827 Risultati per: "Masks"

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).

Supplier: Bioss

Mediates B-cell B-cell interactions. May be involved in the localisation of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

Supplier: ProSci Inc.

Sialic acid-binding Ig-like lectin 9(Siglec 9) is expressed by peripheral blood leukocytes (neutrophils and monocytes but not eosinophils), and found in liver, fetal liver, bone marrow, placenta, spleen and in lower levels in skeletal muscle, fetal brain and so on. It is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It also binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

Supplier: ProSci Inc.

Sialic acid-binding Ig-like lectin 5 (SIGLEC5) is also known as CD33 antigen-like 2 (CD33L2), Obesity-binding protein 2 (OB-BP2), CD antigen CD170, which belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC5 / CD170 is expressed by monocytic / myeloid lineage cells. SIGLEC-5 / CD33-L2 binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (13). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation. Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins. The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues. MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA. The gene encoding human MSY2 maps to chromosome 17p11.2-13.1. YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle. MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element.

Supplier: Bioss

MSY2 and YB-2 (MSY3,4) belong to the Y-box family of multifunctional proteins that regulate both transcription and translation (1–3). Y-box proteins interact with a wide variety of nucleic acid structures to act as transcription factors and mRNA masking proteins (1). The modular structure of Y-box proteins includes a highly conserved N-terminal cold-shock domain (CSD, equivalent to the bacterial cold-shock proteins) and four basic C-terminal domains containing arginine clusters and aromatic residues (4). MSY2 is expressed in testis and ovary where it may repress translation of parental mRNA (5,6). The gene encoding human MSY2 maps to chromosome 17p11.2-13.1 (5). YB-2 (MSY3,4 in mouse) is also known as DNA binding protein A and is highly expressed in the testis, heart and muscle (7,8). MSY2 and YB-2 bind to the consensus sequence 5'-UCCAUCA-3' contained in the Y-box element (9).

Supplier: ProSci Inc.

Sialic acid-binding Ig-like lectin 6 (SIGLEC6) is also known as CD antigen CD327, CD33 antigen-like 1 (CD33L or CD33L1), Obesity-binding protein 1 (OB-BP1). SIGLEC6 belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family, which contains two Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain. SIGLEC6 mediates sialic-acid dependent binding to cells. SIGLEC6 binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

Supplier: ProSci Inc.

Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

Supplier: ProSci Inc.

Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2, 6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

Supplier: Cayman Chemical

Nuclear Factor-κB (NF-κB) is sequestered in the cytoplasm by the IκB family of inhibitory proteins that mask the nuclear localization signal of NF-κB, thereby preventing translocation of NF-κB to the nucleus. External stimuli such as tumor necrosis factor or other cytokines result in phosphorylation and degradation of IκB, releasing NF-κB dimers. NF-κB dimers subsequently translocate to the nucleus and activate target genes. Synthesis of IκBα is autoregulated. IκB proteins are phosphorylated by IκB kinase complex consisting of at least three proteins, IKK1/α, IKK2/β, and IKK3/γ. IKKγ preferentially interacts with IKKβ and is required for activation of IKK complex. IKKγ is also known as NF-κB essential modulator (NEMO). The human T-cell leukemia virus type I Tax oncoprotein that activates NF-κB binds neither to IKKα nor IKKβ, but complexes directly with IKKγ. This suggests that IKKγ may be a key molecule acting as an adapter for oncoprotein specific signaling to IKKα and IKKβ.

Supplier: ProSci Inc.

CD22 mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. [UniProt].

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

Supplier: Bioss

Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.