The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Immunoglobulins
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 278: Protein-glutamine gamma-glutamyltransferase 2

Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

There are 22 GO terms relating to "molecular function"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
6 H0VK88 (/IDA) H0VT19 (/IDA) O95932 (/IDA) Q08188 (/IDA) Q6YCI4 (/IDA) Q8BM11 (/IDA)
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
6 A6QP57 (/ISS) D4A5U3 (/ISS) P21980 (/ISS) P21980 (/ISS) P21980 (/ISS) Q08189 (/ISS)
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
6 P08587 (/IPI) P21980 (/IPI) P21980 (/IPI) P21980 (/IPI) Q6P6R6 (/IPI) Q9WVJ6 (/IPI)
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
4 P21980 (/IMP) P21980 (/IMP) P21980 (/IMP) P21981 (/IMP)
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
4 P21981 (/ISO) Q08189 (/ISO) Q6YCI4 (/ISO) Q8BM11 (/ISO)
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
3 A6QP57 (/ISS) D4A5U3 (/ISS) Q08189 (/ISS)
GTP binding GO:0005525
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
2 Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
2 Q6P6R6 (/IC) Q9WVJ6 (/IC)
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
2 Q6P6R6 (/IPI) Q9WVJ6 (/IPI)
Protein-glutamine gamma-glutamyltransferase activity GO:0003810
Catalysis of the reaction: protein glutamine + alkylamine = protein N5-alkylglutamine + NH3. This reaction is the formation of the N6-(L-isoglutamyl)-L-lysine isopeptide, resulting in cross-linking polypeptide chains; the gamma-carboxamide groups of peptidyl-glutamine residues act as acyl donors, and the 6-amino-groups of peptidyl-lysine residues act as acceptors, to give intra- and intermolecular N6-(5-glutamyl)lysine cross-links.
1 O43548 (/TAS)
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
1 Q08188 (/IDA)
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
1 Q08189 (/ISO)
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
1 Q08189 (/ISS)
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
1 Q08188 (/IDA)
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
1 Q08189 (/ISO)
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
1 P21981 (/NAS)
GTP binding GO:0005525
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
1 P21981 (/ISO)
GTP binding GO:0005525
Interacting selectively and non-covalently with GTP, guanosine triphosphate.
1 P21981 (/NAS)
Transaminase activity GO:0008483
Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
1 P08587 (/IDA)
Transaminase activity GO:0008483
Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
1 P21981 (/ISO)
Transferase activity, transferring acyl groups GO:0016746
Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
1 Q08188 (/TAS)
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
1 P21981 (/ISO)

