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P15529 (MCP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane cofactor protein
Alternative name(s):
TLX
Trophoblast leukocyte common antigen
CD_antigen=CD46
Gene names
Name:CD46
Synonyms:MCP, MIC10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.29 Ref.41

Subunit structure

Interacts with C3b and C4b. Binds to Measles virus H protein, to Human herpesvirus 6 GH protein and to human adenovirus B/D PIV/fiber protein, and acts as a receptor for these viruses. Binds to Streptococcus pyogenes M protein and to type IV pili from Neisseria, and may act as a receptor for these pathogenic bacteria. Ref.1 Ref.19 Ref.23 Ref.25 Ref.30 Ref.31 Ref.34 Ref.36 Ref.38 Ref.39 Ref.42 Ref.44 Ref.45 Ref.46 Ref.47

Subcellular location

Cytoplasmic vesiclesecretory vesicleacrosome inner membrane; Single-pass type I membrane protein. Note: Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide. Ref.35 Ref.37 Ref.43

Tissue specificity

Expressed by all cells except erythrocytes.

Domain

Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b.

Post-translational modification

N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding. Ref.35 Ref.43

Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding. Ref.35 Ref.43

In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by LCK. Ref.28 Ref.33

Involvement in disease

Hemolytic uremic syndrome atypical 2 (AHUS2) [MIM:612922]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations. Ref.40 Ref.49 Ref.50 Ref.51 Ref.53

Sequence similarities

Contains 4 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Biological processComplement pathway
Fertilization
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hemolytic uremic syndrome
   DomainRepeat
Signal
Sushi
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell mediated immunity

Inferred from mutant phenotype PubMed 23086448. Source: UniProt

adaptive immune response

Inferred by curator Ref.41. Source: UniProt

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

interleukin-10 production

Inferred from direct assay PubMed 23086448. Source: UniProt

negative regulation of complement activation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from direct assay PubMed 23086448. Source: UniProt

positive regulation of T cell proliferation

Inferred from direct assay Ref.41. Source: UniProt

positive regulation of gene expression

Inferred from mutant phenotype PubMed 23086448. Source: UniProt

positive regulation of interleukin-10 production

Inferred from direct assay Ref.41. Source: UniProt

positive regulation of memory T cell differentiation

Inferred from direct assay Ref.41. Source: UniProt

positive regulation of regulatory T cell differentiation

Inferred from direct assay Ref.41. Source: UniProt

positive regulation of transforming growth factor beta production

Inferred from direct assay Ref.41. Source: UniProt

proteolysis

Inferred from electronic annotation. Source: Ensembl

regulation of Notch signaling pathway

Inferred from direct assay PubMed 23086448. Source: UniProt

regulation of complement activation

Traceable author statement. Source: Reactome

sequestering of extracellular ligand from receptor

Inferred from direct assay PubMed 23086448. Source: UniProt

single fertilization

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 23086448. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

inner acrosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.3. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncadherin binding

Inferred from physical interaction PubMed 23086448. Source: UniProt

protein binding

Inferred from physical interaction PubMed 23086448. Source: IntAct

receptor activity

Traceable author statement Ref.21. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

JAG1P785045EBI-2623451,EBI-2847071

Alternative products

This entry describes 16 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. The complete sequences of the isoforms are not known. Isoforms are classified as alpha (isoform C and isoform D), beta (isoform E and isoform F), gamma (isoform A and isoform B) and delta (isoform N). Isoforms gamma are preferentially expressed in EBV-B cells and leukemic cells. Isoforms alpha (66 kDa) and isoforms beta (56 kDa) are found in all tissues except sperm. Isoform delta is expressed in spermatozoa. The exon 9 is specifically deleted in some placentae isoforms. All tissues differentially splice exon 13.
Isoform A (identifier: P15529-1)

Also known as: no del; ABC1;

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 B (identifier: P15529-2)

Also known as: del 13; ABC2;

The sequence of this isoform differs from the canonical sequence as follows:
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 384.
Isoform C (identifier: P15529-11)

Also known as: del 7; BC1;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
Isoform D (identifier: P15529-3)

