CPLM-004346

Genbank Nucleotide ID

Membrane cofactor protein

Protein Synonyms/Alias

TLX; Trophoblast leukocyte common antigen; CD46

Homo sapiens (Human)

Position	Peptide	Type	References
314	QRRKKKGKADGGAEY	ubiquitination	[1, 2, 3, 4, 5, 6]
327	EYATYQTKSTTPAEQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]

[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] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] 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]
[5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[6] 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]
[7] A data set of human endogenous protein ubiquitination sites.
Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
[8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[9] 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

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.

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.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR017341; M_CF_CD46.
IPR000436; Sushi_SCR_CCP.