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Protein

Ubiquitin-activating enzyme E1 1

Gene

UBA1

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

Functioni

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei656 – 6561Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi502 – 53130ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. small protein activating enzyme activity Source: InterPro
  3. ubiquitin-protein transferase activity Source: TAIR

GO - Biological processi

  1. modification-dependent protein catabolic process Source: GO_Central
  2. protein ubiquitination Source: TAIR
  3. response to cadmium ion Source: TAIR
  4. response to other organism 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

BRENDAi6.2.1.B9. 399.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1 1
Short name:
AtUBA1
Alternative name(s):
Protein MODIFIER OF SNC1 5
Gene namesi
Name:UBA1
Synonyms:MOS5
Ordered Locus Names:At2g30110
ORF Names:T27E13.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G30110.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. nucleus Source: GO_Central
  3. plasma membrane Source: TAIR
  4. plasmodesma Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1032 – 10376RMDKKV → S in mos5; enhanced disease susceptibility. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10801080Ubiquitin-activating enzyme E1 1PRO_0000399395Add
BLAST

Proteomic databases

PaxDbiP93028.
PRIDEiP93028.

Expressioni

Tissue specificityi

Expressed in leaves, flowers, roots and stems. Detected in germinating seeds, cotyledons, hypocotyls, vascular tissues, anthers, filaments, pollen, style, stigma, sepals, petals, ovary, developing ovules, funiculi and silique walls.1 Publication

Developmental stagei

Expressed over the entire range of development.1 Publication

Gene expression databases

ExpressionAtlasiP93028. baseline and differential.
GenevestigatoriP93028.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi2911. 2 interactions.
IntActiP93028. 1 interaction.
STRINGi3702.AT2G30110.1-P.

Structurei

3D structure databases

ProteinModelPortaliP93028.
SMRiP93028. Positions 73-1077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000167329.
InParanoidiP93028.
KOiK03178.
OMAiSDISMER.
PhylomeDBiP93028.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P93028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHKRASEAN DKNDNTIIGS DLASSKKRRI DFTESSSDKS SSILASGSSR
60 70 80 90 100
GFHGDSVVQQ IDMAFGNSNR QEIDEDLHSR QLAVYGRETM RRLFASNVLI
110 120 130 140 150
SGMHGLGAEI AKNLILAGVK SVTLHDERVV ELWDLSSNFV FSEDDVGKNR
160 170 180 190 200
ADASVQKLQD LNNAVVVSSL TKSLNKEDLS GFQVVVFSDI SMERAIEFDD
210 220 230 240 250
YCHSHQPPIA FVKADVRGLF GSVFCDFGPE FAVLDVDGEE PHTGIIASIS
260 270 280 290 300
NENQAFISCV DDERLEFEDG DLVVFSEVEG MTELNDGKPR KIKSTRPYSF
310 320 330 340 350
TLDEDTTNYG TYVKGGIVTQ VKQPKLLNFK PLREALKDPG DFLFSDFSKF
360 370 380 390 400
DRPPLLHLAF QALDHFKAEA GRFPVAGSEE DAQKLISIAT AINTGQGDLK
410 420 430 440 450
VENVDQKLLR HFSFGAKAVL NPMAAMFGGI VGQEVVKACS GKFHPLFQFF
460 470 480 490 500
YFDSVESLPS EPVDSSDFAP RNSRYDAQIS VFGAKFQKKL EDAKVFTVGS
510 520 530 540 550
GALGCEFLKN LALMGVSCGS QGKLTVTDDD IIEKSNLSRQ FLFRDWNIGQ
560 570 580 590 600
AKSTVAASAA AVINPRFNIE ALQNRVGAET ENVFDDAFWE NLTVVVNALD
610 620 630 640 650
NVNARLYVDS RCLYFQKPLL ESGTLGTKCN TQSVIPHLTE NYGASRDPPE
660 670 680 690 700
KQAPMCTVHS FPHNIDHCLT WARSEFEGLL EKTPAEVNAY LSSPVEYTNS
710 720 730 740 750
MMSAGDAQAR DTLERIVECL EKEKCETFQD CLTWARLRFE DYFVNRVKQL
760 770 780 790 800
IYTFPEDAAT STGAPFWSAP KRFPRPLQYS SSDPSLLNFI TATAILRAET
810 820 830 840 850
FGIPIPEWTK NPKEAAEAVD RVIVPDFEPR QDAKIVTDEK ATTLTTASVD
860 870 880 890 900
DAAVIDDLIA KIDQCRHNLS PDFRMKPIQF EKDDDTNYHM DVIAGLANMR
910 920 930 940 950
ARNYSIPEVD KLKAKFIAGR IIPAIATSTA MATGLVCLEL YKVLDGGHKV
960 970 980 990 1000
EAYRNTFANL ALPLFSMAEP LPPKVVKHRD MAWTVWDRWV LKGNPTLREV
1010 1020 1030 1040 1050
LQWLEDKGLS AYSISCGSCL LFNSMFTRHK ERMDKKVVDL ARDVAKVELP
1060 1070 1080
PYRNHLDVVV ACEDEDDNDV DIPLVSIYFR
Length:1,080
Mass (Da):120,251
Last modified:May 1, 1997 - v1
Checksum:i4B442A35DAFD34D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti883 – 8831D → G in AAP21171 (PubMed:14593172).Curated
Sequence conflicti883 – 8831D → G in AAL90910 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80808 Genomic DNA. Translation: AAB39246.1.
AC004165 Genomic DNA. Translation: AAC16961.1.
CP002685 Genomic DNA. Translation: AEC08346.1.
AY090248 mRNA. Translation: AAL90910.1.
BT006363 mRNA. Translation: AAP21171.1.
PIRiT00587.
RefSeqiNP_565693.1. NM_128566.3.
UniGeneiAt.21347.

