Trip12
entrez
316575
canonical
uniprot
F1LP64
canonical
ensembl
ENSRNOG00000016963
resolver
ensp
ENSRNOP00000068991
resolver
ensp
ENSRNOP00000076130
resolver
ensp
ENSRNOP00000092462
resolver
ensp
ENSRNOP00000104101
resolver
ensp
ENSRNOP00000108120
resolver
enst
ENSRNOT00000079452
resolver
enst
ENSRNOT00000093245
resolver
enst
ENSRNOT00000107698
resolver
enst
ENSRNOT00000163092
resolver
genesymbol
Trip12
resolver
uniprot
A0A0G2JU73
resolver
uniprot
A0A8I6AHN4
resolver
uniprot
A0A8L2RBG4
resolver
uniprot
A0ABK0LF91
resolver
uniprot
F1LP79
resolver
uniprot
Q497C1
resolver
uniprot
Q5I0I0
resolver
uniprot_entry
A0A0G2JU73_RAT
resolver
uniprot_entry
A0A8I6AHN4_RAT
resolver
uniprot_entry
A0A8L2RBG4_RAT
resolver
uniprot_entry
A0ABK0LF91_RAT
resolver
uniprot_entry
TRIPC_RAT
resolver
uniprot_sec
F1LP79
resolver
uniprot_sec
Q497C1
resolver
uniprot_sec
Q5I0I0
resolver
activity_regulation
ACTIVITY REGULATION: Preferentially modifies 'Lys-29' in the proximal ubiquitin in a 'Lys-48'-linked di-ubiquitin chain. {ECO:0000250|UniProtKB:Q14669}.
uniprot
proteins
amino_acid_sequence
MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPRAFQHIESLSETNKPPSKSKKRHLDQEQQLKSAQLPSTSKAHTRKSVAAGSSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPAGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPEGNQETVNSSAARTDEAPQGAAASSSVAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNPLANTNTSGYSDLKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSLGSTTPASSGTATAATNASADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSAQSNSNNIEPARTAGVSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPVGRVEPVGHAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGSGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSVQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESSKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVANPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVCRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMRDKLLIAAREGQQSFHLS
uniprot
proteins
ec_number
2.3.2.26
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (By similarity). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (By similarity). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (By similarity). 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q14669}.
uniprot
proteins
mass_dalton
223928
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q14669}.
uniprot
proteins
protein_family
K-HECT subfamily
uniprot
proteins
protein_family
UPL family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
2025
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14669}.
uniprot
proteins