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Protein

Probable ubiquitin-conjugating enzyme E2 25

Gene

UBC25

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.By similarity

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei418 – 4181Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G15355-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ubiquitin-conjugating enzyme E2 25 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 25
Gene namesi
Name:UBC25
Ordered Locus Names:At3g15355
ORF Names:MJK13.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G15355.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 609609Probable ubiquitin-conjugating enzyme E2 25PRO_0000345190Add
BLAST

Proteomic databases

PaxDbiQ9LUQ5.
PRIDEiQ9LUQ5.

Expressioni

Tissue specificityi

Expressed in seeds, pistils, siliques, hypocotyls and leaves.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G15355.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LUQ5.
SMRiQ9LUQ5. Positions 303-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 5826Poly-Glu

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000237682.
InParanoidiQ9LUQ5.
KOiK10581.
OMAiFKRFDIV.
PhylomeDBiQ9LUQ5.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LUQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPNVVEIAT PPAASCSRIR TPTKAETPEV IDVEEYDLQN GGVPNGNNVD
60 70 80 90 100
YKNKGKAIDF DSMSYGDYGE EDEYAVGSPG DDYGYPESSP LSNSLLDPES
110 120 130 140 150
LIYEDDENYS EQYDFEMEAE PDNYSMYQDL FDGKDIPTGV EVSMDWFPNS
160 170 180 190 200
ADKESASSSK SSHANNGNNS SKKATKASGI HSQFSSDMET PVAQPWNALP
210 220 230 240 250
HKAEGVIPNS AYALPQNSKA FQPPYAVHYS ALKTAFSNYL QPQTPDTVLG
260 270 280 290 300
EAPAPAAGSS GLLPPNTPGF KSNAARFKEE PPILPPDDSR VKRNMEDYLG
310 320 330 340 350
LYLFFKRFDI VEDFSDHHYA SKGTTSKQHS KDWAKRIQDE WRILEKDLPE
360 370 380 390 400
MIFVRAYESR MDLLRAVIIG AQGTPYHDGL FFFDIFFPDT YPSTPPIVHY
410 420 430 440 450
HSGGLRINPN LYNCGKVCLS LLGTWSGNQR EKWIPNTSTM LQVLVSIQGL
460 470 480 490 500
ILNQKPYFNE PGYERSAGSA HGESTSKAYS ENTFILSLKT MVYTMRRPPK
510 520 530 540 550
YFEDFAYGHF FSCAHDVLKA CNAYRNGATP GYLVKGAPDV EENSAGMSSL
560 570 580 590 600
KFRTDVATFV ETVLLKEFIL LGVLGLEPEE EEKTPETIIV AESSKCTRSR

SKRDRVSSS
Length:609
Mass (Da):67,769
Last modified:October 1, 2000 - v1
Checksum:i94A2C2E839DED309
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022218, AP000413 Genomic DNA. Translation: BAB02364.1.
AC024081 Genomic DNA. Translation: AAF35401.1.
CP002686 Genomic DNA. Translation: AEE75657.1.
AF361806 mRNA. Translation: AAK32819.1.
AY059155 mRNA. Translation: AAL15380.1.
DQ027038 mRNA. Translation: AAY44864.1.
RefSeqiNP_188154.1. NM_112402.2.
UniGeneiAt.27040.
At.67741.

Genome annotation databases

EnsemblPlantsiAT3G15355.1; AT3G15355.1; AT3G15355.
GeneIDi820772.
KEGGiath:AT3G15355.

Cross-referencesi

Web resourcesi

PlantsUBQ

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022218, AP000413 Genomic DNA. Translation: BAB02364.1.
AC024081 Genomic DNA. Translation: AAF35401.1.
CP002686 Genomic DNA. Translation: AEE75657.1.
AF361806 mRNA. Translation: AAK32819.1.
AY059155 mRNA. Translation: AAL15380.1.
DQ027038 mRNA. Translation: AAY44864.1.
RefSeqiNP_188154.1. NM_112402.2.
UniGeneiAt.27040.
At.67741.

3D structure databases

ProteinModelPortaliQ9LUQ5.
SMRiQ9LUQ5. Positions 303-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G15355.1.

Proteomic databases

PaxDbiQ9LUQ5.
PRIDEiQ9LUQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G15355.1; AT3G15355.1; AT3G15355.
GeneIDi820772.
KEGGiath:AT3G15355.

Organism-specific databases

TAIRiAT3G15355.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000237682.
InParanoidiQ9LUQ5.
KOiK10581.
OMAiFKRFDIV.
PhylomeDBiQ9LUQ5.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciARA:AT3G15355-MONOMER.

Miscellaneous databases

PROiQ9LUQ5.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
    DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [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. "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] OF 351-609, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiUBC25_ARATH
AccessioniPrimary (citable) accession number: Q9LUQ5
Secondary accession number(s): Q4TYY6, Q9M7X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.