MARCHF2
entrez
51257
canonical
uniprot
Q9P0N8
canonical
ensembl
ENSG00000099785
resolver
ensp
ENSP00000215555
resolver
ensp
ENSP00000370423
resolver
ensp
ENSP00000471536
resolver
ensp
ENSP00000530212
resolver
ensp
ENSP00000530216
resolver
ensp
ENSP00000530218
resolver
ensp
ENSP00000530219
resolver
genesymbol
MARCHF2
resolver
genesymbol_syn
MARCH2
resolver
genesymbol_syn
RNF172
resolver
hgnc
HGNC:28038
resolver
uniprot
A6NP10
resolver
uniprot
Q5H785
resolver
uniprot
Q8N5A3
resolver
uniprot
Q96B78
resolver
uniprot_entry
MARH2_HUMAN
resolver
uniprot_sec
A6NP10
resolver
uniprot_sec
Q5H785
resolver
uniprot_sec
Q8N5A3
resolver
uniprot_sec
Q96B78
resolver
amino_acid_sequence
MTTGDCCHLPGSLCDCSGSPAFSKVVEATGLGPPQYVAQVTSRDGRLLSTVIRALDTPSDGPFCRICHEGANGECLLSPCGCTGTLGAVHKSCLEKWLSSSNTSYCELCHTEFAVEKRPRPLTEWLKDPGPRTEKRTLCCDMVCFLFITPLAAISGWLCLRGAQDHLRLHSQLEAVGLIALTIALFTIYVLWTLVSFRYHCQLYSEWRKTNQKVRLKIREADSPEGPQHSPLAAGLLKKVAEETPV
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that may mediate ubiquitination of TFRC and CD86, 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 (PubMed:14722266, PubMed:16428329). Together with GOPC/CAL mediates the ubiquitination and lysosomal degradation of CFTR (PubMed:23818989). Ubiquitinates and therefore mediates the degradation of DLG1 (PubMed:17980554). Regulates the intracellular trafficking and secretion of alpha1-antitrypsin/SERPINA1 and HP/haptoglobin via ubiquitination and degradation of the cargo receptor ERGIC3 (PubMed:31142615). Negatively regulates the antiviral and antibacterial immune response by repression of the NF-kB and type 1 IFN signaling pathways, via MARCHF2-mediated K48-linked polyubiquitination of IKBKG/NEMO, resulting in its proteasomal degradation (PubMed:32935379). May be involved in endosomal trafficking through interaction with STX6 (PubMed:15689499). {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:15689499, ECO:0000269|PubMed:16428329, ECO:0000269|PubMed:17980554, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:31142615, ECO:0000269|PubMed:32935379}.; FUNCTION: (Microbial infection) Positively regulates the degradation of Vesicular stomatitis virus (VSV) G protein via the lysosomal degradation pathway (PubMed:29573664). Represses HIV-1 viral production and may inhibit the translocation of HIV-1 env to the cell surface, resulting in decreased viral cell-cell transmission (PubMed:29573664). {ECO:0000269|PubMed:29573664}.
uniprot
proteins
mass_dalton
26995
uniprot
proteins
mutagenesis
MUTAGEN 64; /note="C->S: Abolishes ubiquitination of ERGIC3 and CFTR, and degradation of CFTR; when associated with S-67. Reduces ubiquitination of DLG1; when associated with S-67, S-106 and S-109. Reduces inhibition of HIV-1 virus production and VSVG protein expression; when associated with S-67. Abolishes ubiquitination of IKBKG/NEMO; when associated with S-67 and Q-90."; /evidence="ECO:0000269|PubMed:17980554, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:29573664, ECO:0000269|PubMed:31142615, ECO:0000269|PubMed:32935379"; MUTAGEN 67; /note="C->S: Abolishes ubiquitination of ERGIC3 and CFTR, and degradation of CFTR; when associated with S-64. Reduces ubiquitination of DLG1; when associated with S-64, S-106 and S-109. Reduces inhibition of HIV-1 virus production and VSVG protein expression; when associated with S-64. Abolishes ubiquitination of IKBKG/NEMO; when associated with S-64 and Q-90."; /evidence="ECO:0000269|PubMed:17980554, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:29573664, ECO:0000269|PubMed:31142615, ECO:0000269|PubMed:32935379"; MUTAGEN 90; /note="H->Q: Abolishes ubiquitination of IKBKG/NEMO; when associated with S-64 and S-67."; MUTAGEN 97; /note="W->A: Reduces ubiquitination of DLG1. No effect on interaction with DLG1. Abolishes ubiquitination of and interaction with DLG1; when associated with 243-E--V-246 DEL."; /evidence="ECO:0000269|PubMed:17980554"; MUTAGEN 106; /note="C->S: Reduces ubiquitination of DLG1; when associated with S-64, S-67 and S-109."; /evidence="ECO:0000269|PubMed:17980554"; MUTAGEN 109; /note="C->S: Reduces ubiquitination of DLG1; when associated with S-64, S-67 and S-106."; /evidence="ECO:0000269|PubMed:17980554"; MUTAGEN 243..246; /note="ETPV->AAAA: Abolishes ubiquitination of and interaction with DLG1; when associated with A-97."; /evidence="ECO:0000269|PubMed:17980554
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17980554, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:31142615}.
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
14722266
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15689499
uniprot
proteins
pubmed
16428329
uniprot
proteins
pubmed
17980554
uniprot
proteins
pubmed
23166351
uniprot
proteins
pubmed
23818989
uniprot
proteins
pubmed
29573664
uniprot
proteins
pubmed
31142615
uniprot
proteins
pubmed
32935379
uniprot
proteins
sequence_length
246
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5I0I2}. Lysosome membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:23166351}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5I0I2}. Golgi apparatus membrane {ECO:0000269|PubMed:23818989}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:32935379}. Cell membrane {ECO:0000269|PubMed:32935379}; Multi-pass membrane protein {ECO:0000269|PubMed:32935379}.
uniprot
proteins
transmembrane_region
TRANSMEM 138..158; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 175..195; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins