Ubiquitin activating enzyme

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'''Ubiquitin activating enzyme''' (Uba) or '''E1 enzyme''' catalyzes the first step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (E2) (Ubc) cysteine<ref>PMID:7673335</ref>. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. '''Uba3''' is the catalytic subunit of NEDD8 activating enzyme and APPB1 is its regulatory subunit. Similar to ubiquitin and SUMO, NEDD8 binds to proteins after processing of its C-terminal. <br />
'''Ubiquitin activating enzyme''' (Uba) or '''E1 enzyme''' catalyzes the first step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (E2) (Ubc) cysteine<ref>PMID:7673335</ref>. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. '''Uba3''' is the catalytic subunit of NEDD8 activating enzyme and APPB1 is its regulatory subunit. Similar to ubiquitin and SUMO, NEDD8 binds to proteins after processing of its C-terminal. <br />
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For more details on Uba1 see [[Uba1]].
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For more details on Uba1 see [[Uba1]].<br />
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For '''ubiquitin-like modifier-activating enzyme Atg7''' see [[Autophagy-related protein]]
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</StructureSection>
</StructureSection>
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**[[4ii2]] – hUba + E2 Ubc4 + ubiquitin-ribosomal protein L40 + ATP<BR />
**[[4ii2]] – hUba + E2 Ubc4 + ubiquitin-ribosomal protein L40 + ATP<BR />
**[[4ii3]] – hUba + ubiquitin-ribosomal protein L40 + ATP <BR />
**[[4ii3]] – hUba + ubiquitin-ribosomal protein L40 + ATP <BR />
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**[[6dc6]] – hUba (mutant) + ubiquitin <BR />
*Ubiquitin activating enzyme E1-like
*Ubiquitin activating enzyme E1-like
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**[[5ia8]] – hUba residues 1-83 <BR />
**[[5ia8]] – hUba residues 1-83 <BR />
**[[3guc]] – hUba + AMPPNP <BR />
**[[3guc]] – hUba + AMPPNP <BR />
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**[[3h8v]] – hUba + ATP <BR />
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**[[3h8v]], [[6h78]] – hUba + ATP <BR />
**[[5iaa]] – hUba + UFM1 <BR />
**[[5iaa]] – hUba + UFM1 <BR />
**[[5l95]] – hUba + UFM1 + AMP<BR />
**[[5l95]] – hUba + UFM1 + AMP<BR />
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**[[6h77]] – hUba + UFM1 + ATP<BR />
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* Ubiquitin-like 1 activating enzyme E1A or SUMO-1 activating enzyme subunit 1
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**[[1y8r]] – hSAE subunit 1 + hSAE subunit 2 + SMTC3 <BR />
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* Ubiquitin-like modifier-activating enzyme 2 or SUMO-activating enzyme subunit 2
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[[3kyc]] – hSAE subunits 1,2 + SUMO <BR />
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[[3kyd]] – hSAE subunits 1,2 + SUMO + AMP <BR />
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**[[5fq2]], [[4w5v]] – hSAE ubiquitin domain + Ubc9 <BR />
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* Ubiquitin-like modifier-activating enzyme Atg7 see [[Autophagy-related protein]]
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}}
}}

Revision as of 10:17, 18 November 2018

Structure of human ubiquitin activating enzyme Uba3 subunit (green) complex with E2 Ubc12 (grey) (PDB entry 1y8x)

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3D Structures of ubiquitin activating enzyme

Updated on 18-November-2018

3kyc – hSAE subunits 1,2 + SUMO
3kyd – hSAE subunits 1,2 + SUMO + AMP

References

  1. ↑ Nagai Y, Kaneda S, Nomura K, Yasuda H, Seno T, Yamao F. Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase Cdc2. J Cell Sci. 1995 Jun;108 ( Pt 6):2145-52. PMID:7673335

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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