P61086 · UBE2K_HUMAN
- ProteinUbiquitin-conjugating enzyme E2 K
- GeneUBE2K
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids200 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 92 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | filopodium tip | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ubiquitin conjugating enzyme activity | |
Molecular Function | ubiquitin protein ligase binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | ubiquitin-ubiquitin ligase activity | |
Biological Process | cellular response to interferon-beta | |
Biological Process | free ubiquitin chain polymerization | |
Biological Process | positive regulation of peptidyl-threonine phosphorylation | |
Biological Process | positive regulation of tumor necrosis factor-mediated signaling pathway | |
Biological Process | positive regulation of type I interferon-mediated signaling pathway | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin-conjugating enzyme E2 K
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP61086
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 94 | Decreased lysine reactivity and impaired formation of free polyubiquitin chains. | ||||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 77 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000082443 | 2-200 | UniProt | Ubiquitin-conjugating enzyme E2 K | |||
Sequence: ANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN | |||||||
Modified residue | 14 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 14 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Modified residue | 159 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Sumoylation at Lys-14 impairs catalytic activity.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem.
Induction
By aggregated low-density lipoprotein.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RNF138/NARF. Interacts with BRCA1.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-154 | UBC core | ||||
Sequence: IAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAG | ||||||
Domain | 160-200 | UBA | ||||
Sequence: PEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN |
Sequence similarities
Belongs to the ubiquitin-conjugating enzyme family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P61086-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length200
- Mass (Da)22,407
- Last updated2007-01-23 v3
- ChecksumE40668099ED25828
P61086-2
- Name2
- NoteMay be inactive.
- Differences from canonical
- 22-72: Missing
P61086-3
- Name3
- Differences from canonical
- 134-176: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U58522 EMBL· GenBank· DDBJ | AAC50633.1 EMBL· GenBank· DDBJ | mRNA | ||
AB022435 EMBL· GenBank· DDBJ | BAA78555.1 EMBL· GenBank· DDBJ | mRNA | ||
AB022436 EMBL· GenBank· DDBJ | BAA78556.1 EMBL· GenBank· DDBJ | mRNA | ||
BX339118 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK291454 EMBL· GenBank· DDBJ | BAF84143.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315524 EMBL· GenBank· DDBJ | BAG37905.1 EMBL· GenBank· DDBJ | mRNA | ||
AC105287 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108471 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471069 EMBL· GenBank· DDBJ | EAW92948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC022804 EMBL· GenBank· DDBJ | AAH22804.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050600 EMBL· GenBank· DDBJ | AAH50600.1 EMBL· GenBank· DDBJ | mRNA |