The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"SecY subunit domain
".
FunFam 2: Transport Sec61 subunit alpha isoform 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 13 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 |
---|---|---|
Calcium channel activity GO:0005262
Enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
|
129 |
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
(119 more) |
Ribosome binding GO:0043022
Interacting selectively and non-covalently with any part of a ribosome.
|
73 |
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
P61620 (/IDA)
(63 more) |
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).
|
64 |
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
(54 more) |
Calcium channel activity GO:0005262
Enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
|
43 |
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
(33 more) |
Calcium channel activity GO:0005262
Enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Transmembrane transporter activity GO:0022857
Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.
|
43 |
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
P61620 (/EXP)
(33 more) |
Ribosome binding GO:0043022
Interacting selectively and non-covalently with any part of a ribosome.
|
43 |
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
(33 more) |
Signal sequence binding GO:0005048
Interacting selectively and non-covalently with a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
Protein transmembrane transporter activity GO:0008320
Enables the transfer of a protein from one side of a membrane to the other.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
P-P-bond-hydrolysis-driven protein transmembrane transporter activity GO:0015450
Primary active carrier-mediated transport of a protein across a membrane, driven by the hydrolysis of the diphosphate bond of inorganic pyrophosphate, ATP, or another nucleoside triphosphate. The transport protein may or may not be transiently phosphorylated, but the substrate is not phosphorylated.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
P-P-bond-hydrolysis-driven protein transmembrane transporter activity GO:0015450
Primary active carrier-mediated transport of a protein across a membrane, driven by the hydrolysis of the diphosphate bond of inorganic pyrophosphate, ATP, or another nucleoside triphosphate. The transport protein may or may not be transiently phosphorylated, but the substrate is not phosphorylated.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
Peptide transmembrane transporter activity GO:1904680
Enables the transfer of a peptide from one side of a membrane to the other.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
P-P-bond-hydrolysis-driven protein transmembrane transporter activity GO:0015450
Primary active carrier-mediated transport of a protein across a membrane, driven by the hydrolysis of the diphosphate bond of inorganic pyrophosphate, ATP, or another nucleoside triphosphate. The transport protein may or may not be transiently phosphorylated, but the substrate is not phosphorylated.
|
1 | Q54XK2 (/ISS) |
There are 34 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 |
---|---|---|
Pronephric nephron development GO:0039019
The process whose specific outcome is the progression of the pronephric nephron over time, from its formation to the mature structure. A pronephric nephron is the functional unit of the pronephros.
|
147 |
P38377 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
(137 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
132 |
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
(122 more) |
Protein targeting to ER GO:0045047
The process of directing proteins towards the endoplasmic reticulum (ER) using signals contained within the protein. One common mechanism uses a 16- to 30-residue signal sequence, typically located at the N-terminus of the protein and containing positively charged amino acids followed by a continuous stretch of hydrophobic residues, which directs the ribosome to the ER membrane and initiates transport of the growing polypeptide across the ER membrane.
|
102 |
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
(92 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
52 |
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P32915 (/IMP)
P61619 (/IMP)
(42 more) |
Pronephric nephron development GO:0039019
The process whose specific outcome is the progression of the pronephric nephron over time, from its formation to the mature structure. A pronephric nephron is the functional unit of the pronephros.
|
46 |
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
P61620 (/IMP)
(36 more) |
Cotranslational protein targeting to membrane GO:0006613
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
|
43 |
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
(33 more) |
Cotranslational protein targeting to membrane GO:0006613
The targeting of proteins to a membrane that occurs during translation. The transport of most secretory proteins, particularly those with more than 100 amino acids, into the endoplasmic reticulum lumen occurs in this manner, as does the import of some proteins into mitochondria.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
SRP-dependent cotranslational protein targeting to membrane GO:0006614
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
|
43 |
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
(33 more) |
SRP-dependent cotranslational protein targeting to membrane GO:0006614
The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Posttranslational protein targeting to endoplasmic reticulum membrane GO:0006620
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
|
43 |
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
(33 more) |
Posttranslational protein targeting to endoplasmic reticulum membrane GO:0006620
The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 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.
|
43 |
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
P61619 (/IMP)
(33 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.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Response to interferon-gamma GO:0034341
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon-gamma is also known as type II interferon.
|
43 |
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
P61621 (/IEP)
(33 more) |
SRP-dependent cotranslational protein targeting to membrane, translocation GO:0006616
The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
Ubiquitin-dependent ERAD pathway GO:0030433
The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.
|
9 | P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) P32915 (/IPI) |
Retrograde protein transport, ER to cytosol GO:0030970
The directed movement of unfolded or misfolded proteins from the endoplasmic reticulum to the cytosol through the translocon.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
Posttranslational protein targeting to membrane, translocation GO:0031204
The process in which a protein translocates through the ER membrane posttranslationally.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
Protein transmembrane import into intracellular organelle GO:0044743
The directed movement of proteins into an intracellular organelle, across a membrane.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
Misfolded protein transport GO:0070843
The directed movement of misfolded proteins in a cell, including the movement of proteins between specific compartments or structures within a cell.
