TLK1_CAEEL
ID TLK1_CAEEL Reviewed; 965 AA.
AC P34314; P34323; Q6SSJ1; Q8I4N0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase tousled-like 1;
DE EC=2.7.11.1;
DE AltName: Full=Tousled-like kinase 1;
GN Name=tlk-1; ORFNames=C07A9.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AUTOPHOSPHORYLATION,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14614817; DOI=10.1016/j.cub.2003.10.035;
RA Han Z., Saam J.R., Adams H.P., Mango S.E., Schumacher J.M.;
RT "The C. elegans Tousled-like kinase (TLK-1) has an essential role in
RT transcription.";
RL Curr. Biol. 13:1921-1929(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP INTERACTION WITH AIR-2, AND PHOSPHORYLATION AT SER-634.
RX PubMed=15916946; DOI=10.1016/j.cub.2005.04.019;
RA Han Z., Riefler G.M., Saam J.R., Mango S.E., Schumacher J.M.;
RT "The C. elegans Tousled-like kinase contributes to chromosome segregation
RT as a substrate and regulator of the Aurora B kinase.";
RL Curr. Biol. 15:894-904(2005).
CC -!- FUNCTION: Essential for appropriate transcription during embryonic
CC development. May act during transcription elongation to activate the
CC RNA polymerase II large subunit (ama-1) by phosphorylating the Ser-2
CC residues of the C-terminal domain 7-residue repeats. Does not
CC phosphorylate histone H3. {ECO:0000269|PubMed:14614817}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with air-2. {ECO:0000269|PubMed:15916946}.
CC -!- INTERACTION:
CC P34314; O01427: air-2; NbExp=3; IntAct=EBI-3890382, EBI-312947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14614817}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P34314-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P34314-2; Sequence=VSP_011154;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos from the 2-cell stage until
CC morphogenesis. May also be maternally expressed. Not expressed during
CC mitosis. {ECO:0000269|PubMed:14614817}.
CC -!- PTM: Autophosphorylates in vitro. Phosphorylation on Ser-634 by air-2
CC enhances catalytic activity. {ECO:0000269|PubMed:15916946}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AY450852; AAR18092.1; -; mRNA.
DR EMBL; Z29094; CAA82347.3; -; Genomic_DNA.
DR EMBL; Z29094; CAD45580.2; -; Genomic_DNA.
DR PIR; H88562; H88562.
DR PIR; S40704; S40704.
DR PIR; S40712; S40712.
DR RefSeq; NP_499145.2; NM_066744.3. [P34314-2]
DR RefSeq; NP_871642.2; NM_181913.3. [P34314-1]
DR AlphaFoldDB; P34314; -.
DR SMR; P34314; -.
DR BioGRID; 41564; 4.
DR IntAct; P34314; 3.
DR MINT; P34314; -.
DR STRING; 6239.C07A9.3b; -.
DR iPTMnet; P34314; -.
DR EPD; P34314; -.
DR PaxDb; P34314; -.
DR PeptideAtlas; P34314; -.
DR PRIDE; P34314; -.
DR EnsemblMetazoa; C07A9.3a.1; C07A9.3a.1; WBGene00006579. [P34314-2]
DR EnsemblMetazoa; C07A9.3b.1; C07A9.3b.1; WBGene00006579. [P34314-1]
DR GeneID; 176369; -.
DR KEGG; cel:CELE_C07A9.3; -.
DR UCSC; C07A9.3a; c. elegans. [P34314-1]
DR CTD; 176369; -.
DR WormBase; C07A9.3a; CE36353; WBGene00006579; tlk-1. [P34314-2]
DR WormBase; C07A9.3b; CE36354; WBGene00006579; tlk-1. [P34314-1]
DR eggNOG; KOG1151; Eukaryota.
DR InParanoid; P34314; -.
DR OMA; CRIVKQY; -.
DR OrthoDB; 339338at2759; -.
DR PhylomeDB; P34314; -.
DR PRO; PR:P34314; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006579; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; P34314; baseline and differential.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:WormBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..965
FT /note="Serine/threonine-protein kinase tousled-like 1"
FT /id="PRO_0000086756"
FT DOMAIN 651..928
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 657..665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15916946"
FT VAR_SEQ 942..965
FT /note="LLLVIITLCQHSNRSEDRLCVSNV -> VSSPSIPRSPSVNREDDNM (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:14614817"
FT /id="VSP_011154"
SQ SEQUENCE 965 AA; 109274 MW; 22D6CD7DFF2164B0 CRC64;
MSMLSMDGIV AGGGSSSGGG ERSFVLEQKM FNTGPQNKAL PTVQSSGSSS NHAPIVGESP
LGTVSSTMAT GDTGRVGNVT YMSSGMLGAT QFMPQNSSHP STSVMMQQVP PQNGGATRSS
PTEMQQCMQA MSEDSIEMRD YNSGVHHMHP HQMQMQQQQQ HHQQQYNMSY HNHQQQMQQM
HYHQQQQQYQ QQQAQHHQMY APQIQQQQQQ PQQQSQQQSA QQPQQSSAAL QHVNESSNLS
SAGSISDREP EQHGGTPQRP TAPQSSTATD KKTRKRRKAG PTEDQATPKQ ERKITEFMKV
GGEVASGNSV ARCLLTEYHQ NQGSPKRQPA VQQNGSNSYD SQQQQPQMNQ HEMQNSYWGV
ATPSLGVNNR GTPTPTQQQH YSSDSNSNSN QSPPGQGNQS GRMVRTIDEE TQTDSSLSQA
NPQNADEVAK MNRIIEDHRR QIEELNSKNS LERRKNEASK ETIKRLLIDK NQIERKALRD
KTAADSPRIG CFKTTRTGDS FRDQWVDGWA FAEMDKKTEQ INAERNEIAS ASALLKKRKP
LGIGKEPKRP QAVNSQNDSN GMQPSTSSNT NGDDAIFRRP EEPKEIQYQE YIELDEIYKL
RREHLRKEET DLSMEKERLE KEKQHHVREL KRASNESASQ FNDHRLLHKR YLMLNLLGKG
GFSEVWKAFD IEENRYVACK IHHVNKDWKE EKKANYVKHA MREKDIHKSL DHCRIVKQYD
LLTIDNHSFC TVLEYVPGND LDFYLKQNRS ISEKEARSII MQVVSALVYL NEKSTPIIHY
DLKPANILLE SGNTSGAIKI TDFGLSKIME GESDDHDLGI ELTSQFAGTY WYLPPETFIV
PPPKITCKVD VWSIGVIFYQ CIYGKKPFGN DLTQQKILEY NTIINAREVS FPSKPQVSSA
AQDFIRRCLQ YRKEDRADVF ELAKHELFRP RGAIRASVAG SLLLVIITLC QHSNRSEDRL
CVSNV
