Y1461_ARATH
ID Y1461_ARATH Reviewed; 572 AA.
AC Q9ZVM9; B3H626;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable serine/threonine-protein kinase At1g54610;
DE EC=2.7.11.1;
GN OrderedLocusNames=At1g54610; ORFNames=T22H22.5;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 -!- INTERACTION:
CC Q9ZVM9; P25854: CAM4; NbExp=2; IntAct=EBI-1235713, EBI-1235664;
CC Q9ZVM9; P59220: CAM7; NbExp=2; IntAct=EBI-1235713, EBI-1236031;
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=Q9ZVM9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC005388; AAC64876.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33123.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33124.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE33125.1; -; Genomic_DNA.
DR EMBL; AF370510; AAK43887.1; -; mRNA.
DR EMBL; AY128918; AAM91318.1; -; mRNA.
DR PIR; B96588; B96588.
DR RefSeq; NP_001117490.1; NM_001124018.1. [Q9ZVM9-1]
DR RefSeq; NP_001319227.1; NM_001333657.1. [Q9ZVM9-1]
DR RefSeq; NP_175862.1; NM_104338.7. [Q9ZVM9-1]
DR AlphaFoldDB; Q9ZVM9; -.
DR SMR; Q9ZVM9; -.
DR BioGRID; 27128; 6.
DR IntAct; Q9ZVM9; 8.
DR STRING; 3702.AT1G54610.2; -.
DR iPTMnet; Q9ZVM9; -.
DR SwissPalm; Q9ZVM9; -.
DR PaxDb; Q9ZVM9; -.
DR PRIDE; Q9ZVM9; -.
DR ProteomicsDB; 242389; -. [Q9ZVM9-1]
DR EnsemblPlants; AT1G54610.1; AT1G54610.1; AT1G54610. [Q9ZVM9-1]
DR EnsemblPlants; AT1G54610.2; AT1G54610.2; AT1G54610. [Q9ZVM9-1]
DR EnsemblPlants; AT1G54610.3; AT1G54610.3; AT1G54610. [Q9ZVM9-1]
DR GeneID; 841903; -.
DR Gramene; AT1G54610.1; AT1G54610.1; AT1G54610. [Q9ZVM9-1]
DR Gramene; AT1G54610.2; AT1G54610.2; AT1G54610. [Q9ZVM9-1]
DR Gramene; AT1G54610.3; AT1G54610.3; AT1G54610. [Q9ZVM9-1]
DR KEGG; ath:AT1G54610; -.
DR Araport; AT1G54610; -.
DR TAIR; locus:2199491; AT1G54610.
DR eggNOG; KOG0600; Eukaryota.
DR InParanoid; Q9ZVM9; -.
DR OMA; SDPYACE; -.
DR PhylomeDB; Q9ZVM9; -.
DR PRO; PR:Q9ZVM9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVM9; baseline and differential.
DR Genevisible; Q9ZVM9; AT.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..572
FT /note="Probable serine/threonine-protein kinase At1g54610"
FT /id="PRO_0000305183"
FT DOMAIN 118..402
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 124..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 572 AA; 63288 MW; 3C7072B7184310C9 CRC64;
MGCVFGREAA TTTTAEAKQA KSSKASSGVV VVGESSVTKS NGVIADDVEK KKNEEANGDK
ERKSSKGDRR RSTKPNPRLS NPSKHWRGEQ VAAGWPSWLS DACGEALNGW VPRKADTFEK
IDKIGQGTYS NVYKAKDMLT GKIVALKKVR FDNLEPESVK FMAREILVLR RLDHPNVVKL
EGLVTSRMSC SLYLVFQYMD HDLAGLASSP VVKFSESEVK CLMRQLISGL EHCHSRGVLH
RDIKGSNLLI DDGGVLKIAD FGLATIFDPN HKRPMTSRVV TLWYRAPELL LGATDYGVGI
DLWSAGCILA ELLAGRPIMP GRTEVEQLHK IYKLCGSPSE DYWKKGKFTH GAIYKPREPY
KRSIRETFKD FPPSSLPLID ALLSIEPEDR QTASAALKSE FFTSEPYACE PADLPKYPPS
KEIDAKRRDE ETRRQRAASK AQGDGARKNR HRDRSNRALP APEANAELQS NVDRRRLITH
ANAKSKSEKF PPPHQDGGAM GVPLGASQHI DPTFIPRDMV PSFTSSSFNF SKDEPPTQVQ
TWSGPLGHPI TGVSRKKKDN TKSSKGKRAV VA
