RNF138
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Official Full Name
ring finger protein 138, E3 ubiquitin protein ligase -
Overview
The protein encoded by this gene contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. Alternatively spliced transcript variants encoding distinct isoforms have been observed. -
Synonyms
RNF138;ring finger protein 138, E3 ubiquitin protein ligase;ring finger protein 138;E3 ubiquitin-protein ligase RNF138;STRIN;NLK-associated RING finger protein;Nemo-like kinase-associated RING finger protein;NARF;HSD-4;hNARF;MGC8758
Recombinant Proteins
- Mouse
- Rat
- Human
- Mammalian Cell
- HEK293
- His
- Non
- His&Fc&Avi
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| RNF138-14301M | Recombinant Mouse RNF138 Protein | Mammalian Cell | Mouse | His |
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| RNF138-5072R | Recombinant Rat RNF138 Protein | Mammalian Cell | Rat | His |
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| RNF138-2298HCL | Recombinant Human RNF138 293 Cell Lysate | HEK293 | Human | Non |
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| RNF138-4731R | Recombinant Rat RNF138 Protein, His (Fc)-Avi-tagged | HEK293 | Rat | His&Fc&Avi |
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| RNF138-4731R-B | Recombinant Rat RNF138 Protein Pre-coupled Magnetic Beads | HEK293 | Rat |
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| RNF138-7651M | Recombinant Mouse RNF138 Protein, His (Fc)-Avi-tagged | HEK293 | Mouse | His&Fc&Avi |
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| RNF138-7651M-B | Recombinant Mouse RNF138 Protein Pre-coupled Magnetic Beads | HEK293 | Mouse |
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Involved Pathway
RNF138 involved in several pathways and played different roles in them. We selected most pathways RNF138 participated on our site, such as Adaptive Immune System,Antigen processing: Ubiquitination &,Proteasome degradation, which may be useful for your reference. Also, other proteins which involved in the same pathway with RNF138 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Proteasome degradation | TRIM50,RNF6,LRR1,FBXO3,UBE2U,ASB7,RNF41,RNF111,TRIM69,NPEPPS |
| Antigen processing: Ubiquitination & | TRIM69,ASB7,LRR1,RNF41,PJA2,TRIM63,GAN,TRAF7,TRIM41,VPRBP |
| Class I MHC mediated antigen processing & | CTSL1,LTN1,SEC61B,RNF182,CYBB,UBE2L6,SPSB2,TRIM9,FCGR1B,RNF41 |
| Adaptive Immune System | MGC174857,AP1G1,RNF220,RNF41,FGF10B,NCR3LG1,CD300LF,RAP1GAP2,KIF4,TREML2 |
| presentation | DTX3L,NPEPPS,SPSB2,ARIH2,TRIM11,RNF182,LTN1,UBE2V1,CYBA,MKRN1 |
| Immune System | CD96,GHRB,S100A12,HLA-DQB2,SIGLEC14,IFITM2,Mill2,KLHL20,RNF19B,CD200 |
Protein Function
RNF138 has several biochemical functions, for example, ligase activity,protein binding,protein kinase binding. Some of the functions are cooperated with other proteins, some of the functions could acted by RNF138 itself. We selected most functions RNF138 had, and list some proteins which have the same functions with RNF138. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| protein kinase binding | TP73,PRKAG3,TTN,GCSAM,SPDYE2,SKAP1,TNNI3,RPS3,MAPK8IP2,PTEN |
| ligase activity | ZSWIM2,MSL2,UNKL,UHRF1,CNOT4,RNF180,C12orf51,UBE2D1A,MARCH2,PARK2 |
| protein binding | EWSR1A,PCGF1,MTMR2,ANGPT1,PKD2L1,PDIA2,CSF3R,EGLN1,EEF1E1,VSIG4 |
| zinc ion binding | ZCCHC12,PIAS4,ZNF34,MKRN2,VAT1,LDB3A,MMP20,UBR5,XIAP,OTUD7B |
Interacting Protein
RNF138 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 RNF138 here. Most of them are supplied by our site. Hope this information will be useful for your research of RNF138.
UBE2K;HIP2;PCBP4;UBE2D2;TAF9;C6orf165;LNX2;UBE2W;QKI;TRIM8;UBE2D4;SLX4
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References
- Lee, K; Byun, K; et al. Proteome-wide discovery of mislocated proteins in cancer. GENOME RESEARCH 23:1283-1294(2013).
- Long, P; Samnakay, P; et al. A yeast two-hybrid screen reveals that osteopontin associates with MAP1A and MAP1B in addition to other proteins linked to microtubule stability, apoptosis and protein degradation in the human brain. EUROPEAN JOURNAL OF NEUROSCIENCE 36:2733-2742(2012).
