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: waiting to be named.

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.
« Back to all FunFams

FunFam 2: probable E3 ubiquitin-protein ligase MID2

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 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).
18 O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI)
(8 more)
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
17 O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP)
(7 more)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
17 O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA)
(7 more)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
17 O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA)
(7 more)
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
17 O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI)
(7 more)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
15 O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI)
(5 more)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
15 O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI) O15344 (/IPI)
(5 more)
Microtubule binding GO:0008017
Interacting selectively and non-covalently with microtubules, filaments composed of tubulin monomers.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Protein homodimerization activity GO:0042803
Interacting selectively and non-covalently with an identical protein to form a homodimer.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
2 O70583 (/ISO) P82457 (/ISO)
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
1 O95361 (/IDA)
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
1 Q99PP9 (/ISO)
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
1 Q5R760 (/ISS)
Interleukin-1 binding GO:0019966
Interacting selectively and non-covalently with interleukin-1.
1 O95361 (/IPI)
Interleukin-1 binding GO:0019966
Interacting selectively and non-covalently with interleukin-1.
1 Q99PP9 (/ISO)
Interleukin-1 binding GO:0019966
Interacting selectively and non-covalently with interleukin-1.
1 Q5R760 (/ISS)
NACHT domain binding GO:0032089
Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs.
1 O95361 (/IPI)
NACHT domain binding GO:0032089
Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs.
1 Q99PP9 (/ISO)
NACHT domain binding GO:0032089
Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs.
1 Q5R760 (/ISS)

