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Recombinant Human E3 ubiquitin-protein ligase TRIP12 (TRIP12), partial

Recombinant Human E3 ubiquitin-protein ligase TRIP12 (TRIP12), partial

Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Target Background

Product Details

Abbreviation

TRIP12

Purity

>85% (SDS-PAGE)

Target Names

TRIP12

Uniprot NO.

Q14669

Alternative Names

TRIP12; KIAA0045; ULF; E3 ubiquitin-protein ligase TRIP12; EC 2.3.2.26; E3 ubiquitin-protein ligase for Arf; ULF; HECT-type E3 ubiquitin transferase TRIP12; Thyroid receptor-interacting protein 12; TR-interacting protein 12; TRIP-12

Species

Homo sapiens (Human)

Source

Yeast

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex.

Gene References into Functions

p16 overexpression led to downregulation of TRIP12, which in turn led to increased RNF168 levels, repressed DNA damage repair (DDR), increased 53BP1 foci and enhanced radioresponsiveness. PMID:27425591
We describe the TRIP12-associated phenotype, showing that TRIP12 is a risk gene for non-syndromic intellectual disability with and without autism spectrum disorder, and that TRIP12 mutation carriers present with a broad phenotypic range within the neurodevelopmental phenotypes. PMID:27848077
nine presented pathogenic variants further document that TRIP12 haploinsufficiency causes a childhood-onset neurodevelopmental disorder PMID:28251352
Data indicate that E3 ubiquitin ligase thyroid hormone receptor-interacting protein 12 (TRIP12) promotes proteasomal degradation of pancreas transcription factor 1a (PTF1a)and regulates PTF1a activities. PMID:25355311
An exon3-skipping event in TRIP12 was detected in acute myeloid leukemia patients at remission PMID:24961348
HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin. PMID:23209776
Study shows that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. PMID:22884692
data indicate that TRADD shuttles dynamically from the cytoplasm into the nucleus to modulate the interaction between p19(Arf) and its E3 ubiquitin ligase ULF, thereby promoting p19(Arf) protein stability and tumour suppression PMID:22561347
ULF is a bona fide E3 ligase for ARF and also suggest that ULF is an important target for activating the ARF-p53 axis in human acute myeloid leukaemia cells. PMID:20699639
Data show that the mechanism of BAF155-mediated stabilization of BAF57 involves blocking its ubiquitination by preventing interaction with TRIP12. PMID:20829358
TRIP12 promotes degradation of APP-BP1 by catalyzing its ubiquitination, which in turn modulates the neddylation pathway. PMID:18627766
The HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathway. PMID:19028681