Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7L5Y9

- MAEA_HUMAN

UniProt

Q7L5Y9 - MAEA_HUMAN

Protein

Macrophage erythroblast attacher

Gene

MAEA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role in erythroblast enucleation and in the development of the mature macrophages. Mediates the attachment of erythroid cell to mature macrophages, in correlation with the presence of MAEA at cell surface of mature macrophages; This MAEA-mediated contact inhibits erythroid cells apoptosis. Participates to erythroblastic island formation, which is the functional unit of definitive erythropoiesis. Associates with F-actin to regulate actin distribution in erythroblasts and macrophages. May contribute to nuclear architecture and cells division events.2 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. cytoskeleton organization Source: Ensembl
    5. enucleate erythrocyte development Source: Ensembl
    6. erythrocyte maturation Source: UniProtKB-KW
    7. negative regulation of myeloid cell apoptotic process Source: UniProtKB
    8. regulation of mitotic cell cycle Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Erythrocyte maturation

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage erythroblast attacher
    Alternative name(s):
    Cell proliferation-inducing gene 5 protein
    Erythroblast macrophage protein
    Human lung cancer oncogene 10 protein
    Short name:
    HLC-10
    Gene namesi
    Name:MAEA
    Synonyms:EMP
    ORF Names:HLC10, PIG5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:13731. MAEA.

    Subcellular locationi

    Nucleus matrix 1 Publication. Cell membrane 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Localized as nuclear speckled-like pattern.

    GO - Cellular componenti

    1. actomyosin contractile ring Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. integral component of plasma membrane Source: UniProtKB
    4. nuclear matrix Source: UniProtKB
    5. nucleus Source: HPA
    6. spindle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30533.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396Macrophage erythroblast attacherPRO_0000284936Add
    BLAST

    Proteomic databases

    MaxQBiQ7L5Y9.
    PaxDbiQ7L5Y9.
    PRIDEiQ7L5Y9.

    PTM databases

    PhosphoSiteiQ7L5Y9.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Developmental stagei

    Localized with condensed chromatin at prophase; Detected in nuclear spindle poles at metaphase and in the contractile ring during telophase and cytokinesis.1 Publication

    Gene expression databases

    ArrayExpressiQ7L5Y9.
    BgeeiQ7L5Y9.
    CleanExiHS_MAEA.
    GenevestigatoriQ7L5Y9.

    Organism-specific databases

    HPAiHPA036886.

    Interactioni

    Subunit structurei

    Forms a complex with F-actin.1 Publication

    Protein-protein interaction databases

    BioGridi115584. 12 interactions.
    MINTiMINT-4725016.
    STRINGi9606.ENSP00000302830.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7L5Y9.
    SMRiQ7L5Y9. Positions 336-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini121 – 15333LisHPROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 21658CTLHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 124124Extracellular and involved in cell to cell contactAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CTLH domain.PROSITE-ProRule annotation
    Contains 1 LisH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG241866.
    HOVERGENiHBG053270.
    InParanoidiQ7L5Y9.
    OrthoDBiEOG722J8H.
    PhylomeDBiQ7L5Y9.
    TreeFamiTF314273.

    Family and domain databases

    InterProiIPR013144. CRA_dom.
    IPR024964. CTLH/CRA.
    IPR006595. CTLH_C.
    IPR006594. LisH_dimerisation.
    [Graphical view]
    PfamiPF10607. CLTH. 1 hit.
    [Graphical view]
    SMARTiSM00757. CRA. 1 hit.
    SM00668. CTLH. 1 hit.
    SM00667. LisH. 1 hit.
    [Graphical view]
    PROSITEiPS50897. CTLH. 1 hit.
    PS50896. LISH. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7L5Y9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV    50
    VAELEKTLSG CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK 100
    RRIEHLKEHS SDQPAAASVW KRKRMDRMMV EHLLRCGYYN TAVKLARQSG 150
    IEDLVNIEMF LTAKEVEESL ERRETATCLA WCHDNKSRLR KMKSCLEFSL 200
    RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM GMLAFPPDTH 250
    ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP 300
    QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN 350
    NPPMMLPNGY VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM 396
    Length:396
    Mass (Da):45,287
    Last modified:July 5, 2005 - v1
    Checksum:i361FB82BE0240C21
    GO
    Isoform 2 (identifier: Q7L5Y9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-193: Missing.
         265-265: M → TCTVAD

    Show »
    Length:360
    Mass (Da):40,869
    Checksum:i7EDD1E1771B311F0
    GO
    Isoform 3 (identifier: Q7L5Y9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-193: Missing.

