ID MAEA_HUMAN Reviewed; 396 AA.
AC Q7L5Y9; O95285; Q5JB54; Q6ZRD6; Q9BQ11; Q9H9V6; Q9H9Z4; Q9NW84;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=E3 ubiquitin-protein transferase MAEA;
DE EC=2.3.2.27 {ECO:0000269|PubMed:29911972};
DE AltName: Full=Cell proliferation-inducing gene 5 protein {ECO:0000303|Ref.1};
DE AltName: Full=Erythroblast macrophage protein {ECO:0000303|PubMed:9763581};
DE AltName: Full=Human lung cancer oncogene 10 protein;
DE Short=HLC-10;
DE AltName: Full=Macrophage erythroblast attacher;
DE AltName: Full=P44EMLP {ECO:0000303|PubMed:17467196};
GN Name=MAEA;
GN Synonyms=EMP {ECO:0000303|PubMed:16510120, ECO:0000303|PubMed:9763581};
GN ORFNames=HLC10, PIG5 {ECO:0000303|Ref.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene 5.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Embryo, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-396 (ISOFORM 2), REGION, FUNCTION,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=9763581;
RA Hanspal M., Smockova Y., Uong Q.;
RT "Molecular identification and functional characterization of a novel
RT protein that mediates the attachment of erythroblasts to macrophages.";
RL Blood 92:2940-2950(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-396 (ISOFORM 1).
RA Kim J.W.;
RT "Identification of new human cancer-related gene (HLC-10).";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-396 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16510120; DOI=10.1016/j.bbrc.2006.02.060;
RA Bala S., Kumar A., Soni S., Sinha S., Hanspal M.;
RT "Emp is a component of the nuclear matrix of mammalian cells and undergoes
RT dynamic rearrangements during cell division.";
RL Biochem. Biophys. Res. Commun. 342:1040-1048(2006).
RN [8]
RP IDENTIFICATION IN THE CTLH COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=17467196; DOI=10.1016/j.gene.2007.02.032;
RA Kobayashi N., Yang J., Ueda A., Suzuki T., Tomaru K., Takeno M., Okuda K.,
RA Ishigatsubo Y.;
RT "RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins
RT ARMC8alpha and ARMC8beta are components of the CTLH complex.";
RL Gene 396:236-247(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=24143168; DOI=10.1371/journal.pone.0075217;
RA Francis O., Han F., Adams J.C.;
RT "Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in eukaryotic
RT cells and dominated by homologous components, the muskelin/RanBPM/CTLH
RT complex.";
RL PLoS ONE 8:E75217-E75217(2013).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. MAEA and RMND5A are both required for
CC catalytic activity of the CTLH E3 ubiquitin-protein ligase complex
CC (PubMed:29911972). MAEA is required for normal cell proliferation
CC (PubMed:29911972). The CTLH E3 ubiquitin-protein ligase complex is not
CC required for the degradation of enzymes involved in gluconeogenesis,
CC such as FBP1 (PubMed:29911972). Plays a role in erythroblast
CC enucleation during erythrocyte maturation and in the development of
CC mature macrophages (By similarity). Mediates the attachment of
CC erythroid cell to mature macrophages; this MAEA-mediated contact
CC inhibits erythroid cell apoptosis (PubMed:9763581). Participates in
CC erythroblastic island formation, which is the functional unit of
CC definitive erythropoiesis. Associates with F-actin to regulate actin
CC distribution in erythroblasts and macrophages (By similarity). May
CC contribute to nuclear architecture and cells division events
CC (Probable). {ECO:0000250|UniProtKB:Q4VC33, ECO:0000269|PubMed:29911972,
CC ECO:0000269|PubMed:9763581, ECO:0000305|PubMed:16510120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:29911972};
CC -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:17467196,
CC PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively
CC its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the
CC catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles
CC (PubMed:29911972). Interacts with F-actin (PubMed:16510120).
CC {ECO:0000269|PubMed:16510120, ECO:0000269|PubMed:17467196,
CC ECO:0000269|PubMed:29911972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q4VC33}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:17467196,
CC ECO:0000269|PubMed:24143168, ECO:0000269|PubMed:29911972}. Nucleus
CC matrix {ECO:0000269|PubMed:16510120}. Cell membrane
CC {ECO:0000269|PubMed:9763581}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16510120}. Note=Detected in a nuclear, speckled-
CC like pattern (PubMed:16510120). Localized with condensed chromatin at
CC prophase; Detected in nuclear spindle poles at metaphase and in the
CC contractile ring during telophase and cytokinesis (PubMed:16510120).
