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P93028 (UBE11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-activating enzyme E1 1

Short name=AtUBA1
Alternative name(s):
Protein MODIFIER OF SNC1 5
Gene names
Name:UBA1
Synonyms:MOS5
Ordered Locus Names:At2g30110
ORF Names:T27E13.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1080 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer By similarity.

Tissue specificity

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. Ref.1

Developmental stage

Expressed over the entire range of development. Ref.1

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.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10801080Ubiquitin-activating enzyme E1 1
PRO_0000399395

Regions

Nucleotide binding502 – 53130ATP By similarity

Sites

Active site6561Glycyl thioester intermediate By similarity

Experimental info

Mutagenesis1032 – 10376RMDKKV → S in mos5; enhanced disease susceptibility. Ref.5
Sequence conflict8831D → G in AAP21171. Ref.4
Sequence conflict8831D → G in AAL90910. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P93028 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4B442A35DAFD34D0

FASTA1,080120,251
        10         20         30         40         50         60 
MLHKRASEAN DKNDNTIIGS DLASSKKRRI DFTESSSDKS SSILASGSSR GFHGDSVVQQ 

        70         80         90        100        110        120 
IDMAFGNSNR QEIDEDLHSR QLAVYGRETM RRLFASNVLI SGMHGLGAEI AKNLILAGVK 

       130        140        150        160        170        180 
SVTLHDERVV ELWDLSSNFV FSEDDVGKNR ADASVQKLQD LNNAVVVSSL TKSLNKEDLS 

       190        200        210        220        230        240 
GFQVVVFSDI SMERAIEFDD YCHSHQPPIA FVKADVRGLF GSVFCDFGPE FAVLDVDGEE 

       250        260        270        280        290        300 
PHTGIIASIS NENQAFISCV DDERLEFEDG DLVVFSEVEG MTELNDGKPR KIKSTRPYSF 

       310        320        330        340        350        360 
TLDEDTTNYG TYVKGGIVTQ VKQPKLLNFK PLREALKDPG DFLFSDFSKF DRPPLLHLAF 

       370        380        390        400        410        420 
QALDHFKAEA GRFPVAGSEE DAQKLISIAT AINTGQGDLK VENVDQKLLR HFSFGAKAVL 

       430        440        450        460        470        480 
NPMAAMFGGI VGQEVVKACS GKFHPLFQFF YFDSVESLPS EPVDSSDFAP RNSRYDAQIS 

       490        500        510        520        530        540 
VFGAKFQKKL EDAKVFTVGS GALGCEFLKN LALMGVSCGS QGKLTVTDDD IIEKSNLSRQ 

       550        560        570        580        590        600 
FLFRDWNIGQ AKSTVAASAA AVINPRFNIE ALQNRVGAET ENVFDDAFWE NLTVVVNALD 

       610        620        630        640        650        660 
NVNARLYVDS RCLYFQKPLL ESGTLGTKCN TQSVIPHLTE NYGASRDPPE KQAPMCTVHS 

       670        680        690        700        710        720 
FPHNIDHCLT WARSEFEGLL EKTPAEVNAY LSSPVEYTNS MMSAGDAQAR DTLERIVECL 

       730        740        750        760        770        780 
EKEKCETFQD CLTWARLRFE DYFVNRVKQL IYTFPEDAAT STGAPFWSAP KRFPRPLQYS 

       790        800        810        820        830        840 
SSDPSLLNFI TATAILRAET FGIPIPEWTK NPKEAAEAVD RVIVPDFEPR QDAKIVTDEK 

       850        860        870        880        890        900 
ATTLTTASVD DAAVIDDLIA KIDQCRHNLS PDFRMKPIQF EKDDDTNYHM DVIAGLANMR 

       910        920        930        940        950        960 
ARNYSIPEVD KLKAKFIAGR IIPAIATSTA MATGLVCLEL YKVLDGGHKV EAYRNTFANL 

       970        980        990       1000       1010       1020 
ALPLFSMAEP LPPKVVKHRD MAWTVWDRWV LKGNPTLREV LQWLEDKGLS AYSISCGSCL 

      1030       1040       1050       1060       1070       1080 
LFNSMFTRHK ERMDKKVVDL ARDVAKVELP PYRNHLDVVV ACEDEDDNDV DIPLVSIYFR 

« Hide

References

« Hide 'large scale' references
[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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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. expand/collapse author list , 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]"The ubiquitin pathway is required for innate immunity in Arabidopsis."
Goritschnig S., Zhang Y., Li X.
Plant J. 49:540-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 1032-ARG--VAL-1037.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00587.
RefSeqNP_565693.1. NM_128566.3.
UniGeneAt.21347.

3D structure databases

ProteinModelPortalP93028.
SMRP93028. Positions 73-1077.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2911. 2 interactions.
IntActP93028. 1 interaction.
STRING3702.AT2G30110.1-P.

Proteomic databases

PaxDbP93028.
PRIDEP93028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G30110.1; AT2G30110.1; AT2G30110.
GeneID817562.
KEGGath:AT2G30110.

Organism-specific databases

TAIRAT2G30110.

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000167329.
InParanoidP93028.
KOK03178.
OMASYQATGD.
PhylomeDBP93028.
ProtClustDBCLSN2688565.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressP93028.
GenevestigatorP93028.

Family and domain databases

Gene3D1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProIPR009036. 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]
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBE11_ARATH
AccessionPrimary (citable) accession number: P93028
Secondary accession number(s): Q8RX82
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names