These GTPases are classified into three groups: the small 47-KD immunity-related GTPases (IRGs), the Mx proteins (MX1, MX2), and the large 65- to 67-kd GTPases.
protein | Protein subunit | Protein-protein interaction | Hfq protein | protein domain | Protein-protein_interaction | Protein Data Bank | RNA-binding protein | Binding of Isaac | Promyelocytic leukemia protein | G protein | binding | Wiskott–Aldrich syndrome protein | Protein G | protein dimer | Protein A | C-reactive protein | Bone morphogenetic protein 2 | AMP-activated protein kinase | Transmembrane protein | The Binding of Isaac | Tau protein | Sterol regulatory element-binding protein | SR protein | Rab escort protein | Protein structure | protein structure | Protein phosphatase 2 | protein kinase | Protein Information Resource |
Fragile X syndrome disease are implicated to be regulated by the FMRP, a RNA-binding protein.
It inhibits the action of C4, more specifically the classical and the lectin pathways.
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C4BP accelerates decay of C3-convertase and is a cofactor for serine protease factor I which cleaves C4b and C3b.
At least one type of autosomal dominant cone-rod dystrophy is caused by mutations in the guanylate cyclase 2D gene (GUCY2D) on chromosome 17.
DNA damage-binding protein is a protein complex that is responsible for repair of UV-damaged DNA.
An interaction with a novel RNA-binding protein MtRBP1 (Medicago truncatula RNA-binding protein 1) investigated in the development of Root nodule suggests ENOD40 has a function of cytoplasmic relocalization of nuclear proteins.
Epimerisation can be spontaneous (generally a slow process), or catalyzed by enzymes, e.g. the epimerization between the sugars N-acetylglucosamine and N-acetylmannosamine, which is catalyzed by Renin-Binding Protein.
In human cells, in high-iron condition, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2.
Normal serum levels of growth hormone Binding Protein 3 may rule out growth hormone insensitivities, like those seen in Laron syndrome.
The hsrω-n transcript directly or indirectly affects the localization/stability/activity of a variety of proteins including hnRNPs, Sxl, Hsp83, cAMP response element binding binding protein (CBP), Drosophila inhibitor of apoptosis protein 1 (DIAP1), JNK-signalling members, proteasome constituents, lamin C, ISWI, HP1 and poly(ADP)-ribose polymerase.
This gene is a member of the Insulin-like growth factor-binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a type-I thyroglobulin domain.
In 1993, their postdoctoral trainees, Wang Xiaodong and Michael Briggs, purified the Sterol Regulatory Element-Binding Proteins (SREBPs), a family of membrane-bound transcription factors.
This subfamily consists of PCTP, StarD7, StarD10 and collagen type IV alpha-3-binding protein or StarD11, all of which bind phosphatidylcholine except for StarD11 which prefers ceramide.
Polypyrimidine tract-binding protein is an RNA-binding protein, also known as PTB or hnRNP I. PTB functions mainly as a splicing regulator, although it is also involved in alternative 3' end processing, mRNA stability and RNA localization.
Poly(A)-binding protein (PABP) binds to a long poly(A) tail and mediates the interaction between EIF4E and EIF4G which encourages the initiation of translation.
In the circulation, Protein S exists in two forms: a free form and a complex form bound to complement protein C4b-binding protein (C4BP).
Ribonomics is the study of ribonucleic acids (RNAs) associated with RNA-binding proteins (RBPs).
Plasminogen activator inhibitor 1 RNA-binding protein (serbp1, not to be confused with srebp1) is a protein that in humans is encoded by the SERBP1 gene.
This releases the cytoplasmic portion of SREBP, which then travels to the nucleus where it activates transcription of target genes (e.g. LDL receptor gene)
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In addition to S1P and S2P, the regulated release of transcriptionally active SREBP requires the cholesterol-sensing protein SREBP cleavage activating protein (Scap), which forms a complex with SREBP owing to interaction between their respective carboxy-terminal domains.
Calbindin-D9k (S100G) is found in mammalian intestine and calbindin-D28k is in avian intestine and in mammalian kidney and other tissues.