CC Present in cytoplasm, nuclear matrix and at the cell surface in
CC macrophages; predominantly nuclear in immature macrophages and
CC predominantly detected at the cell surface in mature macrophages.
CC Colocalizes with F-actin in macrophages (By similarity).
CC {ECO:0000250|UniProtKB:Q4VC33, ECO:0000269|PubMed:16510120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7L5Y9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L5Y9-2; Sequence=VSP_024786, VSP_024790;
CC Name=3;
CC IsoId=Q7L5Y9-3; Sequence=VSP_024786;
CC Name=4;
CC IsoId=Q7L5Y9-4; Sequence=VSP_024784, VSP_024788;
CC Name=5;
CC IsoId=Q7L5Y9-5; Sequence=VSP_024785, VSP_024789;
CC -!- TISSUE SPECIFICITY: Detected at macrophage membranes (at protein
CC level). Ubiquitous. {ECO:0000269|PubMed:9763581}.
CC -!- DOMAIN: The expected RING-type zinc finger domain is highly divergent
CC and most of the expected Cys residues are not conserved (Probable).
CC Still, the protein is required for CTLH complex E3 ubiquitin-protein
CC transferase activity (PubMed:29911972). In addition, the conserved Cys-
CC 314 in this highly divergent region is required for ubiquitination by
CC the yeast GID complex, suggesting a direct role in catalyzing
CC ubiquitination (Probable). {ECO:0000269|PubMed:29911972, ECO:0000305}.
CC -!- PTM: Autoubiquitinated as component of the CTLH E3 ubiquitin-protein
CC ligase complex (in vitro). {ECO:0000269|PubMed:29911972}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67543.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC67543.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC67543.1; Type=Miscellaneous discrepancy; Note=Sequence differs at N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO85220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AK128302; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY236486; AAP74806.1; -; mRNA.
DR EMBL; AK001088; BAA91499.1; -; mRNA.
DR EMBL; AK128302; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK022515; BAB14072.1; -; mRNA.
DR EMBL; AK022586; BAB14113.1; -; mRNA.
DR EMBL; BC001225; AAH01225.2; -; mRNA.
DR EMBL; BC006470; AAH06470.2; -; mRNA.
DR EMBL; AF084928; AAC67543.1; ALT_SEQ; mRNA.
DR EMBL; AY189687; AAO85220.1; ALT_INIT; mRNA.
DR EMBL; BT006957; AAP35603.1; -; mRNA.
DR CCDS; CCDS33936.1; -. [Q7L5Y9-1]
DR CCDS; CCDS33937.1; -. [Q7L5Y9-3]
DR CCDS; CCDS77887.1; -. [Q7L5Y9-4]
DR RefSeq; NP_001017405.1; NM_001017405.2. [Q7L5Y9-1]
DR RefSeq; NP_001284360.1; NM_001297431.1.
DR RefSeq; NP_005873.2; NM_005882.4. [Q7L5Y9-3]
DR AlphaFoldDB; Q7L5Y9; -.
DR SMR; Q7L5Y9; -.
DR BioGRID; 115584; 162.
DR ComplexPortal; CPX-7901; GID E3 ubiquitin ligase complex, RMND5B-RANBP9 variant.
DR ComplexPortal; CPX-7902; GID E3 ubiquitin ligase complex, RMND5A-RANBP10 variant.
DR ComplexPortal; CPX-7903; GID E3 ubiquitin ligase complex, RMND5B-RANBP10 variant.
DR ComplexPortal; CPX-876; GID E3 ubiquitin ligase complex, RMND5A-RANBP9 variant.
DR CORUM; Q7L5Y9; -.
DR IntAct; Q7L5Y9; 41.
DR MINT; Q7L5Y9; -.
DR STRING; 9606.ENSP00000302830; -.
DR DrugBank; DB05389; Tetrachlorodecaoxide.
DR iPTMnet; Q7L5Y9; -.
DR PhosphoSitePlus; Q7L5Y9; -.
DR BioMuta; MAEA; -.
DR DMDM; 74754297; -.
DR EPD; Q7L5Y9; -.
DR jPOST; Q7L5Y9; -.
DR MassIVE; Q7L5Y9; -.
DR MaxQB; Q7L5Y9; -.
DR PaxDb; 9606-ENSP00000302830; -.
DR PeptideAtlas; Q7L5Y9; -.
DR ProteomicsDB; 68819; -. [Q7L5Y9-1]
DR ProteomicsDB; 68820; -. [Q7L5Y9-2]
DR ProteomicsDB; 68821; -. [Q7L5Y9-3]
DR ProteomicsDB; 68822; -. [Q7L5Y9-4]
DR ProteomicsDB; 68823; -. [Q7L5Y9-5]
DR Pumba; Q7L5Y9; -.
