http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID293968

Outgoing Links

Predicate Object
abstract PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty. This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.
title SPRY_PRY_C-I_1
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12047658
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26966656
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24190618
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21475573
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25137805
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30969298
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25129834
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2686446
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3867492
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16303281
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25536074
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25129557
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19487557
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25602717
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1801348
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12698319
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16319924
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8BJE2
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ6UXG8
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ6UX41

Total number of triples: 23.