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Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

ECR1

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

Functioni

Catalytic subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1 (By similarity).By similarity2 Publications

Pathwayi: protein neddylation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei215 – 2151Glycyl thioester intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 8025ATPBy similarityAdd
BLAST

GO - Molecular functioni

  • acid-amino acid ligase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • NEDD8 activating enzyme activity Source: TAIR
  • protein heterodimerization activity Source: TAIR

GO - Biological processi

  • protein neddylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-activating enzyme E1 catalytic subunit (EC:6.3.2.-)
Alternative name(s):
RUB-activating enzyme
Ubiquitin-activating enzyme E1-like protein
Gene namesi
Name:ECR1
Ordered Locus Names:At5g19180
ORF Names:T24G5_80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G19180.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151C → A: Loss of binding to RUB1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 454453NEDD8-activating enzyme E1 catalytic subunitPRO_0000194948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO65041.
PRIDEiO65041.

Expressioni

Tissue specificityi

Expressed in shoot, root and floral meristems, in vascular tissues of cotyledons and mature leaves, and in the stele of the root.1 Publication

Developmental stagei

Expressed during ovules and embryo development.1 Publication

Inductioni

No accumulation in response to auxin treatment.

Gene expression databases

GenevisibleiO65041. AT.

Interactioni

Subunit structurei

Heterodimer of UBA3/ECR1 and AXR1. Interacts with NEDD8 and RCE1.1 Publication

GO - Molecular functioni

  • protein heterodimerization activity Source: TAIR

Protein-protein interaction databases

STRINGi3702.AT5G19180.1.

Structurei

3D structure databases

ProteinModelPortaliO65041.
SMRiO65041. Positions 18-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000166793.
InParanoidiO65041.
KOiK10686.
OMAiQFNLVIC.
PhylomeDBiO65041.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O65041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLDVPPQV PQSKTRDLDK LLLRHGNLVD PGFVPGPGLR DDIRDYVRIL
60 70 80 90 100
VIGAGGLGCE LLKDLALSGF RNLEVIDMDR IEVTNLNRQF LFRIEDVGKP
110 120 130 140 150
KAEVAAKRVM ERVSGVEIVP HFSRIEDKEI EFYNDFNIIA LGLDSIEARK
160 170 180 190 200
YINGVACGFL EYNEDDTPKR ETIKPMVDGG TEGFKGHARV ILPGVTPCFE
210 220 230 240 250
CTIYLFPPQV KFPLCTLAET PRNAAHCIEY AHLIQWETVH RGKTFDPDEP
260 270 280 290 300
EHMKWVYDEA IRRAELFGIP GVTYSLTQGV VKNIIPAIAS TNAIISAACA
310 320 330 340 350
LETLKIVSAC SKTLVNYLTY NGGEGLYTEV TKFERDTECL VCGPGILIEL
360 370 380 390 400
DTSVTLSKFI EMLEDHPKLL LSKASVKQGE NTLYMQAPPV LEEFHRPKLS
410 420 430 440 450
KPLYDLMGRV QKDTIHVFGQ RALKNNEKES CTTKVRVVFK GADGVADMDT

AIGA
Length:454
Mass (Da):50,541
Last modified:June 12, 2007 - v2
Checksum:i5B725F292DB3576A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891R → K in AAC27035 (PubMed:9624055).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051135 mRNA. Translation: AAC27035.1.
AC069326 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92667.1.
AY050426 mRNA. Translation: AAK91442.1.
AY120692 mRNA. Translation: AAM52235.1.
AK226388 mRNA. Translation: BAE98534.1.
PIRiT52253.
RefSeqiNP_568370.1. NM_121923.3.
UniGeneiAt.21297.

Genome annotation databases

EnsemblPlantsiAT5G19180.1; AT5G19180.1; AT5G19180.
GeneIDi832038.
GrameneiAT5G19180.1; AT5G19180.1; AT5G19180.
KEGGiath:AT5G19180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051135 mRNA. Translation: AAC27035.1.
AC069326 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92667.1.
AY050426 mRNA. Translation: AAK91442.1.
AY120692 mRNA. Translation: AAM52235.1.
AK226388 mRNA. Translation: BAE98534.1.
PIRiT52253.
RefSeqiNP_568370.1. NM_121923.3.
UniGeneiAt.21297.

3D structure databases

ProteinModelPortaliO65041.
SMRiO65041. Positions 18-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G19180.1.

Proteomic databases

PaxDbiO65041.
PRIDEiO65041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G19180.1; AT5G19180.1; AT5G19180.
GeneIDi832038.
GrameneiAT5G19180.1; AT5G19180.1; AT5G19180.
KEGGiath:AT5G19180.

Organism-specific databases

TAIRiAT5G19180.

Phylogenomic databases

eggNOGiKOG2015. Eukaryota.
COG0476. LUCA.
HOGENOMiHOG000166793.
InParanoidiO65041.
KOiK10686.
OMAiQFNLVIC.
PhylomeDBiO65041.

Enzyme and pathway databases

UniPathwayiUPA00885.

Miscellaneous databases

PROiO65041.

Gene expression databases

GenevisibleiO65041. AT.

Family and domain databases

Gene3Di1.10.10.520. 1 hit.
3.10.20.260. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR014929. E2_binding.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023318. Ub_act_enz_dom_a.
IPR030468. Uba3.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PANTHERiPTHR10953:SF6. PTHR10953:SF6. 1 hit.
PfamiPF08825. E2_bind. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]
SMARTiSM01181. E2_bind. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ubiquitin-related protein RUB1 and auxin response in Arabidopsis."
    del Pozo J.C., Timpte C., Tan S., Callis J., Estelle M.
    Science 280:1760-1763(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AXR1 AND RUB1, MUTAGENESIS OF CYS-215, FUNCTION.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
  6. "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1."
    del Pozo J.C., Estelle M.
    Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "AXR1-ECR1-dependent conjugation of RUB1 to the Arabidopsis Cullin AtCUL1 is required for auxin response."
    del Pozo J.C., Dharmasiri S., Hellmann H., Walker L., Gray W.M., Estelle M.
    Plant Cell 14:421-433(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBA3_ARATH
AccessioniPrimary (citable) accession number: O65041
Secondary accession number(s): Q0WWG4, Q94A29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 12, 2007
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The formation of the adenylate intermediate is possible in absence of AXR1 and without the participation of Cys-215.

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

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 one 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.