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
".
FunFam 334: vesicle-associated membrane protein-associated pro...
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 26 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 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).
|
38 |
A8KA83 (/IPI)
O44782 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
(28 more) |
FFAT motif binding GO:0033149
Interacting selectively and non-covalently with the FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family.
|
20 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(10 more) |
Cadherin binding GO:0045296
Interacting selectively and non-covalently with cadherin, a type I membrane protein involved in cell adhesion.
|
20 |
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
O95292 (/HDA)
(10 more) |
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
20 |
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
(10 more) |
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
Enzyme binding GO:0019899
Interacting selectively and non-covalently with any enzyme.
|
13 |
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
(3 more) |
FFAT motif binding GO:0033149
Interacting selectively and non-covalently with the FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family.
|
13 |
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
(3 more) |
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
|
13 |
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
O95292 (/IPI)
(3 more) |
Beta-tubulin binding GO:0048487
Interacting selectively and non-covalently with the microtubule constituent protein beta-tubulin.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
Protein domain specific binding GO:0019904
Interacting selectively and non-covalently with a specific domain of a protein.
|
8 | O44782 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) Q9P0L0 (/IPI) |
Showing 1 to 10 of 26 entries
There are 53 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 |
---|---|---|
Endoplasmic reticulum to Golgi vesicle-mediated transport GO:0006888
The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
|
20 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(10 more) |
Sphingolipid biosynthetic process GO:0030148
The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
|
20 |
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
(10 more) |
COPII-coated vesicle budding GO:0090114
The evagination of an endoplasmic reticulum membrane, resulting in formation of a COPII-coated vesicle.
|
20 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(10 more) |
Cellular calcium ion homeostasis GO:0006874
Any process involved in the maintenance of an internal steady state of calcium ions at the level of a cell.
|
13 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(3 more) |
Endoplasmic reticulum organization GO:0007029
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
|
13 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(3 more) |
Modulation by virus of host morphology or physiology GO:0019048
The process in which a virus effects a change in the structure or processes of its host organism.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
13 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(3 more) |
IRE1-mediated unfolded protein response GO:0036498
A series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
Positive regulation of viral genome replication GO:0045070
Any process that activates or increases the frequency, rate or extent of viral genome replication.
|
13 |
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
O95292 (/IMP)
(3 more) |
Protein localization to endoplasmic reticulum GO:0070972
A process in which a protein is transported to, or maintained in, a location within the endoplasmic reticulum.
|
10 | Q0VCY1 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q5R601 (/ISS) Q9WV55 (/ISS) Q9Z270 (/ISS) |
Showing 1 to 10 of 53 entries
There are 32 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 |
---|---|---|
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
23 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(13 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
20 |
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
O95292 (/TAS)
(10 more) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
15 |
A5GFS8 (/ISS)
Q0VCY1 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5R601 (/ISS)
Q5U511 (/ISS)
(5 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
14 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(4 more) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
13 |
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
O95292 (/IDA)
(3 more) |
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.
|
9 | Q7KVX5 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9W4N8 (/IDA) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
7 | Q9P0L0 (/HDA) Q9P0L0 (/HDA) Q9P0L0 (/HDA) Q9P0L0 (/HDA) Q9P0L0 (/HDA) Q9P0L0 (/HDA) Q9P0L0 (/HDA) |
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.
|
7 | Q9P0L0 (/TAS) Q9P0L0 (/TAS) Q9P0L0 (/TAS) Q9P0L0 (/TAS) Q9P0L0 (/TAS) Q9P0L0 (/TAS) Q9P0L0 (/TAS) |
Vesicle GO:0031982
Any small, fluid-filled, spherical organelle enclosed by membrane.
|
7 | Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) Q9P0L0 (/IDA) |
Showing 1 to 10 of 32 entries