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UniProtKB - Q8TD19 (NEK9_HUMAN)

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Protein

Serine/threonine-protein kinase Nek9

Gene

NEK9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-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 eukaryotic nuclear pore complex (e-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

EuPathDBiHostDB:ENSG00000119638.12
HGNCiHGNC:18591 NEK9
MIMi609798 gene
neXtProtiNX_Q8TD19

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Lethal congenital contracture syndrome 10 (LCCS10)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth.
See also OMIM:617022
Nevus comedonicus (NC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare type of epidermal nevus characterized by closely arranged, dilated, plugged follicular ostia in a honeycomb pattern. The plugged ostia contain lamellated keratinaceous material, and their appearance resembles black dots. NC may be non-pyogenic with an acne-like appearance or associated with the formation of cysts, papules, pustules, and abscesses. Most commonly it affects the face and neck area and, by exception, other anatomical regions, including genital area, palms, and soles. NC lesions might present with various patterns of distribution: unilateral, bilateral, linear, interrupted, segmental, or blaschkoid.
See also OMIM:617025
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077801167I → T in NC; increased autophosphorylation at T-210. 1 PublicationCorresponds to variant dbSNP:rs879253775EnsemblClinVar.1
Natural variantiVAR_077802573I → T in NC; increased autophosphorylation at T-210. 1 Publication1
Arthrogryposis, Perthes disease, and upward gaze palsy (APUG)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, syndromic form of arthrogryposis, a disease characterized by persistent joints flexure or contracture. APUG patients manifest an unusual combination of arthrogryposis, upward gaze palsy, and avascular necrosis of the hip (Perthes disease).
See also OMIM:614262
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_077803681R → H in APUG. 1 PublicationCorresponds to variant dbSNP:rs142859694EnsemblClinVar.1

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi91754
MalaCardsiNEK9
MIMi614262 phenotype
617022 phenotype
617025 phenotype
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 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 (PubMed:27153399). When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr-210. Phosphorylated by CDK1 in vitro.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8TD19
MaxQBiQ8TD19
PaxDbiQ8TD19
PeptideAtlasiQ8TD19
PRIDEiQ8TD19
ProteomicsDBi74219

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

Show more details

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi124876, 35 interactors
CORUMiQ8TD19
IntActiQ8TD19, 28 interactors
MINTiQ8TD19
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

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0589 Eukaryota
KOG1426 Eukaryota
ENOG410Y7JF LUCA
GeneTreeiENSGT00760000118997
HOVERGENiHBG039572
InParanoidiQ8TD19
KOiK20878
OMAiEYERHCD
OrthoDBiEOG091G0181
PhylomeDBiQ8TD19
TreeFamiTF106472

Family and domain databases

Gene3Di2.130.10.30, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR009091 RCC1/BLIP-II
IPR000408 Reg_chr_condens
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PF00415 RCC1, 4 hits
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF50985 SSF50985, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
PS50012 RCC1_3, 6 hits

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_077801167I → T in NC; increased autophosphorylation at T-210. 1 PublicationCorresponds to variant dbSNP:rs879253775EnsemblClinVar.1
Natural variantiVAR_027900429R → H3 PublicationsCorresponds to variant dbSNP:rs10146482Ensembl.1
Natural variantiVAR_077802573I → T in NC; increased autophosphorylation at T-210. 1 Publication1
Natural variantiVAR_077803681R → H in APUG. 1 PublicationCorresponds to variant dbSNP:rs142859694EnsemblClinVar.1
Natural variantiVAR_040926828P → T1 PublicationCorresponds to variant dbSNP:rs36014869Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiNEK9_HUMAN
AccessioniPrimary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6
, Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 17, 2006
Last modified: June 20, 2018
This is version 179 of the entry and version 2 of the sequence. See 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

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