Maea
entrez
59003
canonical
uniprot
Q4VC33
canonical
ensembl
ENSMUSG00000079562
resolver
ensp
ENSMUSP00000110093
resolver
genesymbol
Maea
resolver
genesymbol_syn
Emp
resolver
uniprot
Q3TFH0
resolver
uniprot
Q3U7T6
resolver
uniprot
Q5XKE6
resolver
uniprot
Q8BPI3
resolver
uniprot
Q8BSA1
resolver
uniprot
Q9JK49
resolver
uniprot_entry
MAEA_MOUSE
resolver
uniprot_sec
Q3TFH0
resolver
uniprot_sec
Q3U7T6
resolver
uniprot_sec
Q5XKE6
resolver
uniprot_sec
Q8BPI3
resolver
uniprot_sec
Q8BSA1
resolver
uniprot_sec
Q9JK49
resolver
amino_acid_sequence
MAVQESAAQLSMTLKVQEYPTLKVPYETLNKRFRAAQKNIDRETSHVTMVVAELEKTLSSCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASMWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELVRQNKRLDAVRHARKHFSQAEGSQLDEVRQVMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNSSVFTLTLQAGLSAIKTPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANSRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVVCPRTKEVFHFSQAEKVYIM
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. MAEA is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1 (By similarity). Plays a role in erythroblast enucleation during erythrocyte maturation and in the development of mature macrophages (PubMed:16707498). Mediates the attachment of erythroid cell to mature macrophages; this MAEA-mediated contact inhibits erythroid cell apoptosis (By similarity). Participates in erythroblastic island formation, which is the functional unit of definitive erythropoiesis (PubMed:16707498, PubMed:17071116). Associates with F-actin to regulate actin distribution in erythroblasts and macrophages (PubMed:16707498). May contribute to nuclear architecture and cells division events (By similarity). {ECO:0000250|UniProtKB:Q7L5Y9, ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}.
uniprot
proteins
mass_dalton
45336
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated as component of the CTLH E3 ubiquitin-protein ligase complex (in vitro). {ECO:0000250|UniProtKB:Q7L5Y9}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16510120
uniprot
proteins
pubmed
16707498
uniprot
proteins
pubmed
17071116
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17071116}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7L5Y9}. Nucleus matrix {ECO:0000269|PubMed:17071116}. Cell membrane {ECO:0000269|PubMed:17071116}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}. Note=Detected in a nuclear, speckled-like pattern (PubMed:17071116). Localized with condensed chromatin at prophase; Detected in nuclear spindle poles at metaphase and in the contractile ring during telophase and cytokinesis (By similarity). Present in cytoplasm, nuclear matrix and at the cell surface in macrophages; predominantly nuclear in immature macrophages and predominantly detected at the cell surface in mature macrophages (PubMed:17071116). Colocalizes with F-actin in macrophages (PubMed:16707498). {ECO:0000250|UniProtKB:Q7L5Y9, ECO:0000269|PubMed:16707498, ECO:0000269|PubMed:17071116}.
uniprot
proteins