Full text data of MAEA
MAEA
(EMP)
[Confidence: low (only semi-automatic identification from reviews)]
Macrophage erythroblast attacher (Cell proliferation-inducing gene 5 protein; Erythroblast macrophage protein; Human lung cancer oncogene 10 protein; HLC-10)
Macrophage erythroblast attacher (Cell proliferation-inducing gene 5 protein; Erythroblast macrophage protein; Human lung cancer oncogene 10 protein; HLC-10)
UniProt
Q7L5Y9
ID MAEA_HUMAN Reviewed; 396 AA.
AC Q7L5Y9; O95285; Q5JB54; Q6ZRD6; Q9BQ11; Q9H9V6; Q9H9Z4; Q9NW84;
read moreDT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 22-JAN-2014, entry version 76.
DE RecName: Full=Macrophage erythroblast attacher;
DE AltName: Full=Cell proliferation-inducing gene 5 protein;
DE AltName: Full=Erythroblast macrophage protein;
DE AltName: Full=Human lung cancer oncogene 10 protein;
DE Short=HLC-10;
GN Name=MAEA; Synonyms=EMP; ORFNames=HLC10, PIG5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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, AND
RP 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
RT 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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE, AND
RP 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
RT undergoes dynamic rearrangements during cell division.";
RL Biochem. Biophys. Res. Commun. 342:1040-1048(2006).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role in erythroblast enucleation and in the
CC development of the mature macrophages. Mediates the attachment of
CC erythroid cell to mature macrophages, in correlation with the
CC presence of MAEA at cell surface of mature macrophages; This MAEA-
CC mediated contact inhibits erythroid cells apoptosis. Participates
CC to erythroblastic island formation, which is the functional unit
CC of definitive erythropoiesis. Associates with F-actin to regulate
CC actin distribution in erythroblasts and macrophages. May
CC contribute to nuclear architecture and cells division events.
CC -!- SUBUNIT: Forms a complex with F-actin.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Cell membrane. Cytoplasm,
CC cytoskeleton. Note=Localized as nuclear speckled-like pattern.
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 Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q7L5Y9-5; Sequence=VSP_024785, VSP_024789;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Localized with condensed chromatin at
CC prophase; Detected in nuclear spindle poles at metaphase and in
CC the contractile ring during telophase and cytokinesis.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67543.1; Type=Erroneous termination; Positions=397; Note=Translated as stop;
CC Sequence=AAC67543.1; Type=Frameshift; Positions=253, 327;
CC Sequence=AAC67543.1; Type=Miscellaneous discrepancy; Note=Sequence differs at N-terminus;
CC Sequence=AAO85220.1; Type=Erroneous initiation;
CC Sequence=AK128302; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001017405.1; NM_001017405.1.
DR RefSeq; NP_005873.2; NM_005882.3.
DR UniGene; Hs.139896; -.
DR ProteinModelPortal; Q7L5Y9; -.
DR MINT; MINT-4725016; -.
DR STRING; 9606.ENSP00000302830; -.
DR PhosphoSite; Q7L5Y9; -.
DR DMDM; 74754297; -.
DR PaxDb; Q7L5Y9; -.
DR PRIDE; Q7L5Y9; -.
DR DNASU; 10296; -.
DR Ensembl; ENST00000264750; ENSP00000264750; ENSG00000090316.
DR Ensembl; ENST00000303400; ENSP00000302830; ENSG00000090316.
DR GeneID; 10296; -.
DR KEGG; hsa:10296; -.
DR UCSC; uc003gda.3; human.
DR CTD; 10296; -.
DR GeneCards; GC04P001273; -.
DR HGNC; HGNC:13731; MAEA.
DR HPA; HPA036886; -.
DR MIM; 606801; gene.
DR neXtProt; NX_Q7L5Y9; -.
DR PharmGKB; PA30533; -.
DR eggNOG; NOG241866; -.
DR HOVERGEN; HBG053270; -.
DR InParanoid; Q7L5Y9; -.
DR OrthoDB; EOG722J8H; -.
DR PhylomeDB; Q7L5Y9; -.
DR ChiTaRS; MAEA; human.
DR GenomeRNAi; 10296; -.
DR NextBio; 39018; -.
