Human Gene MARCHF9 (ENST00000266643.6) from GENCODE V44
Description: Homo sapiens membrane associated ring-CH-type finger 9 (MARCHF9), mRNA. (from RefSeq NM_138396) RefSeq Summary (NM_138396): MARCH9 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH9 induces internalization of several membrane glycoproteins and directs them to the endosomal compartment (Bartee et al., 2004 [PubMed 14722266]; Hoer et al., 2007 [PubMed 17174307]).[supplied by OMIM, Apr 2010]. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. Gencode Transcript: ENST00000266643.6 Gencode Gene: ENSG00000139266.6 Transcript (Including UTRs) Position: hg38 chr12:57,755,103-57,760,411 Size: 5,309 Total Exon Count: 4 Strand: + Coding Region Position: hg38 chr12:57,755,529-57,758,897 Size: 3,369 Coding Exon Count: 4
ID:MARH9_HUMAN DESCRIPTION: RecName: Full=E3 ubiquitin-protein ligase MARCH9; EC=6.3.2.-; AltName: Full=Membrane-associated RING finger protein 9; AltName: Full=Membrane-associated RING-CH protein IX; Short=MARCH-IX; AltName: Full=RING finger protein 179; FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: Ubiquitously expressed. DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase activity. SIMILARITY: Contains 1 RING-CH-type zinc finger. SEQUENCE CAUTION: Sequence=AAH50397.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q86YJ5
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
