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 confidence score
0.38
Supporting publications (n)
2
Transmembrane count
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
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 (3)
EnzymesMetabolic proteinsPredicted intracellular proteins
Protein Function (3)
  • ENZYME proteins:Transferases
  • Enzymes
  • Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (4)
AXOTMARCH-VIIMARCH7RNF177
Gene Description
Membrane associated ring-CH-type finger 7
Chromosome
2
Position
159712457-159771027
Supporting publications (n)
2
EVMP confidence score
0.38
Fluorescence & Localization2
Tissue SpecificbrainCell SpecificBergmann glia
Function & Pathway5
Relations & Evidence147

Ligand-Receptor Signaling (4)

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network (138)

138 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
MARH7Q9H992TAUP10636YesNoYesLit-BM-17SIGNORSIGNOR:24905733Lit-BM-17:24905733
MARH7Q9H992IQCB1Q15051YesNoYesSIGNORSIGNOR:28498859
COMPLEX:P0CG47_P60604MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P62253_P62987MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P62987_Q13404MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P62987_Q16763MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P0CG47_P62256MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P0CG48_Q13404MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P0CG48_Q96B02MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
COMPLEX:P0CG47_Q5VVX9MARH7Q9H992YesYesNoSIGNORSIGNOR:34199813
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Protein Complex Composition (4)

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
Ub:RING_E3MARCHF7UBBP0CG47Q9H9920:0SIGNORSIGNOR:SIGNOR-C519
Ub:RING_E3MARCHF7UBCP0CG48Q9H9920:0SIGNORSIGNOR:SIGNOR-C519
Ub:RING_E3MARCHF7RPS27AP62979Q9H9920:0SIGNORSIGNOR:SIGNOR-C519
Ub:RING_E3MARCHF7UBA52P62987Q9H9920:0SIGNORSIGNOR:SIGNOR-C519

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry [LTQ-FT Ultra]Mass spectrometry137250483
Sequence, Structure & Domains9

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)

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
Clinical Relevance4
Interaction Protein (3)
ENSG00000078140ENSG00000101367ENSG00000163513
Interaction Count
3
Interaction Dataset (3)
intact_biogridintact_biogrid_opencellbiogrid_bioplex
Supporting Publications2
PMIDTitleAbstract
30865381Surfaceome of Exosomes Secreted from the Colorectal Cancer Cell Line SW480: Peripheral and Integral Membrane Proteins Analyzed by Proteolysis and TX114.No abstract available
32384937Alzheimer's disease progression characterized by alterations in the molecular profiles and biogenesis of brain extracellular vesicles.No abstract available