| Tag | Content |
|---|
| CPLM ID | CPLM-023094 |
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 |
|---|
| 721 | TEVQFPVKPVVSSEA | ubiquitination | [1] |
|
Reference | [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C. Nat Cell Biol. 2012 Oct;14(10):1089-98. [ PMID: 23000965] |
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 NESSQGFPNL PVFQSLAYWE MGRTAGGKSI GGRGHKISDY FEYQGGNGSS 180
PVRGIPPAIR SPQNSHSHST PSSSVRPNSP SPTALAFGDH PIVQPKQLSF KIIQTDLTML 240
KLAALESNKI QDLEKKEGRI DDLLRANCDL RRQIDEQQKL LEKYKERLNK CISMSKKLLI 300
EKSTQEKLSS REKSMQDRLR LGHFTTVRHG ASFTEQWTDG FAFQNLVKQQ EWVNQQREDI 360
ERQRKLLAKR KPPTANNSQA PSTNSEPKQR KNKAVNGAEN DPFVRPNLPQ LLTLAEYHEQ 420
EEIFKLRLGH LKKEEAEIQA ELERLERVRN LHIRELKRIN NEDNSQFKDH PTLNERYLLL 480
HLLGRGGFSE VYKAFDLYEQ RYAAVKIHQL NKSWRDEKKE NYHKHACREY RIHKELDHPR 540
IVKLYDYFSL DTDTFCTVLE YCEGNDLDFY LKQHKLMSEK EARSIVMQIV NALRYLNEIK 600
PPIIHYDLKP GNILLVDGTA CGEIKITDFG LSKIMDDDSY GVDGMDLTSQ GAGTYWYLPP 660
ECFVVGKEPP KISNKVDVWS VGVIFFQCLY GRKPFGHNQS QQDILQENTI LKATEVQFPV 720
KPVVSSEAKA FIRRCLAYRK EDRFDVHQLA NDPYLLPHMR RSNSSGNLHM AGLTASPTPP 780
SSSIITY 787 |
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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