Also known as: del 7-13; BC2;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 369.
Isoform E (identifier: P15529-12)

Also known as: del 7-8; C1;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.
Isoform F (identifier: P15529-4)

Also known as: del 7-8-13; C2;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 354.
Isoform G (identifier: P15529-13)

Also known as: del 9;

The sequence of this isoform differs from the canonical sequence as follows:
     316-329: Missing.
Isoform H (identifier: P15529-5)

Also known as: del 9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     316-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 370.
Isoform I (identifier: P15529-14)

Also known as: del 7-9;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     316-329: Missing.
Isoform J (identifier: P15529-6)

Also known as: del 7-9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     316-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 355.
Isoform K (identifier: P15529-15)

Also known as: del 7-8-9;

The sequence of this isoform differs from the canonical sequence as follows:
     286-329: Missing.
Isoform L (identifier: P15529-7)

Also known as: del 7-8-9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 340.
Isoform M (identifier: P15529-8)

Also known as: del 7-12a-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     355-367: Missing.
     368-392: YLQRRKKKGTYLTDETHREVKFTSL → GKQMVELNMPLTRLNQPLQQSREAE
Isoform N (identifier: P15529-9)

Also known as: del 7-8-12-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.
     355-392: VVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL → GKQMVELNMPLTRLNQPLQQSREAE
Note: No experimental confirmation available.
Isoform 2 (identifier: P15529-10)

The sequence of this isoform differs from the canonical sequence as follows:
     301-305: Missing.
Isoform 3 (identifier: P15529-16)

The sequence of this isoform differs from the canonical sequence as follows:
     33-33: D → G
     34-96: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG
Note: Contains a phosphotyrosine at position 321.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.1 Ref.16 Ref.17 Ref.18
Chain35 – 392358Membrane cofactor protein
PRO_0000006008

Regions

Topological domain35 – 343309Extracellular Potential
Transmembrane344 – 36623Helical; Potential
Topological domain367 – 39226Cytoplasmic Potential
Domain35 – 9662Sushi 1
Domain97 – 15963Sushi 2
Domain160 – 22566Sushi 3
Domain226 – 28560Sushi 4
Compositional bias302 – 32625Ser/Thr-rich

Amino acid modifications

Glycosylation831N-linked (GlcNAc...)
Glycosylation1141N-linked (GlcNAc...)
Glycosylation1631O-linked (GalNAc...) Potential
Glycosylation2731N-linked (GlcNAc...)
Glycosylation2901O-linked (GalNAc...) Potential
Glycosylation2911O-linked (GalNAc...) Potential
Glycosylation2921O-linked (GalNAc...) Potential
Glycosylation2981O-linked (GalNAc...) Potential
Glycosylation3001O-linked (GalNAc...) Potential
Glycosylation3021O-linked (GalNAc...) Potential
Glycosylation3031O-linked (GalNAc...) Potential
Glycosylation3041O-linked (GalNAc...) Potential
Glycosylation3051O-linked (GalNAc...) Potential
Glycosylation3061O-linked (GalNAc...) Potential
Glycosylation3071O-linked (GalNAc...) Potential
Glycosylation3091O-linked (GalNAc...) Potential
Glycosylation3121O-linked (GalNAc...) Potential
Glycosylation3131O-linked (GalNAc...) Potential
Glycosylation3151O-linked (GalNAc...) Potential
Glycosylation3201O-linked (GalNAc...) Potential
Glycosylation3261O-linked (GalNAc...) Potential
Disulfide bond35 ↔ 80 By similarity
Disulfide bond64 ↔ 94 By similarity
Disulfide bond99 ↔ 141 By similarity
Disulfide bond127 ↔ 157 By similarity
Disulfide bond162 ↔ 210 By similarity
Disulfide bond191 ↔ 223 By similarity
Disulfide bond228 ↔ 270 By similarity
Disulfide bond256 ↔ 283 By similarity

