CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004345
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Membrane cofactor protein 
Protein Synonyms/Alias
 TLX; Trophoblast leukocyte common antigen; CD46 
Gene Name
 CD46 
Gene Synonyms/Alias
 MCP; MIC10 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66RVDYKCKKGYFYIPPubiquitination[1]
224SRAAPECKVVKCRFPubiquitination[1]
375YLQRRKKKGTYLTDEubiquitination[2, 3, 4]
388DETHREVKFTSL***ubiquitination[3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement- mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T- cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. A number of viral and bacterial pathogens seem to exploit this property and directly induce an immunosuppressive phenotype in T-cells by binding to CD46. 
Sequence Annotation
 DOMAIN 35 96 Sushi 1.
 DOMAIN 97 159 Sushi 2.
 DOMAIN 160 225 Sushi 3.
 DOMAIN 226 285 Sushi 4.
 CARBOHYD 83 83 N-linked (GlcNAc...).
 CARBOHYD 114 114 N-linked (GlcNAc...).
 CARBOHYD 163 163 O-linked (GalNAc...) (Potential).
 CARBOHYD 273 273 N-linked (GlcNAc...).
 CARBOHYD 290 290 O-linked (GalNAc...) (Potential).
 CARBOHYD 291 291 O-linked (GalNAc...) (Potential).
 CARBOHYD 292 292 O-linked (GalNAc...) (Potential).
 CARBOHYD 298 298 O-linked (GalNAc...) (Potential).
 CARBOHYD 300 300 O-linked (GalNAc...) (Potential).
 CARBOHYD 302 302 O-linked (GalNAc...) (Potential).
 CARBOHYD 303 303 O-linked (GalNAc...) (Potential).
 CARBOHYD 304 304 O-linked (GalNAc...) (Potential).
 CARBOHYD 305 305 O-linked (GalNAc...) (Potential).
 CARBOHYD 306 306 O-linked (GalNAc...) (Potential).
 CARBOHYD 307 307 O-linked (GalNAc...) (Potential).
 CARBOHYD 309 309 O-linked (GalNAc...) (Potential).
 CARBOHYD 312 312 O-linked (GalNAc...) (Potential).
 CARBOHYD 313 313 O-linked (GalNAc...) (Potential).
 CARBOHYD 315 315 O-linked (GalNAc...) (Potential).
 CARBOHYD 320 320 O-linked (GalNAc...) (Potential).
 CARBOHYD 326 326 O-linked (GalNAc...) (Potential).
 DISULFID 35 80 By similarity.
 DISULFID 64 94 By similarity.
 DISULFID 99 141 By similarity.
 DISULFID 127 157 By similarity.
 DISULFID 162 210 By similarity.
 DISULFID 191 223 By similarity.
 DISULFID 228 270 By similarity.
 DISULFID 256 283 By similarity.  
Keyword
 3D-structure; Alternative splicing; Complement pathway; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Disease mutation; Disulfide bond; Fertilization; Glycoprotein; Hemolytic uremic syndrome; Host-virus interaction; Immunity; Innate immunity; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal; Sushi; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 392 AA 
Protein Sequence
MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 60
DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 120
YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 180
FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 240
GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 300
VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI VIAIVVGVAV 360
ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL 392 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0004872; F:receptor activity; TAS:ProtInc.
 GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0045916; P:negative regulation of complement activation; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:Compara.
 GO:0030449; P:regulation of complement activation; TAS:Reactome.
 GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR017341; M_CF_CD46.
 IPR000436; Sushi_SCR_CCP. 
Pfam
 PF00084; Sushi 
SMART
 SM00032; CCP 
PROSITE
 PS50923; SUSHI 
PRINTS