DR PRO; PR:Q7L5Y9; -.
DR ArrayExpress; Q7L5Y9; -.
DR Bgee; Q7L5Y9; -.
DR CleanEx; HS_MAEA; -.
DR Genevestigator; Q7L5Y9; -.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
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: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; IPR006594; LisH_dimerisation.
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.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
KW Erythrocyte maturation; Membrane; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 396 Macrophage erythroblast attacher.
FT /FTId=PRO_0000284936.
FT DOMAIN 121 153 LisH.
FT DOMAIN 159 216 CTLH.
FT REGION 1 124 Extracellular and involved in cell to
FT cell contact.
FT VAR_SEQ 152 232 EDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKM
FT KSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQ
FT -> GTCKKALQPSRREPAGRGAPGHGHAGLPARHAHLPVQG
FT PSGPCTVADADPAVPVRQLPTTPAGKQFCVHPHPAGWPLSH
FT QD (in isoform 4).
FT /FTId=VSP_024784.
FT VAR_SEQ 153 245 DLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMK
FT SCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLD
FT EVRQAMGMLAF -> TCKKALQPSRREPAGRGAPGHGHAGL
FT PARHAHLPVQGPSGPCTVADADPAVPVRQLPTTPAGKQFCV
FT HPHPAGRPLSHQDTTVLQGGRQLQEP (in isoform
FT 5).
FT /FTId=VSP_024785.
FT VAR_SEQ 153 193 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_024786.
FT VAR_SEQ 233 300 Missing (in isoform 4).
FT /FTId=VSP_024788.
FT VAR_SEQ 246 396 Missing (in isoform 5).
FT /FTId=VSP_024789.
FT VAR_SEQ 265 265 M -> TCTVAD (in isoform 2).
FT /FTId=VSP_024790.
FT VARIANT 34 34 R -> C (in dbSNP:rs34082974).
FT /FTId=VAR_051150.
FT CONFLICT 32 32 R -> C (in Ref. 1; AAP74806).
FT CONFLICT 56 56 K -> R (in Ref. 4; AAC67543).
FT CONFLICT 101 101 R -> L (in Ref. 4; AAC67543).
FT CONFLICT 123 123 K -> R (in Ref. 2; BAA91499).
FT CONFLICT 313 313 D -> V (in Ref. 4; AAC67543).
FT CONFLICT 327 327 P -> R (in Ref. 4; AAC67543).
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
//
ID MAEA_HUMAN Reviewed; 396 AA.
AC Q7L5Y9; O95285; Q5JB54; Q6ZRD6; Q9BQ11; Q9H9V6; Q9H9Z4; Q9NW84;
read moreDT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 22-JAN-2014, entry version 76.
DE RecName: Full=Macrophage erythroblast attacher;
DE AltName: Full=Cell proliferation-inducing gene 5 protein;
DE AltName: Full=Erythroblast macrophage protein;
DE AltName: Full=Human lung cancer oncogene 10 protein;
DE Short=HLC-10;
GN Name=MAEA; Synonyms=EMP; ORFNames=HLC10, PIG5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: 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, AND
RP 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
RT 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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE, AND
RP 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
RT undergoes dynamic rearrangements during cell division.";
RL Biochem. Biophys. Res. Commun. 342:1040-1048(2006).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role in erythroblast enucleation and in the
CC development of the mature macrophages. Mediates the attachment of
CC erythroid cell to mature macrophages, in correlation with the
CC presence of MAEA at cell surface of mature macrophages; This MAEA-
CC mediated contact inhibits erythroid cells apoptosis. Participates
CC to erythroblastic island formation, which is the functional unit
CC of definitive erythropoiesis. Associates with F-actin to regulate
CC actin distribution in erythroblasts and macrophages. May
CC contribute to nuclear architecture and cells division events.
CC -!- SUBUNIT: Forms a complex with F-actin.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Cell membrane. Cytoplasm,
CC cytoskeleton. Note=Localized as nuclear speckled-like pattern.
