Prolactin-inducible (PIP) is a 17kDa glycoprotein that binds to many proteins including fibrinogen, actin, keratin, myosin, immunoglobulin G, CD4, and human zinc-alpha-2 glycoprotein []. It forms a complex with human serum albumin (HSA) in seminal plasma and may affect male fertility/infertility []. It also acts as a factor capable of suppressing T-cell apoptosis through itsinteraction with CD4 [].
This entry represents archaeal Nre proteins. While most archaeal organisms encode only a single Nre protein, some encode two, NreA and NreB.NreA is an archaeal PCNA interacting protein that works together with the UvrABC proteins in repairing DNA damage resulting from exposure to DNA damaging agent MMC. NreA contains a putative PIP motif at its C terminus that is important for its function [].
This conserved region is found in the N-terminal region of archaeal Nre proteins. While most archaeal organisms encode only a single Nre protein, some encode two, NreA and NreB. NreA is an archaeal PCNA interacting protein that works together with the UvrABC proteins in repairing DNA damage resulting from exposure to DNA damaging agent MMC. NreA contains a putative PIP motif at its C terminus that is important for its function [].
This conserved region is found in the C-terminal region of archaeal Nre proteins. While most archaeal organisms encode only a single Nre protein, some encode two, NreA and NreB. NreA is an archaeal PCNA interacting protein that works together with the UvrABC proteins in repairing DNA damage resulting from exposure to DNA damaging agent MMC. NreA contains a putative PIP motif atits C terminus that is important for its function [].
Myotubularin-related protein 14 (MTMR14, also known as Jumpy) belongs to the myotubularin family, whose members are dual-specificity phosphatases that act primarily to dephosphorylate phosphoinositides (PIs). They act specifically on PI3P and PI3,5P2, dephosphorylating them to form PIP and PI5P, respectively []. MTMR14 interacts with early autophagosomes and negatively regulates progression through the steps of autophagy []. It has been linked to the a congenital muscle disorder known as myopathy, centronuclear, 1 (CNM1) [].
Myotubularin-related protein 14 (MTMR14, also known as Jumpy) belongs to the myotubularin family, whose members are dual-specificity phosphatases that act primarily to dephosphorylate phosphoinositides (PIs). They act specifically on PI3P and PI3,5P2, dephosphorylating them to form PIP and PI5P, respectively []. MTMR14 interacts with early autophagosomes and negatively regulates progression through the steps of autophagy []. It has been linked to the a congenital muscle disorder known as myopathy, centronuclear, 1 (CNM1) [].MTMR14 contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an active PTP domain, a SET-interaction domain (SID), a coiled-coil region, and a C-terminal PDZ domain. This entry represents the PH-GRAM domain that binds to phosphoinositide lipid [].
The mature U2 snRNP (small nuclear ribonucleoprotein particle) relies on the spliceosome assembly for its function, which involves the Splicing factor 3a (SF3a), an evolutionary eukaryotic conserved heterotrimeric complex, essential for pre-mRNA splicing []. This complex includes three subunits: SF3a60, SF3a66 and SF3a120 in the human complex, being Prp9, Prp11 and Prp21 the counterparts in Saccharomyces cerevisiae. SF3a60 possess a highly conserved C2H2-type zinc-finger domain at the C-terminal, while Prp9 has two such domains; SF3a66 and Prp11 contain one C2H2-type zinc-finger domain and SF3a120/Prp21 has two suppressor-of-white-apricot and prp21/spp91 (SURP) domains, followed by a short segment of charged residues. The SURP2 domain of SF3a120/Prp21 has a role in SF3a60/Prp9 binding, however, SURP1 domain function is unknown. The yeast structure shows that Prp9 interacts with Prp21 via a bidentate-binding mode, and Prp21 is wrapped around Prp11 [].This entry represents the C-terminal region of SF3a60 subunit (also known as SF3a3 and Spliceosome-associated protein 61 or Prp9 from yeast) from SF3a complex, found in eukaryotes. This domain has two conserved sequence motifs: PIP and CEICG. It contains a zinc-finger domain of the C2H2-type which might be important for RNA binding and protein-protein interactions with components of the SF3b complex [].
