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MAEA_HUMAN
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   03-AUG-2022, entry version 140.
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; 151.
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; Q7L5Y9; -.
DR   PeptideAtlas; Q7L5Y9; -.
DR   PRIDE; 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   Antibodypedia; 8374; 280 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   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; DVKYDEW; -.
DR   OrthoDB; 1087488at2759; -.
DR   PhylomeDB; Q7L5Y9; -.
DR   TreeFam; TF314273; -.
DR   PathwayCommons; Q7L5Y9; -.
DR   SignaLink; Q7L5Y9; -.
DR   BioGRID-ORCS; 10296; 209 hits in 1090 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 204 other 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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; 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   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR027714; Fyv10/MAEA.
DR   InterPro; IPR045098; Fyv10_fam.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR044063; ZF_RING_GID.
DR   PANTHER; PTHR12170; PTHR12170; 1.
DR   PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
DR   Pfam; PF10607; CLTH; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 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
 
 
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