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Protein

Serine/threonine-protein kinase tousled-like 1

Gene

Tlk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10' (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

Enzyme regulationi

Cell-cycle regulated, maximal activity in S-phase. Inactivated by phosphorylation at Ser-743, potentially by CHEK1 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei485 – 4851ATPPROSITE-ProRule annotation
Active sitei586 – 5861Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi462 – 4709ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase tousled-like 1 (EC:2.7.11.1)
Alternative name(s):
Tousled-like kinase 1
Gene namesi
Name:Tlk1
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2441683. Tlk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766Serine/threonine-protein kinase tousled-like 1PRO_0000086753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei159 – 1591PhosphoserineCombined sources
Modified residuei743 – 7431PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8C0V0.
MaxQBiQ8C0V0.
PaxDbiQ8C0V0.
PRIDEiQ8C0V0.

PTM databases

iPTMnetiQ8C0V0.
PhosphoSiteiQ8C0V0.

Expressioni

Tissue specificityi

Ubiquitously expressed in all tissues examined.1 Publication

Gene expression databases

BgeeiQ8C0V0.
CleanExiMM_TLK1.
GenevisibleiQ8C0V0. MM.

Interactioni

Subunit structurei

Heterodimerizes with TLK2. Interacts with ASF1A and ASF1B (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035961.

Structurei

3D structure databases

ProteinModelPortaliQ8C0V0.
SMRiQ8C0V0. Positions 406-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini456 – 734279Protein kinasePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili229 – 28052Sequence analysisAdd
BLAST
Coiled coili397 – 44549Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1151. Eukaryota.
ENOG410Y3FX. LUCA.
GeneTreeiENSGT00790000123008.
HOGENOMiHOG000259522.
HOVERGENiHBG007938.
InParanoidiQ8C0V0.
KOiK08864.
OMAiDVQFPVK.
OrthoDBiEOG78H3SF.
PhylomeDBiQ8C0V0.
TreeFamiTF315233.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C0V0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVQSSSGSL EGPPSWSRLS TSPTPGSAAA ARSLLNHTPP SGRPREGAMD
60 70 80 90 100
ELHSLDPRRQ ELLEARFTGV ATGSTGSTGS CSVGAKASTN NESSNHSFGS
110 120 130 140 150
LGSLSDKESE TPEKKQSESS RGRKRKAESQ NESSQGKSIG GRGHKISDYF
160 170 180 190 200
EYQGGNGSSP VRGIPPAIRS PQNSHSHSTP SSSVRPNSPS PTALAFGDHP
210 220 230 240 250
VVQPKQLSFK ITQTDLTMLK LAALESTKNQ DLEKKEGRID DLLRANCDLR
260 270 280 290 300
RQIDDQQKLL EKYKERLNKC ISMSKKLLIE KSTQEKLSSR EKSMQDRLRL
310 320 330 340 350
GHFTTVRHGA SFTEQWTDGF AFQNLVKQQE WVNQQREDIE RQRKLLGKRK
360 370 380 390 400
PPTANNSQAP ATNSEAKQRK TKAVNGAEND PFVRPNLPQL LTLAEYHEQE
410 420 430 440 450
EIFKLRLGHL KKEEAEIQAE LERLERVRNL HIRELKRINN EDNSQFKDHP
460 470 480 490 500
TLNERYLLLH LLGRGGFSEV YKAFDLYEQR YAAVKIHQLN KSWRDEKKEN
510 520 530 540 550
YHKHACREYR IHKELDHPRI VKLYDYFSLD TDTFCTVLEY CEGNDLDFYL
560 570 580 590 600
KQHKLMSEKE ARSIVMQIVN ALRYLNEIKP PIIHYDLKPG NILLVDGTAC
610 620 630 640 650
GEIKITDFGL SKIMDDDSYG VDGMDLTSQG AGTYWYLPPE CFVVGKEPPK
660 670 680 690 700
ISNKVDVWSV GVIFFQCLYG RKPFGHNQSQ QDILQENTIL KATEVQFPVK
710 720 730 740 750
PVVSSEAKAF IRRCLAYRKE DRFDVHQLAN DPYLLPHMRR SNSSGNLHMS
760
GLTATPTPPS SSIITY
Length:766
Mass (Da):86,624
Last modified:August 22, 2003 - v2
Checksum:i19634346118E6551
GO

Sequence cautioni

The sequence AAH51641.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC051641 mRNA. Translation: AAH51641.1. Different initiation.
AK029773 mRNA. Translation: BAC26610.1. Sequence problems.
CCDSiCCDS50599.1.
RefSeqiNP_766252.2. NM_172664.3.
XP_006499253.1. XM_006499190.2.
UniGeneiMm.136511.

Genome annotation databases

EnsembliENSMUST00000038584; ENSMUSP00000035961; ENSMUSG00000041997.
GeneIDi228012.
KEGGimmu:228012.
UCSCiuc008jzt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC051641 mRNA. Translation: AAH51641.1. Different initiation.
AK029773 mRNA. Translation: BAC26610.1. Sequence problems.
CCDSiCCDS50599.1.
RefSeqiNP_766252.2. NM_172664.3.
XP_006499253.1. XM_006499190.2.
UniGeneiMm.136511.

3D structure databases

ProteinModelPortaliQ8C0V0.
SMRiQ8C0V0. Positions 406-759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035961.

PTM databases

iPTMnetiQ8C0V0.
PhosphoSiteiQ8C0V0.

Proteomic databases

EPDiQ8C0V0.
MaxQBiQ8C0V0.
PaxDbiQ8C0V0.
PRIDEiQ8C0V0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038584; ENSMUSP00000035961; ENSMUSG00000041997.
GeneIDi228012.
KEGGimmu:228012.
UCSCiuc008jzt.1. mouse.

Organism-specific databases

CTDi9874.
MGIiMGI:2441683. Tlk1.

Phylogenomic databases

eggNOGiKOG1151. Eukaryota.
ENOG410Y3FX. LUCA.
GeneTreeiENSGT00790000123008.
HOGENOMiHOG000259522.
HOVERGENiHBG007938.
InParanoidiQ8C0V0.
KOiK08864.
OMAiDVQFPVK.
OrthoDBiEOG78H3SF.
PhylomeDBiQ8C0V0.
TreeFamiTF315233.

Miscellaneous databases

PROiQ8C0V0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0V0.
CleanExiMM_TLK1.
GenevisibleiQ8C0V0. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: LimbImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-766.
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "Mammalian homologues of the plant tousled gene code for cell-cycle-regulated kinases with maximal activities linked to ongoing DNA replication."
    Sillje H.H.W., Takahashi K., Tanaka K., Van Houwe G., Nigg E.A.
    EMBO J. 18:5691-5702(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "The radioresistance kinase TLK1B protects the cells by promoting repair of double strand breaks."
    Sunavala-Dossabhoy G., Balakrishnan S.K., Sen S., Nuthalapaty S., De Benedetti A.
    BMC Mol. Biol. 6:19-19(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTLK1_MOUSE
AccessioniPrimary (citable) accession number: Q8C0V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: June 8, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.