Overview
| Uniprot ID | Q7L5Y9 |
|---|
| Protein Name | E3 ubiquitin-protein transferase MAEA |
|---|
| Gene Name | MAEA |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 31 |
VPYETLNKRFRAAQK |
| 84 |
KLSVLKRKAVESIQA |
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 (PubMed:29911972). MAEA is required for normal cell proliferation (PubMed:29911972). The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1 (PubMed:29911972). Plays a role in erythroblast enucleation during erythrocyte maturation and in the development of mature macrophages (By similarity). Mediates the attachment of erythroid cell to mature macrophages; this MAEA-mediated contact inhibits erythroid cell apoptosis (PubMed:9763581). Participates in erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages (By similarity). May contribute to nuclear architecture and cells division events (Probable)
Protein Sequence
10
MAVQESAAQL
20
SMTLKVQEYP
30
TLKVPYETLN
40
KRFRAAQKNI
50
DRETSHVTMV
60
VAELEKTLSG
70
CPAVDSVVSL
80
LDGVVEKLSV
90
LKRKAVESIQ
100
AEDESAKLCK
110
RRIEHLKEHS
120
SDQPAAASVW
130
KRKRMDRMMV
140
EHLLRCGYYN
150
TAVKLARQSG
160
IEDLVNIEMF
170
LTAKEVEESL
180
ERRETATCLA
190
WCHDNKSRLR
200
KMKSCLEFSL
210
RIQEFIELIR
220
QNKRLDAVRH
230
ARKHFSQAEG
240
SQLDEVRQAM
250
GMLAFPPDTH
260
ISPYKDLLDP
270
ARWRMLIQQF
280
RYDNYRLHQL
290
GNNSVFTLTL
300
QAGLSAIKTP
310
QCYKEDGSSK
320
SPDCPVCSRS
330
LNKLAQPLPM
340
AHCANSRLVC
350
KISGDVMNEN
360
NPPMMLPNGY
370
VYGYNSLLSI
380
RQDDKVVCPR
390
TKEVFHFSQA
EKVYIM
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005826 |
actomyosin contractile ring |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005856 |
cytoskeleton |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0034657 |
GID complex |
| Cellular Component |
GO:0016363 |
nuclear matrix |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Cellular Component |
GO:0005819 |
spindle |
| Cellular Component |
GO:0000151 |
ubiquitin ligase complex |
| Molecular Function |
GO:0003779 |
actin binding |
| Molecular Function |
GO:0061630 |
ubiquitin protein ligase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0007155 |
cell adhesion |
| Biological Process |
GO:0051301 |
cell division |
| Biological Process |
GO:0043249 |
erythrocyte maturation |
| Biological Process |
GO:0033033 |
negative regulation of myeloid cell apoptotic process |
| Biological Process |
GO:0043161 |
proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0007346 |
regulation of mitotic cell cycle |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.