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Links from Protein

Items: 13

1.

GNAT family N-acetyltransferase

This family contains proteins with N-acetyltransferase functions. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024871.5
Method:
HMM
2.

Arginine-tRNA-protein transferase, N terminus

This family represents the N terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyses the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a de-stabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified [1]. In S cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity [2]. Of these, only Cys 94 appears to be completely conserved in this family. [1]. 9858543. Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Kwon YT, Kashina AS, Varshavsky A;. Mol Cell Biol 1999;19:182-193. [2]. 7495814. Binding of phenylarsenoxide to Arg-tRNA protein transferase is independent of vicinal thiols. Li J, Pickart CM;. Biochemistry 1995;34:15829-15837. (from Pfam)

GO Terms:
Molecular Function:
arginyl-tRNA--protein transferase activity (GO:0004057)
Biological Process:
protein arginylation (GO:0016598)
Date:
2024-10-16
Family Accession:
NF016276.5
Method:
HMM
3.

Arginine-tRNA-protein transferase, C terminus

This family represents the C terminal region of the enzyme arginine-tRNA-protein transferase (EC 2.3.2.8), which catalyses the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a destabilising amino acid to the amino terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis. N terminal cysteine is sometimes modified [1]. [1]. 9858543. Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Kwon YT, Kashina AS, Varshavsky A;. Mol Cell Biol 1999;19:182-193. (from Pfam)

GO Terms:
Molecular Function:
arginyl-tRNA--protein transferase activity (GO:0004057)
Biological Process:
protein arginylation (GO:0016598)
Date:
2024-10-16
Family Accession:
NF016277.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

arginyl-transferase family protein

arginyl-transferase family protein such as aspartate/glutamate leucyltransferase, which functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate

Date:
2018-03-09
Family Accession:
11479522
Method:
Sparcle
11.

arginyltransferase

GO Terms:
Molecular Function:
arginyl-tRNA--protein transferase activity (GO:0004057)
Biological Process:
protein arginylation (GO:0016598)
Date:
2021-09-22
Family Accession:
NF002341.0
Method:
HMM
12.

arginyltransferase

Date:
2020-10-26
Family Accession:
NF002346.0
Method:
HMM
13.

arginyltransferase

GO Terms:
Molecular Function:
arginyl-tRNA--protein transferase activity (GO:0004057)
Molecular Function:
leucyl-tRNA--protein transferase activity (GO:0008914)
Biological Process:
protein arginylation (GO:0016598)
Date:
2021-10-13
Family Accession:
NF002342.0
Method:
HMM
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