Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q8TD19 (NEK9_HUMAN)

UniProt

Q8TD19 - NEK9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Mg2+

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811ATP
Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 669ATPPROSITE-ProRule annotation

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

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811K → M: Loss of activity and autophosphorylation. 1 Publication
Mutagenesisi210 – 2101T → A: Significant reduction of autophosphorylation. 1 Publication
Mutagenesisi214 – 2141T → A: No effect on autophosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA38593.

Chemistry

ChEMBLiCHEMBL5257.
GuidetoPHARMACOLOGYi2124.

Polymorphism and mutation databases

BioMutaiNEK9.
DMDMi116242675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 979978Serine/threonine-protein kinase Nek9PRO_0000086435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
Modified residuei29 – 291PhosphoserineCombined sources
Modified residuei52 – 521PhosphotyrosineCombined sources
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei210 – 2101Phosphothreonine; by autocatalysis1 Publication
Modified residuei254 – 2541PhosphothreonineCombined sources
Modified residuei331 – 3311PhosphoserineCombined sources
Modified residuei333 – 3331PhosphothreonineCombined sources
Modified residuei741 – 7411PhosphoserineCombined sources
Modified residuei801 – 8011PhosphoserineCombined sources
Modified residuei832 – 8321PhosphoserineCombined sources
Modified residuei868 – 8681PhosphoserineCombined sources
Modified residuei869 – 8691PhosphoserineCombined sources
Modified residuei886 – 8861PhosphothreonineCombined sources
Modified residuei944 – 9441PhosphoserineCombined sources
Modified residuei978 – 9781PhosphoserineCombined sources

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.
PhosphoSiteiQ8TD19.

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
DYNLL1P631673EBI-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 interactions.
IntActiQ8TD19. 23 interactions.
MINTiMINT-2984282.
STRINGi9606.ENSP00000238616.

Chemistry

BindingDBiQ8TD19.

Structurei

Secondary structure

1
979
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi942 – 9487Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortaliQ8TD19.
SMRiQ8TD19. Positions 52-751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 308257Protein kinasePROSITE-ProRule annotationAdd
BLAST
Repeati388 – 44457RCC1 1Add
BLAST
Repeati445 – 49854RCC1 2Add
BLAST
Repeati499 – 55052RCC1 3Add
BLAST
Repeati551 – 61565RCC1 4Add
BLAST
Repeati616 – 66853RCC1 5Add
BLAST
Repeati669 – 72658RCC1 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 891160Interaction with NEK6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili892 – 93948Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi752 – 7609Poly-Gly
Compositional biasi765 – 888124Pro/Ser/Thr-richAdd
BLAST

Domaini

Dimerizes through its coiled-coil domain.

Sequence similaritiesi

Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.Curated
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511V → I in AAL87410 (PubMed:12101123).Curated
Sequence conflicti967 – 9671W → G in AAL87410 (PubMed:12101123).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291R → H.3 Publications
Corresponds to variant rs10146482 [ dbSNP | Ensembl ].		VAR_027900
Natural varianti828 – 8281P → T.1 Publication
Corresponds to variant rs36014869 [ dbSNP | Ensembl ].		VAR_040926
Natural varianti870 – 8701P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_040927

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_149107.4. NM_033116.4.
UniGeneiHs.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_149107.4. NM_033116.4.
UniGeneiHs.7200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortaliQ8TD19.
SMRiQ8TD19. Positions 52-751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124876. 32 interactions.
IntActiQ8TD19. 23 interactions.
MINTiMINT-2984282.
STRINGi9606.ENSP00000238616.

Chemistry

BindingDBiQ8TD19.
ChEMBLiCHEMBL5257.
GuidetoPHARMACOLOGYi2124.

Protein family/group databases

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

PTM databases

iPTMnetiQ8TD19.
PhosphoSiteiQ8TD19.

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

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 161 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.