UBC16_ARATH
ID UBC16_ARATH Reviewed; 161 AA.
AC Q9FWT2; O48953;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 16;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 16;
DE AltName: Full=Ubiquitin carrier protein 16;
GN Name=UBC16; OrderedLocusNames=At1g75440; ORFNames=F1B16.3;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Yan N., Doelling J., Vierstra R.D.;
RT "A new family of ubiquitin-conjugating enzymes (E2S) AtUBC15/16/17/18 in
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-174(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000250|UniProtKB:P42743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF028339; AAC39325.1; -; Genomic_DNA.
DR EMBL; DQ027030; AAY44856.1; -; mRNA.
DR EMBL; AC023754; AAG13066.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35720.1; -; Genomic_DNA.
DR EMBL; AY065459; AAL38900.1; -; mRNA.
DR EMBL; AY091226; AAM14165.1; -; mRNA.
DR PIR; A96785; A96785.
DR RefSeq; NP_565110.1; NM_106198.5.
DR AlphaFoldDB; Q9FWT2; -.
DR SMR; Q9FWT2; -.
DR BioGRID; 29099; 3.
DR IntAct; Q9FWT2; 3.
DR STRING; 3702.AT1G75440.1; -.
DR PaxDb; Q9FWT2; -.
DR PRIDE; Q9FWT2; -.
DR ProteomicsDB; 243211; -.
DR EnsemblPlants; AT1G75440.1; AT1G75440.1; AT1G75440.
DR GeneID; 843880; -.
DR Gramene; AT1G75440.1; AT1G75440.1; AT1G75440.
DR KEGG; ath:AT1G75440; -.
DR Araport; AT1G75440; -.
DR TAIR; locus:2018447; AT1G75440.
DR eggNOG; KOG0427; Eukaryota.
DR HOGENOM; CLU_030988_15_1_1; -.
DR InParanoid; Q9FWT2; -.
DR OMA; YANDTYQ; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; Q9FWT2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FWT2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWT2; baseline and differential.
DR Genevisible; Q9FWT2; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..161
FT /note="Probable ubiquitin-conjugating enzyme E2 16"
FT /id="PRO_0000345182"
FT DOMAIN 15..161
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 99
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 11
FT /note="T -> V (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..84
FT /note="IFLH -> SFSS (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="L -> S (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> A (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..149
FT /note="GRSP -> EDSSA (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="D -> N (in Ref. 1; AAC39325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18485 MW; EC527C112BA88D89 CRC64;
MSSSGAPSRK TLSKIATNRL QKELVEWQMN PPTGFKHKVT DNLQRWIIEV IGAPGTLYAN
DTYQLQVDFP EHYPMESPQV IFLHPAPLHP HIYSNGHICL DILYDSWSPA MTVSSICISI
LSMLSSSTEK QRPTDNDRYV KNCKNGRSPK ETRWWFHDDK V
