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Shaggy-related protein kinase beta (EC 2.7.11.1) (ASK-beta)

 KSG2_ARATH              Reviewed;         431 AA.
O23145; O81710;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 137.
RecName: Full=Shaggy-related protein kinase beta {ECO:0000303|PubMed:9804971};
EC=2.7.11.1;
AltName: Full=ASK-beta {ECO:0000303|PubMed:9804971};
Name=ASK2 {ECO:0000303|PubMed:9804971};
OrderedLocusNames=At3g61160 {ECO:0000312|Araport:AT3G61160};
ORFNames=T20K12.60 {ECO:0000312|EMBL:CAB71046.1};
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 [GENOMIC DNA / MRNA].
STRAIN=cv. Columbia; TISSUE=Pollen;
PubMed=9804971; DOI=10.1016/S0167-4781(98)00187-0;
Tichtinsky G., Tavares R., Takvorian A., Schwebel-Dugue N., Twell D.,
Kreis M.;
"An evolutionary conserved group of plant GSK-3/shaggy-like protein
kinase genes preferentially expressed in developing pollen.";
Biochim. Biophys. Acta 1442:261-273(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10809443; DOI=10.1023/A:1006368316413;
Tavares R., Aubourg S., Lecharny A., Kreis M.;
"Organization and structural evolution of four multigene families in
Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
Plant Mol. Biol. 42:703-717(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(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).
-!- FUNCTION: May mediate extracellular signals to regulate
transcription in differentiating cells. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=O23145-1; Sequence=Displayed;
-!- 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}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ002280; CAA05292.1; -; mRNA.
EMBL; AJ224338; CAA11903.2; -; Genomic_DNA.
EMBL; AL137898; CAB71046.1; -; Genomic_DNA.
EMBL; CP002686; AEE80162.1; -; Genomic_DNA.
PIR; T47908; T47908.
RefSeq; NP_191675.1; NM_115980.4. [O23145-1]
UniGene; At.172; -.
ProteinModelPortal; O23145; -.
SMR; O23145; -.
BioGrid; 10602; 2.
IntAct; O23145; 7.
STRING; 3702.AT3G61160.2; -.
iPTMnet; O23145; -.
PaxDb; O23145; -.
PRIDE; O23145; -.
EnsemblPlants; AT3G61160.1; AT3G61160.1; AT3G61160. [O23145-1]
GeneID; 825288; -.
Gramene; AT3G61160.1; AT3G61160.1; AT3G61160. [O23145-1]
KEGG; ath:AT3G61160; -.
Araport; AT3G61160; -.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233017; -.
InParanoid; O23145; -.
PhylomeDB; O23145; -.
BRENDA; 2.7.11.26; 399.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:O23145; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; O23145; baseline and differential.
Genevisible; O23145; AT.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; Complete proteome; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 431 Shaggy-related protein kinase beta.
/FTId=PRO_0000086217.
DOMAIN 102 386 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 108 116 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 227 227 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 131 131 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 262 262 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q39011}.
SEQUENCE 431 AA; 49313 MW; 1FB3E6BE19BA8AD0 CRC64;
MNVVRRLTSI ASGRNFVSSD NVGETETPRS KPNQNREETE STETTSYEKD SVSSSENSDH
LPKEIREDMD CGIIKGNGTE SGRIITTKKK GLNDQKDKTI SYRAEHVIGT GSFGVVFQAK
CLETEEKVAI KKVLQDKRYK NRELQIMRML DHPNVVELKH SFFSTTEKDE LYLNLVLEYV
PETIYRASRS YTKMNQHMPL IYIQLYTYQI CRAMNYLHQV VGVCHRDIKP QNLLVNNVTH
EVKICDFGSA KMLIPGEPNI SYICSRYYRA PELIFGATEY TSAIDMWSVG CVMAELFLGH
PLFPGETSVD QLVEIIKILG TPAREEIKNM NPRYNDFKFP QIKAQPWHKI FRRQVSPEAM
DLASRLLQYS PNLRCTALEA CAHPFFDDLR DPRASLPNGR ALPPLFDFTA QELAGASVEL
RHRLIPEHAR K


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