TRIP12
entrez
9320
canonical
uniprot
Q14669
canonical
ensembl
ENSG00000153827
resolver
ensp
ENSP00000283943
resolver
ensp
ENSP00000373696
resolver
ensp
ENSP00000373697
resolver
ensp
ENSP00000400967
resolver
ensp
ENSP00000502271
resolver
ensp
ENSP00000502713
resolver
ensp
ENSP00000502768
resolver
ensp
ENSP00000515952
resolver
ensp
ENSP00000515953
resolver
ensp
ENSP00000515955
resolver
ensp
ENSP00000515956
resolver
ensp
ENSP00000515960
resolver
ensp
ENSP00000525171
resolver
ensp
ENSP00000525172
resolver
ensp
ENSP00000525173
resolver
ensp
ENSP00000525174
resolver
ensp
ENSP00000525175
resolver
ensp
ENSP00000525176
resolver
ensp
ENSP00000525177
resolver
ensp
ENSP00000525178
resolver
ensp
ENSP00000525179
resolver
ensp
ENSP00000525180
resolver
ensp
ENSP00000525181
resolver
ensp
ENSP00000525183
resolver
ensp
ENSP00000525184
resolver
ensp
ENSP00000602335
resolver
ensp
ENSP00000602337
resolver
ensp
ENSP00000602343
resolver
ensp
ENSP00000602345
resolver
ensp
ENSP00000602352
resolver
ensp
ENSP00000630341
resolver
ensp
ENSP00000630342
resolver
ensp
ENSP00000630343
resolver
ensp
ENSP00000630353
resolver
ensp
ENSP00000630354
resolver
ensp
ENSP00000630355
resolver
ensp
ENSP00000630359
resolver
ensp
ENSP00000783639
resolver
ensp
ENSP00000783640
resolver
enst
ENST00000283943
resolver
enst
ENST00000453485
resolver
enst
ENST00000675453
resolver
enst
ENST00000704578
resolver
enst
ENST00000704581
resolver
enst
ENST00000704585
resolver
enst
ENST00000855112
resolver
enst
ENST00000855113
resolver
enst
ENST00000855118
resolver
enst
ENST00000855124
resolver
enst
ENST00000932278
resolver
enst
ENST00000932286
resolver
enst
ENST00000960295
resolver
genesymbol
TRIP12
resolver
genesymbol_syn
KIAA0045
resolver
genesymbol_syn
ULF
resolver
hgnc
HGNC:12306
resolver
uniprot
A0A6Q8PGG9
resolver
uniprot
A0A6Q8PHK0
resolver
uniprot
A0A994J4J0
resolver
uniprot
A0A994J569
resolver
uniprot
A0A994J755
resolver
uniprot
D4HL82
resolver
uniprot
H7C1L9
resolver
uniprot
Q14CA3
resolver
uniprot
Q14CF1
resolver
uniprot
Q15644
resolver
uniprot
Q53R87
resolver
uniprot
Q53TE7
resolver
uniprot_entry
A0A6Q8PGG9_HUMAN
resolver
uniprot_entry
A0A994J4J0_HUMAN
resolver
uniprot_entry
A0A994J569_HUMAN
resolver
uniprot_entry
A0A994J755_HUMAN
resolver
uniprot_entry
H7C1L9_HUMAN
resolver
uniprot_entry
TRIPC_HUMAN
resolver
uniprot_sec
A0A6Q8PHK0
resolver
uniprot_sec
D4HL82
resolver
uniprot_sec
Q14CA3
resolver
uniprot_sec
Q14CF1
resolver
uniprot_sec
Q15644
resolver
uniprot_sec
Q53R87
resolver
uniprot_sec
Q53TE7
resolver
activity_regulation
ACTIVITY REGULATION: Preferentially modifies 'Lys-29' in the proximal ubiquitin in a 'Lys-48'-linked di-ubiquitin chain. {ECO:0000269|PubMed:40419785}.
