CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015777
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Macrophage erythroblast attacher 
Protein Synonyms/Alias
 Cell proliferation-inducing gene 5 protein; Erythroblast macrophage protein; Human lung cancer oncogene 10 protein; HLC-10 
Gene Name
 MAEA 
Gene Synonyms/Alias
 EMP; HLC10; PIG5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23VQEYPTLKVPYETLNubiquitination[1, 2, 3]
31VPYETLNKRFRAAQKubiquitination[2, 4, 5]
84KLSVLKRKAVESIQAubiquitination[2]
107KRRIEHLKEHSSDQPubiquitination[2]
121PAAASVWKRKRMDRMubiquitination[2]
144GYYNTAVKLARQSGIubiquitination[4]
323VCSRSLNKLAQPLPMubiquitination[5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 121 153 LisH.
 DOMAIN 159 216 CTLH.
 REGION 1 124 Extracellular and involved in cell to  
Keyword
 Actin-binding; Alternative splicing; Cell cycle; Cell division; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Erythrocyte maturation; Membrane; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 396 AA 
Protein Sequence
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSG 60
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAASVW 120
KRKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERRETATCLA 180
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQAM 240
GMLAFPPDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTLTL QAGLSAIKTP 300
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY 360
VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM 396 
Gene Ontology
 GO:0005826; C:actomyosin contractile ring; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
 GO:0016363; C:nuclear matrix; IDA:UniProtKB.
 GO:0005819; C:spindle; IDA:UniProtKB.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0007155; P:cell adhesion; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007010; P:cytoskeleton organization; IEA:Compara.
 GO:0048822; P:enucleate erythrocyte development; IEA:Compara.
 GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
 GO:0033033; P:negative regulation of myeloid cell apoptotic process; IDA:UniProtKB.
 GO:0007346; P:regulation of mitotic cell cycle; NAS:UniProtKB. 
Interpro
 IPR013144; CRA_dom.
 IPR024964; CTLH/CRA.
 IPR006595; CTLH_C.
 IPR006594; LisH_dimerisation.
 IPR027370; zf-RING_LisH. 
Pfam
 PF10607; CLTH
 PF13445; zf-RING_LisH 
SMART
 SM00757; CRA
 SM00668; CTLH
 SM00667; LisH 
PROSITE
 PS50897; CTLH
 PS50896; LISH 
PRINTS