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KSG4_ARATH
ID   KSG4_ARATH              Reviewed;         420 AA.
AC   Q9FVS6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Shaggy-related protein kinase delta;
DE            EC=2.7.11.1;
DE   AltName: Full=ASK-delta;
DE   AltName: Full=Shaggy-related protein kinase 42;
DE            Short=AtSK42;
GN   Name=ASK4; Synonyms=SK42;
GN   OrderedLocusNames=At1g57870 {ECO:0000312|Araport:AT1G57870};
GN   ORFNames=F12K22.12 {ECO:0000312|EMBL:AAG29234.1},
GN   F13D13.5 {ECO:0000312|EMBL:AAG50665.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: May mediate extracellular signals to regulate transcription
CC       in differentiating cells. {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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FVS6-1; Sequence=Displayed;
CC   -!- PTM: Autophosphorylated mainly on threonine and serine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; AC079732; AAG29234.1; -; Genomic_DNA.
DR   EMBL; AC079991; AAG50665.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33475.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33476.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM57937.1; -; Genomic_DNA.
DR   EMBL; BT002018; AAN72029.1; -; mRNA.
DR   EMBL; BT008861; AAP68300.1; -; mRNA.
DR   PIR; A96613; A96613.
DR   RefSeq; NP_001319262.1; NM_001333808.1. [Q9FVS6-1]
DR   RefSeq; NP_001320412.1; NM_001333809.1. [Q9FVS6-1]
DR   RefSeq; NP_176096.1; NM_104580.5. [Q9FVS6-1]
DR   AlphaFoldDB; Q9FVS6; -.
DR   SMR; Q9FVS6; -.
DR   BioGRID; 27387; 24.
DR   IntAct; Q9FVS6; 23.
DR   STRING; 3702.AT1G57870.3; -.
DR   iPTMnet; Q9FVS6; -.
DR   PaxDb; Q9FVS6; -.
DR   ProteomicsDB; 237110; -. [Q9FVS6-1]
DR   EnsemblPlants; AT1G57870.1; AT1G57870.1; AT1G57870. [Q9FVS6-1]
DR   EnsemblPlants; AT1G57870.2; AT1G57870.2; AT1G57870. [Q9FVS6-1]
DR   EnsemblPlants; AT1G57870.4; AT1G57870.4; AT1G57870. [Q9FVS6-1]
DR   GeneID; 842162; -.
DR   Gramene; AT1G57870.1; AT1G57870.1; AT1G57870. [Q9FVS6-1]
DR   Gramene; AT1G57870.2; AT1G57870.2; AT1G57870. [Q9FVS6-1]
DR   Gramene; AT1G57870.4; AT1G57870.4; AT1G57870. [Q9FVS6-1]
DR   KEGG; ath:AT1G57870; -.
DR   Araport; AT1G57870; -.
DR   eggNOG; KOG0658; Eukaryota.
DR   HOGENOM; CLU_000288_181_20_1; -.
DR   InParanoid; Q9FVS6; -.
DR   OMA; WHELEAC; -.
DR   PhylomeDB; Q9FVS6; -.
DR   PRO; PR:Q9FVS6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FVS6; baseline and differential.
DR   Genevisible; Q9FVS6; AT.
DR   GO; GO:0005737; C:cytoplasm; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14137; STKc_GSK3; 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   InterPro; IPR039192; STKc_GSK3.
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   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..420
FT                   /note="Shaggy-related protein kinase delta"
FT                   /id="PRO_0000086219"
FT   DOMAIN          82..366
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         88..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         242
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39011"
SQ   SEQUENCE   420 AA;  47835 MW;  06F1E07E1B82145C CRC64;
     MESHLGNGVG SSRSAKNTKN TSSSVDWLSR DMLEMKIRDK TEADEERDSE PDIIDGVGAE
     PGHVITTTLP GRNGQSRQTV SYIAEHVVGT GSFGMVFQAK CRETGEVVAI KKVLQDKRYK
     NRELQIMQML DHPNVVCLKH SFYSRTENEE VYLNLVLEFV PETVNRTARS YSRMNQLMPL
     IYVKLYTYQI CRGLAYLHNC CGLCHRDIKP QNLLVNPHTH QLKICDFGSA KVLVKGEPNI
     SYICSRYYRA PELIFGATEY TTAIDIWSTG CVMAELLLGQ PLFPGESGVD QLVEIIKVLG
     TPTREEIKCM NPNYTEFKFP QIKPHPWHKV FQKRLPPEAV DLLCRFFQYS PNLRCTAVEA
     CIHPFFDELR DPNARLPNGR PLPPLFNFKP QELSGIPPET VDRLVPEHAR KQNHFMALHS
 
 
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