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Ubiquitin-fold modifier

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<StructureSection load='5iaa' size='340' side='right' caption='Human ubiquitin-fold modifier (pink, yellow) complex with ubiquitin-like modifier activating enzyme (green, grey) (PDB code [[5iaa]]' scene='' >
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<StructureSection load='5iaa' size='340' side='right' caption='Human ubiquitin-fold modifier (pink, yellow) complex with ubiquitin-like modifier activating enzyme (green, cyan) (PDB code [[5iaa]]' scene='87/873802/Cv/1' >
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__TOC__
== Function ==
== Function ==
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'''Ubiquitin-fold modifier''' (Ufm1) is a member of the ubiquitin-like family. Ufm1 is covalently attached to Lys residues of substrate proteins<ref>PMID:21494687</ref>. This attachment is called Ufmylation and requires '''Ubiquitin-like modifier activating enzyme''' (UBA5) and '''Umf1-conjugating enzyme''' (Ufc1). Ufmylation is a type of post-translational modification that deals with fine-tuned and complex cellular activities and is involved in reticulophagy induced by ER stress<ref>PMID:31129212</ref>. Ufmylation is aribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER<ref>PMID:30626644</ref>.
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'''Ubiquitin-fold modifier''' (Ufm1) is a member of the ubiquitin-like family. Ufm1 is covalently attached to Lys residues of substrate proteins<ref>PMID:21494687</ref>. This attachment is called Ufmylation and requires '''Ubiquitin-like modifier activating enzyme''' (Uba5) and '''Ufm1-conjugating enzyme''' (Ufc1). Ufmylation is a type of post-translational modification that deals with fine-tuned and complex cellular activities and is involved in reticulophagy induced by ER stress<ref>PMID:31129212</ref>. Ufmylation is aribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER<ref>PMID:30626644</ref>.
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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<scene name='Sandbox_27/Role_i997_vinculin_head-tail_1/1'>Vinculin Autoinhibition</scene> is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains ([[1st6]]). Energetically, I997 is key to maintaining this autoinhibition.
 
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</StructureSection>
 
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== 3D Structures of Ubiquitin-fold modifier ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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<scene name='87/873802/Cv/2'>The 3D structure of the complex between Ufm1 and UBA</scene> shows the Ufm1 critical binding sequence and the <scene name='87/873802/Cv/4'>interactions between the 2 modifying enzymes</scene> <ref>PMID:27653677</ref>.
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Ubiquitin-fold modifier
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== 3D Structures of Ubiquitin-fold modifier ==
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**[[5ia7]] – hUmf1 - human<br />
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[[Ubiquitin-fold modifier 3D structures]]
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**[[1wxs]] – hUmf1 - NMR<br />
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**[[5hkh]] – hUmf1 + peptide<br />
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**[[5iaa]] – hUmf1 + UBA5<br />
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**[[5l95]] – hUmf1 + UBA5 + AMP<br />
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**[[6h77]] – hUmf1 + UBA5 + ATP<br />
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**[[5xda]] – Umf1 + Umf1-specific protease - ''Caenorhabditis elegans''<br />
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**[[6izg]] – Umf1 - ''Trypanosoma brucei'' - NMR<br />
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*Umf1-conjugating enzyme
 
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**[[2z6o]], [[2z6p]], [[3evx]] – hUfc1<br />
 
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**[[2k07]] – hUfc1 - NMR<br />
 
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*Ubiquitin-like modifier activating enzyme
 
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**[[3h8v]], [[6h78]] – hUBA5 + ATP<br />
 
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**[[3guc]] – hUBA5 + AMPPNP<br />
 
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}}
 
==References==
==References==
<references />
<references />
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human ubiquitin-fold modifier (pink, yellow) complex with ubiquitin-like modifier activating enzyme (green, cyan) (PDB code 5iaa

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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