TMEM59
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Official Full Name
transmembrane protein 59 -
Overview
Transmembrane protein 59 is a protein that in humans is encoded by the TMEM59 gene. -
Synonyms
TMEM59;transmembrane protein 59;C1orf8, chromosome 1 open reading frame 8;HSPC001;C1orf8;HSPC001,;Liver membrane-bound protein;TMEM59 transmembrane protein 59;TMM59_HUMAN
Recombinant Proteins
- Cynomolgus
- Chicken
- Mouse
- Rhesus macaque
- Zebrafish
- Human
- Mammalian Cells
- HEK293
- E.coli
- His
- Non
- DDK
- Myc
- Avi
- Fc
Involved Pathway
TMEM59 involved in several pathways and played different roles in them. We selected most pathways TMEM59 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with TMEM59 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
Protein Function
TMEM59 has several biochemical functions, for example, endopeptidase activity,protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by TMEM59 itself. We selected most functions TMEM59 had, and list some proteins which have the same functions with TMEM59. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| endopeptidase activity | NAPSA,FAP,TRAPPC12,PSMA3,KLK1B4,APH1B,PSMB8F,PSMA6,ECE1,PSMB5 |
| protein binding | ANKRD27,RAP1GDS1,SNX31,TEK,DIP2A,EMP3,MKNK2,DNMT1,KRTAP10-5,DHRS2 |
Interacting Protein
TMEM59 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 TMEM59 here. Most of them are supplied by our site. Hope this information will be useful for your research of TMEM59.
ATG16L1;PARP2;AP2M1;AP1M1;MAP1LC3A
Resources
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References
- Kaprio, T; Fermer, C; et al. Podocalyxin is a marker of poor prognosis in colorectal cancer. BMC CANCER 14:-(2014).
- Douam, F; Thi, VL; et al. Critical Interaction Between E1 and E2 Glycoproteins Determines Binding and Fusion Properties of Hepatitis C Virus During Cell Entry. HEPATOLOGY 59:776-788(2014).