    Show »
    Length:355
    Mass (Da):40,410
    Checksum:iC949C3631DCD33E1
    GO
    Isoform 4 (identifier: Q7L5Y9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         152-232: EDLVNIEMFL...KHFSQAEGSQ → GTCKKALQPS...PAGWPLSHQD
         233-300: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):36,122
    Checksum:iD7E3935AB82BE82D
    GO
    Isoform 5 (identifier: Q7L5Y9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-245: DLVNIEMFLT...VRQAMGMLAF → TCKKALQPSR...LQGGRQLQEP
         246-396: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:245
    Mass (Da):26,802
    Checksum:i937AAE595F6C83BF
    GO

    Sequence cautioni

    The sequence AAC67543.1 differs from that shown. Reason: Sequence differs at N-terminus.
    The sequence AK128302 differs from that shown. Reason: Intron retention.
    The sequence AAC67543.1 differs from that shown. Reason: Frameshift at positions 253 and 327.
    The sequence AAO85220.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAC67543.1 differs from that shown. Reason: Erroneous termination at position 397. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321R → C in AAP74806. 1 PublicationCurated
    Sequence conflicti56 – 561K → R in AAC67543. (PubMed:9763581)Curated
    Sequence conflicti101 – 1011R → L in AAC67543. (PubMed:9763581)Curated
    Sequence conflicti123 – 1231K → R in BAA91499. (PubMed:14702039)Curated
    Sequence conflicti313 – 3131D → V in AAC67543. (PubMed:9763581)Curated
    Sequence conflicti327 – 3271P → R in AAC67543. (PubMed:9763581)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341R → C.
    Corresponds to variant rs34082974 [ dbSNP | Ensembl ].
    VAR_051150

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei152 – 23281EDLVN…AEGSQ → GTCKKALQPSRREPAGRGAP GHGHAGLPARHAHLPVQGPS GPCTVADADPAVPVRQLPTT PAGKQFCVHPHPAGWPLSHQ D in isoform 4. 1 PublicationVSP_024784Add
    BLAST
    Alternative sequencei153 – 24593DLVNI…GMLAF → TCKKALQPSRREPAGRGAPG HGHAGLPARHAHLPVQGPSG PCTVADADPAVPVRQLPTTP AGKQFCVHPHPAGRPLSHQD TTVLQGGRQLQEP in isoform 5. 1 PublicationVSP_024785Add
    BLAST
    Alternative sequencei153 – 19341Missing in isoform 2 and isoform 3. 2 PublicationsVSP_024786Add
    BLAST
    Alternative sequencei233 – 30068Missing in isoform 4. 1 PublicationVSP_024788Add
    BLAST
    Alternative sequencei246 – 396151Missing in isoform 5. 1 PublicationVSP_024789Add
    BLAST
    Alternative sequencei265 – 2651M → TCTVAD in isoform 2. 1 PublicationVSP_024790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY236486 mRNA. Translation: AAP74806.1.
    AK001088 mRNA. Translation: BAA91499.1.
    AK128302 mRNA. No translation available.
    AK022515 mRNA. Translation: BAB14072.1.
    AK022586 mRNA. Translation: BAB14113.1.
    BC001225 mRNA. Translation: AAH01225.2.
    BC006470 mRNA. Translation: AAH06470.2.
    AF084928 mRNA. Translation: AAC67543.1. Sequence problems.
    AY189687 mRNA. Translation: AAO85220.1. Different initiation.
    BT006957 mRNA. Translation: AAP35603.1.
    CCDSiCCDS33936.1. [Q7L5Y9-1]
    CCDS33937.1. [Q7L5Y9-3]
    RefSeqiNP_001017405.1. NM_001017405.1. [Q7L5Y9-1]
    NP_005873.2. NM_005882.3. [Q7L5Y9-3]
    UniGeneiHs.139896.

