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RPKL1_PONAB
ID   RPKL1_PONAB             Reviewed;         549 AA.
AC   Q5RA67;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ribosomal protein S6 kinase-like 1;
DE            EC=2.7.11.1;
GN   Name=RPS6KL1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. S6 kinase subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; CR859152; CAH91343.1; -; mRNA.
DR   RefSeq; NP_001125795.1; NM_001132323.2.
DR   AlphaFoldDB; Q5RA67; -.
DR   SMR; Q5RA67; -.
DR   STRING; 9601.ENSPPYP00000006814; -.
DR   GeneID; 100172723; -.
DR   KEGG; pon:100172723; -.
DR   CTD; 83694; -.
DR   eggNOG; KOG0603; Eukaryota.
DR   InParanoid; Q5RA67; -.
DR   OrthoDB; 255297at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd05576; STKc_RPK118_like; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR035050; RPS6KL1.
DR   InterPro; IPR035053; STK_RPK118-like.
DR   PANTHER; PTHR15508:SF4; PTHR15508:SF4; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF116846; SSF116846; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..549
FT                   /note="Ribosomal protein S6 kinase-like 1"
FT                   /id="PRO_0000232643"
FT   DOMAIN          87..115
FT                   /note="MIT"
FT   DOMAIN          145..539
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          260..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         151..159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   549 AA;  59973 MW;  7BD447184E2FEF31 CRC64;
     MSLVACECLP SPGLEPEPCS RARSQACVYL EQIRNRVALG VPDMTKRDYL VDAATQIRLA
     LERDVSEDYE AAFNHYQNGV DVLLRGIHVD PNKERREAVK LKITKYLRRA EEIFNCHLQR
     PLSSGASPST GFSSLRLRPI RTLGSAVEQL RGCRVVGVIE KVQLVQDSAT GGTFVVKSLP
     RCHMVSRERL TIIPHGVPYM TKLLRYFMSE DSIFLHLEHV QGGTLWSHLL SQAHPRHSGL
     SSGSTQERMK AQLNPHLNLL TPARLPSGHA PGKDRIALEP PRTSPSLPLA GEAPSIRPQR
     EAEGEPTART STSGSSDLPK APGGHLHLQA RRAGQNSDAG PPRGLTWVPE GAGPVLGGCG
     RGMDQSCLSA DGAGRGCGRA TWSVREEQVK QWAAETLVAL EALHEQGVLC RDLHPGNLLL
     DQAGHIRLTY FGQWSEVEPQ CCGEAVDNLY SAPEVGGISE LTEACDWWSF GSLLYELLTG
     MALSQSHPSG IQAHTQLQLP EWLSRPAASL LTELLQFEPT RRLGMGEGGV SKLKSHPFFS
     TIQWSKLVG
 
 
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