There are 49 GO terms relating to "biological process"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
5 P21980 (/IMP) P21980 (/IMP) P21980 (/IMP) Q6P6R6 (/IMP) Q9WVJ6 (/IMP)
Negative regulation of endoplasmic reticulum calcium ion concentration GO:0032471
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
4 P21980 (/IMP) P21980 (/IMP) P21980 (/IMP) P21981 (/IMP)
Positive regulation of mitochondrial calcium ion concentration GO:0051561
Any process that increases the concentration of calcium ions in mitochondria.
4 P21980 (/IMP) P21980 (/IMP) P21980 (/IMP) P21981 (/IMP)
Peptide cross-linking GO:0018149
The formation of a covalent cross-link between or within protein chains.
3 H0VK88 (/IDA) H0VT19 (/IDA) Q08188 (/IDA)
Peptide cross-linking GO:0018149
The formation of a covalent cross-link between or within protein chains.
3 A6QP57 (/ISS) D4A5U3 (/ISS) Q08189 (/ISS)
Apoptotic cell clearance GO:0043277
The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte.
3 P21980 (/IDA) P21980 (/IDA) P21980 (/IDA)
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
3 P21980 (/ISS) P21980 (/ISS) P21980 (/ISS)
Blood vessel remodeling GO:0001974
The reorganization or renovation of existing blood vessels.
2 Q6P6R6 (/IMP) Q9WVJ6 (/IMP)
Epidermis development GO:0008544
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
2 O43548 (/TAS) Q08189 (/TAS)
Peptide cross-linking GO:0018149
The formation of a covalent cross-link between or within protein chains.
2 P21981 (/TAS) Q08189 (/TAS)
Isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine GO:0018153
The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glutamine to produce N6-(L-isoglutamyl)-L-lysine.
2 Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
2 Q6P6R6 (/IMP) Q9WVJ6 (/IMP)
Positive regulation of smooth muscle cell proliferation GO:0048661
Any process that activates or increases the rate or extent of smooth muscle cell proliferation.
2 Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Positive regulation of inflammatory response GO:0050729
Any process that activates or increases the frequency, rate or extent of the inflammatory response.
2 Q6P6R6 (/IMP) Q9WVJ6 (/IMP)
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
2 Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway GO:0051482
Any process that increases the concentration of calcium ions in the cytosol that occurs as part of a PLC-activating G protein-coupled receptor signaling pathway. G-protein-activated PLC hydrolyses phosphatidylinositol-bisphosphate (PIP2) to release diacylglycerol (DAG) and inositol trisphosphate (IP3). IP3 then binds to calcium release channels in the endoplasmic reticulum (ER) to trigger calcium ion release into the cytosol.
2 Q6P6R6 (/IMP) Q9WVJ6 (/IMP)
Blood vessel remodeling GO:0001974
The reorganization or renovation of existing blood vessels.
1 P21981 (/ISO)
Cellular protein modification process GO:0006464
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
1 Q08188 (/NAS)
Cellular protein modification process GO:0006464
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
1 O43548 (/TAS)
G protein-coupled receptor signaling pathway GO:0007186
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription. The pathway can start from the plasma membrane, Golgi or nuclear membrane (PMID:24568158 and PMID:16902576).
1 P21981 (/TAS)
Phospholipase C-activating G protein-coupled receptor signaling pathway GO:0007200
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
1 Q9WVJ6 (/IDA)
Phospholipase C-activating G protein-coupled receptor signaling pathway GO:0007200
The series of molecular signals generated as a consequence of a G protein-coupled receptor binding to its physiological ligand, where the pathway proceeds with activation of phospholipase C (PLC) and a subsequent increase in the concentration of inositol trisphosphate (IP3) and diacylglycerol (DAG).
1 P21981 (/ISA)
Peptide cross-linking GO:0018149
The formation of a covalent cross-link between or within protein chains.
1 Q08189 (/ISO)
Isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine GO:0018153
The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glutamine to produce N6-(L-isoglutamyl)-L-lysine.
1 P21981 (/ISO)
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
1 Q08188 (/IEP)
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
1 Q08189 (/ISS)
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
1 Q08188 (/TAS)
Hair follicle morphogenesis GO:0031069
The process in which the anatomical structures of the hair follicle are generated and organized.
1 Q08188 (/TAS)
Negative regulation of endoplasmic reticulum calcium ion concentration GO:0032471
Any process that decreases the concentration of calcium ions in the endoplasmic reticulum.
1 P21981 (/ISO)
Hair cell differentiation GO:0035315
The process in which a relatively unspecialized cell acquires specialized features of a hair cell.
1 Q08189 (/TAS)
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
1 P21981 (/ISO)
Positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0043123
Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
1 P21981 (/ISO)
Cell envelope organization GO:0043163
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cell envelope, everything external to, but not including, the cytoplasmic membrane of bacteria, encompassing the periplasmic space, cell wall, and outer membrane if present.
1 Q08188 (/IDA)
Cell envelope organization GO:0043163
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cell envelope, everything external to, but not including, the cytoplasmic membrane of bacteria, encompassing the periplasmic space, cell wall, and outer membrane if present.
1 Q08189 (/ISO)
Cell envelope organization GO:0043163
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the cell envelope, everything external to, but not including, the cytoplasmic membrane of bacteria, encompassing the periplasmic space, cell wall, and outer membrane if present.
1 Q08189 (/ISS)
Apoptotic cell clearance GO:0043277
The recognition and removal of an apoptotic cell by a neighboring cell or by a phagocyte.
1 P21981 (/ISO)
Skin development GO:0043588
The process whose specific outcome is the progression of the skin over time, from its formation to the mature structure. The skin is the external membranous integument of an animal. In vertebrates the skin generally consists of two layers, an outer nonsensitive and nonvascular epidermis (cuticle or skarfskin) composed of cells which are constantly growing and multiplying in the deeper, and being thrown off in the superficial layers, as well as an inner vascular dermis (cutis, corium or true skin) composed mostly of connective tissue.
1 Q08189 (/TAS)
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
1 P21981 (/IMP)
Positive regulation of smooth muscle cell proliferation GO:0048661
Any process that activates or increases the rate or extent of smooth muscle cell proliferation.
1 P21981 (/ISO)
Positive regulation of inflammatory response GO:0050729
Any process that activates or increases the frequency, rate or extent of the inflammatory response.
1 P21981 (/ISO)
Protein homooligomerization GO:0051260
The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
1 P21981 (/ISO)
Protein tetramerization GO:0051262
The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
1 Q08188 (/IDA)
Protein tetramerization GO:0051262
The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
1 Q08189 (/ISO)
Protein tetramerization GO:0051262
The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
1 Q08189 (/ISS)
Positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway GO:0051482
Any process that increases the concentration of calcium ions in the cytosol that occurs as part of a PLC-activating G protein-coupled receptor signaling pathway. G-protein-activated PLC hydrolyses phosphatidylinositol-bisphosphate (PIP2) to release diacylglycerol (DAG) and inositol trisphosphate (IP3). IP3 then binds to calcium release channels in the endoplasmic reticulum (ER) to trigger calcium ion release into the cytosol.
1 P21981 (/ISO)
Positive regulation of mitochondrial calcium ion concentration GO:0051561
Any process that increases the concentration of calcium ions in mitochondria.
1 P21981 (/ISO)
Branching involved in salivary gland morphogenesis GO:0060445
The process in which the branching structure of the salivary gland is generated and organized.
1 P21981 (/IMP)
Salivary gland cavitation GO:0060662
The process in which the solid core of salivary epithelium gives rise to the hollow tube of the gland.
1 P21981 (/IMP)
Cornification GO:0070268
A type of programmed cell death that occurs in the epidermis, morphologically and biochemically distinct from apoptosis. It leads to the formation of corneocytes, i.e. dead keratinocytes containing an amalgam of specific proteins (e.g., keratin, loricrin, SPR and involucrin) and lipids (e.g., fatty acids and ceramides), which are necessary for the function of the cornified skin layer (mechanical resistance, elasticity, water repellence and structural stability).
1 O43548 (/TAS)