There are 50 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
Protein localization to microtubule GO:0035372
A process in which a protein is transported to, or maintained at, a microtubule.
17 O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP)
(7 more)
Microtubule cytoskeleton organization GO:0000226
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
15 O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS)
(5 more)
Pattern specification process GO:0007389
Any developmental process that results in the creation of defined areas or spaces within an organism to which cells respond and eventually are instructed to differentiate.
15 O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS)
(5 more)
Positive regulation of stress-activated MAPK cascade GO:0032874
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
15 O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP) O15344 (/IMP)
(5 more)
Interferon-gamma-mediated signaling pathway GO:0060333
A series of molecular signals initiated by the binding of interferon-gamma to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription. Interferon gamma is the only member of the type II interferon found so far.
15 O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS)
(5 more)
Protein localization to microtubule GO:0035372
A process in which a protein is transported to, or maintained at, a microtubule.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/ISO)
Negative regulation of microtubule depolymerization GO:0007026
Any process that stops, prevents, or reduces the frequency, rate or extent of microtubule depolymerization; prevention of depolymerization of a microtubule can result from binding by 'capping' at the plus end (e.g. by interaction with another cellular protein of structure) or by exposing microtubules to a stabilizing drug such as taxol.
2 O70583 (/IGI) P82457 (/IGI)
Positive regulation of autophagy GO:0010508
Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
2 Q9UJV3 (/IMP) Q9UJV3 (/IMP)
Positive regulation of stress-activated MAPK cascade GO:0032874
Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade.
2 O70583 (/ISO) P82457 (/ISO)
Negative regulation of viral transcription GO:0032897
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
2 Q9UJV3 (/IDA) Q9UJV3 (/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 Q9UJV3 (/IDA) Q9UJV3 (/IDA)
Innate immune response GO:0045087
Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
2 Q9UJV3 (/IDA) Q9UJV3 (/IDA)
Negative regulation of viral entry into host cell GO:0046597
Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell.
2 Q9UJV3 (/IDA) Q9UJV3 (/IDA)
Positive regulation of DNA-binding transcription factor activity GO:0051091
Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
2 Q9UJV3 (/IMP) Q9UJV3 (/IMP)
Positive regulation of NF-kappaB transcription factor activity GO:0051092
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
2 Q9UJV3 (/IMP) Q9UJV3 (/IMP)
Negative regulation of viral release from host cell GO:1902187
Any process that stops, prevents or reduces the frequency, rate or extent of viral release from host cell.
2 Q9UJV3 (/IDA) Q9UJV3 (/IDA)
Positive regulation of autophagy GO:0010508
Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
1 Q9QUS6 (/ISO)
Positive regulation of autophagy GO:0010508
Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
1 Q9QUS6 (/ISS)
Response to retinoic acid GO:0032526
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 a retinoic acid stimulus.
1 O95361 (/IEP)
Response to retinoic acid GO:0032526
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 a retinoic acid stimulus.
1 Q5R760 (/ISS)
Negative regulation of viral transcription GO:0032897
Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.
1 Q9QUS6 (/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 Q9QUS6 (/ISO)
Histone H3 acetylation GO:0043966
The modification of histone H3 by the addition of an acetyl group.
1 O95361 (/IDA)
Histone H3 acetylation GO:0043966
The modification of histone H3 by the addition of an acetyl group.
1 Q99PP9 (/ISO)
Histone H3 acetylation GO:0043966
The modification of histone H3 by the addition of an acetyl group.
1 Q5R760 (/ISS)
Histone H4 acetylation GO:0043967
The modification of histone H4 by the addition of an acetyl group.
1 O95361 (/IDA)
Histone H4 acetylation GO:0043967
The modification of histone H4 by the addition of an acetyl group.
1 Q99PP9 (/ISO)
Histone H4 acetylation GO:0043967
The modification of histone H4 by the addition of an acetyl group.
1 Q5R760 (/ISS)
Innate immune response GO:0045087
Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
1 Q9QUS6 (/ISO)
Positive regulation of keratinocyte differentiation GO:0045618
Any process that activates or increases the frequency, rate or extent of keratinocyte differentiation.
1 O95361 (/IDA)
Positive regulation of keratinocyte differentiation GO:0045618
Any process that activates or increases the frequency, rate or extent of keratinocyte differentiation.
1 Q99PP9 (/ISO)
Positive regulation of keratinocyte differentiation GO:0045618
Any process that activates or increases the frequency, rate or extent of keratinocyte differentiation.
1 Q5R760 (/ISS)
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
1 O95361 (/IDA)
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
1 Q99PP9 (/ISO)
Positive regulation of transcription, DNA-templated GO:0045893
Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.
1 Q5R760 (/ISS)
Negative regulation of viral entry into host cell GO:0046597
Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell.
1 Q9QUS6 (/ISO)
Response to organophosphorus GO:0046683
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 organophosphorus stimulus. Organophosphorus is a compound containing phosphorus bound to an organic molecule; several organophosphorus compounds are used as insecticides, and they are highly toxic cholinesterase inhibitors.
1 O95361 (/IEP)
Response to organophosphorus GO:0046683
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 organophosphorus stimulus. Organophosphorus is a compound containing phosphorus bound to an organic molecule; several organophosphorus compounds are used as insecticides, and they are highly toxic cholinesterase inhibitors.
1 Q5R760 (/ISS)
Positive regulation of retinoic acid receptor signaling pathway GO:0048386
Any process that activates or increases the frequency, rate or extent of retinoic acid receptor signaling pathway activity.
1 O95361 (/IDA)
Positive regulation of retinoic acid receptor signaling pathway GO:0048386
Any process that activates or increases the frequency, rate or extent of retinoic acid receptor signaling pathway activity.
1 Q99PP9 (/ISO)
Positive regulation of retinoic acid receptor signaling pathway GO:0048386
Any process that activates or increases the frequency, rate or extent of retinoic acid receptor signaling pathway activity.
1 Q5R760 (/ISS)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
1 O95361 (/IMP)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
1 Q99PP9 (/ISO)
Positive regulation of interleukin-1 beta secretion GO:0050718
Any process that activates or increases the frequency, rate or extent of the regulated release of interleukin-1 beta from a cell.
1 Q5R760 (/ISS)
Positive regulation of DNA-binding transcription factor activity GO:0051091
Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
1 Q9QUS6 (/ISO)
Positive regulation of NF-kappaB transcription factor activity GO:0051092
Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
1 Q9QUS6 (/ISO)
Response to growth hormone GO:0060416
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 a growth hormone stimulus. Growth hormone is a peptide hormone that binds to the growth hormone receptor and stimulates growth.
1 O95361 (/IDA)
Response to growth hormone GO:0060416
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 a growth hormone stimulus. Growth hormone is a peptide hormone that binds to the growth hormone receptor and stimulates growth.
1 Q99PP9 (/ISO)
Response to growth hormone GO:0060416
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 a growth hormone stimulus. Growth hormone is a peptide hormone that binds to the growth hormone receptor and stimulates growth.
1 Q5R760 (/ISS)
Negative regulation of viral release from host cell GO:1902187
Any process that stops, prevents or reduces the frequency, rate or extent of viral release from host cell.
1 Q9QUS6 (/ISO)

There are 16 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
Microtubule GO:0005874
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
17 O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA) O15344 (/IDA)
(7 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.
15 O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS)
(5 more)
Microtubule associated complex GO:0005875
Any multimeric complex connected to a microtubule.
15 O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS) O15344 (/TAS)
(5 more)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
4 O70583 (/IDA) O95361 (/IDA) P82457 (/IDA) Q99PP9 (/IDA)
Microtubule GO:0005874
Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
3 O70583 (/ISO) P82457 (/ISO) Q9QUS6 (/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.
2 H0Y626 (/IDA) O95361 (/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.
2 H0Y626 (/IDA) O95361 (/IDA)
Microtubule cytoskeleton GO:0015630
The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins.
2 O70583 (/IDA) P82457 (/IDA)
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.
2 Q9UJV3 (/HDA) Q9UJV3 (/HDA)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q99PP9 (/ISO)
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
1 Q5R760 (/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.
1 Q99PP9 (/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 Q99PP9 (/ISO)
PML body GO:0016605
A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
1 O95361 (/IDA)
PML body GO:0016605
A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
1 Q99PP9 (/ISO)
PML body GO:0016605
A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
1 Q5R760 (/ISS)