uniprot
proteins
amino_acid_sequence
MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSHLGQAKHKGYSPPESRKSNSKAPKVQSNTTSELSRGHLSKRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPKALQHTESPSETNKPHSKSKKRHLDQEQQLKSAQSPSTSKAHTRKSGATGGSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPPGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSLRRSTRQKTTGSCASTSRRGSGLGKRGAAEARRQEKMADPESNQEAVNSSAARTDEAPQGAAASSSVAGAVGMTTSGESESDDSEMGRLQALLEARGLPPHLFGPLGPRMSQLFHRTIGSGASSKAQQLLQGLQASDESQQLQAVIEMCQLLVMGNEETLGGFPVKSVVPALITLLQMEHNFDIMNHACRALTYMMEALPRSSAVVVDAIPVFLEKLQVIQCIDVAEQALTALEMLSRRHSKAILQAGGLADCLLYLEFFSINAQRNALAIAANCCQSITPDEFHFVADSLPLLTQRLTHQDKKSVESTCLCFARLVDNFQHEENLLQQVASKDLLTNVQQLLVVTPPILSSGMFIMVVRMFSLMCSNCPTLAVQLMKQNIAETLHFLLCGASNGSCQEQIDLVPRSPQELYELTSLICELMPCLPKEGIFAVDTMLKKGNAQNTDGAIWQWRDDRGLWHPYNRIDSRIIEAAHQVGEDEISLSTLGRVYTIDFNSMQQINEDTGTARAIQRKPNPLANSNTSGYSESKKDDARAQLMKEDPELAKSFIKTLFGVLYEVYSSSAGPAVRHKCLRAILRIIYFADAELLKDVLKNHAVSSHIASMLSSQDLKIVVGALQMAEILMQKLPDIFSVYFRREGVMHQVKHLAESESLLTSPPKACTNGSGSMGSTTSVSSGTATAATHAAADLGSPSLQHSRDDSLDLSPQGRLSDVLKRKRLPKRGPRRPKYSPPRDDDKVDNQAKSPTTTQSPKSSFLASLNPKTWGRLSTQSNSNNIEPARTAGGSGLARAASKDTISNNREKIKGWIKEQAHKFVERYFSSENMDGSNPALNVLQRLCAATEQLNLQVDGGAECLVEIRSIVSESDVSSFEIQHSGFVKQLLLYLTSKSEKDAVSREIRLKRFLHVFFSSPLPGEEPIGRVEPVGNAPLLALVHKMNNCLSQMEQFPVKVHDFPSGNGTGGSFSLNRGSQALKFFNTHQLKCQLQRHPDCANVKQWKGGPVKIDPLALVQAIERYLVVRGYGRVREDDEDSDDDGSDEEIDESLAAQFLNSGNVRHRLQFYIGEHLLPYNMTVYQAVRQFSIQAEDERESTDDESNPLGRAGIWTKTHTIWYKPVREDEESNKDCVGGKRGRAQTAPTKTSPRNAKKHDELWHDGVCPSVSNPLEVYLIPTPPENITFEDPSLDVILLLRVLHAISRYWYYLYDNAMCKEIIPTSEFINSKLTAKANRQLQDPLVIMTGNIPTWLTELGKTCPFFFPFDTRQMLFYVTAFDRDRAMQRLLDTNPEINQSDSQDSRVAPRLDRKKRTVNREELLKQAESVMQDLGSSRAMLEIQYENEVGTGLGPTLEFYALVSQELQRADLGLWRGEEVTLSNPKGSQEGTKYIQNLQGLFALPFGRTAKPAHIAKVKMKFRFLGKLMAKAIMDFRLVDLPLGLPFYKWMLRQETSLTSHDLFDIDPVVARSVYHLEDIVRQKKRLEQDKSQTKESLQYALETLTMNGCSVEDLGLDFTLPGFPNIELKKGGKDIPVTIHNLEEYLRLVIFWALNEGVSRQFDSFRDGFESVFPLSHLQYFYPEELDQLLCGSKADTWDAKTLMECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQQSFHLS
uniprot
proteins
disease_involvement
DISEASE: Clark-Baraitser syndrome (CLABARS) [MIM:617752]: An autosomal dominant disease characterized by intellectual disability, delayed psychomotor development, behavioral abnormalities, variable dysmorphic facial features, tall stature, obesity, and macrocephaly. {ECO:0000269|PubMed:27848077, ECO:0000269|PubMed:28251352}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:19028681, PubMed:22884692, PubMed:40419785). 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 (PubMed:19028681). 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 (PubMed:22884692). 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 (PubMed:20208519). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (PubMed:20208519). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (PubMed:20208519). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (PubMed:18627766). 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 (PubMed:20829358). 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 (PubMed:30982744). {ECO:0000269|PubMed:18627766, ECO:0000269|PubMed:19028681, ECO:0000269|PubMed:20208519, ECO:0000269|PubMed:20829358, ECO:0000269|PubMed:22884692, ECO:0000269|PubMed:30982744, ECO:0000269|PubMed:40419785}.
uniprot
proteins
mass_dalton
228484
uniprot
proteins
mutagenesis
MUTAGEN 2034; /note="C->A: Abolishes E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:20208519"; MUTAGEN 2037; /note="Y->A: Abolishes E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:40419785"; MUTAGEN 2039; /note="K->D: Abolishes E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:40419785"; MUTAGEN 2067; /note="S->A,D,N,H,V,L: Impairs E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:40419785"; MUTAGEN 2067; /note="S->E,Y,I: Abolishes E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:40419785
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18627766, ECO:0000269|PubMed:20208519, ECO:0000269|PubMed:30982744}.
uniprot
proteins
protein_family
K-HECT subfamily
uniprot
proteins
protein_family
UPL family
uniprot
proteins
pubmed
11237011
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15496913
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18627766
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19028681
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20208519
uniprot
proteins
pubmed
20829358
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22561347
uniprot
proteins
pubmed
22884692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27848077
uniprot
proteins
pubmed
28251352
uniprot
proteins
pubmed
30982744
uniprot
proteins
pubmed
40419785
uniprot
proteins
pubmed
7584044
uniprot
proteins
pubmed
7776974
uniprot
proteins
sequence_length
2067
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:20208519}.
uniprot
proteins