TRIP12 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006974Biological processDNA damage response
GO_0006511Biological processubiquitin-dependent protein catabolic process
GO_0006281Biological processDNA repair
GO_0045995Biological processregulation of embryonic development
GO_0000209Biological processprotein polyubiquitination
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0140861Biological processDNA repair-dependent chromatin remodeling
GO_0033696Biological processheterochromatin boundary formation
GO_0016607Cellular componentnuclear speck
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0005634Cellular componentnucleus
GO_0046966Molecular functionnuclear thyroid hormone receptor binding
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameTRIP12
Protein nameE3 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)
Thyroid hormone receptor interactor 12
E3 ubiquitin-protein ligase (EC 2.3.2.26)
Alternative protein TRIP12
SynonymshCG_1811426
ULF
KIAA0045
DescriptionFUNCTION: 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 . .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: 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. .

FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. .

FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. .

FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. .

FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. .

AccessionsENST00000453485.2
A0A6Q8PGG9
A0A994J752
A0A994J4J6
C9JLJ5
ENST00000704583.1
ENST00000389044.8 [Q14669-3]
G5E9G6
ENST00000675903.1
ENST00000430954.6
A0A994J569
A0A994J7J0
Q14669
ENST00000704580.1 [Q14669-2]
A0A6Q8PHK0
Q57Z94
ENST00000283943.9 [Q14669-1]
ENST00000428959.5
ENST00000704577.1
ENST00000704585.1
C9JSX9
ENST00000675453.1
A0A994J4S0
ENST00000704582.1
ENST00000704581.1
ENST00000704579.1
ENST00000389045.7 [Q14669-4]
F8W9P3
ENST00000409677.5
L0R5E3
ENST00000675423.1
A0A994J4J0
A0A994J755
C9JLD7
H7C2Y1
ENST00000435716.5
ENST00000343290.5
H7C1L9
ENST00000418123.1
ENST00000704584.1
ENST00000704578.1