Q8VCM5

PR
Gene name
Mul1 (Gide)
Protein name
Mitochondrial ubiquitin ligase activator of NFKB 1
Names
E3 ubiquitin-protein ligase MUL1, Growth inhibition and death E3 ligase, Protein Hades, RING-type E3 ubiquitin transferase NFKB 1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:68350
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

244-325 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8VCM5

Entry ID Method Resolution Chain Position Source
AF-Q8VCM5-F1 Predicted AlphaFoldDB

22 variants for Q8VCM5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388709575 20 M>K No EVA
rs3388725568 23 A>T No EVA
rs3388725588 36 A>T No EVA
rs864279249 54 I>V No EVA
rs3388723193 57 E>* No EVA
rs3394692828 127 D>V No EVA
rs3395090989 130 P>A No EVA
rs3394967516 130 P>R No EVA
rs3388716549 135 V>M No EVA
rs3388725591 153 E>V No EVA
rs3388716565 154 T>I No EVA
rs3388730293 173 Y>F No EVA
rs3388712989 175 S>N No EVA
rs3388716559 185 T>K No EVA
rs3394864603 220 Y>L No EVA
rs3394864603 222 S>Q No EVA
rs3394864602 223 S>R No EVA
rs27576633 242 I>V No EVA
rs3388720854 264 L>F No EVA
rs3388719063 285 Q>H No EVA
rs3388723240 288 S>G No EVA
rs3388716574 343 I>F No EVA

No associated diseases with Q8VCM5

2 regional properties for Q8VCM5

Type Name Position InterPro Accession
domain Zinc finger, RING-type 302 - 340 IPR001841
domain E3 Ubiquitin ligase MUL1-like 98 - 251 IPR022170

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Mitochondrion outer membrane ; Multi-pass membrane protein
  • Peroxisome
  • Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
integral component of mitochondrial outer membrane The component of the mitochondrial outer membrane consisting of the gene products having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondrion 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.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

7 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.
p53 binding Binding to one of the p53 family of proteins.
SUMO transferase activity Catalysis of the transfer of SUMO from one protein to another via the reaction X-SUMO + Y --> Y-SUMO + X, where both X-SUMO and Y-SUMO are covalent linkages.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

25 GO annotations of biological process

Name Definition
activation of cysteine-type endopeptidase activity involved in apoptotic process Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
cellular response to exogenous dsRNA 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 an exogenous double-stranded RNA stimulus.
mitochondrial fission The division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
mitochondrion localization Any process in which a mitochondrion or mitochondria are transported to, and/or maintained in, a specific location within the cell.
negative regulation of cell growth Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
negative regulation of chemokine (C-C motif) ligand 5 production Any process that stops, prevents, or reduces the frequency, rate, or extent of production of chemokine (C-C motif) ligand 5.
negative regulation of defense response to virus by host Any host process that results in the inhibition of antiviral immune response mechanisms, thereby facilitating viral replication. The host is defined as the larger of the organisms involved in a symbiotic interaction.
negative regulation of innate immune response Any process that stops, prevents, or reduces the frequency, rate or extent of the innate immune response.
negative regulation of mitochondrial fusion Any process that decreases the frequency, rate or extent of merging of two or more mitochondria within a cell to form a single compartment.
negative regulation of protein kinase B signaling Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
negative regulation of type I interferon-mediated signaling pathway Any process that decreases the rate, frequency or extent of a type I interferon-mediated signaling pathway.
positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization Any process that activates or increases the frequency, rate or extent of autophagy of the mitochondrion in response to mitochondrial depolarization.
positive regulation of dendrite extension Any process that activates or increases the frequency, rate or extent of dendrite extension.
positive regulation of I-kappaB kinase/NF-kappaB signaling Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
positive regulation of mitochondrial fission Any process that increases the rate, frequency or extent of mitochondrial fission. Mitochondrial fission is the division of a mitochondrion within a cell to form two or more separate mitochondrial compartments.
positive regulation of protein sumoylation Any process that activates or increases the frequency, rate or extent of the addition of SUMO groups to a protein.
protein destabilization Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
regulation of mitochondrial membrane potential Any process that modulates the establishment or extent of the mitochondrial membrane potential, the electric potential existing across the mitochondrial membrane arising from charges in the membrane itself and from the charges present in the media on either side of the membrane.
regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Any process that modulates the frequency, rate or extent of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway.
regulation of mitochondrion organization Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a mitochondrion.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O35618 Mdm4 Protein Mdm4 Mus musculus (Mouse) SS
Q6ZQM0 Rffl E3 ubiquitin-protein ligase rififylin Mus musculus (Mouse) PR
10 20 30 40 50 60
MESGSRPSLG QVILLGTSSM VTAVLYSIYR QKAQVAQELK GAKKIHLGED LKGILSEAPG
70 80 90 100 110 120
KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLSLQEHK MVWNRTTHLW NDYSKIIHQR
130 140 150 160 170 180
TNTVPFDLVP HEDGVAVSVR VLKPLDSVDL GLETVYEKFH PSVQSFTDAI GHYISGERPK
190 200 210 220 230 240
GIQETEEMLK VGATLTGIGE LVLDNNAVRL QPPKQGMQYY LSSQDFDSLL HRQESSVRLW
250 260 270 280 290 300
KILVLVFGFA TCATLFFILR KQYLHRQERL RQQQLQEEFL EHEAQLLSQA SPEDRESLKS
310 320 330 340 350
ACVVCLSNFK SCVFLECGHV CSCRQCYLAL PEPKRCPICR REITRVIPLY NS