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AB317878

Recombinant Human UBE2D3 protein (His-tag)

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Recombinant Human UBE2D3 protein (His-tag) is a Human Full Length protein, expressed in HEK 293 cells, with >95%, <1.83 EU/mg endotoxin level, suitable for HPLC, Mass Spec.

View Alternative Names

UBC5C, UBCH5C, UBE2D3, Ubiquitin-conjugating enzyme E2 D3, (E3-independent) E2 ubiquitin-conjugating enzyme D3, E2 ubiquitin-conjugating enzyme D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2(17)KB 3, Ubiquitin-conjugating enzyme E2-17 kDa 3, Ubiquitin-protein ligase D3

2 Images
Mass Spectrometry - Recombinant Human UBE2D3 protein (His-tag) (AB317878)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human UBE2D3 protein (His-tag) (AB317878)

Mass determination by ESI-TOF. Predicted MW is 18870 Da (+/- 10 Da by ESI-TOF). Observed MW is 18866.46 Da.

HPLC - Recombinant Human UBE2D3 protein (His-tag) (AB317878)
  • HPLC

Supplier Data

HPLC - Recombinant Human UBE2D3 protein (His-tag) (AB317878)

HPLC analysis of ab317878

Key facts

Purity

>95% HPLC

Endotoxin level

<1.83 EU/mg

Expression system

HEK 293 cells

Tags

His tag N-Terminus

Applications

Mass Spec, HPLC

applications

Biologically active

No

Mass Spectrometry

LC-MS/MS

Accession

P61077

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

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Complementary Products

Proteins & Peptides

AB131927

Recombinant Human RNF8 protein

SDS-PAGE - Recombinant Human RNF8 protein (AB131927)

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  • 0
Primary Antibodies

AB29

Anti-PCNA antibody [PC10]

BOND RX™ Validated|Lab Essentials

Western blot - Anti-PCNA antibody [PC10] (AB29)

  • 5
  • 72
Primary Antibodies

AB176568

Anti-UBE2D3 antibody [EPR13001(B)] - N-terminal

RabMAb|Recombinant

Immunoprecipitation - Anti-UBE2D3 antibody [EPR13001(B)] - N-terminal (AB176568)

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  • 0
Proteins & Peptides

AB283920

Recombinant human CD28 protein

Mass Spectrometry - Recombinant human CD28 protein (AB283920)

  • 0
  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM","proteinLength":"Full Length","predictedMolecularWeight":"18.87 kDa","actualMolecularWeight":"18.87 kDa","aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P61077","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

UBE2D3 also known as UbcH5c or E2-17k is a ubiquitin-conjugating enzyme. It plays a critical role in the ubiquitination process by interacting with ligase enzymes adding ubiquitin to target proteins. This protein has a molecular mass of approximately 16 kDa. UBE2D3 is widely expressed in various tissues indicating its role in several cellular functions.
Biological function summary

UBE2D3 acts as an important component in protein degradation and regulation. It participates in the ubiquitin-proteasome system which controls protein levels in cells. UBE2D3 forms part of larger protein complexes such as the SCF (Skp Cullin F-box containing) complex contributing to the regulation of cell cycle and signal transduction. This interaction helps control cell division and response to external signals.

Pathways

UBE2D3 plays an important role in the NF-kB signaling and DNA damage response pathways. It interacts with proteins such as IKK (IκB kinase) to regulate inflammation and immune response. Additionally UBE2D3's involvement in the DNA repair pathway supports maintaining genome stability by collaborating with other proteins like BRCA1 which is essential for repairing DNA double-strand breaks.

UBE2D3 shows a connection to cancer and neurodegenerative diseases. Its role in the NF-kB signaling pathway links it to cancer development due to its regulation of genes involved in cell growth and survival. In neurodegenerative disorders such as Alzheimer's disease abnormal ubiquitination due to UBE2D3 dysfunction may lead to protein aggregation affecting normal cellular activities. Its interaction with proteins like p53 a well-known tumor suppressor illustrates its importance in disease progression and regulation.
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Specifications

Form

Liquid

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General info

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592, PubMed : 28322253). In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592). Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 20347421). Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin (PubMed : 10329681). Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin (PubMed : 10329681). Also acts as an initiator E2, in conjunction with RNF8, for the priming of PCNA (PubMed : 18948756). Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase (PubMed : 18948756). Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair (PubMed : 16628214). Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus (PubMed : 18515077). In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53 (PubMed : 12646252, PubMed : 15280377). In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes (PubMed : 18508924). In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (PubMed : 11743028). Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed : 28469175). Together with ZNF598, catalyzes ubiquitination of 40S ribosomal proteins in response to ribosome collisions (PubMed : 28685749). In cooperation with the GATOR2 complex, catalyzes 'Lys-6'-linked ubiquitination of NPRL2 (PubMed : 36528027).

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Post-translational modifications

Phosphorylated by AURKB.

Subcellular localisation

Endosome membrane

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Product protocols

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Target data

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592, PubMed : 28322253). In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination (PubMed : 15247280, PubMed : 15496420, PubMed : 18284575, PubMed : 20061386, PubMed : 21532592). Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation (PubMed : 20347421). Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin (PubMed : 10329681). Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin (PubMed : 10329681). Also acts as an initiator E2, in conjunction with RNF8, for the priming of PCNA (PubMed : 18948756). Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase (PubMed : 18948756). Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair (PubMed : 16628214). Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus (PubMed : 18515077). In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53 (PubMed : 12646252, PubMed : 15280377). In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes (PubMed : 18508924). In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction (PubMed : 11743028). Together with RNF135, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (PubMed : 28469175). Together with ZNF598, catalyzes ubiquitination of 40S ribosomal proteins in response to ribosome collisions (PubMed : 28685749). In cooperation with the GATOR2 complex, catalyzes 'Lys-6'-linked ubiquitination of NPRL2 (PubMed : 36528027).
See full target information UBE2D3
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