| RASSF9 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | RASSF9 , P-CIP1, PAMCI, PCIP1, Ras association domain family member 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 610383 MGI: 2384307 HomoloGene: 3976 GeneCards: RASSF9 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Ras association domain-containing protein 9 (RASSF9), also known as PAM COOH-terminal interactor protein 1 (PCIP1) or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor (PAMCI) is a protein that in humans is encoded by the RASSF9 gene. [5]
RASSF9 the N-terminal RASSF family member Ras association (RalGDS/AF-6) domain family (N-terminal) member 9 12q21.31, [6] [7] is one of two new wild type RASSF9 and RASSF10 [7] proteins. Three proteins that interact with a fragment of the PAM cytosolic domain containing signaling switch I and II the RA1 and RA2ras complex. [8] RASSF7, the first member of the N-terminal RASSF family is required for mitosis. [7] RASSF9 is recently found to be involved in regulation of epidermal homeostasis. [9]
The mutant proregion encoding PAM COOH-terminal interactor protein-1 (P-CIP1) is comparable to that of human band 4.1-like TF (blood plasma protein) as a recycling endosomal pathway [6] in microtubule locations, does NOT bind RasGTP. [10] Specificity of interaction may all be related to microtubule locations of the endosomal-lysosomal system localized within the centrosome with Transferrin and different Ras proteins or with that one (N-Ras), but on the other hand, it interacts with three [11] (Ha-Ras, Ki-Ras, [12] and Rap [13] ) residues function, [14] blocked by a mutation that affects Ras effector function [15] is the critical product of the t (6:11) abnormality associated with some human leukemias. [12] Phosphatidylinositol-3-kinase make contacts with both (6:11) switch I and II [12] regions of ras [8] and yeast adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro. [16] Ras-interacting residues, are appreciably different from that of RalGDS -RBD [17] through their C-terminal Ras-binding domains (RBD). [18] Such outliers as afadin/AF-6 and Rin1 [16] were found to inhibit the binding of Raf to Ras. [14] Adenylyl cyclase molecules carrying these mutations are rendered unactivatable by Ras in vitro with the Ras-associating domain-RA, [16] not all RA domains bind RasGTP it is a primary Ras-binding site.
Adenylate cyclase is an enzyme with systematic name ATP diphosphate-lyase . It catalyzes the following reaction:
RAF proto-oncogene serine/threonine-protein kinase, also known as proto-oncogene c-RAF or simply c-Raf or even Raf-1, is an enzyme that in humans is encoded by the RAF1 gene. The c-Raf protein is part of the ERK1/2 pathway as a MAP kinase (MAP3K) that functions downstream of the Ras subfamily of membrane associated GTPases. C-Raf is a member of the Raf kinase family of serine/threonine-specific protein kinases, from the TKL (Tyrosine-kinase-like) group of kinases.
Signal recognition particle (SRP) receptor, also called the docking protein, is a dimer composed of 2 different subunits that are associated exclusively with the rough ER in mammalian cells. Its main function is to identify the SRP units. SRP is a molecule that helps the ribosome-mRNA-polypeptide complexes to settle down on the membrane of the endoplasmic reticulum.
The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).
In enzymology, a peptidylglycine monooxygenase (EC 1.14.17.3) is an enzyme that catalyzes the chemical reaction
RAS p21 protein activator 1 or RasGAP, also known as RASA1, is a 120-kDa cytosolic human protein that provides two principal activities:
Epidermal growth factor receptor substrate 15 is a protein that in humans is encoded by the EPS15 gene.
C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene. CtBP1 is one of two CtBP proteins, the other protein being CtBP2.
Peptidyl-glycine alpha-amidating monooxygenase, or PAM, is an enzyme that catalyzes the conversion of an n+1 residue long peptide with a C-terminal glycine into an n-residue peptide with a terminal amide group. In the process, one molecule of O2 is consumed and the glycine residue is removed from the peptide and converted to glyoxylic acid.
RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene.
Ral guanine nucleotide dissociation stimulator is a protein that is encoded by the RALGDS gene in humans.
Adenylyl cyclase type 5 is an enzyme that in humans is encoded by the ADCY5 gene.
Centromere protein C 1 is a protein that in humans is encoded by the CENPC1 gene.
Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the RALB gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.
Probable E3 ubiquitin-protein ligase MYCBP2 also known as myc-binding protein 2 or protein associates with myc (PAM) is an enzyme that in humans is encoded by the MYCBP2 gene.
Adenylyl cyclase-associated protein 1 is an enzyme that in humans is encoded by the CAP1 gene.
Ras association domain-containing protein 2 is a protein that in humans is encoded by the RASSF2 gene.
Ras association domain-containing protein 8 is a protein that in humans is encoded by the RASSF8 gene.
Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain or through protein–protein interactions with membrane-associated protein complexes Some members of this family have been shown to facilitate protein sorting.
In molecular biology, the cyclase-associated protein family (CAP) is a family of highly conserved actin-binding proteins present in a wide range of organisms including yeast, flies, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium discoideum, CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly. In mammals, there are two different CAPs that share 64% amino acid identity.
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