LOCUS KSG5_ARATH 410 aa linear PLN 27-NOV-2024
DEFINITION RecName: Full=Shaggy-related protein kinase epsilon; AltName:
Full=ASK-epsilon; AltName: Full=Shaggy-related protein kinase 13;
Short=AtSK13.
ACCESSION Q8VZD5
VERSION Q8VZD5.1
DBSOURCE UniProtKB: locus KSG5_ARATH, accession Q8VZD5;
class: standard.
extra accessions:Q9LYJ6
created: Apr 26, 2004.
sequence updated: Mar 1, 2002.
annotation updated: Nov 27, 2024.
xrefs: AL163792.1, CAB87631.1, CP002688.1, AED92057.1, ANM68202.1,
AY065043.1, AAL57679.1, BT010466.1, AAQ65089.1, T48637,
NP_001329975.1, NP_196968.2
xrefs (non-sequence databases): AlphaFoldDB:Q8VZD5, SMR:Q8VZD5,
BioGRID:16593, IntAct:Q8VZD5, STRING:3702.Q8VZD5, iPTMnet:Q8VZD5,
PaxDb:3702-AT5G14640.1, ProteomicsDB:237111,
EnsemblPlants:AT5G14640.1, EnsemblPlants:AT5G14640.1,
EnsemblPlants:AT5G14640, EnsemblPlants:AT5G14640.2,
EnsemblPlants:AT5G14640.2, GeneID:831316, Gramene:AT5G14640.1,
Gramene:AT5G14640.2, KEGG:ath:AT5G14640, Araport:AT5G14640,
TAIR:AT5G14640, eggNOG:KOG0658, HOGENOM:CLU_000288_181_20_1,
InParanoid:Q8VZD5, OMA:TKMATGR, OrthoDB:2872909at2759,
PhylomeDB:Q8VZD5, PRO:PR:Q8VZD5, Proteomes:UP000006548,
ExpressionAtlas:Q8VZD5, GO:0005524, GO:0044024, GO:0106310,
GO:0004674, GO:0006972, GO:0046777, GO:0009651, CDD:cd14137,
FunFam:3.30.200.20:FF:000009, FunFam:1.10.510.10:FF:000082,
Gene3D:1.10.510.10, InterPro:IPR050591, InterPro:IPR011009,
InterPro:IPR000719, InterPro:IPR017441, InterPro:IPR008271,
InterPro:IPR039192, PANTHER:PTHR24057, PANTHER:PTHR24057:SF0,
Pfam:PF00069, SMART:SM00220, SUPFAM:SSF56112, PROSITE:PS00107,
PROSITE:PS50011, PROSITE:PS00108
KEYWORDS Acetylation; ATP-binding; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein
kinase; Transferase.
SOURCE Arabidopsis thaliana (thale cress)
ORGANISM Arabidopsis thaliana
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
Camelineae; Arabidopsis.
REFERENCE 1 (residues 1 to 410)
AUTHORS Tabata,S., Kaneko,T., Nakamura,Y., Kotani,H., Kato,T., Asamizu,E.,
Miyajima,N., Sasamoto,S., Kimura,T., Hosouchi,T., Kawashima,K.,
Kohara,M., Matsumoto,M., Matsuno,A., Muraki,A., Nakayama,S.,
Nakazaki,N., Naruo,K., Okumura,S., Shinpo,S., Takeuchi,C., Wada,T.,
Watanabe,A., Yamada,M., Yasuda,M., Sato,S., de la Bastide,M.,
Huang,E., Spiegel,L., Gnoj,L., O'Shaughnessy,A., Preston,R.,
Habermann,K., Murray,J., Johnson,D., Rohlfing,T., Nelson,J.,
Stoneking,T., Pepin,K., Spieth,J., Sekhon,M., Armstrong,J.,
Becker,M., Belter,E., Cordum,H., Cordes,M., Courtney,L.,
Courtney,W., Dante,M., Du,H., Edwards,J., Fryman,J., Haakensen,B.,
Lamar,E., Latreille,P., Leonard,S., Meyer,R., Mulvaney,E.,
Ozersky,P., Riley,A., Strowmatt,C., Wagner-McPherson,C., Wollam,A.,
Yoakum,M., Bell,M., Dedhia,N., Parnell,L., Shah,R., Rodriguez,M.,
See,L.H., Vil,D., Baker,J., Kirchoff,K., Toth,K., King,L.,
