PUB32_ARATH
ID PUB32_ARATH Reviewed; 805 AA.
AC Q94A51; Q67YL5; Q67YP5; Q9SMU3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=U-box domain-containing protein 32;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 32;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB32 {ECO:0000305};
GN Name=PUB32; OrderedLocusNames=At3g49060; ORFNames=T2J13.100;
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase. {ECO:0000250}.
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 -!- INTERACTION:
CC Q94A51; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25519743, EBI-4426557;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94A51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A51-2; Sequence=VSP_031881;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {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=CAB62004.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g49060 has been split into 2 genes: At3g49055 and At3g49060.; Evidence={ECO:0000305};
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DR EMBL; AL132967; CAB62004.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78494.1; -; Genomic_DNA.
DR EMBL; AY050369; AAK91387.1; -; mRNA.
DR EMBL; BT004526; AAO42772.1; -; mRNA.
DR EMBL; AK176246; BAD44009.1; -; mRNA.
DR EMBL; AK176327; BAD44090.1; -; mRNA.
DR EMBL; AK176453; BAD44216.1; -; mRNA.
DR EMBL; AK176423; BAD44186.1; -; mRNA.
DR PIR; T46124; T46124.
DR RefSeq; NP_566915.1; NM_114765.3. [Q94A51-1]
DR AlphaFoldDB; Q94A51; -.
DR SMR; Q94A51; -.
DR BioGRID; 9386; 1.
DR IntAct; Q94A51; 1.
DR STRING; 3702.AT3G49060.1; -.
DR iPTMnet; Q94A51; -.
DR PaxDb; Q94A51; -.
DR PRIDE; Q94A51; -.
DR EnsemblPlants; AT3G49060.1; AT3G49060.1; AT3G49060. [Q94A51-1]
DR GeneID; 824068; -.
DR Gramene; AT3G49060.1; AT3G49060.1; AT3G49060. [Q94A51-1]
DR KEGG; ath:AT3G49060; -.
DR Araport; AT3G49060; -.
DR TAIR; locus:2101353; AT3G49060.
DR eggNOG; ENOG502QZPS; Eukaryota.
DR InParanoid; Q94A51; -.
DR OMA; AMFLEGP; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q94A51; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94A51; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94A51; baseline and differential.
DR Genevisible; Q94A51; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF04564; U-box; 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; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..805
FT /note="U-box domain-containing protein 32"
FT /id="PRO_0000322139"
FT DOMAIN 460..718
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 734..805
FT /note="U-box"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..434
FT /evidence="ECO:0000255"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..296
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_031881"
FT CONFLICT 476
FT /note="K -> R (in Ref. 4; BAD44216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 91593 MW; 376DEC67F1A088AE CRC64;
MGEIGGEELV LDVDETIFVA VAEDVERSKT TVLWAARNFS GKKICLLYVH RTARAASWTH
KKLVGGSFKK HDVKVIERVE KPKVDELMNS YLQLLSETEI QTDKLCIAGQ NIEECIVELI
ARHKIKWLVM GAASDKHYSW KMTDLKSKKA IFVCKKAPDS CHIWFLCKGY LIFTRASNDD
SNNRQTMPPL VQLDSDNETR KSEKLESSYM RRRLRYWRSL LEQDGEKDTG QLEREKVEPR
APPLFSSGSS SSFGEPVGPE PVSPELVDSD TLNTSNVEEK EREGDVARKV HRYDKAMHDI
GQSDRTVYGE AGKKWEEDAS TTEALCKAKA LEGLCIKESS QRKRLEELLE KEKLEVKMVI
EQNNGFMKEL QMVQGRNLKL ESQMRKLQDL EKEHGEKFDT AMELLKSFRQ KRDEIRIDHE
NAVKEVNALR RLVKGETGES SGSEMLDYSF MEINEATNEF DPSWKLGEGK YGSVYKGNLQ
HLQVAVKMLP SYGSLNHFEF ERRVEILSRV RHPNLVTLMG ACPESRSLIY QYIPNGSLED
CFSSENNVPA LSWESRIRIA SEICSALLFL HSNIPCIIHG NLKPSKILLD SNLVTKINDY
GISQLIPIDG LDKSDPHVDP HYFVSREMTL ESDIYAFGII LLQLLTRRPV SGILRDVKCA
LENDNISAVL DNSAGDWPVA RGKKLANVAI RCCKKNPMNR PDLAVVLRFI DRMKAPEVPS
SETSSYANQN VPRRPPSHYL CPIFQEVMKD PLIAADGFTY EAEAIREWLA NGHDTSPMTN
LKMEDCNLIP NHALHLAIQD WQNQW
