CleanExiHS_NEK8.
HS_NEK9.
ExpressionAtlasiQ8TD19. baseline and differential.
GenevisibleiQ8TD19. HS.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00415. RCC1. 4 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50985. SSF50985. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50012. RCC1_3. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEK9_HUMAN
AccessioniPrimary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6
, Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.