Bahret,A., Miller,B., Marra,M., Martienssen,R., McCombie,W.R.,
Wilson,R.K., Murphy,G., Bancroft,I., Volckaert,G., Wambutt,R.,
Dusterhoft,A., Stiekema,W., Pohl,T., Entian,K.D., Terryn,N.,
Hartley,N., Bent,E., Johnson,S., Langham,S.A., McCullagh,B.,
Robben,J., Grymonprez,B., Zimmermann,W., Ramsperger,U., Wedler,H.,
Balke,K., Wedler,E., Peters,S., van Staveren,M., Dirkse,W.,
Mooijman,P., Lankhorst,R.K., Weitzenegger,T., Bothe,G., Rose,M.,
Hauf,J., Berneiser,S., Hempel,S., Feldpausch,M., Lamberth,S.,
Villarroel,R., Gielen,J., Ardiles,W., Bents,O., Lemcke,K.,
Kolesov,G., Mayer,K., Rudd,S., Schoof,H., Schueller,C.,
Zaccaria,P., Mewes,H.W., Bevan,M. and Fransz,P.
CONSRTM Kazusa DNA Research Institute; Cold Spring Harbor and Washington
University in St Louis Sequencing Consortium; European Union
Arabidopsis Genome Sequencing Consortium
TITLE Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana
JOURNAL Nature 408 (6814), 823-826 (2000)
PUBMED 11130714
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=cv. Columbia
REFERENCE 2 (residues 1 to 410)
AUTHORS Cheng,C.Y., Krishnakumar,V., Chan,A.P., Thibaud-Nissen,F.,
Schobel,S. and Town,C.D.
TITLE Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome
JOURNAL Plant J 89 (4), 789-804 (2017)
PUBMED 27862469
REMARK GENOME REANNOTATION.;
STRAIN=cv. Columbia
REFERENCE 3 (residues 1 to 410)
AUTHORS Yamada,K., Lim,J., Dale,J.M., Chen,H., Shinn,P., Palm,C.J.,
Southwick,A.M., Wu,H.C., Kim,C., Nguyen,M., Pham,P., Cheuk,R.,
Karlin-Newmann,G., Liu,S.X., Lam,B., Sakano,H., Wu,T., Yu,G.,
Miranda,M., Quach,H.L., Tripp,M., Chang,C.H., Lee,J.M., Toriumi,M.,
Chan,M.M., Tang,C.C., Onodera,C.S., Deng,J.M., Akiyama,K.,
Ansari,Y., Arakawa,T., Banh,J., Banno,F., Bowser,L., Brooks,S.,
Carninci,P., Chao,Q., Choy,N., Enju,A., Goldsmith,A.D., Gurjal,M.,
Hansen,N.F., Hayashizaki,Y., Johnson-Hopson,C., Hsuan,V.W.,
Iida,K., Karnes,M., Khan,S., Koesema,E., Ishida,J., Jiang,P.X.,
Jones,T., Kawai,J., Kamiya,A., Meyers,C., Nakajima,M., Narusaka,M.,
Seki,M., Sakurai,T., Satou,M., Tamse,R., Vaysberg,M.,
Wallender,E.K., Wong,C., Yamamura,Y., Yuan,S., Shinozaki,K.,
Davis,R.W., Theologis,A. and Ecker,J.R.
TITLE Empirical analysis of transcriptional activity in the Arabidopsis
genome
JOURNAL Science 302 (5646), 842-846 (2003)
PUBMED 14593172
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
STRAIN=cv. Columbia
REFERENCE 4 (residues 1 to 410)
AUTHORS Zhu,J.Y., Li,Y., Cao,D.M., Yang,H., Oh,E., Bi,Y., Zhu,S. and
Wang,Z.Y.
TITLE The F-box Protein KIB1 Mediates Brassinosteroid-Induced
Inactivation and Degradation of GSK3-like Kinases in Arabidopsis
JOURNAL Mol Cell 66 (5), 648-657 (2017)
PUBMED 28575660
REMARK INTERACTION WITH KIB1.;
STRAIN=cv. Columbia, and cv. Wassilewskija
COMMENT On Jul 5, 2005 this sequence version replaced gi:11259751.
