PUB52_ARATH
ID PUB52_ARATH Reviewed; 845 AA.
AC Q9FKG6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=U-box domain-containing protein 52;
DE AltName: Full=Plant U-box protein 52;
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=PUB52; OrderedLocusNames=At5g61550; ORFNames=K11J9.12;
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].
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FKG6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK228422; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB012239; BAB08999.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97486.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70540.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70541.1; -; Genomic_DNA.
DR EMBL; AK228422; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001332142.1; NM_001345481.1. [Q9FKG6-1]
DR RefSeq; NP_001332143.1; NM_001345480.1. [Q9FKG6-1]
DR RefSeq; NP_200963.1; NM_125548.4. [Q9FKG6-1]
DR AlphaFoldDB; Q9FKG6; -.
DR SMR; Q9FKG6; -.
DR STRING; 3702.AT5G61550.2; -.
DR PaxDb; Q9FKG6; -.
DR PRIDE; Q9FKG6; -.
DR EnsemblPlants; AT5G61550.1; AT5G61550.1; AT5G61550. [Q9FKG6-1]
DR EnsemblPlants; AT5G61550.3; AT5G61550.3; AT5G61550. [Q9FKG6-1]
DR EnsemblPlants; AT5G61550.4; AT5G61550.4; AT5G61550. [Q9FKG6-1]
DR GeneID; 836276; -.
DR Gramene; AT5G61550.1; AT5G61550.1; AT5G61550. [Q9FKG6-1]
DR Gramene; AT5G61550.3; AT5G61550.3; AT5G61550. [Q9FKG6-1]
DR Gramene; AT5G61550.4; AT5G61550.4; AT5G61550. [Q9FKG6-1]
DR KEGG; ath:AT5G61550; -.
DR Araport; AT5G61550; -.
DR eggNOG; ENOG502QQ92; Eukaryota.
DR HOGENOM; CLU_000288_153_1_1; -.
DR InParanoid; Q9FKG6; -.
DR OMA; ALANMNK; -.
DR PhylomeDB; Q9FKG6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FKG6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKG6; baseline and differential.
DR Genevisible; Q9FKG6; AT.
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; 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; 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..845
FT /note="U-box domain-containing protein 52"
FT /id="PRO_0000322145"
FT DOMAIN 490..754
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 774..845
FT /note="U-box"
FT REGION 180..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..468
FT /evidence="ECO:0000255"
FT COMPBIAS 182..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 612
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 496..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 845 AA; 94632 MW; 5A880D7C167ED098 CRC64;
MEEKKVVRAL SEHLSLPPPP SPSVAVAING KKKSKYVVFW ALEKFIPEGF TDFKLLYVRP
PVSYIPTPMG IAVAVSELRE DVVSAYKQEL DWSANEMLRP YKKMFERRKV QVEVLLLDSL
EPAAAIAEEI AGTGVTKLVI GMSLRGFFSR KIDMSSLIAT AVPRFCTVYV ISKGKLASVR
PSESDASGSI RFERSSSTSG STDSPRLPPE YQDFLSAVSE AQSRVSPFSP ALKHSMGSNA
VAQMDTSSSG TDQEEVSTGR GMEIVHSGIE GKKNKDESFS ASFPMGTEAY NSMSWTSKWR
DHEDRREMRS SSSSNNHDLV NMDWGAVVPE NYSWVSHTAS HMSDGLLSVH SITDNQVNLN
FEIEKLRAEL KHVQEMYAMA QTETVGASKK LTELNQRRFE ESEKLVELKE KEEVAKDTAS
KEKQRYEEAM KEAEKVKELM MKEALHRREA EFKAERDARE KDKLQASLVS PGVQYQHYTW
EEIAAATSDF AENLKIGIGA YGSVYKCNLH HTTGAVKVLH AGETQLSKQF DQELEILSKI
RHPHLVLLLG ACPERGCLVY EYMDNGSLDD RLMLVNDTPP IPWFERFRIA LEVASALVFL
HKSKPRPIIH RDLKPGNILL DHNFVSKLGD VGLSTMVNQD DVSSRTIFKQ TSPVGTLCYI
DPEYQRTGII SPKSDVYSLG VVILQLITAK PAIAITHMVE EAIGDDAEFM AILDKKAGSW
PISDTRELAA LGLCCTEMRR RDRPDLKDQI IPALERLRKV ADKAQNLLSR TPSGPPSHFI
CPLLKGVMNE PCVAADGYTY DREAIEEWLR QKDTSPVTNL PLPNKNLIAN YTLYSAIMEW
KSNKR
