This entry represents a group of plant proteins, including VAN3-binding protein (VAB, also known as FORKED1 or AT3G63300) from Arabidopsis. FORKED1 is a PH domain protein required for PIN1 localization in developing leaf veins []. It interacts with SCARFACE/VAN3 (SFC), an ADP ribosylation factor GTPase-activating protein (ARF-GAP) important for vein patterning [, ].
This domain describes a pleckstrin homology (PH)-like region found in several plant proteins, including VAN3-binding protein from Arabidopsis thaliana (also known as FORKED1), a component of the auto-regulatory loop which enables auxin canalisation by recruitment of the PIN1 auxin efflux protein to the cell membrane [].
This domain can be found at the N-terminal end of several plant proteins, including VAN3-binding protein from Arabidopsis thaliana (also known as FORKED1), a component of the auto-regulatory loop which enables auxin canalisation by recruitment of the PIN1 auxin efflux protein to the cell membrane []. This domain is frequently found on proteins containing at the C terminus.
This superfamily represents the peptidyl-prolyl cis-trans isomerase domain found in a wide range of proteins, including trigger factor [, ], FK506-binding proteins [, ], proteins from the parvulin family such as Par10 from E.coli, Pin1 and Par14 from human or Pin from plants [], chaperone SurA [, ]and foldase protein PrsA []. This domain catalyses cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding.This domain consists of a flattened β-barrel of four/six-stranded, antiparallel sheets, surrounded by four/six α-helices.
This entry represents Fcp1 and its homologues, including CTDP1 from humans and CPL1/2/3/4/5 from Arabidopsis. They are carboxy-terminal domain (CTD) phosphatases. CPL1 has been shown to interact with two NMD (nonsense-mediated decay) factors, eIF4AIII and UPF3, and is involved in the dephosphorylation of eIF4AIII []. CPL4 functions as a pol II CTD phosphatase and has been shown to dephosphorylate both Ser2- and Ser5-PO(4) of CTD in vitro []. Budding yeast Fcp1 has been shown to dephosphorylate RNA polymerase (RNAP) II subunit, and this interaction is modulated by the Pin1 protein [].
The function of nuclear protein Sp140 is not known, though it contains several chromatin related modules such as plant homeodomain (PHD), bromodomain (BRD) and SAND domain, which suggests a role in chromatin-mediated regulation of gene expression []. It also harbours a nuclear localisation signal and a dimerisation domain (HSR or CARD domain). The PHD finger of Sp140 presents an atypical fold which does not bind to histone H3 tails but binds to peptidylprolyl isomerase Pin1. Pin1 catalyses the isomerisation of a phospho-Threonine-Proline bond in Sp140-PHD and thus may modulate Sp140 function [].Human Sp140 is an interferon inducible nuclear leukocyte-specific protein that may be involved in the pathogenesis of acute promyelocytic leukemia and viral infection []. It localises to LYSP100-associated nuclear dots and is also a component of the promyelocytic leukemia nuclear body (PML-NBs) [, ]. The Sp140 locus has been identified as a lymphocytic leukemia (CLL) risk locus [].This family also includes protein Sp140-like (SP140L) [].
This entry includes a group of nuclear dot-associated proteins, including Sp110/Sp140/Sp140L from humans. They are proteins with a constituent of nuclear domains, also known as nuclear dots (NDs). Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region) [].Sp110 is a leukocyte-specific component of the nuclear body []. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells []. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers [, ]. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population []. The function of nuclear protein Sp140 is not known, though it contains several chromatin related modules such as plant homeodomain (PHD), bromodomain (BRD) and SAND domain, which suggests a role in chromatin-mediated regulation of gene expression []. It also harbours a nuclear localisation signal and a dimerisation domain (HSR or CARD domain). The PHD finger of Sp140 presents an atypical fold which does not bind to histone H3 tails but binds to peptidylprolyl isomerase Pin1. Pin1 catalyses the isomerisation of a phospho-Threonine-Proline bond in Sp140-PHD and thus may modulate Sp140 function [].Human Sp140 is an interferon inducible nuclear leukocyte-specific protein that may be involved in the pathogenesis of acute promyelocytic leukemia and viral infection []. It localises to LYSP100-associated nuclear dots and is also a component of the promyelocytic leukemia nuclear body (PML-NBs) [, ]. The Sp140 locus has been identified as a lymphocytic leukemia (CLL) risk locus [].This family also includes protein Sp140-like (SP140L) [].
