ID Q5XEP8_ARATH Unreviewed; 525 AA.
AC Q5XEP8;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=JUL1 {ECO:0000313|TAIR:AT5G10650};
GN Synonyms=MAJ23.10 {ECO:0000313|EMBL:AED91576.1}, MAJ23_10
GN {ECO:0000313|EMBL:AED91576.1};
GN OrderedLocusNames=At5g10650 {ECO:0000313|Araport:AT5G10650,
GN ECO:0000313|EMBL:AED91576.1};
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 {ECO:0000313|EMBL:AAU95454.1};
RN [1] {ECO:0000313|EMBL:AED91576.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|EMBL:AAU95454.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AED91576.1}
RP NUCLEOTIDE SEQUENCE.
RG TAIR;
RA Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AED91576.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; BT015918; AAU95454.1; -; mRNA.
DR EMBL; BT020582; AAW80855.1; -; mRNA.
DR EMBL; CP002688; AED91576.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91577.1; -; Genomic_DNA.
DR RefSeq; NP_001031869.1; NM_001036792.3.
DR RefSeq; NP_196626.2; NM_121102.6.
DR AlphaFoldDB; Q5XEP8; -.
DR SMR; Q5XEP8; -.
DR STRING; 3702.Q5XEP8; -.
DR PaxDb; 3702-AT5G10650-2; -.
DR EnsemblPlants; AT5G10650.1; AT5G10650.1; AT5G10650.
DR EnsemblPlants; AT5G10650.2; AT5G10650.2; AT5G10650.
DR GeneID; 830929; -.
DR Gramene; AT5G10650.1; AT5G10650.1; AT5G10650.
DR Gramene; AT5G10650.2; AT5G10650.2; AT5G10650.
DR Araport; AT5G10650; -.
DR TAIR; AT5G10650; JUL1.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_027302_1_0_1; -.
DR OMA; CITQWFR; -.
DR OrthoDB; 988298at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5XEP8; baseline and differential.
DR GO; GO:0097427; C:microtubule bundle; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:TAIR.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF195; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q5XEP8};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 475..516
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 79..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 57071 MW; 87B9E03B2E138BEC CRC64;
MDGCAGKRSV DRLVVPRKAS GLTLRENMNK TDGKNVPFCS RVGCTAKVTS TKRSRIGSTD
NNTKVGLPPV PSTLNRKEIV GSSSRTPGGF GYLRKPAKVT ARRQPSSSLD TESSETSCIH
DDPAATEPTL PRQKTKRVTI NVHPQSAVSR EVVITKAGSS SRGTSRISHP KSELGTRDAL
TGPSVSTSSG NSEHTVRGGL SRHRLRNLSC NSVSDVLPTN SNSATKISVT KKKNADGESS
LSSKGSKTSV LVPKVRNQIS SHGNGVTVSD NRRNRVVPSI RDSSTVVSNG CRRAGYFGRS
ERLGATASSA TSRQMPHPTT PTDPNPSLSF CPSNIYSSTG RVHSNMPGSP TEADPSSSLV
NRDGLSHYNM NGIAEVLLAL ERIEHDEELT YEQLASIETN LFSSGMFRFY DQHRDMRLDI
DNMSYEELLA LGDKMGTVST ALSEEALSRS LKQSIYQETD ETGSISLYKD DDIKCSICQE
EYVDGDELGT IPCQHMYHVS CVQQWLRMKN WCPICKTSAE EEKSI
//
