TLK2
entrez
11011
canonical
uniprot
Q86UE8
canonical
ensembl
ENSG00000146872
resolver
ensp
ENSP00000275780
resolver
ensp
ENSP00000316512
resolver
ensp
ENSP00000340800
resolver
ensp
ENSP00000463595
resolver
ensp
ENSP00000506744
resolver
ensp
ENSP00000507584
resolver
ensp
ENSP00000507712
resolver
ensp
ENSP00000507724
resolver
ensp
ENSP00000507902
resolver
ensp
ENSP00000508242
resolver
ensp
ENSP00000508315
resolver
ensp
ENSP00000572408
resolver
ensp
ENSP00000572409
resolver
ensp
ENSP00000572411
resolver
ensp
ENSP00000572412
resolver
ensp
ENSP00000601930
resolver
ensp
ENSP00000601933
resolver
ensp
ENSP00000601934
resolver
ensp
ENSP00000601937
resolver
ensp
ENSP00000601939
resolver
ensp
ENSP00000633514
resolver
ensp
ENSP00000633515
resolver
ensp
ENSP00000633516
resolver
ensp
ENSP00000633519
resolver
ensp
ENSP00000633520
resolver
enst
ENST00000582809
resolver
enst
ENST00000682203
resolver
enst
ENST00000683536
resolver
enst
ENST00000684440
resolver
enst
ENST00000684772
resolver
enst
ENST00000931874
resolver
enst
ENST00000931878
resolver
enst
ENST00000963457
resolver
enst
ENST00000963460
resolver
genesymbol
TLK2
resolver
hgnc
HGNC:11842
resolver
uniprot
A0A804HJZ9
resolver
uniprot
A0A804HK10
resolver
uniprot
B4DUC2
resolver
uniprot
D3DU07
resolver
uniprot
J3QLK5
resolver
uniprot
Q9UKI7
resolver
uniprot
Q9Y4F7
resolver
uniprot_entry
A0A804HJZ9_HUMAN
resolver
uniprot_entry
A0A804HK10_HUMAN
resolver
uniprot_entry
B4DUC2_HUMAN
resolver
uniprot_entry
J3QLK5_HUMAN
resolver
uniprot_entry
TLK2_HUMAN
resolver
uniprot_sec
D3DU07
resolver
uniprot_sec
Q9UKI7
resolver
uniprot_sec
Q9Y4F7
resolver
activity_regulation
ACTIVITY REGULATION: Cell cycle-regulated, with maximal activity in the S-phase (PubMed:10523312, PubMed:20016786). Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase, probably by CHEK1, possibly at Ser-750 (PubMed:12660173, PubMed:12955071). This inhibition is cell cycle checkpoint- and ATM-dependent (PubMed:12955071). {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786}.
uniprot
proteins
amino_acid_sequence
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPRGHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLDTEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal dominant 57 (MRD57) [MIM:618050]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD57 is characterized by delayed psychomotor development apparent in infancy or early childhood, and a variety of behavioral abnormalities. Affected individuals may have severe gastro-intestinal problems, and facial dysmorphism. {ECO:0000269|PubMed:21572417, ECO:0000269|PubMed:27479843, ECO:0000269|PubMed:29861108, ECO:0000269|PubMed:29955062, ECO:0000269|PubMed:33323470}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (PubMed:10523312, PubMed:11470414, PubMed:12660173, PubMed:12955071, PubMed:29955062, PubMed:33323470, PubMed:9427565). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (PubMed:11470414, PubMed:20016786, PubMed:29955062, PubMed:35136069). Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly (PubMed:20016786). Negative regulator of amino acid starvation-induced autophagy (PubMed:22354037). {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:20016786, ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:29955062, ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:35136069, ECO:0000269|PubMed:9427565}.
uniprot
proteins
mass_dalton
87661
uniprot
proteins
mutagenesis
MUTAGEN 518; /note="H->N: Reduced kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 592; /note="D->V: Loss of kinase activity. No impact on interaction with ASF1A."; /evidence="ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:35136069"; MUTAGEN 613; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:11470414, ECO:0000269|PubMed:29955062"; MUTAGEN 617; /note="S->A: Increase in autophosphorylation."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 617; /note="S->D: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 659; /note="S->A: Reduced kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 686; /note="S->A: Reduced kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 686; /note="S->D: Reduced kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 695; /note="T->A: Reduced kinase activity."; /evidence="ECO:0000269|PubMed:29955062"; MUTAGEN 720; /note="R->A: Reduced phosphorylation of ASF1A."; /evidence="ECO:0000269|PubMed:29955062
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-750, probably by CHEK1. {ECO:0000269|PubMed:12955071}.; PTM: Autophosphorylated; phosphorylation promotes the assembly of higher order oligomers and enzymatic activity. {ECO:0000269|PubMed:29955062}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
10455159
uniprot
proteins
pubmed
10523312
uniprot
proteins
pubmed
11470414
uniprot
proteins
pubmed
12660173
uniprot
proteins
pubmed
12955071
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16484223
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20016786
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21572417
uniprot
proteins
pubmed
22354037
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27479843
uniprot
proteins
pubmed
29861108
uniprot
proteins
pubmed
29955062
uniprot
proteins
pubmed
33323470
uniprot
proteins
pubmed
35136069
uniprot
proteins
pubmed
9427565
uniprot
proteins
pubmed
9662073
uniprot
proteins
sequence_length
772
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:29955062, ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:9427565}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:33323470}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:33323470}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle (PubMed:10455159). Present in the perinuclear region at S phase and in the nucleus at late G2 (PubMed:10455159). {ECO:0000269|PubMed:10455159}.
uniprot
proteins