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 Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q7L5Y9-5; Sequence=VSP_024785, VSP_024789;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DEVELOPMENTAL STAGE: Localized with condensed chromatin at
CC prophase; Detected in nuclear spindle poles at metaphase and in
CC the contractile ring during telophase and cytokinesis.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67543.1; Type=Erroneous termination; Positions=397; Note=Translated as stop;
CC Sequence=AAC67543.1; Type=Frameshift; Positions=253, 327;
CC Sequence=AAC67543.1; Type=Miscellaneous discrepancy; Note=Sequence differs at N-terminus;
CC Sequence=AAO85220.1; Type=Erroneous initiation;
CC Sequence=AK128302; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001017405.1; NM_001017405.1.
DR RefSeq; NP_005873.2; NM_005882.3.
DR UniGene; Hs.139896; -.
DR ProteinModelPortal; Q7L5Y9; -.
DR MINT; MINT-4725016; -.
DR STRING; 9606.ENSP00000302830; -.
DR PhosphoSite; Q7L5Y9; -.
DR DMDM; 74754297; -.
DR PaxDb; Q7L5Y9; -.
DR PRIDE; Q7L5Y9; -.
DR DNASU; 10296; -.
DR Ensembl; ENST00000264750; ENSP00000264750; ENSG00000090316.
DR Ensembl; ENST00000303400; ENSP00000302830; ENSG00000090316.
DR GeneID; 10296; -.
DR KEGG; hsa:10296; -.
DR UCSC; uc003gda.3; human.
DR CTD; 10296; -.
DR GeneCards; GC04P001273; -.
DR HGNC; HGNC:13731; MAEA.
DR HPA; HPA036886; -.
DR MIM; 606801; gene.
DR neXtProt; NX_Q7L5Y9; -.
DR PharmGKB; PA30533; -.
DR eggNOG; NOG241866; -.
DR HOVERGEN; HBG053270; -.
DR InParanoid; Q7L5Y9; -.
DR OrthoDB; EOG722J8H; -.
DR PhylomeDB; Q7L5Y9; -.
DR ChiTaRS; MAEA; human.
DR GenomeRNAi; 10296; -.
DR NextBio; 39018; -.
DR PRO; PR:Q7L5Y9; -.
DR ArrayExpress; Q7L5Y9; -.
DR Bgee; Q7L5Y9; -.
DR CleanEx; HS_MAEA; -.
DR Genevestigator; Q7L5Y9; -.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
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: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; IPR006594; LisH_dimerisation.
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.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
KW Erythrocyte maturation; Membrane; Nucleus; Polymorphism;
KW Reference proteome.
FT CHAIN 1 396 Macrophage erythroblast attacher.
FT /FTId=PRO_0000284936.
FT DOMAIN 121 153 LisH.
FT DOMAIN 159 216 CTLH.
FT REGION 1 124 Extracellular and involved in cell to
FT cell contact.
FT VAR_SEQ 152 232 EDLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKM
FT KSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQ
FT -> GTCKKALQPSRREPAGRGAPGHGHAGLPARHAHLPVQG
FT PSGPCTVADADPAVPVRQLPTTPAGKQFCVHPHPAGWPLSH
FT QD (in isoform 4).
FT /FTId=VSP_024784.
FT VAR_SEQ 153 245 DLVNIEMFLTAKEVEESLERRETATCLAWCHDNKSRLRKMK
FT SCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLD
FT EVRQAMGMLAF -> TCKKALQPSRREPAGRGAPGHGHAGL
FT PARHAHLPVQGPSGPCTVADADPAVPVRQLPTTPAGKQFCV
FT HPHPAGRPLSHQDTTVLQGGRQLQEP (in isoform
FT 5).
FT /FTId=VSP_024785.
FT VAR_SEQ 153 193 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_024786.
FT VAR_SEQ 233 300 Missing (in isoform 4).
FT /FTId=VSP_024788.
FT VAR_SEQ 246 396 Missing (in isoform 5).
FT /FTId=VSP_024789.
FT VAR_SEQ 265 265 M -> TCTVAD (in isoform 2).
FT /FTId=VSP_024790.
FT VARIANT 34 34 R -> C (in dbSNP:rs34082974).
FT /FTId=VAR_051150.
FT CONFLICT 32 32 R -> C (in Ref. 1; AAP74806).
FT CONFLICT 56 56 K -> R (in Ref. 4; AAC67543).
FT CONFLICT 101 101 R -> L (in Ref. 4; AAC67543).
