PUB14_ARATH
ID PUB14_ARATH Reviewed; 632 AA.
AC Q8VZ40; Q9SV34;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=U-box domain-containing protein 14;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase PUB14;
DE AltName: Full=Plant U-box protein 14;
DE AltName: Full=Prototypical U-box domain protein 14;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB14 {ECO:0000305};
GN Name=PUB14; OrderedLocusNames=At3g54850; ORFNames=F28P10.170;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11495788; DOI=10.1016/s1360-1385(01)01960-4;
RA Azevedo C., Santos-Rosa M.J., Shirasu K.;
RT "The U-box protein family in plants.";
RL Trends Plant Sci. 6:354-358(2001).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND STRUCTURE BY NMR OF 244-321.
RX PubMed=15231834; DOI=10.1074/jbc.m405057200;
RA Andersen P., Kragelund B.B., Olsen A.N., Larsen F.H., Chua N.H.,
RA Poulsen F.M., Skriver K.;
RT "Structure and biochemical function of a prototypical Arabidopsis U-box
RT domain.";
RL J. Biol. Chem. 279:40053-40061(2004).
RN [6]
RP GENE FAMILY ORGANIZATION.
RX PubMed=14657406; DOI=10.1104/pp.103.029553;
RA Mudgil Y., Shiu S.-H., Stone S.L., Salt J.N., Goring D.R.;
RT "A large complement of the predicted Arabidopsis ARM repeat proteins are
RT members of the U-box E3 ubiquitin ligase family.";
RL Plant Physiol. 134:59-66(2004).
RN [7]
RP INTERACTION WITH SNL1.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
RN [8]
RP INTERACTION WITH SD11; SD16; SD17; SD18; SD113; SD129 AND SD25.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase with specific E2
CC ubiquitin-conjugating enzymes. Undergoes auto-ubiquitination.
CC {ECO:0000269|PubMed:15231834}.
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 -!- SUBUNIT: Homodimer (Probable). Interacts with SNL1. Binds to SD11,
CC SD16, SD17, SD18, SD113, SD129 and SD25. {ECO:0000269|PubMed:18552232,
CC ECO:0000269|PubMed:19962994, ECO:0000305}.
CC -!- INTERACTION:
CC Q8VZ40; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4434802, EBI-4426557;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, green siliques, seeds and
CC rosette leaves. {ECO:0000269|PubMed:15231834}.
CC -!- DOMAIN: The U-box N-terminal domain (UND) is not required for in vitro
CC ubiquitination activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41099.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL049655; CAB41099.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79300.1; -; Genomic_DNA.
DR EMBL; AY065279; AAL38755.1; -; mRNA.
DR EMBL; AY096530; AAM20180.1; -; mRNA.
DR PIR; T06735; T06735.
DR RefSeq; NP_191045.2; NM_115342.5.
DR PDB; 1T1H; NMR; -; A=249-321.
DR PDBsum; 1T1H; -.
DR AlphaFoldDB; Q8VZ40; -.
DR BMRB; Q8VZ40; -.
DR SMR; Q8VZ40; -.
DR BioGRID; 9966; 15.
DR IntAct; Q8VZ40; 15.
DR STRING; 3702.AT3G54850.1; -.
DR PaxDb; Q8VZ40; -.
DR PRIDE; Q8VZ40; -.
DR ProteomicsDB; 226070; -.
DR EnsemblPlants; AT3G54850.1; AT3G54850.1; AT3G54850.
DR GeneID; 824650; -.
DR Gramene; AT3G54850.1; AT3G54850.1; AT3G54850.
DR KEGG; ath:AT3G54850; -.
DR Araport; AT3G54850; -.
DR TAIR; locus:2082682; AT3G54850.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_5_1_1; -.
DR InParanoid; Q8VZ40; -.
DR OMA; SKRMYSN; -.
DR OrthoDB; 389393at2759; -.
DR PhylomeDB; Q8VZ40; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q8VZ40; -.
DR PRO; PR:Q8VZ40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VZ40; baseline and differential.
DR Genevisible; Q8VZ40; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070696; F:transmembrane receptor protein serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..632
FT /note="U-box domain-containing protein 14"
FT /id="PRO_0000097097"
FT DOMAIN 247..321
FT /note="U-box"
FT REPEAT 377..416
FT /note="ARM 1"
FT REPEAT 418..457
FT /note="ARM 2"
FT REPEAT 459..498
FT /note="ARM 3"
FT REPEAT 500..539
FT /note="ARM 4"
FT REPEAT 541..580
FT /note="ARM 5"
FT SITE 256
FT /note="Putative E2 binding site"
FT SITE 281
FT /note="Putative E2 binding site"
FT SITE 290
FT /note="Putative E2 binding site"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1T1H"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1T1H"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1T1H"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:1T1H"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1T1H"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:1T1H"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1T1H"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1T1H"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1T1H"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:1T1H"
SQ SEQUENCE 632 AA; 69397 MW; B9D82E373B9A6619 CRC64;
MGLTNCCSHE ELMSRLVDSV KEISGFSSSR GFIGKIQGDL VRRITLLSPF FEELIDVNVE
LKKDQITGFE AMRIALDSSL ELFRSVNGGS KLFQLFDRDS LVEKFRDMTV EIEAALSQIP
YEKIEVSEEV REQVQLLHFQ FKRAKERWEE SDLQLSHDLA MAENVMDPDP IILKRLSQEL
QLTTIDELKK ESHAIHEYFL SYDGDPDDCF ERMSSLLKNL VDFVTMESSD PDPSTGSRIV
SRHRSPVIPE YFRCPISLEL MKDPVIVSTG QTYERSSIQK WLDAGHKTCP KSQETLLHAG
LTPNYVLKSL IALWCESNGI ELPQNQGSCR TTKIGGSSSS DCDRTFVLSL LEKLANGTTE
QQRAAAGELR LLAKRNVDNR VCIAEAGAIP LLVELLSSPD PRTQEHSVTA LLNLSINEGN
KGAIVDAGAI TDIVEVLKNG SMEARENAAA TLFSLSVIDE NKVAIGAAGA IQALISLLEE
GTRRGKKDAA TAIFNLCIYQ GNKSRAVKGG IVDPLTRLLK DAGGGMVDEA LAILAILSTN
QEGKTAIAEA ESIPVLVEII RTGSPRNREN AAAILWYLCI GNIERLNVAR EVGADVALKE
LTENGTDRAK RKAASLLELI QQTEGVAVTT VP
