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Protein

E3 ubiquitin-protein transferase MAEA

Gene

MAEA

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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 (By similarity). 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. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages (By similarity). May contribute to nuclear architecture and cells division events (By similarity).By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei314Essential for ubiquitin ligase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri314 – 381RING-Gid-typePROSITE-ProRule annotationAdd BLAST68

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin-binding, Transferase
Biological processCell cycle, Cell division, Erythrocyte maturation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein transferase MAEA (EC:2.3.2.27By similarity)
Alternative name(s):
Macrophage erythroblast attacher
Gene namesi
Name:MAEA
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002849391 – 396E3 ubiquitin-protein transferase MAEAAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphothreonineBy similarity1

Post-translational modificationi

Autoubiquitinated as component of the CTLH E3 ubiquitin-protein ligase complex (in vitro).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with F-actin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000016233

Structurei

3D structure databases

ProteinModelPortaliQ5R532
SMRiQ5R532
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini121 – 153LisHPROSITE-ProRule annotationAdd BLAST33
Domaini159 – 216CTLHPROSITE-ProRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 124Extracellular and involved in cell to cell contactBy similarityAdd BLAST124

Domaini

The expected RING-type zinc finger domain is highly divergent and most of the expected Cys residues are not conserved. Still, the protein is required for CTLH complex E3 ubiquitin-protein transferase activity. In addition, the conserved Cys-314 in this highly divergent region is required for ubiquitination by the yeast GID complex, suggesting a direct role in catalyzing ubiquitination.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri314 – 381RING-Gid-typePROSITE-ProRule annotationAdd BLAST68

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0396 Eukaryota
ENOG410XPGU LUCA
HOVERGENiHBG053270
InParanoidiQ5R532
KOiK18624

Family and domain databases

InterProiView protein in InterPro
IPR013144 CRA_dom
IPR024964 CTLH/CRA
IPR006595 CTLH_C
IPR027714 Fyv10/EMP
IPR006594 LisH
PANTHERiPTHR12170:SF2 PTHR12170:SF2, 1 hit
PfamiView protein in Pfam
PF10607 CLTH, 1 hit
SMARTiView protein in SMART
SM00757 CRA, 1 hit
SM00668 CTLH, 1 hit
SM00667 LisH, 1 hit
PROSITEiView protein in PROSITE
PS50897 CTLH, 1 hit
PS50896 LISH, 1 hit
PS51867 ZF_RING_GID, 1 hit

Sequencei

Sequence statusi: Complete.

Q5R532-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV
60 70 80 90 100
VAELEKTLSG CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK
110 120 130 140 150
RRIEHLKEHS SDQPAAASVW KRKRMDRMMV EHLLRCGYYN TAVKLARQSG
160 170 180 190 200
IEDLVNIEMF LTAKEVEESL ERRETATCLA WCHDNKSRLR KMKSCLEFSL
210 220 230 240 250
RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM GMLAFPPDTH
260 270 280 290 300
ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP
310 320 330 340 350
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN
360 370 380 390
NPPMMLPNGY VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM
Length:396
Mass (Da):45,287
Last modified:December 21, 2004 - v1
Checksum:i361FB82BE0240C21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR861046 mRNA Translation: CAH93134.1
RefSeqiNP_001126854.1, NM_001133382.1

Genome annotation databases

GeneIDi100173862
KEGGipon:100173862

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR861046 mRNA Translation: CAH93134.1
RefSeqiNP_001126854.1, NM_001133382.1

3D structure databases

ProteinModelPortaliQ5R532
SMRiQ5R532
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000016233

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173862
KEGGipon:100173862

Organism-specific databases

CTDi10296

Phylogenomic databases

eggNOGiKOG0396 Eukaryota
ENOG410XPGU LUCA
HOVERGENiHBG053270
InParanoidiQ5R532
KOiK18624

Family and domain databases

InterProiView protein in InterPro
IPR013144 CRA_dom
IPR024964 CTLH/CRA
IPR006595 CTLH_C
IPR027714 Fyv10/EMP
IPR006594 LisH
PANTHERiPTHR12170:SF2 PTHR12170:SF2, 1 hit
PfamiView protein in Pfam
PF10607 CLTH, 1 hit
SMARTiView protein in SMART
SM00757 CRA, 1 hit
SM00668 CTLH, 1 hit
SM00667 LisH, 1 hit
PROSITEiView protein in PROSITE
PS50897 CTLH, 1 hit
PS50896 LISH, 1 hit
PS51867 ZF_RING_GID, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMAEA_PONAB
AccessioniPrimary (citable) accession number: Q5R532
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: November 7, 2018
This is version 69 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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