O60291 · MGRN1_HUMAN
- ProteinE3 ubiquitin-protein ligase MGRN1
- GeneMGRN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids552 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
Pathway
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | early endosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | endosome to lysosome transport | |
Biological Process | negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway | |
Biological Process | negative regulation of cAMP-mediated signaling | |
Biological Process | negative regulation of G protein-coupled receptor signaling pathway | |
Biological Process | negative regulation of smoothened signaling pathway | |
Biological Process | protein monoubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase MGRN1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60291
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Isoform 3
Isoform 4
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 406-409 | Loss of TSG101-binding and drastic reduction of TSG101-ubiquitination. | ||||
Sequence: PSAP → ASAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 895 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000246687 | 2-552 | UniProt | E3 ubiquitin-protein ligase MGRN1 | |||
Sequence: GSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKKSKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPALGPDSCSVGIDE | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 153 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 402 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 411 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 471 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 524 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 524 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O60291 | TSG101 Q99816 | 5 | EBI-2129851, EBI-346882 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 278-317 | RING-type | ||||
Sequence: CVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICR | ||||||
Region | 355-384 | Disordered | ||||
Sequence: SCPFKKSKPHPASLASKKPKRETNSDSVPP | ||||||
Motif | 406-409 | Required for TSG101-binding | ||||
Sequence: PSAP | ||||||
Region | 439-552 | Disordered | ||||
Sequence: SSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPALGPDSCSVGIDE | ||||||
Compositional bias | 443-458 | Polar residues | ||||
Sequence: KGRPQSKAPDSTLRSP | ||||||
Compositional bias | 491-522 | Polar residues | ||||
Sequence: SSPESFITEEVDESSSPQQGTRAASIENVLQD |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O60291-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Synonyms(+)S
- Length552
- Mass (Da)60,753
- Last updated2006-07-25 v2
- Checksum1F923D25FB49DB4D
O60291-2
- Name2
- Synonyms(+)L
- Differences from canonical
- 540-552: ALGPDSCSVGIDE → GRPTSMETAHGLATTSPTWPPLGGPSPDPSAAELTPL
O60291-3
- Name3
- Synonyms(-)L
O60291-4
- Name4
- Synonyms(-)S
- Differences from canonical
- 356-377: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 248 | in Ref. 1; ABO69623/ABO69624 | ||||
Sequence: Y → H | ||||||
Alternative sequence | VSP_036462 | 356-377 | in isoform 3 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 443-458 | Polar residues | ||||
Sequence: KGRPQSKAPDSTLRSP | ||||||
Compositional bias | 491-522 | Polar residues | ||||
Sequence: SSPESFITEEVDESSSPQQGTRAASIENVLQD | ||||||
Sequence conflict | 537 | in Ref. 1; ABO69623/ABO69624 | ||||
Sequence: Y → H | ||||||
Alternative sequence | VSP_019853 | 540-552 | in isoform 2 and isoform 3 | |||
Sequence: ALGPDSCSVGIDE → GRPTSMETAHGLATTSPTWPPLGGPSPDPSAAELTPL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EF471397 EMBL· GenBank· DDBJ | ABO69623.2 EMBL· GenBank· DDBJ | mRNA | ||
EF471398 EMBL· GenBank· DDBJ | ABO69624.2 EMBL· GenBank· DDBJ | mRNA | ||
AB011116 EMBL· GenBank· DDBJ | BAA25470.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC023830 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC050389 EMBL· GenBank· DDBJ | AAH50389.1 EMBL· GenBank· DDBJ | mRNA |