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TLK2_XENTR
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   03-AUG-2022, entry version 84.
DE   RecName: Full=Serine/threonine-protein kinase tousled-like 2 {ECO:0000250|UniProtKB:Q86UE8};
DE            EC=2.7.11.1;
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: Negative regulator of amino acid starvation-induced
CC       autophagy. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {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   PaxDb; Q08CW1; -.
DR   DNASU; 780168; -.
DR   GeneID; 780168; -.
DR   KEGG; xtr:780168; -.
DR   CTD; 11011; -.
DR   Xenbase; XB-GENE-5747259; tlk2.
DR   eggNOG; KOG1151; Eukaryota.
DR   HOGENOM; CLU_000288_85_1_1; -.
DR   InParanoid; Q08CW1; -.
DR   OrthoDB; 693214at2759; -.
DR   PhylomeDB; Q08CW1; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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   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   InterPro; IPR027086; TLK2.
DR   PANTHER; PTHR22974:SF20; PTHR22974:SF20; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; 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
 
 
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