TRAF interacting protein

TRAIP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTRAIP, RNF206, TRIP, SCKL9, TRAF interacting protein
External IDsOMIM: 605958; MGI: 1096377; HomoloGene: 31343; GeneCards: TRAIP; OMA:TRAIP - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005879

NM_011634

RefSeq (protein)

NP_005870

NP_035764

Location (UCSC)Chr 3: 49.83 – 49.86 MbChr 9: 107.83 – 107.85 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
The AlphaFold predicted structure of the TRAIP protein Q9BWF2. The highlighted region has been found to bind to the PCNA PIP box. This image was generated using ChimeraX version 1.7.1.
Detailed view of residue sequence 447-469 of the TRAIP protein in its binding conformation with the PCNA PIP box.[5] This This image was generated using ChimeraX version 1.7.1.

TRAF-interacting protein is a protein that in humans is encoded by the TRAIP gene.[6][7]

This gene encodes a protein that contains an N-terminal RING finger motif and a putative coiled-coil domain. A similar murine protein interacts with TNFR-associated factor 1 (TRAF1), TNFR-associated factor 2 (TRAF2), and cylindromatosis. The interaction with TRAF2 inhibits TRAF2-mediated nuclear factor kappa-B, subunit 1 activation that is required for cell activation and protection against apoptosis.[7]

Interactions

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TRAF interacting protein has been shown to interact with FLII,[8] TRAF1[6] and TRAF2.[6]

Role in mitotic DNA synthesis

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Mitotic DNA synthesis (MiDAS) is thought to be a DNA repair mechanism to salvage DNA that has not finished replication during S phase, which may be due to DNA replication stress (RS).[9] Intrinsic sources of RS include transcription-replication conflicts and “difficult-to-replicate’’ regions.[9] Extrinsic RS includes exposure to genotoxic agents, depletion of dNTPs, and premature S phase activity which can occur in precancerous cells after oncogene activation.[9] Some MiDAS pathways require the TRAIP protein to disassemble the replication complex at the stalled replication fork in cases where RS causes the fork to stall during replication.[9]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000183763Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032586Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Hoffmann S, Smedegaard S, Nakamura K, Mortuza GB, Räschle M, Ibañez de Opakua A, et al. (January 2016). "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress". The Journal of Cell Biology. 212 (1): 63–75. doi:10.1083/jcb.201506071. PMC 4700480. PMID 26711499.
  6. ^ a b c Lee SY, Lee SY, Choi Y (April 1997). "TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation". The Journal of Experimental Medicine. 185 (7): 1275–1285. doi:10.1084/jem.185.7.1275. PMC 2196258. PMID 9104814.
  7. ^ a b "Entrez Gene: TRAIP TRAF interacting protein".
  8. ^ Wilson SA, Brown EC, Kingsman AJ, Kingsman SM (August 1998). "TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I". Nucleic Acids Research. 26 (15): 3460–3467. doi:10.1093/nar/26.15.3460. PMC 147727. PMID 9671805.
  9. ^ a b c d Bhowmick R, Hickson ID, Liu Y (October 2023). "Completing genome replication outside of S phase". Molecular Cell. 83 (20): 3596–3607. doi:10.1016/j.molcel.2023.08.023. PMID 37716351.

Further reading

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