| Tag | Content |
|---|
| CPLM ID | CPLM-023093 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine/threonine-protein kinase tousled-like 1 |
Protein Synonyms/Alias | PKU-beta; Tousled-like kinase 1 |
Gene Name | TLK1 |
Gene Synonyms/Alias | KIAA0137 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 700 | TEVQFPVKPVVSSEA | ubiquitination | [1] |
|
Reference | [1] Integrated proteomic analysis of post-translational modifications by serial enrichment. Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA. Nat Methods. 2013 Jul;10(7):634-7. [ PMID: 23749302] |
Functional Description | Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S- phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'. |
Sequence Annotation | DOMAIN 456 734 Protein kinase.
NP_BIND 462 470 ATP (By similarity).
ACT_SITE 586 586 Proton acceptor.
BINDING 485 485 ATP (By similarity).
MOD_RES 159 159 Phosphoserine.
MOD_RES 743 743 Phosphoserine. |
Keyword | Alternative splicing; ATP-binding; Cell cycle; Chromatin regulator; Coiled coil; Complete proteome; DNA damage; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 766 AA |
Protein Sequence | MSVQSSSGSL EGPPSWSQLS TSPTPGSAAA ARSLLNHTPP SGRPREGAMD ELHSLDPRRQ 60
ELLEARFTGV ASGSTGSTGS CSVGAKASTN NESSNHSFGS LGSLSDKESE TPEKKQSESS 120
RGRKRKAENQ NESSQGKSIG GRGHKISDYF EYQGGNGSSP VRGIPPAIRS PQNSHSHSTP 180
SSSVRPNSPS PTALAFGDHP IVQPKQLSFK IIQTDLTMLK LAALESNKIQ DLEKKEGRID 240
DLLRANCDLR RQIDEQQKLL EKYKERLNKC ISMSKKLLIE KSTQEKLSSR EKSMQDRLRL 300
GHFTTVRHGA SFTEQWTDGF AFQNLVKQQE WVNQQREDIE RQRKLLAKRK PPTANNSQAP 360
STNSEPKQRK NKAVNGAEND PFVRPNLPQL LTLAEYHEQE EIFKLRLGHL KKEEAEIQAE 420
LERLERVRNL HIRELKRINN EDNSQFKDHP TLNERYLLLH LLGRGGFSEV YKAFDLYEQR 480
YAAVKIHQLN KSWRDEKKEN YHKHACREYR IHKELDHPRI VKLYDYFSLD TDTFCTVLEY 540
CEGNDLDFYL KQHKLMSEKE ARSIVMQIVN ALRYLNEIKP PIIHYDLKPG NILLVDGTAC 600
GEIKITDFGL SKIMDDDSYG VDGMDLTSQG AGTYWYLPPE CFVVGKEPPK ISNKVDVWSV 660
GVIFFQCLYG RKPFGHNQSQ QDILQENTIL KATEVQFPVK PVVSSEAKAF IRRCLAYRKE 720
DRFDVHQLAN DPYLLPHMRR SNSSGNLHMA GLTASPTPPS SSIITY 766 |
Gene Ontology | GO:0005634; C:nucleus; IDA:UniProtKB. GO:0005524; F:ATP binding; IDA:UniProtKB. GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. GO:0007049; P:cell cycle; IEA:UniProtKB-KW. GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. GO:0006886; P:intracellular protein transport; IDA:UniProtKB. GO:0035556; P:intracellular signal transduction; IDA:UniProtKB. GO:0001672; P:regulation of chromatin assembly or disassembly; IDA:UniProtKB. GO:0006974; P:response to DNA damage stimulus; IEA:UniProtKB-KW. |
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