[FUNCTION] May mediate extracellular signals to regulate
transcription in differentiating cells. {ECO:0000250}.
[CATALYTIC ACTIVITY] Reaction=L-seryl-[protein] + ATP =
O-phospho-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:17989,
Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.1.
[CATALYTIC ACTIVITY] Reaction=L-threonyl-[protein] + ATP =
O-phospho-L-threonyl-[protein] + ADP + H(+); Xref=Rhea:RHEA:46608,
Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.1.
[SUBUNIT] Binds to KIB1. {ECO:0000269|PubMed:28575660}.
[PTM] Autophosphorylated mainly on threonine and serine residues.
{ECO:0000250}.
[SIMILARITY] Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
[SEQUENCE CAUTION] Sequence=CAB87631.1; Type=Erroneous gene model
prediction; Evidence={ECO:0000305}.
FEATURES Location/Qualifiers
source 1..410
/organism="Arabidopsis thaliana"
/db_xref="taxon:3702"
gene 1..410
/gene="ASK5"
/locus_tag="At5g14640"
/gene_synonym="SK13"
/gene_synonym="T15N1.130"
Protein 1..410
/product="Shaggy-related protein kinase epsilon"
/EC_number="2.7.11.1"
/note="ASK-epsilon; Shaggy-related protein kinase 13;
AtSK13"
/UniProtKB_evidence="Evidence at protein level"
Region 2..410
/region_name="Mature chain"
/note="Shaggy-related protein kinase epsilon.
/id=PRO_0000086220."
Site 2
/site_type="acetylation"
/note="N-acetylalanine.
/evidence=ECO:0000250|UniProtKB:P43288."
Region 69..361
/region_name="STKc_GSK3"
/note="The catalytic domain of the Serine/Threonine
Kinase, Glycogen Synthase Kinase 3; cd14137"
/db_xref="CDD:271039"
Region 74..358
/region_name="Domain"
/note="Protein kinase.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00159."
Site order(80..84,88,101,103,114,128,149..152,155,157..158,199,
201,203..204,206,218,221,232,234..237,239,277)
/site_type="active"
/db_xref="CDD:271039"
Site order(80..83,88,101,103,128,149..152,155,201,203..204,206,
218)
/site_type="other"
/note="ATP binding site [chemical binding]"
/db_xref="CDD:271039"
Site order(84..85,230..238,246..247,278..282,284..285,289,
309..312)
/site_type="other"
/note="dimer interface [polypeptide binding]"
/db_xref="CDD:271039"
Site order(114,157,199,201,221,232,234..237,239,277)
/site_type="other"
/note="polypeptide substrate binding site [polypeptide
binding]"
/db_xref="CDD:271039"
Site 199
/site_type="active"
/note="Proton acceptor.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027."
Site order(217..227,229..239)
/site_type="other"
/note="activation loop (A-loop)"
/db_xref="CDD:271039"
Site 234
/site_type="phosphorylation"
/note="Phosphotyrosine.
/evidence=ECO:0000250|UniProtKB:Q39011."
Site order(246,281..282,284..285,288..289,309..314)
/site_type="other"
/note="axin binding site [polypeptide binding]"
/db_xref="CDD:271039"
ORIGIN
1 masvgtlpas smatkqsnas icaeklpegi nemkikddke meaavvdgng tetghiivtt
61 iggkngqpkq tisymaeriv gqgsfgivfq akcletgetv aikkvlqdkr yknrelqtmr
121 lldhpnvvsl khcffsttek delylnlvle yvpetvyrvs khysranqrm piiyvklyty
181 qicralayih ggvgvchrdi kpqnllvnph thqvklcdfg sakvlvkgep nisyicsryy
241 rapelifgat eytttidiws agcvlaelll gqplfpgesg vdqlveiikv lgtptreeik
301 cmnpnytefk fpqikahpwh kifhkrtppe avdlvsrllq yspnlrstam eaivhpffde
361 lrdpntrlpn gralpplfnf kpqelkgasl ellsklipdh arkqcsflal
//