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Database: UniProt
Entry: PUB32_ARATH
LinkDB: PUB32_ARATH
Original site: 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   24-JAN-2024, entry version 161.
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.Q94A51; -.
DR   iPTMnet; Q94A51; -.
DR   PaxDb; 3702-AT3G49060-1; -.
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; AT3G49060; -.
DR   eggNOG; ENOG502QZPS; Eukaryota.
DR   InParanoid; Q94A51; -.
DR   OMA; AMFLEGP; -.
DR   OrthoDB; 37517at2759; -.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR   CDD; cd01989; STK_N; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR   PANTHER; PTHR45647:SF22; U-BOX DOMAIN-CONTAINING PROTEIN 32; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57850; RING/U-box; 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
//
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