TRAIP
entrez
10293
canonical
uniprot
Q9BWF2
canonical
ensembl
ENSG00000183763
resolver
ensp
ENSP00000328203
resolver
ensp
ENSP00000561907
resolver
enst
ENST00000331456
resolver
genesymbol
TRAIP
resolver
genesymbol_syn
RNF206
resolver
genesymbol_syn
TRIP
resolver
hgnc
HGNC:30764
resolver
uniprot
B5BU84
resolver
uniprot
B5BUL3
resolver
uniprot
O00467
resolver
uniprot_entry
TRAIP_HUMAN
resolver
uniprot_sec
B5BU84
resolver
uniprot_sec
B5BUL3
resolver
uniprot_sec
O00467
resolver
amino_acid_sequence
MPIRALCTICSDFFDHSRDVAAIHCGHTFHLQCLIQWFETAPSRTCPQCRIQVGKRTIINKLFFDLAQEEENVLDAEFLKNELDNVRAQLSQKDKEKRDSQVIIDTLRDTLEERNATVVSLQQALGKAEMLCSTLKKQMKYLEQQQDETKQAQEEARRLRSKMKTMEQIELLLQSQRPEVEEMIRDMGVGQSAVEQLAVYCVSLKKEYENLKEARKASGEVADKLRKDLFSSRSKLQTVYSELDQAKLELKSAQKDLQSADKEIMSLKKKLTMLQETLNLPPVASETVDRLVLESPAPVEVNLKLRRPSFRDDIDLNATFDVDTPPARPSSSQHGYYEKLCLEKSHSPIQDVPKKICKGPRKESQLSLGGQSCAGEPDEELVGAFPIFVRNAILGQKQPKRPRSESSCSKDVVRTGFDGLGGRTKFIQPTDTVMIRPLPVKPKTKVKQRVRVKTVPSLFQAKLDTFLWS
uniprot
proteins
disease_involvement
DISEASE: Seckel syndrome 9 (SCKL9) [MIM:616777]: A form of Seckel syndrome, a rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and intellectual disability. {ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:30165463}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin ligase required to protect genome stability in response to replication stress (PubMed:25335891, PubMed:26595769, PubMed:26711499, PubMed:26781088, PubMed:27462463, PubMed:31545170). Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription (By similarity). Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex (By similarity). Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3 (By similarity). If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway (By similarity). Only catalyzes ubiquitination of MCM7 when forks converge (By similarity). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome (By similarity). Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity (PubMed:24553286). The function in translesion synthesis is however controversial (PubMed:26595769). Acts as a regulator of the spindle assembly checkpoint (PubMed:25335891). Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF (PubMed:22945920). Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation (PubMed:22945920). {ECO:0000250|UniProtKB:Q6NRV0, ECO:0000269|PubMed:22945920, ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:31545170}.
uniprot
proteins
mass_dalton
53294
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="C->A: Abolished accumulation in nucleolus."; /evidence="ECO:0000269|PubMed:27462463"; MUTAGEN 25; /note="C->A: Abolished ability to regulate nuclear envelope breakdown to anaphase."; /evidence="ECO:0000269|PubMed:25335891"; MUTAGEN 80; /note="K->A: Abolished sumoylation and localization to the nucleus; when associated with A-127, A-205, A-247 and A-462."; /evidence="ECO:0000269|PubMed:26820530"; MUTAGEN 127; /note="K->A: Abolished sumoylation and localization to the nucleus; when associated with A-80, A-205, A-247 and A-462."; /evidence="ECO:0000269|PubMed:26820530"; MUTAGEN 205; /note="K->A: Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-247 and A-462."; /evidence="ECO:0000269|PubMed:26820530"; MUTAGEN 247; /note="K->A: Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-205 and A-462."; /evidence="ECO:0000269|PubMed:26820530"; MUTAGEN 460..463; /note="QAKL->AAKA: Abolished interaction with PCNA and localization to DNA damage sites."; /evidence="ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:30165463"; MUTAGEN 462; /note="K->A: Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-205 and A-247."; /evidence="ECO:0000269|PubMed:26820530"; MUTAGEN 466; /note="F->A: Abolished interaction with PCNA."; /evidence="ECO:0000269|PubMed:26711499
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17544371, ECO:0000269|PubMed:22945920}.
uniprot
proteins
post_translational_modification
PTM: Sumoylated; sumoylation is required for nuclear localization (PubMed:26820530). Sumoylation increases protein stability, possibly by preventing ubiquitination (PubMed:26820530). {ECO:0000269|PubMed:26820530}.; PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q8VIG6}.
uniprot
proteins
protein_family
TRAIP family
uniprot
proteins
pubmed
14676304
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17544371
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
22945920
uniprot
proteins
pubmed
24553286
uniprot
proteins
pubmed
25335891
uniprot
proteins
pubmed
26595769
uniprot
proteins
pubmed
26711499
uniprot
proteins
pubmed
26781088
uniprot
proteins
pubmed
26820530
uniprot
proteins
pubmed
27462463
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30165463
uniprot
proteins
pubmed
31545170
uniprot
proteins
pubmed
9104814
uniprot
proteins
sequence_length
469
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26820530, ECO:0000269|PubMed:30165463}. Nucleus, nucleolus {ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:24553286, ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:30165463}. Chromosome {ECO:0000269|PubMed:25335891, ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088, ECO:0000269|PubMed:30165463}. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14676304}. Note=In the nucleus, found in close proximity to PCNA, suggesting localization at replication foci (PubMed:26595769). Localizes to DNA damage sites in response to replication stress (PubMed:26595769, PubMed:26711499, PubMed:26781088). {ECO:0000269|PubMed:26595769, ECO:0000269|PubMed:26711499, ECO:0000269|PubMed:26781088}.
uniprot
proteins