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Ubiquitin-conjugating enzyme E2 8 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 8) (UBCAT4A) (Ubiquitin carrier protein 8) (Ubiquitin-conjugating enzyme E2-17 kDa 8) (Ubiquitin-protein ligase 8)

 UBC8_ARATH              Reviewed;         148 AA.
P35131; Q3E8J2; Q3E8J3; Q42308; Q43276; Q4TZ02; Q8LE19;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 166.
RecName: Full=Ubiquitin-conjugating enzyme E2 8;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme 8;
AltName: Full=UBCAT4A;
AltName: Full=Ubiquitin carrier protein 8;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 8;
AltName: Full=Ubiquitin-protein ligase 8;
Name=UBC8; Synonyms=UBC4A; OrderedLocusNames=At5g41700;
ORFNames=MBK23.24;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=8220461; DOI=10.1046/j.1365-313X.1993.03040545.x;
Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L.,
Vierstra R.D.;
"Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and
5 in yeast are encoded by a multigene family in Arabidopsis
thaliana.";
Plant J. 3:545-552(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
GENE FAMILY, AND NOMENCLATURE.
PubMed=16339806; DOI=10.1104/pp.105.067983;
Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
Callis J.;
"Genome analysis and functional characterization of the E2 and RING-
type E3 ligase ubiquitination enzymes of Arabidopsis.";
Plant Physiol. 139:1597-1611(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9330910; DOI=10.1093/dnares/4.3.215;
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
features of the 1.6 Mb regions covered by twenty physically assigned
P1 clones.";
DNA Res. 4:215-230(1997).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-74.
STRAIN=cv. Columbia;
PubMed=8580968; DOI=10.1046/j.1365-313X.1996.09010101.x;
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y.,
Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes:
analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-148.
STRAIN=cv. Columbia; TISSUE=Green siliques;
PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial
sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[9]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=8078482; DOI=10.1007/BF00583906;
Genschik P., Durr A., Fleck J.;
"Differential expression of several E2-type ubiquitin carrier protein
genes at different developmental stages in Arabidopsis thaliana and
Nicotiana sylvestris.";
Mol. Gen. Genet. 244:548-556(1994).
[10]
INTERACTION WITH CIP8.
PubMed=12028569; DOI=10.1046/j.1365-313X.2002.01298.x;
Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.;
"Biochemical evidence for ubiquitin ligase activity of the Arabidopsis
COP1 interacting protein 8 (CIP8).";
Plant J. 30:385-394(2002).
[11]
INTERACTION WITH CHIP.
PubMed=16640601; DOI=10.1111/j.1365-313X.2006.02730.x;
Luo J., Shen G., Yan J., He C., Zhang H.;
"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
subunits and alters plant response to abscisic acid treatment.";
Plant J. 46:649-657(2006).
[12]
INTERACTION WITH XERICO.
PubMed=16792696; DOI=10.1111/j.1365-313X.2006.02782.x;
Ko J.-H., Yang S.H., Han K.-H.;
"Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought
tolerance through increased abscisic acid biosynthesis.";
Plant J. 47:343-355(2006).
[13]
INTERACTION WITH NLA.
PubMed=17355433; DOI=10.1111/j.1365-313X.2007.03050.x;
Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J.;
"A mutation in NLA, which encodes a RING-type ubiquitin ligase,
disrupts the adaptability of Arabidopsis to nitrogen limitation.";
Plant J. 50:320-337(2007).
-!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes
its covalent attachment to other proteins. Mediates the selective
degradation of short-lived and abnormal proteins.
{ECO:0000269|PubMed:16339806}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with CIP8, CHIP, NLA and XERICO.
{ECO:0000269|PubMed:12028569, ECO:0000269|PubMed:16640601,
ECO:0000269|PubMed:16792696, ECO:0000269|PubMed:17355433}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P35131-1; Sequence=Displayed;
Name=2;
IsoId=P35131-2; Sequence=VSP_034925;
Note=Derived from EST data. No experimental confirmation
available.;
Name=3;
IsoId=P35131-3; Sequence=VSP_034926;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Highest expression in young stems, old leaves.
Lowest levels in floral buds, anthers and young leaves.
{ECO:0000269|PubMed:16339806}.
-!- DEVELOPMENTAL STAGE: Up-regulated during senescence, but not
during the G0 to S phase transition. {ECO:0000269|PubMed:8078482}.
-!- INDUCTION: Not induced by heat shock or wounding.
{ECO:0000269|PubMed:8078482}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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EMBL; Z14989; CAA78713.1; -; Genomic_DNA.
EMBL; DQ027022; AAY44848.1; -; mRNA.
EMBL; AB005233; BAB11476.1; -; Genomic_DNA.
