PUB51_ARATH
ID PUB51_ARATH Reviewed; 796 AA.
AC Q9FKG5; Q0WQF2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=U-box domain-containing protein 51;
DE AltName: Full=Plant U-box protein 51;
DE Includes:
DE RecName: Full=E3 ubiquitin ligase;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000305};
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.-;
GN Name=PUB51; OrderedLocusNames=At5g61560; ORFNames=K11J9.9;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. {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;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FKG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKG5-2; Sequence=VSP_031882;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012239; BAB09000.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97488.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69008.1; -; Genomic_DNA.
DR EMBL; AK228747; BAF00647.1; -; mRNA.
DR RefSeq; NP_001330718.1; NM_001345484.1. [Q9FKG5-1]
DR RefSeq; NP_200964.2; NM_125549.3. [Q9FKG5-1]
DR AlphaFoldDB; Q9FKG5; -.
DR SMR; Q9FKG5; -.
DR STRING; 3702.AT5G61560.1; -.
DR iPTMnet; Q9FKG5; -.
DR PaxDb; Q9FKG5; -.
DR EnsemblPlants; AT5G61560.1; AT5G61560.1; AT5G61560. [Q9FKG5-1]
DR EnsemblPlants; AT5G61560.5; AT5G61560.5; AT5G61560. [Q9FKG5-1]
DR GeneID; 836277; -.
DR Gramene; AT5G61560.1; AT5G61560.1; AT5G61560. [Q9FKG5-1]
DR Gramene; AT5G61560.5; AT5G61560.5; AT5G61560. [Q9FKG5-1]
DR KEGG; ath:AT5G61560; -.
DR Araport; AT5G61560; -.
DR TAIR; locus:2151641; AT5G61560.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR InParanoid; Q9FKG5; -.
DR PhylomeDB; Q9FKG5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FKG5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKG5; baseline and differential.
DR Genevisible; Q9FKG5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 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.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..796
FT /note="U-box domain-containing protein 51"
FT /id="PRO_0000322144"
FT DOMAIN 429..700
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 724..796
FT /note="U-box"
FT REGION 163..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..407
FT /evidence="ECO:0000255"
FT COMPBIAS 163..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 557
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 435..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_031882"
SQ SEQUENCE 796 AA; 90223 MW; 0E28A8D73813DF83 CRC64;
MGDGALIVAV AIKGNNSKTK GVVRWALQEF ASQEHVVFKL LHVQPRDSNS VSTTRKDLTT
SVYKKDVDRK TREMLLPSRD MFVHREVQLD IMVLESDDIA DAISKAVQDH GISELVIGAS
SSIIFSWKLK RSNLSSRIAD ATPRFCSVHV ISKGKLLNVR KSDMDTETSI ADDRSESRFS
SDSHSGTVSS TSSHQFSSTP LLFQRIQALT TVNQKVGTNI GKQNNEPHHH HHNRAGSLDV
DESKLLNQKG FYRTSSSGIG YGGSDISSWR SSQMEEASSS STYSDPTSSS SQIHKDFELE
KLKIELRHIK GMYAVAQSEV IDASKKMQDL NQRRSEEATR LKNLTIREEE ADEVVEMERE
RQEDAENEAE LVRECIERET EERLEAEARA EEVRKEKQRL EDALEGGPLQ RQQYMKFEWE
EIVEATSSFS DELKIGVGGY GSVYRCNLHH TTVAVKVLHS DKSSLTKQFH QELEILSKIR
HPHLLLLLGA CPERGSLVYE YMHNGSLEER LMKRRPNVDT PQPPPLRWFE RFRIAWEIAS
ALYFLHTNEP RPIVHRDLKP ANILLDRNNV SKIGDVGLSK MVNLDPSHAS TVFNETGPVG
TFFYIDPEYQ RTGVVTPESD IYAFGIILLQ LVTARSAMGL AHSIEKALRD QTGKFTEILD
KTAGDWPVKE AKEMVMIGLR CAEMRKRDRP DLGKEILPVL ERLKEVASIA RNMFADNLID
HHHNAPTHFY CPITKDVMEN PCVASDGYTY EKRAIKEWLQ KNHKSPMTDL PFPSDSLLPN
HSLLSAIKEW RSQLIK
