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PUB35_ARATH
ID   PUB35_ARATH             Reviewed;         835 AA.
AC   Q9SW11;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=U-box domain-containing protein 35;
DE   AltName: Full=Plant U-box protein 35;
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=PUB35; OrderedLocusNames=At4g25160; ORFNames=F13M23.300, F24A6.13;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX828107; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB36758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035523; CAB36758.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161562; CAB79425.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85018.1; -; Genomic_DNA.
DR   EMBL; BX828107; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T05537; T05537.
DR   RefSeq; NP_194246.2; NM_118648.5.
DR   AlphaFoldDB; Q9SW11; -.
DR   SMR; Q9SW11; -.
DR   BioGRID; 13906; 32.
DR   STRING; 3702.AT4G25160.1; -.
DR   PaxDb; Q9SW11; -.
DR   PRIDE; Q9SW11; -.
DR   ProteomicsDB; 226065; -.
DR   EnsemblPlants; AT4G25160.1; AT4G25160.1; AT4G25160.
DR   GeneID; 828619; -.
DR   Gramene; AT4G25160.1; AT4G25160.1; AT4G25160.
DR   KEGG; ath:AT4G25160; -.
DR   Araport; AT4G25160; -.
DR   TAIR; locus:2117343; AT4G25160.
DR   eggNOG; ENOG502QQ92; Eukaryota.
DR   HOGENOM; CLU_000288_153_1_1; -.
DR   InParanoid; Q9SW11; -.
DR   OMA; DTTHSRA; -.
DR   OrthoDB; 149242at2759; -.
DR   PhylomeDB; Q9SW11; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SW11; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SW11; baseline and differential.
DR   Genevisible; Q9SW11; 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; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR006016; UspA.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF00582; Usp; 1.
DR   SMART; SM00220; S_TKc; 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; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..835
FT                   /note="U-box domain-containing protein 35"
FT                   /id="PRO_0000322142"
FT   DOMAIN          480..745
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          765..835
FT                   /note="U-box"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          340..459
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        602
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         486..494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         507
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   835 AA;  93754 MW;  2BC570AB1A87024C CRC64;
     MSRSPDKLAL PPPPPPPPSR TVVVALSGSS KSKYVVTWAI EKFATEGNVG FKLLHIHPMI
     TSVPTPMGNA IPISEVRDDV VTAYRQEILW QSEEMLKPYT KLFVRRKVAV EVLVIESDNV
     AAAIAEEVTR DSIDRIVIGG SSRSFFSRKA DICSVISALM PNFCTVYVVS KGKLSCVRPS
     DSDGNATIRE DGSERTNSSS GSSGPTSDSS DVMSSAHDSQ SRPLSLPVRR MQHFPAIAGQ
     ASVPMETSSV GSDETRCMSL DAEEARDVSS INRSSTDTTS RWTPRRRDYE ERKEAMSSSS
     SNREYGNFGT RFSWSGMGVD TTHSRASQQA SNMSDALSEQ SYTDNQVNLN FEVEKLRAEL
     RHVQEMYAVA QTETFDASRK LGELNQRRLE EAIKLEELKL KEYEARELAE KEKQNFEKAR
     RDAESMRERA EREIAQRREA ERKSARDTKE KEKLEGTLGS PQLQYQHFAW EEIMAATSSF
     SEELKIGMGA YGAVYKCNLH HTTAVVKVLQ SAENQLSKQF QQELEILSKI RHPHLVLLLG
     ACPEQGALVY EYMENGSLED RLFQVNNSPP LPWFERFRIA WEVAAALVFL HKSKPKPIIH
     RDLKPANILL DHNFVSKVGD VGLSTMVQVD PLSTKFTIYK QTSPVGTLCY IDPEYQRTGR
     ISSKSDIYSF GMILLQLLTA KPAIALTHFV ESAMDSNDEF LKILDQKAGN WPIEETRELA
     ALALCCTELR GKDRPDLKDQ ILPALENLKK VAEKARNSFS GVSTQPPTHF ICPLLKDVMN
     EPCVAADGYT YDRHAIEEWL KEHNTSPMTD SPLHSKNLLP NYTLYTAIME WRSTR
 
 
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