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Q1EC66 (UBQ3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Polyubiquitin 3

Cleaved into the following chain:

  1. Ubiquitin
Gene names
Name:UBQ3
Ordered Locus Names:At5g03240
ORF Names:F15A17_270, MOK16.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Miscellaneous

Ubiquitin is encoded by 16 different genes. Ubiquitin is generally synthesized as a polyubiquitin precursor with tandem head to tail repeats. Often, there is one to three additional amino acids after the last repeat, removed in the mature protein. Alternatively, ubiquitin extension protein is synthesized as a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a ubiquitin-related protein (either RUB1 or RUB2). Following translation, extension protein is cleaved from ubiquitin.

For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Sequence similarities

Belongs to the ubiquitin family.

Contains 4 ubiquitin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396877
Chain77 – 15276Ubiquitin
PRO_0000396878
Chain153 – 22876Ubiquitin
PRO_0000396879
Chain229 – 30476Ubiquitin
PRO_0000396880
Propeptide305 – 3062 Probable
PRO_0000396881

Regions

Domain1 – 7676Ubiquitin-like 1
Domain77 – 15276Ubiquitin-like 2
Domain153 – 22876Ubiquitin-like 3
Domain229 – 30476Ubiquitin-like 4

Amino acid modifications

Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1EC66 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: B8BC6C32F1D4F3BE

FASTA30634,279
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKAKIQDKE GIPPDQQRLI 

       130        140        150        160        170        180 
FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA 

       190        200        210        220        230        240 
KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 

       250        260        270        280        290        300 
ITLEVESSDT IDNVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR 


LRGGSF 

« Hide

References

« Hide 'large scale' references
[1]"Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia."
Callis J., Carpenter T., Sun C.W., Vierstra R.D.
Genetics 139:921-939(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones."
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S.
DNA Res. 4:215-230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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.
[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. 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.
[6]"Arabidopsis ORF clones."
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[7]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
Tissue: Rosette leaf.
[8]"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-29; LYS-33; LYS-48 AND LYS-63.
Strain: cv. Landsberg erecta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05363 Genomic DNA. No translation available.
AB005240 Genomic DNA. Translation: BAB08384.1.
AL163002 Genomic DNA. Translation: CAB86091.1.
CP002688 Genomic DNA. Translation: AED90574.1.
CP002688 Genomic DNA. Translation: AED90575.1.
CP002688 Genomic DNA. Translation: AED90576.1.
BT002420 mRNA. Translation: AAO00780.1.
BT025868 mRNA. Translation: ABF85770.1.
AK317101 mRNA. Translation: BAH19791.1.
RefSeqNP_001031824.1. NM_001036747.1.
NP_568112.2. NM_120402.2.
NP_851029.1. NM_180698.2.
UniGeneAt.46169.
At.49314.
At.68083.
At.75559.
At.75636.

3D structure databases

ProteinModelPortalQ1EC66.
SMRQ1EC66. Positions 1-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17175. 1308 interactions.

Proteomic databases

PRIDEQ1EC66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G03240.1; AT5G03240.1; AT5G03240.
AT5G03240.2; AT5G03240.2; AT5G03240.
AT5G03240.3; AT5G03240.3; AT5G03240.
AT5G20620.1; AT5G20620.1; AT5G20620.
GeneID831899.
KEGGath:AT5G03240.

Organism-specific databases

TAIRAT5G03240.

Phylogenomic databases

KOK08770.

Gene expression databases

ArrayExpressQ1EC66.
GenevestigatorQ1EC66.

Family and domain databases

InterProIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 4 hits.
PROSITEPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBQ3_ARATH
AccessionPrimary (citable) accession number: Q1EC66
Secondary accession number(s): O80715 expand/collapse secondary AC list , P59263, Q38875, Q9LDJ2, Q9LYW1, Q9M0W3, Q9M1P9, Q9S7X3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: July 11, 2006
Last modified: July 9, 2014
This is version 58 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names