PMID- 7639698
OWN - NLM
STAT- MEDLINE
DCOM- 19950913
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 309 ( Pt 3)
IP  - Pt 3
DP  - 1995 Aug 1
TI  - Association of a RING finger protein with the cytoplasmic domain of the human 
      type-2 tumour necrosis factor receptor.
PG  - 825-9
AB  - A human gene encoding a protein that specifically binds to the intracellular 
      domain of the 75 kDa type-2 tumour necrosis factor (TNF) receptor (TNFR-2IC) has 
      been identified using the yeast-based two-hybrid system. The N-terminal half of 
      the TNF receptor-associated protein (TRAP) contains RING finger and zinc finger 
      motifs often found in DNA-binding proteins including transcription factors. The 
      2.4 kb TRAP mRNA was barely detectable, if present at all, in lung, and variably 
      expressed in heart, liver, placenta, brain, skeletal muscle, kidney and the 
      pancreas; interestingly, the TRAP was more highly expressed in transformed cell 
      lines than in normal tissues. This observation may be consistent with a role for 
      this TRAP in promoting or regulating cellular proliferation. After in vitro 
      transcription/translation and 35S labelling the TRAP was precipitated using a 
      fusion protein consisting of glutathione S-transferase and the intracellular 
      domain of TNFR-2 (TNFR-2IC), which showed that the two proteins directly interact 
      in a mammalian cell-free system and also that identification of the TRAP was not 
      an artifact of the two-hybrid system. By using truncated TNFR-2ICs for in vitro 
      precipitation of 35S-TRAP, it was shown that the C-terminal half of the TNFR-2IC 
      contains the domain necessary for interaction with TRAP. The TRAP identified in 
      the present study shares considerable homology with, and may be the human 
      homologue of, a mouse protein, TNF receptor-associated factor 2 (TRAF2), that 
      binds mouse TNFR-2.
FAU - Song, H Y
AU  - Song HY
AD  - Department of Physiology and Biophysics, Indiana University School of Medicine, 
      Indianapolis 46202, USA.
FAU - Donner, D B
AU  - Donner DB
LA  - eng
SI  - GENBANK/U12597
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Receptors, Tumor Necrosis Factor)
RN  - 147205-72-9 (CD40 Ligand)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CD40 Ligand
MH  - DNA, Complementary
MH  - Humans
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - RNA, Messenger/genetics/metabolism
MH  - Receptors, Tumor Necrosis Factor/*metabolism
MH  - Sequence Homology, Amino Acid
PMC - PMC1135706
EDAT- 1995/08/01 00:00
MHDA- 1995/08/01 00:01
PMCR- 1996/02/01
CRDT- 1995/08/01 00:00
PHST- 1995/08/01 00:00 [pubmed]
PHST- 1995/08/01 00:01 [medline]
PHST- 1995/08/01 00:00 [entrez]
PHST- 1996/02/01 00:00 [pmc-release]
AID - 10.1042/bj3090825 [doi]
PST - ppublish
SO  - Biochem J. 1995 Aug 1;309 ( Pt 3)(Pt 3):825-9. doi: 10.1042/bj3090825.