ID TLK2_XENTR Reviewed; 697 AA.
AC Q08CW1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Serine/threonine-protein kinase tousled-like 2 {ECO:0000250|UniProtKB:Q86UE8};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q86UE8};
DE AltName: Full=Tousled-like kinase 2 {ECO:0000312|EMBL:AAI24065.1};
GN Name=tlk2 {ECO:0000312|EMBL:AAI24065.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI24065.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6 {ECO:0000312|EMBL:AAI24065.1};
RC TISSUE=Skin {ECO:0000312|EMBL:AAI24065.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the process of
CC chromatin assembly and probably also DNA replication, transcription,
CC repair, and chromosome segregation (By similarity). Negative regulator
CC of amino acid starvation-induced autophagy (By similarity).
CC {ECO:0000250|UniProtKB:Q86UE8}.
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 Evidence={ECO:0000250|UniProtKB:Q86UE8};
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; Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86UE8};
CC -!- SUBUNIT: Monomer (By similarity). May form homodimers; homodimerization
CC may enhance autophosphoylation and enzymatic activity (By similarity).
CC Heterodimer with TLK1 (By similarity). {ECO:0000250|UniProtKB:Q86UE8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86UE8}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q86UE8}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:Q86UE8}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q86UE8}. Note=Colocalizes with the cytoplasmic
CC intermediate filament system during the G1 phase of the cell cycle (By
CC similarity). Present in the perinuclear region at S phase and in the
CC nucleus at late G2 (By similarity). {ECO:0000250|UniProtKB:Q86UE8}.
CC -!- PTM: Phosphorylated (By similarity). Autophosphorylated;
CC phosphorylation promotes the assembly of higher order oligomers and
CC enzymatic activity (By similarity). {ECO:0000250|UniProtKB:Q86UE8}.
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; BC124064; AAI24065.1; -; mRNA.
DR RefSeq; NP_001072711.1; NM_001079243.1.
DR AlphaFoldDB; Q08CW1; -.
DR SMR; Q08CW1; -.
DR STRING; 8364.ENSXETP00000048197; -.
DR PaxDb; 8364-ENSXETP00000017169; -.
DR DNASU; 780168; -.
DR GeneID; 780168; -.
DR KEGG; xtr:780168; -.
DR AGR; Xenbase:XB-GENE-5747259; -.
DR CTD; 11011; -.
DR Xenbase; XB-GENE-5747259; tlk2.
DR eggNOG; KOG1151; Eukaryota.
DR HOGENOM; CLU_000288_85_1_1; -.
DR InParanoid; Q08CW1; -.
DR OMA; SSFNIGM; -.
DR OrthoDB; 1523at2759; -.
DR PhylomeDB; Q08CW1; -.
DR Proteomes; UP000008143; Chromosome 10.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14041; STKc_TLK2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR22974; MIXED LINEAGE PROTEIN KINASE; 1.
DR PANTHER; PTHR22974:SF20; SERINE_THREONINE-PROTEIN KINASE TOUSLED-LIKE 2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..697
FT /note="Serine/threonine-protein kinase tousled-like 2"
FT /id="PRO_0000367034"
FT DOMAIN 387..666
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 27..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..293
FT /evidence="ECO:0000255"
FT COILED 334..372
FT /evidence="ECO:0000255"
FT COMPBIAS 28..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 517
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 393..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 697 AA; 80071 MW; 76E1A0B9B75D3D2A CRC64;
MMEELHSLDP RRQELLEARF TGVGVAKAPL NSESSNQSLC SLGSLSDKEL EQTPEKKQND
QRNRKRKADP YETSQGKNTP RGHKISDYFE FACGSGPGTS PGRSVPPVAR SSPQHSLSNP
LPLPSQQCSP PSTAPVNPEH SCASFKHISV QHRCTQSDLT MDKISALENS KSSDLEKKEG
RIDDLLRVNC DLRRQMDEQK KMLEKYKERL NRCVTMSKKL LIEKSKQEKM ACRDKSMQDR
LRLGHFTTVR HGASFTEQWT DGYAFQNLIK QQERINTQRE EIERQRKMLA KRKPPAMGQT
PPANNEQKQR KNKTNGAENE ALTLAEYHEQ EEIFKLRLGH LKKEEAEIQA ELERLERVRN
LHIRELKRIH NEDNSQFKDH PTLNDRYLLL HLLGRGGFSE VYKAFDLTEQ RYVAVKIHQL
NKNWRDEKKE NYHKHACREY RIHKELDHPR IVKLYDYFSL DTDSFCTVLE YCEGNDLDFY
LKQHKLMTEK EARSIIMQIV NALKYLNEIK PPIIHYDLKP GNILLVNGTA CGEIKITDFG
LSKIMDDDSY NSVDGMELTS QGAGTYWYLP PECFVVGKEP PKISNKVDVW SVGVIFYQCL
YGRKPFGHNQ SQQDILQENT ILKATEVQFP PKPVVTPEAK AFIRRCLAYR KEDRIDVQQL
ACDPYLLPHI RKSVSTSIPA NAAVASTSGS SNNSLSN
//
