UBC37_ARATH
ID UBC37_ARATH Reviewed; 409 AA.
AC Q941B6; Q9LV54;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 37;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 37;
DE AltName: Full=Ubiquitin carrier protein 37;
GN Name=UBC37; OrderedLocusNames=At3g24515; ORFNames=MOB24.7;
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 [MRNA], FUNCTION, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
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 ECO:0000269|PubMed:16339806}.
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; DQ027050; AAY44876.1; -; mRNA.
DR EMBL; AB020746; BAB02001.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76912.1; -; Genomic_DNA.
DR EMBL; AY052292; AAK96485.1; -; mRNA.
DR EMBL; AY061922; AAL31249.1; -; mRNA.
DR RefSeq; NP_566751.1; NM_113362.2.
DR AlphaFoldDB; Q941B6; -.
DR SMR; Q941B6; -.
DR STRING; 3702.AT3G24515.1; -.
DR PaxDb; Q941B6; -.
DR PRIDE; Q941B6; -.
DR ProteomicsDB; 228690; -.
DR EnsemblPlants; AT3G24515.1; AT3G24515.1; AT3G24515.
DR GeneID; 822045; -.
DR Gramene; AT3G24515.1; AT3G24515.1; AT3G24515.
DR KEGG; ath:AT3G24515; -.
DR Araport; AT3G24515; -.
DR TAIR; locus:505006371; AT3G24515.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_028226_0_0_1; -.
DR InParanoid; Q941B6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q941B6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q941B6; baseline and differential.
DR Genevisible; Q941B6; 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:0006974; P:cellular response to DNA damage stimulus; 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..409
FT /note="Probable ubiquitin-conjugating enzyme E2 37"
FT /id="PRO_0000345202"
FT DOMAIN 6..165
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 207..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 398
FT /note="S -> L (in Ref. 1; AAY44876 and 4; AAK96485/
FT AAL31249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 45083 MW; D8E0591E25489ACE CRC64;
MAQAARLSLR MQKELKLLLS DPPHGASFPH LSSAANGSGD FSTFSTIDAQ IEGPEDTVYA
NGIFNLKIQI PERYPFQPPI VSFATPIYHP NIDNSGRICL DILNLPPKGA WQPSLNISTV
LTSMRLLLSE PNPDDGLMCE VSREYKYNRQ TFDYKAREMT EKYAKVKADG CSTSLQIKNH
GDEKSGESGN SVKLKLTVES SLSIAHTVKR ETAGRDEQED GNGKRKAVVG FGEGNSFGND
GIKRSRKKLS LALPSQSQKK DLCGEEELTR GVSAACKENK KPNLNGKKLS LGLKQPCNDT
LASFRTSAAK SDNNRLSRKL SLRSPLGELN EVSKPEVLAQ TDMKLEMNQN EDARSLRGEF
ENSVLEETSM AESIVVLDSD DSGQEEEERV SSSRSRLSLA KRRVLKCRP