There are 24 GO terms relating to "cellular component"

The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.
GO Term Annotations Evidence
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
5 O95932 (/IDA) Q08188 (/IDA) Q6YCI4 (/IDA) Q8BM11 (/IDA) Q9WVJ6 (/IDA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
5 P21980 (/IDA) P21980 (/IDA) P21980 (/IDA) Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Collagen-containing extracellular matrix GO:0062023
An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
5 P21980 (/HDA) P21980 (/HDA) P21980 (/HDA) P21981 (/HDA) Q08189 (/HDA)
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
4 P21980 (/HDA) P21980 (/HDA) P21980 (/HDA) Q08188 (/HDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
3 Q08189 (/ISO) Q6YCI4 (/ISO) Q8BM11 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
3 A6QP57 (/ISS) D4A5U3 (/ISS) Q08189 (/ISS)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
3 P21980 (/IDA) P21980 (/IDA) P21980 (/IDA)
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
3 P21980 (/HDA) P21980 (/HDA) P21980 (/HDA)
Intrinsic component of plasma membrane GO:0031226
The component of the plasma membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
3 P21980 (/IDA) P21980 (/IDA) P21980 (/IDA)
Intrinsic component of plasma membrane GO:0031226
The component of the plasma membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
3 P21980 (/IMP) P21980 (/IMP) P21980 (/IMP)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
2 Q6P6R6 (/IDA) Q9WVJ6 (/IDA)
Cornified envelope GO:0001533
A type of plasma membrane that has been modified through addition of distinct intracellular and extracellular components, including ceramide, found in cornifying epithelial cells (corneocytes).
1 Q08189 (/TAS)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 P21981 (/ISA)
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
1 P21981 (/ISO)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P21981 (/ISO)
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
1 P21981 (/TAS)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 P21981 (/ISO)
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
1 O43548 (/TAS)
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
1 P21981 (/TAS)
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
1 P21981 (/TAS)
Intrinsic component of plasma membrane GO:0031226
The component of the plasma membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane.
1 P21981 (/ISO)
Extrinsic component of cytoplasmic side of plasma membrane GO:0031234
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
1 Q08188 (/IDA)
Extrinsic component of cytoplasmic side of plasma membrane GO:0031234
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
1 Q08189 (/ISO)
Extrinsic component of cytoplasmic side of plasma membrane GO:0031234
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
1 Q08189 (/ISS)
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