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Shaggy-related protein kinase alpha (EC 2.7.11.1) (ASK-alpha) (Shaggy-related protein kinase 11) (AtSK11)

 KSG1_ARATH              Reviewed;         405 AA.
P43288; O04625; O23151; Q93VJ5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 3.
18-JUL-2018, entry version 149.
RecName: Full=Shaggy-related protein kinase alpha {ECO:0000303|PubMed:7509023};
EC=2.7.11.1;
AltName: Full=ASK-alpha {ECO:0000303|PubMed:7509023};
AltName: Full=Shaggy-related protein kinase 11 {ECO:0000303|PubMed:28575660};
Short=AtSK11 {ECO:0000303|PubMed:28575660};
Name=ASK1 {ECO:0000303|PubMed:7509023};
Synonyms=SK11 {ECO:0000303|PubMed:28575660};
OrderedLocusNames=At5g26751 {ECO:0000312|Araport:AT5G26751};
ORFNames=F2P16.21 {ECO:0000312|EMBL:AAB61055.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Shoot;
PubMed=7509023; DOI=10.1007/BF00280424;
Bianchi M.W., Guivarc'H D., Thomas M., Woodgett J.R., Kreis M.;
"Arabidopsis homologs of the shaggy and GSK-3 protein kinases:
molecular cloning and functional expression in Escherichia coli.";
Mol. Gen. Genet. 242:337-345(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Dornelas M.C., Kreis M.;
"Plant homologues of SGG/GSK-3 protein kinases.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
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., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft 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., Klein Lankhorst R.,
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.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
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.J.,
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.Y., 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., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[7]
INTERACTION WITH KIB1.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S.,
Wang Z.-Y.;
"The F-box protein KIB1 mediates brassinosteroid-induced inactivation
and degradation of GSK3-like kinases in Arabidopsis.";
Mol. Cell 66:648-657(2017).
-!- FUNCTION: May mediate extracellular signals to regulate
transcription in differentiating cells.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Binds to KIB1. {ECO:0000269|PubMed:28575660}.
-!- INTERACTION:
Q94AH6:CUL1; NbExp=2; IntAct=EBI-4463633, EBI-532411;
-!- TISSUE SPECIFICITY: Roots, shoots and leaves.
-!- PTM: Autophosphorylated mainly on threonine and serine residues.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB61055.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA04265.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X68525; CAA48538.1; -; mRNA.
EMBL; X75432; CAA53181.1; -; mRNA.
EMBL; AJ000732; CAA04265.1; ALT_SEQ; Genomic_DNA.
EMBL; AF007270; AAB61055.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED93596.1; -; Genomic_DNA.
EMBL; AF428327; AAL16257.1; -; mRNA.
EMBL; AY046024; AAK76698.1; -; mRNA.
EMBL; AY142595; AAN13164.1; -; mRNA.
PIR; S41596; S41596.
PIR; T01756; T01756.
RefSeq; NP_568486.1; NM_122557.3.
UniGene; At.132; -.
ProteinModelPortal; P43288; -.
SMR; P43288; -.
BioGrid; 18008; 1.
DIP; DIP-46124N; -.
IntAct; P43288; 3.
STRING; 3702.AT5G26751.1; -.
iPTMnet; P43288; -.
PaxDb; P43288; -.
PRIDE; P43288; -.
EnsemblPlants; AT5G26751.1; AT5G26751.1; AT5G26751.
GeneID; 832733; -.
Gramene; AT5G26751.1; AT5G26751.1; AT5G26751.
KEGG; ath:AT5G26751; -.
Araport; AT5G26751; -.
TAIR; locus:2832141; AT5G26751.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233017; -.
InParanoid; P43288; -.
KO; K00924; -.
OMA; KSHELNG; -.
OrthoDB; EOG093609V0; -.
PhylomeDB; P43288; -.
BRENDA; 2.7.11.26; 399.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:P43288; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P43288; baseline and differential.
Genevisible; P43288; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
GO; GO:1901002; P:positive regulation of response to salt stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
CDD; cd14137; STKc_GSK3; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR039192; STKc_GSK3.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 405 Shaggy-related protein kinase alpha.
/FTId=PRO_0000086216.
DOMAIN 69 353 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 75 83 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 194 194 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 98 98 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 229 229 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q39011}.
CONFLICT 281 281 E -> H (in Ref. 1; CAA53181/CAA48538 and
2; CAA04265). {ECO:0000305}.
CONFLICT 372 374 LFN -> AFH (in Ref. 1; CAA53181/CAA48538
and 2; CAA04265). {ECO:0000305}.
SEQUENCE 405 AA; 46035 MW; ACC949DD58479FBB CRC64;
MASVGIAPNP GARDSTGVDK LPEEMNDMKI RDDKEMEATV VDGNGTETGH IIVTTIGGRN
GQPKQTISYM AERVVGHGSF GVVFQAKCLE TGETVAIKKV LQDRRYKNRE LQTMRLLDHP
NVVSLKHCFF STTEKDELYL NLVLEYVPET VHRVIKHYNK LNQRMPLIYV KLYTYQIFRA
LSYIHRCIGV CHRDIKPQNL LVNPHTHQVK LCDFGSAKVL VKGEPNISYI CSRYYRAPEL
IFGATEYTTA IDVWSAGCVL AELLLGQPLF PGESGVDQLV EIIKVLGTPT REEIKCMNPN
YTEFKFPQIK AHPWHKIFHK RMPPEAVDLV SRLLQYSPNL RSAALDTLVH PFFDELRDPN
ARLPNGRFLP PLFNFKPHEL KGVPLEMVAK LVPEHARKQC PWLGL


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