Genome annotation databases

EnsemblPlantsiAT2G30110.1; AT2G30110.1; AT2G30110.
GeneIDi817562.
KEGGiath:AT2G30110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80808 Genomic DNA. Translation: AAB39246.1.
AC004165 Genomic DNA. Translation: AAC16961.1.
CP002685 Genomic DNA. Translation: AEC08346.1.
AY090248 mRNA. Translation: AAL90910.1.
BT006363 mRNA. Translation: AAP21171.1.
PIRiT00587.
RefSeqiNP_565693.1. NM_128566.3.
UniGeneiAt.21347.

3D structure databases

ProteinModelPortaliP93028.
SMRiP93028. Positions 73-1077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2911. 2 interactions.
IntActiP93028. 1 interaction.
STRINGi3702.AT2G30110.1-P.

Proteomic databases

PaxDbiP93028.
PRIDEiP93028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G30110.1; AT2G30110.1; AT2G30110.
GeneIDi817562.
KEGGiath:AT2G30110.

Organism-specific databases

TAIRiAT2G30110.

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000167329.
InParanoidiP93028.
KOiK03178.
OMAiSDISMER.
PhylomeDBiP93028.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.2.1.B9. 399.

Gene expression databases

ExpressionAtlasiP93028. baseline and differential.
GenevestigatoriP93028.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana."
    Hatfield P.M., Gosink M.M., Carpenter T.B., Vierstra R.D.
    Plant J. 11:213-226(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. Columbia.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The ubiquitin pathway is required for innate immunity in Arabidopsis."
    Goritschnig S., Zhang Y., Li X.
    Plant J. 49:540-551(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 1032-ARG--VAL-1037.

Entry informationi

Entry nameiUBE11_ARATH
AccessioniPrimary (citable) accession number: P93028
Secondary accession number(s): Q8RX82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 1997
Last modified: April 1, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Both UBA1 and UBA2 are able to activate ubiquitin and transfer it to the E2s with equal efficiency.
Mutation in UBA1 (mos5) suppresses snc1-mediated constitutive resistance and affects the resistance responses conferred by only a subset of R-proteins.

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.