FT CONFLICT 123 123 K -> R (in Ref. 2; BAA91499).
FT CONFLICT 313 313 D -> V (in Ref. 4; AAC67543).
FT CONFLICT 327 327 P -> R (in Ref. 4; AAC67543).
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
//
MIM
606801
*RECORD*
*FIELD* NO
606801
*FIELD* TI
*606801 MACROPHAGE ERYTHROBLAST ATTACHER; MAEA
;;ERYTHROBLAST MACROPHAGE PROTEIN; EMP
read more*FIELD* TX
DESCRIPTION
The association of erythroblasts with macrophages plays a central role
in the terminal maturation and enucleation of erythroblasts. MAEA
mediates attachment of erythroblasts to macrophages.
CLONING
Hanspal et al. (1998) cloned an MAEA cDNA from a human macrophage cDNA
expression library using antibody to the purified protein as probe. The
deduced 395-amino acid protein has a small N-terminal domain, a single
transmembrane domain, and a large cytoplasmic domain containing several
tyrosine residues that, when phosphorylated, could interact with protein
recognition modules. MAEA has a calculated molecular mass of 43 kD.
Recombinant protein, and protein expressed by transfected COS-7 cells,
showed an apparent molecular mass of 36 kD by SDS-PAGE. By Northern blot
analysis, Hanspal et al. (1998) found ubiquitous expression of a 2.1-kb
transcript in all tissues and cells examined. By Western blot analysis,
they identified 2 isoforms with apparent molecular masses of 36 kD and
33 kD in macrophage membranes.
GENE FUNCTION
Using several cell attachment assays, Hanspal et al. (1998) found that
both MAEA isoforms could bind erythroblasts and that binding was
mediated by the extracellular N terminus. They also determined that
MAEA-mediated cell-cell contact prevents apoptosis in maturing
erythroblasts.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MAEA
gene to chromosome 4 (TMAP WI-13069).
*FIELD* RF
1. Hanspal, M.; Smockova, Y.; Uong, Q.: Molecular identification
and functional characterization of a novel protein that mediates the
attachment of erythroblasts to macrophages. Blood 92: 2940-2950,
1998.
*FIELD* CD
Patricia A. Hartz: 3/27/2002
*FIELD* ED
carol: 03/27/2002
*RECORD*
*FIELD* NO
606801
*FIELD* TI
*606801 MACROPHAGE ERYTHROBLAST ATTACHER; MAEA
;;ERYTHROBLAST MACROPHAGE PROTEIN; EMP
read more*FIELD* TX
DESCRIPTION
The association of erythroblasts with macrophages plays a central role
in the terminal maturation and enucleation of erythroblasts. MAEA
mediates attachment of erythroblasts to macrophages.
CLONING
Hanspal et al. (1998) cloned an MAEA cDNA from a human macrophage cDNA
expression library using antibody to the purified protein as probe. The
deduced 395-amino acid protein has a small N-terminal domain, a single
transmembrane domain, and a large cytoplasmic domain containing several
tyrosine residues that, when phosphorylated, could interact with protein
recognition modules. MAEA has a calculated molecular mass of 43 kD.
Recombinant protein, and protein expressed by transfected COS-7 cells,
showed an apparent molecular mass of 36 kD by SDS-PAGE. By Northern blot
analysis, Hanspal et al. (1998) found ubiquitous expression of a 2.1-kb
transcript in all tissues and cells examined. By Western blot analysis,
they identified 2 isoforms with apparent molecular masses of 36 kD and
33 kD in macrophage membranes.
GENE FUNCTION
Using several cell attachment assays, Hanspal et al. (1998) found that
both MAEA isoforms could bind erythroblasts and that binding was
mediated by the extracellular N terminus. They also determined that
MAEA-mediated cell-cell contact prevents apoptosis in maturing
erythroblasts.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MAEA
gene to chromosome 4 (TMAP WI-13069).
*FIELD* RF
1. Hanspal, M.; Smockova, Y.; Uong, Q.: Molecular identification
and functional characterization of a novel protein that mediates the
attachment of erythroblasts to macrophages. Blood 92: 2940-2950,
1998.
*FIELD* CD
Patricia A. Hartz: 3/27/2002
*FIELD* ED
carol: 03/27/2002