P25865 (UBC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 1
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein 1
Ubiquitin-conjugating enzyme E2-17 kDa 1
Ubiquitin-protein ligase 1

Gene names

Name:	UBC1
Ordered Locus Names:	At1g14400
ORF Names:	F14L17.17, F14L17_35

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	152 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. Ref.3 Ref.10
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Tissue specificity	Ubiquitously expressed. Ref.3 Ref.11
Induction	Not induced by heat shock. Ref.11
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H2B ubiquitination Inferred from genetic interaction PubMed 18849490. Source: TAIR leaf morphogenesis Inferred from genetic interaction PubMed 18798874. Source: TAIR negative regulation of flower development Inferred from genetic interaction PubMed 18798874. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.3. Source: TAIR vegetative to reproductive phase transition of meristem Inferred from genetic interaction PubMed 18849490. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.3. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 152

152

Ubiquitin-conjugating enzyme E2 1

PRO_0000082570

Sites

Active site

88

1

Glycyl thioester intermediate

Experimental info

Mutagenesis

88

1

C → S: Stabilization of the ester bond with the ubiquitin. Ref.10

Secondary structure

1

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152

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

24 – 29

6

Beta strand

32 – 41

10

Turn

47 – 50

4

Beta strand

52 – 58

7

Turn

61 – 65

5

Beta strand

69 – 74

6

Beta strand

85 – 87

3

Helix

90 – 92

3

Helix

102 – 113

12

Helix

124 – 132

9

Helix

134 – 148

15

Sequences

	Sequence		Length	Mass (Da)
	P25865 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 896D911930C39045	FASTA	152	17,281
	10 20 30 40 50 60 MSTPARKRLM RDFKRLQQDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG GTFKLSLQFS 70 80 90 100 110 120 EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAILTSIQ SLLCDPNPNS 130 140 150 PANSEAARMY SESKREYNRR VRDVVEQSWT AD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a 16-kDa ubiquitin carrier protein from wheat and Arabidopsis thaliana. Identification of functional domains by in vitro mutagenesis." Sullivan M.L., Vierstra R.D. J. Biol. Chem. 266:23878-23885(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are encoded by small multigene families in Arabidopsis thaliana." Sullivan M.L., Carpenter T.B., Vierstra R.D. Plant Mol. Biol. 24:651-661(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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], FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[4]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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.
[7]	"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].
[8]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[9]	"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 1-98. Strain: cv. Columbia. Tissue: Dry seed.
[10]	"Formation of a stable adduct between ubiquitin and the Arabidopsis ubiquitin-conjugating enzyme, AtUBC1+." Sullivan M.L., Vierstra R.D. J. Biol. Chem. 268:8777-8780(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-88.
[11]	"Members of two gene families encoding ubiquitin-conjugating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially expressed." Thoma S., Sullivan M.L., Vierstra R.D. Plant Mol. Biol. 31:493-505(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[12]	"Three-dimensional structure of a ubiquitin-conjugating enzyme (E2)." Cook W.J., Jeffrey L.C., Sullivan M.L., Vierstra R.D. J. Biol. Chem. 267:15116-15121(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	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

M62721 mRNA. Translation: AAA32903.1.
L19351 Genomic DNA. Translation: AAA32897.1.
DQ027016 mRNA. Translation: AAY44842.1.
AC012188 Genomic DNA. Translation: AAF43940.1.
CP002684 Genomic DNA. Translation: AEE29158.1.
CP002684 Genomic DNA. Translation: AEE29159.1.
AF332451 mRNA. Translation: AAG48814.1.
AY070074 mRNA. Translation: AAL49769.1.
AY091330 mRNA. Translation: AAM14269.1.
AY085783 mRNA. Translation: AAM63000.1.
AK226391 mRNA. Translation: BAE98537.1.
Z27262 mRNA. Translation: CAA81773.1.

IPI

IPI00524846.

PIR

S43781.

RefSeq

NP_563951.1. NM_101307.4.
NP_973825.1. NM_202096.2.

UniGene

At.331.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AAK	X-ray	2.40	A	1-152	[»]

ProteinModelPortal

P25865.

SMR

P25865. Positions 1-150.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25865. 2 interactions.

STRING

3702.AT1G14400.1-P.

Proteomic databases

PaxDb

P25865.

PRIDE

P25865.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT1G14400.1; AT1G14400.1; AT1G14400.
AT1G14400.2; AT1G14400.2; AT1G14400.

GeneID

838002.

KEGG

ath:AT1G14400.

Organism-specific databases

GeneFarm

4743. 464.

TAIR

At1g14400.

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233454.

InParanoid

P25865.

KO

K10573.

OMA

YANGELC.

PhylomeDB

P25865.

ProtClustDB

CLSN2687804.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

Genevestigator

P25865.

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...

Other

EvolutionaryTrace

P25865.

Entry information

Entry name

UBC1_ARATH

Accession

Primary (citable) accession number: P25865
Secondary accession number(s): Q4TZ08

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program