P35131 (UBC8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 8
EC=6.3.2.19

Alternative name(s):
UBCAT4A
Ubiquitin carrier protein 8
Ubiquitin-conjugating enzyme E2-17 kDa 8
Ubiquitin-protein ligase 8

Gene names

Name:	UBC8
Synonyms:	UBC4A
Ordered Locus Names:	At5g41700
ORF Names:	MBK23.24

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with CIP8, CHIP, NLA and XERICO. Ref.10 Ref.11 Ref.12 Ref.13
Tissue specificity	Highest expression in young stems, old leaves. Lowest levels in floral buds, anthers and young leaves. Ref.2
Developmental stage	Up-regulated during senescence, but not during the G0 to S phase transition. Ref.9
Induction	Not induced by heat shock or wounding. Ref.9
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endosperm development Inferred from expression pattern PubMed 21914649. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.2. Source: TAIR
Cellular_component	cytoplasm Inferred from direct assay Ref.13. Source: TAIR nucleus Inferred from direct assay Ref.13. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.2Ref.1. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35131-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P35131-2)

The sequence of this isoform differs from the canonical sequence as follows:
     21-22: CS → CIF

Note: Derived from EST data. No experimental confirmation available.

Isoform 3 (identifier: P35131-3)

The sequence of this isoform differs from the canonical sequence as follows:
     103-148: LLSICSLLTD...RNWTQKYAMG → TLIFQKHRFS...QALLLECLCM

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 148	148	Ubiquitin-conjugating enzyme E2 8		PRO_0000082576
Sites
	Active site	85	1	Glycyl thioester intermediate By similarity
Natural variations
	Alternative sequence	21 – 22	2	CS → CIF in isoform 2.		VSP_034925
	Alternative sequence	103 – 148	46	LLSIC…KYAMG → TLIFQKHRFSNVRLCSKSIA RASTFSARILLNAQALLLEC LCM in isoform 3.		VSP_034926
Experimental info
	Sequence conflict	72	1	K → M in AAL34248. Ref.5
	Sequence conflict	80	1	S → D in AAK44072. Ref.5
	Sequence conflict	80	1	S → D in AAL66929. Ref.5
	Sequence conflict	80	1	S → D in AAL15262. Ref.5
	Sequence conflict	80	1	S → D in AAK96786. Ref.5
	Sequence conflict	80	1	S → D in AAG40361. Ref.5
	Sequence conflict	98	1	T → P in AAK44072. Ref.5
	Sequence conflict	98	1	T → P in AAL66929. Ref.5
	Sequence conflict	98	1	T → P in AAL15262. Ref.5
	Sequence conflict	98	1	T → P in AAK96786. Ref.5
	Sequence conflict	98	1	T → P in AAG40361. Ref.5
	Sequence conflict	135	1	E → K in AAM62889. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 27CAAEABBBE74972	FASTA	148	16,533
	10 20 30 40 50 60 MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY 70 80 90 100 110 120 PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV 130 140 PEIAHMYKTD RAKYEATARN WTQKYAMG
	Isoform 2 [UniParc]. Checksum: 11D4DF7CB733D0B8	FASTA	149	16,706
	10 20 30 40 50 60 MASKRILKEL KDLQKDPPTS CIFAGPVAED MFHWQATIMG PAESPYSGGV FLVTIHFPPD 70 80 90 100 110 120 YPFKPPKVAF RTKVFHPNIN SNGSICLDIL KEQWSPALTI SKVLLSICSL LTDPNPDDPL 130 140 VPEIAHMYKT DRAKYEATAR NWTQKYAMG
	Isoform 3 [UniParc]. Checksum: 4727400F23743DDD	FASTA	145	16,163
	10 20 30 40 50 60 MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY 70 80 90 100 110 120 PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVTLIFQKHR FSNVRLCSKS 130 140 IARASTFSAR ILLNAQALLL ECLCM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana." Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D. Plant J. 3:545-552(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis." Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W., Callis J. Plant Physiol. 139:1597-1611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs." 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. Plant J. 9:101-124(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-74. Strain: cv. Columbia.
[8]	"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana." 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. Plant J. 4:1051-1061(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-148. Strain: cv. Columbia. Tissue: Green siliques.
[9]	"Differential expression of several E2-type ubiquitin carrier protein genes at different developmental stages in Arabidopsis thaliana and Nicotiana sylvestris." Genschik P., Durr A., Fleck J. Mol. Gen. Genet. 244:548-556(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, INDUCTION.
[10]	"Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8)." Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W. Plant J. 30:385-394(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CIP8.
[11]	"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment." Luo J., Shen G., Yan J., He C., Zhang H. Plant J. 46:649-657(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHIP.
[12]	"Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought tolerance through increased abscisic acid biosynthesis." Ko J.-H., Yang S.H., Han K.-H. Plant J. 47:343-355(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XERICO.
[13]	"A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts the adaptability of Arabidopsis to nitrogen limitation." Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J. Plant J. 50:320-337(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLA.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z14989 Genomic DNA. Translation: CAA78713.1. DQ027022 mRNA. Translation: AAY44848.1. AB005233 Genomic DNA. Translation: BAB11476.1. CP002688 Genomic DNA. Translation: AED94711.1. CP002688 Genomic DNA. Translation: AED94712.1. CP002688 Genomic DNA. Translation: AED94713.1. CP002688 Genomic DNA. Translation: AED94714.1. CP002688 Genomic DNA. Translation: AED94715.1. AF325009 mRNA. Translation: AAG40361.1. AY063074 mRNA. Translation: AAL34248.1. AF370257 mRNA. Translation: AAK44072.1. AY054595 mRNA. Translation: AAK96786.1. AY057631 mRNA. Translation: AAL15262.1. AY072514 mRNA. Translation: AAL66929.1. AY085670 mRNA. Translation: AAM62889.1. Z37225 mRNA. Translation: CAA85527.1. Z17692 mRNA. Translation: CAA79036.1.
IPI	IPI00526510. IPI00536307. IPI00537689.
RefSeq	NP_001190447.1. NM_001203518.1. NP_568595.2. NM_123535.2. NP_851114.1. NM_180783.1. NP_851115.1. NM_180784.1. NP_851116.1. NM_180785.2.
UniGene	At.23971. At.24180.
3D structure databases
ProteinModelPortal	P35131.
SMR	P35131. Positions 1-147.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35131. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G41700.1; AT5G41700.1; AT5G41700. AT5G41700.2; AT5G41700.2; AT5G41700. AT5G41700.5; AT5G41700.5; AT5G41700.
GeneID	834173.
KEGG	ath:AT5G41700.
Organism-specific databases
TAIR	At5g41700.
Phylogenomic databases
InParanoid	P35131.
KO	K06689.
OMA	IARASTF.
PhylomeDB	P35131.
ProtClustDB	CLSN2680399.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	P35131.
Genevestigator	P35131.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC8_ARATH

Accession

Primary (citable) accession number: P35131
Secondary accession number(s): Q3E8J2 , Q3E8J3, Q42308, Q43276, Q4TZ02, Q8LE19

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program