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URM1 protein (Saccharomyces cerevisiae) - STRING interaction network
"URM1" - Ubiquitin-like protein involved in thiolation of cytoplasmic tRNAs in Saccharomyces cerevisiae
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Predicted Interactions
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URM1Ubiquitin-like protein involved in thiolation of cytoplasmic tRNAs; receives sulfur from the E1-like enzyme Uba4p and transfers it to tRNA; also functions as a protein tag with roles in nutrient sensing and oxidative stress response; Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2- thiolation reaction by being thiocarboxylated (-COSH) at its C- terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modifica [...] (99 aa)    
Predicted Functional Partners:
UBA4
E1-like protein that activates Urm1p before urmylation; also acts in thiolation of the wobble base of cytoplasmic tRNAs by adenylating and then thiolating Urm1p; receives sulfur from Tum1p; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The re [...] (440 aa)
       
  0.997
NCS2
Protein required for thiolation of the uridine at the wobble position of Lys(UUU) and Glu(UUC) tRNAs; has a role in urmylation and in invasive and pseudohyphal growth; inhibits replication of Brome mosaic virus in S. cerevisiae; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in p [...] (493 aa)
       
 
  0.968
AHP1
Thiol-specific peroxiredoxin, reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H(2)O(2). Involved in cellular Mn(2+) homeostasis (176 aa)
       
  0.961
NCS6
Protein required for thiolation of the uridine at the wobble position of Gln, Lys, and Glu tRNAs; has a role in urmylation and in invasive and pseudohyphal growth; inhibits replication of Brome mosaic virus in S. cerevisiae; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wo [...] (359 aa)
       
 
  0.951
ELP2
Subunit of Elongator complex, which is required for modification of wobble nucleosides in tRNA; target of Kluyveromyces lactis zymocin; Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeli [...] (788 aa)
     
 
  0.841
IKI3
Subunit of Elongator complex, which is required for modification of wobble nucleosides in tRNA; maintains structural integrity of Elongator; homolog of human IKAP, mutations in which cause familial dysautonomia (FD); Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can ac [...] (1349 aa)
       
 
  0.827
ELP6
Subunit of Elongator complex, which is required for modification of wobble nucleosides in tRNA; required for Elongator structural integrity; Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin rem [...] (273 aa)
     
 
  0.816
KTI11
Zn-ribbon protein that co-purifies with Dph1 and Dph2 in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p involved in modification of wobble nucleosides in tRNAs; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L- methionine to a histidine residue. Diphthamide is a post- translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin (82 aa)
     
   
  0.813
ELP3
Subunit of Elongator complex, which is required for modification of wobble nucleosides in tRNA; exhibits histone acetyltransferase activity that is directed to histones H3 and H4; disruption confers resistance to K. lactis zymotoxin; Acts as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked an [...] (557 aa)
     
 
  0.787
VMA1
Subunit A of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maint [...] (1071 aa)
       
      0.749
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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