EMBL; CP002688; AED94711.1; -; Genomic_DNA.
EMBL; CP002688; AED94712.1; -; Genomic_DNA.
EMBL; CP002688; AED94713.1; -; Genomic_DNA.
EMBL; CP002688; AED94714.1; -; Genomic_DNA.
EMBL; CP002688; AED94715.1; -; Genomic_DNA.
EMBL; AF325009; AAG40361.1; -; mRNA.
EMBL; AY063074; AAL34248.1; -; mRNA.
EMBL; AF370257; AAK44072.1; -; mRNA.
EMBL; AY054595; AAK96786.1; -; mRNA.
EMBL; AY057631; AAL15262.1; -; mRNA.
EMBL; AY072514; AAL66929.1; -; mRNA.
EMBL; AY085670; AAM62889.1; -; mRNA.
EMBL; Z37225; CAA85527.1; -; mRNA.
EMBL; Z17692; CAA79036.1; -; mRNA.
RefSeq; NP_001190447.1; NM_001203518.1. [P35131-1]
RefSeq; NP_568595.2; NM_123535.2. [P35131-2]
RefSeq; NP_851114.1; NM_180783.2. [P35131-1]
RefSeq; NP_851115.1; NM_180784.2. [P35131-1]
RefSeq; NP_851116.1; NM_180785.2. [P35131-3]
UniGene; At.23971; -.
UniGene; At.24180; -.
PDB; 4X57; X-ray; 2.80 A; A/C=1-148.
PDBsum; 4X57; -.
ProteinModelPortal; P35131; -.
SMR; P35131; -.
BioGrid; 19424; 17.
IntAct; P35131; 2.
STRING; 3702.AT5G41700.4; -.
PaxDb; P35131; -.
PRIDE; P35131; -.
EnsemblPlants; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
EnsemblPlants; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
EnsemblPlants; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
EnsemblPlants; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
EnsemblPlants; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
GeneID; 834173; -.
Gramene; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
Gramene; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
Gramene; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
Gramene; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
Gramene; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
KEGG; ath:AT5G41700; -.
Araport; AT5G41700; -.
TAIR; locus:2160462; AT5G41700.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
InParanoid; P35131; -.
OMA; PPTSCIF; -.
PhylomeDB; P35131; -.
BRENDA; 6.3.2.19; 399.
Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-ATH-5689896; Ovarian tumor domain proteases.
Reactome; R-ATH-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-ATH-9033241; Peroxisomal protein import.
Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:P35131; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P35131; baseline and differential.
Genevisible; P35131; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
GO; GO:0009960; P:endosperm development; IEP:TAIR.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Nucleotide-binding; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 148 Ubiquitin-conjugating enzyme E2 8.
/FTId=PRO_0000082576.
ACT_SITE 85 85 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
VAR_SEQ 21 22 CS -> CIF (in isoform 2). {ECO:0000305}.
/FTId=VSP_034925.
VAR_SEQ 103 148 LLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYEATARNWTQ
KYAMG -> TLIFQKHRFSNVRLCSKSIARASTFSARILLN
AQALLLECLCM (in isoform 3).
{ECO:0000305}.
/FTId=VSP_034926.
CONFLICT 72 72 K -> M (in Ref. 5; AAL34248).
{ECO:0000305}.
CONFLICT 80 80 S -> D (in Ref. 5; AAK44072/AAL66929/
AAL15262/AAK96786/AAG40361).
{ECO:0000305}.
CONFLICT 98 98 T -> P (in Ref. 5; AAK44072/AAL66929/
AAL15262/AAK96786/AAG40361).
{ECO:0000305}.
CONFLICT 135 135 E -> K (in Ref. 6; AAM62889).
{ECO:0000305}.
HELIX 1 15 {ECO:0000244|PDB:4X57}.
STRAND 21 28 {ECO:0000244|PDB:4X57}.
STRAND 32 38 {ECO:0000244|PDB:4X57}.
TURN 44 47 {ECO:0000244|PDB:4X57}.
STRAND 49 55 {ECO:0000244|PDB:4X57}.
TURN 58 61 {ECO:0000244|PDB:4X57}.
STRAND 66 69 {ECO:0000244|PDB:4X57}.
HELIX 87 89 {ECO:0000244|PDB:4X57}.
TURN 90 92 {ECO:0000244|PDB:4X57}.
HELIX 99 111 {ECO:0000244|PDB:4X57}.
HELIX 121 129 {ECO:0000244|PDB:4X57}.
HELIX 131 145 {ECO:0000244|PDB:4X57}.
SEQUENCE 148 AA; 16533 MW; 27CAAEABBBE74972 CRC64;
MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY
PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
PEIAHMYKTD RAKYEATARN WTQKYAMG


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