|
9 | P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) P32915 (/IMP) |
Dorsal closure GO:0007391
The process during Drosophila embryogenesis whereby the ectodermal cells of the lateral epithelium stretch in a coordinated fashion to internalize the amnioserosa cells and close the embryo dorsally.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Head involution GO:0008258
Movement of the anterior ectoderm to the interior of the embryo.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Negative regulation of autophagy GO:0010507
Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Positive regulation of cell death GO:0010942
Any process that increases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Positive regulation of iron ion transmembrane transport GO:0034761
Any process that activates or increases the frequency, rate or extent of the directed movement of iron ions from one side of a membrane to the other by means of some agent such as a transporter or pore.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Cuticle development GO:0042335
The chemical reactions and pathways resulting in the formation of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Positive regulation of viral entry into host cell GO:0046598
Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Cellular response to virus GO:0098586
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a virus.
|
8 | Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) Q8STG9 (/IMP) |
Habenula development GO:0021986
The progression of the habenula over time from its initial formation until its mature state. The habenula is the group of nuclei that makes up the stalk of the pineal gland.
|
3 | Q90ZM2 (/IMP) Q90ZM2 (/IMP) Q90ZM2 (/IMP) |
Protein transport GO:0015031
The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
|
2 | Q9P8E3 (/IMP) Q9P8E3 (/IMP) |
Pronephros development GO:0048793
The process whose specific outcome is the progression of the pronephros over time, from its formation to the mature structure. In mammals, the pronephros is the first of the three embryonic kidneys to be established and exists only transiently. In lower vertebrates such as fish and amphibia, the pronephros is the fully functional embryonic kidney and is indispensable for larval life.
|
2 | Q90YL4 (/IMP) Q90YL4 (/IMP) |
Protein targeting to ER GO:0045047
The process of directing proteins towards the endoplasmic reticulum (ER) using signals contained within the protein. One common mechanism uses a 16- to 30-residue signal sequence, typically located at the N-terminus of the protein and containing positively charged amino acids followed by a continuous stretch of hydrophobic residues, which directs the ribosome to the ER membrane and initiates transport of the growing polypeptide across the ER membrane.
|
1 | P38377 (/IDA) |
There are 22 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 membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
149 |
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
P61620 (/ISS)
(139 more) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
102 |
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
P61619 (/ISS)
(92 more) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
73 |
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
P61619 (/TAS)
(63 more) |
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
|
51 |
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
P61621 (/IDA)
(41 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
45 |
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
(35 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
43 |
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
P61619 (/IDA)
(33 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Rough endoplasmic reticulum GO:0005791
The rough (or granular) endoplasmic reticulum (ER) has ribosomes adhering to the outer surface; the ribosomes are the site of translation of the mRNA for those proteins which are either to be retained within the cisternae (ER-resident proteins), the proteins of the lysosomes, or the proteins destined for export from the cell. Glycoproteins undergo their initial glycosylation within the cisternae.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
43 |
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
P61620 (/ISO)
(33 more) |
Phagocytic vesicle membrane GO:0030670
The lipid bilayer surrounding a phagocytic vesicle.
|
43 |
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
P61620 (/TAS)
(33 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).
|
17 |
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
P32915 (/HDA)
Q8STG9 (/HDA)
(7 more) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
12 |
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
O80774 (/IPI)
(2 more) |
Sec61 translocon complex GO:0005784
A translocon complex that contains a core heterotrimer of conserved alpha, beta and gamma subunits, and may contain additional proteins (translocon-associated proteins or TRAPs); in budding yeast the core proteins are Sec61p, Sbh1p, and Sss1p. The Sec61 translocon complex functions in cotranslational and posttranslational translocation events.
|
9 | P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) P32915 (/IDA) |
Endomembrane system GO:0012505
A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
|
8 | Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) Q8STG9 (/HDA) |
Fusome GO:0045169
A large intracellular spectrin-rich structure that has been found in insect germline cells and mammalian hematopoietic cells. The fusome is an elongated, branched structure, formed from the spherical spectrosome organelle.
|
8 | Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) Q8STG9 (/IDA) |
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.
|
4 | Q8RWJ5 (/IDA) Q8RWJ5 (/IDA) Q9P8E3 (/IDA) Q9P8E3 (/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.
|
2 | Q8RWJ5 (/IDA) Q8RWJ5 (/IDA) |
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.
|
2 | Q8RWJ5 (/IDA) Q8RWJ5 (/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).
|
1 | Q9ZV90 (/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).
|
1 | Q54XK2 (/ISS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P38377 (/TAS) |
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | P38377 (/IDA) |