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