Q1EC66 · UBQ3_ARATH

Function

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).

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 eL40 or eS31) 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.

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular Componentplant-type vacuole
Cellular Componentplasma membrane
Molecular FunctionmRNA binding
Biological Processresponse to UV-B
Biological Processubiquitin-dependent protein catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Polyubiquitin 3
  • Cleaved into 1 chains

Gene names

    • Name
      UBQ3
    • ORF names
      F15A17_270, MOK16.15
    • Ordered locus names
      At5g03240

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q1EC66
  • Secondary accessions
    • O80715
    • P59263
    • Q38875
    • Q9LDJ2
    • Q9LYW1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, cross-link, propeptide.

Type
IDPosition(s)Description
ChainPRO_00003968771-76Ubiquitin
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainPRO_000039687877-152Ubiquitin
ChainPRO_0000396879153-228Ubiquitin
ChainPRO_0000396880229-304Ubiquitin
PropeptidePRO_0000396881305-306

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-76Ubiquitin-like 1
Domain77-152Ubiquitin-like 2
Domain153-228Ubiquitin-like 3
Domain229-304Ubiquitin-like 4

Sequence similarities

Belongs to the ubiquitin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    306
  • Mass (Da)
    34,279
  • Last updated
    2006-07-11 v1
  • Checksum
    B8BC6C32F1D4F3BE
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGSF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L05363
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AB005240
EMBL· GenBank· DDBJ
BAB08384.1
EMBL· GenBank· DDBJ
Genomic DNA
AL163002
EMBL· GenBank· DDBJ
CAB86091.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90574.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90575.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90576.1
EMBL· GenBank· DDBJ
Genomic DNA
BT002420
EMBL· GenBank· DDBJ
AAO00780.1
EMBL· GenBank· DDBJ
mRNA
BT025868
EMBL· GenBank· DDBJ
ABF85770.1
EMBL· GenBank· DDBJ
mRNA
AK317101
EMBL· GenBank· DDBJ
BAH19791.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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