TTL
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Official Full Name
tubulin tyrosine ligase -
Overview
TTL is a cytosolic enzyme involved in the posttranslational modification of alpha-tubulin (see MIM 602529).;Alpha-tubulin within assembled microtubules is detyrosinated over time at the C terminus. After microtubule;disassembly, TTL restores the tyrosine residues and consequently participates in a cycle of tubulin detyrosination and;tyrosination (Erck et al., 2003 (PubMed 14571137)).
Recombinant Proteins
- Human
- Chicken
- Zebrafish
- Rhesus macaque
- Rat
- Mouse
- E.coli
- Mammalian Cell
- HEK293
- HEK293T
- His
- GST
- Non
- His&Fc&Avi
- His&GST
- Myc&DDK
Involved Pathway
TTL involved in several pathways and played different roles in them. We selected most pathways TTL participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with TTL were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Protein Function
TTL has several biochemical functions, for example, ATP binding,tubulin-tyrosine ligase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by TTL itself. We selected most functions TTL had, and list some proteins which have the same functions with TTL. You can find most of the proteins on our site.
Function | Related Protein |
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ATP binding | GKUP,ILF2,ACLY,STK38A,SPG7,NME4,ACSF2,NTRK3A,EPHA2,TTF2 |
Interacting Protein
TTL has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with TTL here. Most of them are supplied by our site. Hope this information will be useful for your research of TTL.
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References
- Wloga, D; Rogowski, K; et al. Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila. EUKARYOTIC CELL 7:1362-1372(2008).
- Bisig, CG; Purro, SA; et al. Incorporation of 3-nitrotyrosine into the C-terminus of alpha-tubulin is reversible and not detrimental to dividing cells. EUROPEAN JOURNAL OF BIOCHEMISTRY 269:5037-5045(2002).