    Genome annotation databases

    EnsembliENST00000264750; ENSP00000264750; ENSG00000090316. [Q7L5Y9-3]
    ENST00000303400; ENSP00000302830; ENSG00000090316. [Q7L5Y9-1]
    GeneIDi10296.
    KEGGihsa:10296.
    UCSCiuc003gda.3. human. [Q7L5Y9-1]
    uc003gdb.3. human. [Q7L5Y9-3]

    Polymorphism databases

    DMDMi74754297.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY236486 mRNA. Translation: AAP74806.1 .
    AK001088 mRNA. Translation: BAA91499.1 .
    AK128302 mRNA. No translation available.
    AK022515 mRNA. Translation: BAB14072.1 .
    AK022586 mRNA. Translation: BAB14113.1 .
    BC001225 mRNA. Translation: AAH01225.2 .
    BC006470 mRNA. Translation: AAH06470.2 .
    AF084928 mRNA. Translation: AAC67543.1 . Sequence problems.
    AY189687 mRNA. Translation: AAO85220.1 . Different initiation.
    BT006957 mRNA. Translation: AAP35603.1 .
    CCDSi CCDS33936.1. [Q7L5Y9-1 ]
    CCDS33937.1. [Q7L5Y9-3 ]
    RefSeqi NP_001017405.1. NM_001017405.1. [Q7L5Y9-1 ]
    NP_005873.2. NM_005882.3. [Q7L5Y9-3 ]
    UniGenei Hs.139896.

    3D structure databases

    ProteinModelPortali Q7L5Y9.
    SMRi Q7L5Y9. Positions 336-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115584. 12 interactions.
    MINTi MINT-4725016.
    STRINGi 9606.ENSP00000302830.

    PTM databases

    PhosphoSitei Q7L5Y9.

    Polymorphism databases

    DMDMi 74754297.

    Proteomic databases

    MaxQBi Q7L5Y9.
    PaxDbi Q7L5Y9.
    PRIDEi Q7L5Y9.

    Protocols and materials databases

    DNASUi 10296.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264750 ; ENSP00000264750 ; ENSG00000090316 . [Q7L5Y9-3 ]
    ENST00000303400 ; ENSP00000302830 ; ENSG00000090316 . [Q7L5Y9-1 ]
    GeneIDi 10296.
    KEGGi hsa:10296.
    UCSCi uc003gda.3. human. [Q7L5Y9-1 ]
    uc003gdb.3. human. [Q7L5Y9-3 ]

    Organism-specific databases

    CTDi 10296.
    GeneCardsi GC04P001273.
    HGNCi HGNC:13731. MAEA.
    HPAi HPA036886.
    MIMi 606801. gene.
    neXtProti NX_Q7L5Y9.
    PharmGKBi PA30533.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241866.
    HOVERGENi HBG053270.
    InParanoidi Q7L5Y9.
    OrthoDBi EOG722J8H.
    PhylomeDBi Q7L5Y9.
    TreeFami TF314273.

    Miscellaneous databases

    ChiTaRSi MAEA. human.
    GenomeRNAii 10296.
    NextBioi 39018.
    PROi Q7L5Y9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7L5Y9.
    Bgeei Q7L5Y9.
    CleanExi HS_MAEA.
    Genevestigatori Q7L5Y9.

    Family and domain databases

    InterProi IPR013144. CRA_dom.
    IPR024964. CTLH/CRA.
    IPR006595. CTLH_C.
    IPR006594. LisH_dimerisation.
    [Graphical view ]
    Pfami PF10607. CLTH. 1 hit.
    [Graphical view ]
    SMARTi SM00757. CRA. 1 hit.
    SM00668. CTLH. 1 hit.
    SM00667. LisH. 1 hit.
    [Graphical view ]
    PROSITEi PS50897. CTLH. 1 hit.
    PS50896. LISH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human cell proliferation gene 5."
      Kim J.W.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
      Tissue: Embryo and Thymus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    4. "Molecular identification and functional characterization of a novel protein that mediates the attachment of erythroblasts to macrophages."
      Hanspal M., Smockova Y., Uong Q.
      Blood 92:2940-2950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-396 (ISOFORM 2), REGION, FUNCTION, TISSUE SPECIFICITY.
    5. "Identification of new human cancer-related gene (HLC-10)."
      Kim J.W.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-396 (ISOFORM 1).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-396 (ISOFORM 1).
    7. "Emp is a component of the nuclear matrix of mammalian cells and undergoes dynamic rearrangements during cell division."
      Bala S., Kumar A., Soni S., Sinha S., Hanspal M.
      Biochem. Biophys. Res. Commun. 342:1040-1048(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAEA_HUMAN
    AccessioniPrimary (citable) accession number: Q7L5Y9
    Secondary accession number(s): O95285
    , Q5JB54, Q6ZRD6, Q9BQ11, Q9H9V6, Q9H9Z4, Q9NW84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3