Protein detail
MARH7
E3 ubiquitin-protein ligase MARCHF7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING finger protein 177) (RING-type E3 ubiquitin transferase MARCHF7)
Entry name MARH7 | UniProt ID | EVMP score 0.38 |
Frequency 2 | Transmembrane count | Protein classification EnzymesMetabolic proteinsPredicted intracellular proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
E3 ubiquitin-protein ligase MARCHF7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING finger protein 177) (RING-type E3 ubiquitin transferase MARCHF7)
Protein Class
EnzymesMetabolic proteinsPredicted intracellular proteins
Protein Function
- ENZYME proteins:Transferases
- Enzymes
- Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
AXOTMARCH-VIIMARCH7RNF177
Gene Description
Membrane associated ring-CH-type finger 7
Chromosome
2
Position
159712457-159771027
Frequency
2
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificbrainCell SpecificBergmann glia
Function & Pathway
Protein Function
- ENZYME proteins:Transferases
- Enzymes
- Predicted intracellular proteins
Cellular Component
Molecular Function
Biological Process
Mediation Categories
Adhesion and uptake mediationImmune mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
4 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
138 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| COMPLEX:P62987_Q9NPD8 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P62979_P63279 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P62987_Q9Y385 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:A0A1B0GUS4_P62987 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P0CG48_Q9Y385 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P0CG48_P49459 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:O00762_P0CG47 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P0CG48_P51668 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P0CG47_Q7Z7E8 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 | |
| COMPLEX:P62253_P62979 | MARH7 | Q9H992 | Yes | Yes | No | SIGNOR | SIGNOR:34199813 |
Protein Complex Composition
4 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Ub:RING_E3 | MARCHF7UBB | P0CG47Q9H992 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | MARCHF7UBC | P0CG48Q9H992 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | MARCHF7RPS27A | P62979Q9H992 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 | |
| Ub:RING_E3 | MARCHF7UBA52 | P62987Q9H992 | 0:0 | SIGNOR | SIGNOR:SIGNOR-C519 |
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | Mass spectrometry [LTQ-FT Ultra]Mass spectrometry | 1 | 37250483 |
Sequence, Structure & Domains
Sequences
Length
704
Mass
78,051
Sequence
MESKPSRIPRRISVQPSSSLSARMMSGSRGSSLNDTYHSRDSSFRLDSEYQSTSASASASPFQSAWYSESEITQGARSRSQNQQRDHDSKRPKLSCTNCTTSAGRNVGNGLNTLSDSSWRHSQVPRSSSMVLGSFGTDLMRERRDLERRTDSSISNLMDYSHRSGDFTTSSYVQDRVPSYSQGARPKENSMSTLQLNTSSTNHQLPSEHQTILSSRDSRNSLRSNFSSRESESSRSNTQPGFSYSSSRDEAPIISNSERVVSSQRPFQESSDNEGRRTTRRLLSRIASSMSSTFFSRRSSQDSLNTRSLNSENSYVSPRILTASQSRSNVPSASEVPDNRASEASQGFRFLRRRWGLSSLSHNHSSESDSENFNQESEGRNTGPWLSSSLRNRCTPLFSRRRREGRDESSRIPTSDTSSRSHIFRRESNEVVHLEAQNDPLGAAANRPQASAASSSATTGGSTSDSAQGGRNTGISGILPGSLFRFAVPPALGSNLTDNVMITVDIIPSGWNSADGKSDKTKSAPSRDPERLQKIKESLLLEDSEEEEGDLCRICQMAAASSSNLLIEPCKCTGSLQYVHQDCMKKWLQAKINSGSSLEAVTTCELCKEKLELNLEDFDIHELHRAHANEQAEYEFISSGLYLVVLLHLCEQSFSDMMGNTNEPSTRVRFINLARTLQAHMEDLETSEDDSEEDGDHNRTFDIA
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H992-1; Sequence=Displayed; Name=2; IsoId=Q9H992-2; Sequence=VSP_054406
Alternative Sequence
1..51; MESKPSRIPRRISVQPSSSLSARMMSGSRGSSLNDTYHSRDSSFRLDSEYQ -> MIGNYDHLMSLVT (in isoform 2)
3D Structural Models
Domain & Motif Annotations
Compositional Bias
17..33; Low complexity; 37..48; Basic and acidic residues; 52..65; Low complexity; 66..83; Polar residues; 95..126; Polar residues; 189..212; Polar residues; 237..246; Polar residues; 254..270; Polar residues; 294..303; Low complexity; 304..313; Polar residues; 319..332; Polar residues; 412..421; Polar residues; 444..470; Low complexity; 684..695; Acidic residues
Zinc Finger
544..614; RING-CH-type
Domain (CC)
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Region
1..126; Disordered; 157..279; Disordered; 294..313; Disordered; 319..343; Disordered; 361..425; Disordered; 444..473; Disordered; 683..704; Disordered