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DYR1A_XENLA
ID   DYR1A_XENLA             Reviewed;         750 AA.
AC   Q2TAE3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A;
DE            EC=2.7.12.1;
DE   AltName: Full=Protein kinase minibrain homolog;
GN   Name=dyrk1a {ECO:0000250|UniProtKB:Q13627};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAI10969.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAI10969.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=16720323; DOI=10.2741/1979;
RA   Qu Y., Adler V., Chu T., Platica O., Michl J., Pestka S., Izotova L.,
RA   Boutjdir M., Pincus M.R.;
RT   "Two dual specificity kinases are preferentially induced by wild-type
RT   rather than by oncogenic RAS-P21 in Xenopus oocytes.";
RL   Front. Biosci. 11:2420-2427(2006).
CC   -!- FUNCTION: May play a role in a signaling pathway regulating nuclear
CC       functions of cell proliferation. Phosphorylates serine, threonine and
CC       tyrosine residues in its sequence and in exogenous substrates (By
CC       similarity). {ECO:0000250|UniProtKB:Q13627}.
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=2.7.12.1;
CC         Evidence={ECO:0000305};
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=2.7.12.1; Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}.
CC   -!- INDUCTION: By insulin. {ECO:0000269|PubMed:16720323}.
CC   -!- DOMAIN: The polyhistidine repeats act as targeting signals to nuclear
CC       speckles. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on tyrosine residues.
CC       {ECO:0000250|UniProtKB:Q13627}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR   EMBL; BC110968; AAI10969.1; -; mRNA.
DR   RefSeq; NP_001156669.1; NM_001163197.1.
DR   AlphaFoldDB; Q2TAE3; -.
DR   SMR; Q2TAE3; -.
DR   DNASU; 446302; -.
DR   GeneID; 446302; -.
DR   KEGG; xla:446302; -.
DR   CTD; 446302; -.
DR   Xenbase; XB-GENE-1017110; dyrk1a.S.
DR   OrthoDB; 689446at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 446302; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   CDD; cd14226; PKc_DYRK1; 1.
DR   InterPro; IPR028318; DYRK1A/B_MNB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR044131; PKc_DYR1A/1B.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24058:SF121; PTHR24058:SF121; 1.
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; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..750
FT                   /note="Dual specificity tyrosine-phosphorylation-regulated
FT                   kinase 1A"
FT                   /id="PRO_0000284707"
FT   DOMAIN          151..471
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          56..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           109..126
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        56..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..612
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        279
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         157..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         230..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   750 AA;  84157 MW;  2A14AA063E7EBC0E CRC64;
     MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AGQMSHSHQQ YSDRHQQNLN DQQASALPYN
     DQTPQPLPNQ RRMPQTFRDP ATAPLRKLSV DLIKTYKHIN EVYYAKKKRR HQQGQGDDSS
     HKKERKVYND GYDDDNYDYI VKNGEKWMDR YEIDSLIGKG SFGQVVKAYD RVEQEWVAIK
     IIKNKKAFLN QAQIEVRLLE LMNKHDTEMK YYIVHLKRHF MFRNHLCLVF EMLSYNLYDL
     LRNTNFRGVS LNLTRKFAQQ MCTALLFLAT PELSIIHCDL KPENILLCNP KRSAIKIVDF
     GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG CILVEMHTGE PLFSGANEVD
     QMSKIVEVLG IPPAHILDQA PKARKFFEKM PEGTWNLKKT KDGKKEYKPP GTRKLHNILG
     VENGGPGGRR AGESGHTVAD YLKFKDVILR MLDYDAKTRI QPYYALQHSF FKKTADEGTN
     TSNSVSTSPA MEQSQSSGTT SSTSSSSGGS SGTSNSGRAR SDPTHQHRHS GGHFTTAVAM
     DCETHSPQVR QQFPPGWTVP EAPTQVTIET HPVQETTFHV PPSQKNVPHH HGNGSHHHHH
     HHHHHHGQHI LSNRTRTRIY NSPSTSSSTQ DSMDIGNSHH SMTSLSSSTT SSSTSSSSTG
     NQGNQAYQNR PVAANTLDFG QNGTLDVNLT VYSNPRQETG ITGHPDYQYS ANTGPGHYVT
     EGQLTMRQGI DREDSPMTGV CVQQSPVASS
 
 
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