DR Antibodypedia; 8374; 305 antibodies from 32 providers.
DR DNASU; 10296; -.
DR Ensembl; ENST00000264750.10; ENSP00000264750.6; ENSG00000090316.16. [Q7L5Y9-3]
DR Ensembl; ENST00000303400.9; ENSP00000302830.4; ENSG00000090316.16. [Q7L5Y9-1]
DR GeneID; 10296; -.
DR KEGG; hsa:10296; -.
DR MANE-Select; ENST00000303400.9; ENSP00000302830.4; NM_001017405.3; NP_001017405.1.
DR UCSC; uc003gda.4; human. [Q7L5Y9-1]
DR AGR; HGNC:13731; -.
DR CTD; 10296; -.
DR DisGeNET; 10296; -.
DR GeneCards; MAEA; -.
DR HGNC; HGNC:13731; MAEA.
DR HPA; ENSG00000090316; Low tissue specificity.
DR MIM; 606801; gene.
DR neXtProt; NX_Q7L5Y9; -.
DR OpenTargets; ENSG00000090316; -.
DR PharmGKB; PA30533; -.
DR VEuPathDB; HostDB:ENSG00000090316; -.
DR eggNOG; KOG0396; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_027445_0_1_1; -.
DR InParanoid; Q7L5Y9; -.
DR OMA; CHDNRSK; -.
DR OrthoDB; 1429623at2759; -.
DR PhylomeDB; Q7L5Y9; -.
DR TreeFam; TF314273; -.
DR PathwayCommons; Q7L5Y9; -.
DR SignaLink; Q7L5Y9; -.
DR SIGNOR; Q7L5Y9; -.
DR BioGRID-ORCS; 10296; 214 hits in 1168 CRISPR screens.
DR ChiTaRS; MAEA; human.
DR GenomeRNAi; 10296; -.
DR Pharos; Q7L5Y9; Tbio.
DR PRO; PR:Q7L5Y9; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q7L5Y9; Protein.
DR Bgee; ENSG00000090316; Expressed in middle frontal gyrus and 206 other cell types or tissues.
DR ExpressionAtlas; Q7L5Y9; baseline and differential.
DR Genevisible; Q7L5Y9; HS.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:UniProtKB.
DR CDD; cd16659; RING-Ubox_Emp; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170:SF2; E3 UBIQUITIN-PROTEIN TRANSFERASE MAEA; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cytoplasm; Cytoskeleton; Erythrocyte maturation; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..396
FT /note="E3 ubiquitin-protein transferase MAEA"
FT /id="PRO_0000284936"
FT DOMAIN 121..153
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 159..216
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 314..381
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT REGION 1..124
FT /note="Extracellular and involved in cell to cell contact"
FT /evidence="ECO:0000269|PubMed:9763581"
FT SITE 314
FT /note="Essential for ubiquitin ligase activity"
FT /evidence="ECO:0000250|UniProtKB:P40492"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 152..232
FT /note="EDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQ
FT EFIELIRQNKRLDAVRHARKHFSQAEGSQ -> GTCKKALQPSRREPAGRGAPGHGHAG
FT LPARHAHLPVQGPSGPCTVADADPAVPVRQLPTTPAGKQFCVHPHPAGWPLSHQD (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024784"
FT VAR_SEQ 153..245
FT /note="DLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQE
FT FIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQAMGMLAF -> TCKKALQPSRREPA
FT GRGAPGHGHAGLPARHAHLPVQGPSGPCTVADADPAVPVRQLPTTPAGKQFCVHPHPAG
FT RPLSHQDTTVLQGGRQLQEP (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024785"
FT VAR_SEQ 153..193
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9763581"
FT /id="VSP_024786"
FT VAR_SEQ 233..300
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024788"
FT VAR_SEQ 246..396
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_024789"
FT VAR_SEQ 265
FT /note="M -> TCTVAD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9763581"
FT /id="VSP_024790"
FT VARIANT 34
FT /note="R -> C (in dbSNP:rs34082974)"
FT /id="VAR_051150"
FT CONFLICT 32
FT /note="R -> C (in Ref. 1; AAP74806)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="K -> R (in Ref. 4; AAC67543)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> L (in Ref. 4; AAC67543)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="K -> R (in Ref. 2; BAA91499)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="D -> V (in Ref. 4; AAC67543)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="P -> R (in Ref. 4; AAC67543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45287 MW; 361FB82BE0240C21 CRC64;
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSG
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAASVW
KRKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERRETATCLA
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM
GMLAFPPDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY
VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM
//
