Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7L5Y9 (MAEA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MAEA
Synonyms:EMP
ORF Names:HLC10, PIG5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7

Subunit structure

Forms a complex with F-actin. Ref.7

Subcellular location

Nucleus matrix. Cell membrane. Cytoplasmcytoskeleton. Note: Localized as nuclear speckled-like pattern. Ref.7

Tissue specificity

Ubiquitous. Ref.4 Ref.7

Developmental stage

Localized with condensed chromatin at prophase; Detected in nuclear spindle poles at metaphase and in the contractile ring during telophase and cytokinesis. Ref.7

Sequence similarities

Contains 1 CTLH domain.

Contains 1 LisH domain.

Sequence caution

The sequence AAC67543.1 differs from that shown. Reason: Erroneous termination at position 397. Translated as stop.

The sequence AAC67543.1 differs from that shown. Reason: Frameshift at positions 253 and 327.

The sequence AAC67543.1 differs from that shown. Reason: Sequence differs at N-terminus.

The sequence AAO85220.1 differs from that shown. Reason: Erroneous initiation.

The sequence AK128302 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Erythrocyte maturation
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from direct assay Ref.4. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

enucleate erythrocyte development

Inferred from electronic annotation. Source: Ensembl

erythrocyte maturation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of myeloid cell apoptotic process

Inferred from direct assay Ref.4. Source: UniProtKB

regulation of mitotic cell cycle

Non-traceable author statement Ref.7. Source: UniProtKB

   Cellular_componentactomyosin contractile ring

Inferred from direct assay Ref.7. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.7. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

nuclear matrix

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7L5Y9-1)

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.
Isoform 2 (identifier: Q7L5Y9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-193: Missing.
     265-265: M → TCTVAD
Isoform 3 (identifier: Q7L5Y9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     153-193: Missing.
Isoform 4 (identifier: Q7L5Y9-4)

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.
Isoform 5 (identifier: Q7L5Y9-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Macrophage erythroblast attacher
PRO_0000284936

Regions

Domain121 – 15333LisH
Domain159 – 21658CTLH
Region1 – 124124Extracellular and involved in cell to cell contact

Natural variations

Alternative sequence152 – 23281EDLVN…AEGSQ → GTCKKALQPSRREPAGRGAP GHGHAGLPARHAHLPVQGPS GPCTVADADPAVPVRQLPTT PAGKQFCVHPHPAGWPLSHQ D in isoform 4.
VSP_024784
Alternative sequence153 – 24593DLVNI…GMLAF → TCKKALQPSRREPAGRGAPG HGHAGLPARHAHLPVQGPSG PCTVADADPAVPVRQLPTTP AGKQFCVHPHPAGRPLSHQD TTVLQGGRQLQEP in isoform 5.
VSP_024785
Alternative sequence153 – 19341Missing in isoform 2 and isoform 3.
VSP_024786
Alternative sequence233 – 30068Missing in isoform 4.
VSP_024788
Alternative sequence246 – 396151Missing in isoform 5.
VSP_024789
Alternative sequence2651M → TCTVAD in isoform 2.
VSP_024790
Natural variant341R → C.
Corresponds to variant rs34082974 [ dbSNP | Ensembl ].
VAR_051150

Experimental info

Sequence conflict321R → C in AAP74806. Ref.1
Sequence conflict561K → R in AAC67543. Ref.4
Sequence conflict1011R → L in AAC67543. Ref.4
Sequence conflict1231K → R in BAA91499. Ref.2
Sequence conflict3131D → V in AAC67543. Ref.4
Sequence conflict3271P → R in AAC67543. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 361FB82BE0240C21

FASTA39645,287
        10         20         30         40         50         60 
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSG 

        70         80         90        100        110        120 
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAASVW 

       130        140        150        160        170        180 
KRKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERRETATCLA 

       190        200        210        220        230        240 
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM 

       250        260        270        280        290        300 
GMLAFPPDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP 

       310        320        330        340        350        360 
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY 

       370        380        390 
VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM 

« Hide

Isoform 2 [UniParc].

Checksum: 7EDD1E1771B311F0
Show »

FASTA36040,869
Isoform 3 [UniParc].

Checksum: C949C3631DCD33E1
Show »

FASTA35540,410
Isoform 4 [UniParc].

Checksum: D7E3935AB82BE82D
Show »

FASTA32836,122
Isoform 5 [UniParc].

Checksum: 937AAE595F6C83BF
Show »

FASTA24526,802

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33936.1. [Q7L5Y9-1]
CCDS33937.1. [Q7L5Y9-3]
RefSeqNP_001017405.1. NM_001017405.1. [Q7L5Y9-1]
NP_005873.2. NM_005882.3. [Q7L5Y9-3]
UniGeneHs.139896.

3D structure databases

ProteinModelPortalQ7L5Y9.
SMRQ7L5Y9. Positions 336-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115584. 12 interactions.
MINTMINT-4725016.
STRING9606.ENSP00000302830.

PTM databases

PhosphoSiteQ7L5Y9.

Polymorphism databases

DMDM74754297.

Proteomic databases

MaxQBQ7L5Y9.
PaxDbQ7L5Y9.
PRIDEQ7L5Y9.

Protocols and materials databases

DNASU10296.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264750; ENSP00000264750; ENSG00000090316. [Q7L5Y9-3]
ENST00000303400; ENSP00000302830; ENSG00000090316. [Q7L5Y9-1]
GeneID10296.
KEGGhsa:10296.
UCSCuc003gda.3. human. [Q7L5Y9-1]
uc003gdb.3. human. [Q7L5Y9-3]

Organism-specific databases

CTD10296.
GeneCardsGC04P001273.
HGNCHGNC:13731. MAEA.
HPAHPA036886.
MIM606801. gene.
neXtProtNX_Q7L5Y9.
PharmGKBPA30533.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241866.
HOVERGENHBG053270.
InParanoidQ7L5Y9.
OrthoDBEOG722J8H.
PhylomeDBQ7L5Y9.
TreeFamTF314273.

Gene expression databases

ArrayExpressQ7L5Y9.
BgeeQ7L5Y9.
CleanExHS_MAEA.
GenevestigatorQ7L5Y9.

Family and domain databases

InterProIPR013144. CRA_dom.
IPR024964. CTLH/CRA.
IPR006595. CTLH_C.
IPR006594. LisH_dimerisation.
[Graphical view]
PfamPF10607. CLTH. 1 hit.
[Graphical view]
SMARTSM00757. CRA. 1 hit.
SM00668. CTLH. 1 hit.
SM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50897. CTLH. 1 hit.
PS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAEA. human.
GenomeRNAi10296.
NextBio39018.
PROQ7L5Y9.
SOURCESearch...

Entry information

Entry nameMAEA_HUMAN
AccessionPrimary (citable) accession number: Q7L5Y9
Secondary accession number(s): O95285 expand/collapse secondary AC list , Q5JB54, Q6ZRD6, Q9BQ11, Q9H9V6, Q9H9Z4, Q9NW84
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM