NEK9
entrez
91754
canonical
uniprot
Q8TD19
canonical
ensembl
ENSG00000119638
resolver
ensp
ENSP00000238616
resolver
ensp
ENSP00000503827
resolver
ensp
ENSP00000504104
resolver
ensp
ENSP00000504620
resolver
enst
ENST00000238616
resolver
enst
ENST00000678037
resolver
enst
ENST00000678531
resolver
enst
ENST00000678749
resolver
genesymbol
NEK9
resolver
genesymbol_syn
KIAA1995
resolver
genesymbol_syn
NEK8
resolver
genesymbol_syn
NERCC
resolver
hgnc
HGNC:18591
resolver
uniprot
A0A7I2V454
resolver
uniprot
A0A7I2V5R1
resolver
uniprot
Q52LK6
resolver
uniprot
Q6PKF2
resolver
uniprot
Q8NCN0
resolver
uniprot
Q8TCY4
resolver
uniprot
Q9UPI4
resolver
uniprot
Q9Y6S4
resolver
uniprot
Q9Y6S5
resolver
uniprot
Q9Y6S6
resolver
uniprot_entry
A0A7I2V454_HUMAN
resolver
uniprot_entry
A0A7I2V5R1_HUMAN
resolver
uniprot_entry
NEK9_HUMAN
resolver
uniprot_entry
Q6PKF2_HUMAN
resolver
uniprot_sec
Q52LK6
resolver
uniprot_sec
Q8NCN0
resolver
uniprot_sec
Q8TCY4
resolver
uniprot_sec
Q9UPI4
resolver
uniprot_sec
Q9Y6S4
resolver
uniprot_sec
Q9Y6S5
resolver
uniprot_sec
Q9Y6S6
resolver
activity_regulation
ACTIVITY REGULATION: Activated during mitosis by intramolecular autophosphorylation (PubMed:11864968). Activity and autophosphorylation is activated by manganese >> magnesium ions (PubMed:11864968). Sensitive to increasing concentration of detergents (PubMed:11864968). It is not cell-cycle regulated but activity is higher in G0-arrested cells (PubMed:11864968). {ECO:0000269|PubMed:11864968}.
uniprot
proteins
amino_acid_sequence
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL
uniprot
proteins
disease_involvement
DISEASE: Lethal congenital contracture syndrome 10 (LCCS10) [MIM:617022]: A 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. {ECO:0000269|PubMed:26908619}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Nevus comedonicus (NC) [MIM:617025]: A 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. {ECO:0000269|PubMed:27153399}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Arthrogryposis, Perthes disease, and upward gaze palsy (APUG) [MIM:614262]: An 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). {ECO:0000269|PubMed:26633546}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.38
uniprot
proteins
function
FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817, PubMed:26522158). {ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:12101123, ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158}.
uniprot
proteins
mass_dalton
107168
uniprot
proteins
mutagenesis
MUTAGEN 81; /note="K->M: Loss of activity and autophosphorylation."; /evidence="ECO:0000269|PubMed:12101123"; MUTAGEN 210; /note="T->A: Significant reduction of autophosphorylation."; /evidence="ECO:0000269|PubMed:11864968"; MUTAGEN 214; /note="T->A: No effect on autophosphorylation."; /evidence="ECO:0000269|PubMed:11864968
uniprot
proteins
post_translational_modification
PTM: 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 (PubMed:14660563). {ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:27153399}.
uniprot
proteins
protein_family
NEK Ser/Thr protein kinase family
uniprot
proteins
protein_family
NIMA subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11864968
uniprot
proteins
pubmed
12056414
uniprot
proteins
pubmed
12101123
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12840024
uniprot
proteins
pubmed
14660563
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19001501
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19941817
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23482567
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26522158
uniprot
proteins
pubmed
26633546
uniprot
proteins
pubmed
26908619
uniprot
proteins
pubmed
27153399
uniprot
proteins
sequence_length
979
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14660563}. Nucleus {ECO:0000269|PubMed:14660563}.
uniprot
proteins