Natural variations

Alternative sequence331D → G in isoform 3.
VSP_019005
Alternative sequence34 – 9663Missing in isoform 3.
VSP_019006
Alternative sequence286 – 32944Missing in isoform K and isoform L.
VSP_009176
Alternative sequence286 – 31530Missing in isoform E, isoform F and isoform N.
VSP_009175
Alternative sequence286 – 30015Missing in isoform C, isoform D, isoform I, isoform J and isoform M.
VSP_009174
Alternative sequence301 – 3055Missing in isoform 2.
VSP_001201
Alternative sequence316 – 32914Missing in isoform G, isoform H, isoform I and isoform J.
VSP_009177
Alternative sequence355 – 39238VVGVA…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform N.
VSP_009178
Alternative sequence355 – 36713Missing in isoform M.
VSP_001202
Alternative sequence368 – 39225YLQRR…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform M.
VSP_001203
Alternative sequence377 – 39216TYLTD…KFTSL → KADGGAEYATYQTKSTTPAE QRG in isoform B, isoform D, isoform F, isoform H, isoform J, isoform L and isoform 3.
VSP_001204
Natural variant131S → F. Ref.9 Ref.14
Corresponds to variant rs138843816 [ dbSNP | Ensembl ].
VAR_026567
Natural variant351C → Y in AHUS2. Ref.50
VAR_063656
Natural variant591R → Q. Ref.14
VAR_026568
Natural variant1651P → S in AHUS2; reduced cell surface expression. Ref.51
VAR_026569
Natural variant2161W → C in AHUS2. Ref.53
VAR_063657
Natural variant2281C → Y in a colorectal cancer sample; somatic mutation. Ref.52
VAR_035828
Natural variant2311P → R in AHUS2. Ref.53
VAR_063658
Natural variant2401S → P in AHUS2; no change in cell surface expression but reduced activity. Ref.49
VAR_026570
Natural variant2661D → N. Ref.10
Corresponds to variant rs17006830 [ dbSNP | Ensembl ].
VAR_022262
Natural variant271 – 2722Missing in AHUS2; no cell surface expression.
VAR_026571
Natural variant3241P → L. Ref.10
Corresponds to variant rs41317833 [ dbSNP | Ensembl ].
VAR_022263
Natural variant3531A → V. Ref.10 Ref.52
Corresponds to variant rs35366573 [ dbSNP | Ensembl ].
VAR_022264
Natural variant3551V → G. Ref.10
VAR_022265

Experimental info

Mutagenesis831N → Q: No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding. Ref.24 Ref.26 Ref.31
Mutagenesis1141N → Q: Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding. Ref.24 Ref.26 Ref.31
Mutagenesis2731N → Q: Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding. Ref.24 Ref.26 Ref.31
Sequence conflict251V → A in CAE45719. Ref.8
Sequence conflict1081G → S in CAD97694. Ref.8
Sequence conflict1591K → S in CAD97694. Ref.8
Sequence conflict1621C → R in CAI45983. Ref.8

Secondary structure

........................................................ 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (no del) (ABC1) [UniParc].

Last modified January 16, 2004. Version 3.
Checksum: 85FE0CF100EA703E

FASTA39243,747
        10         20         30         40         50         60 
MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 

        70         80         90        100        110        120 
DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 

       130        140        150        160        170        180 
YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 

       190        200        210        220        230        240 
FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 

       250        260        270        280        290        300 
GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 

       310        320        330        340        350        360 
VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI VIAIVVGVAV 

       370        380        390 
ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL 

« Hide

Isoform B (del 13) (ABC2) [UniParc].

Checksum: 8E4C641F2BD8AC15
Show »

FASTA39944,238
Isoform C (del 7) (BC1) [UniParc].

Checksum: 2CA6F61752570B57
Show »

FASTA37742,248
Isoform D (del 7-13) (BC2) [UniParc].

Checksum: F45B03CBB466AA8C
Show »

FASTA38442,738
Isoform E (del 7-8) (C1) [UniParc].

Checksum: AA3F3F3110E8727D
Show »

FASTA36240,868
Isoform F (del 7-8-13) (C2) [UniParc].

Checksum: 3BD3000428BBA2EA
Show »

FASTA36941,359
Isoform G (del 9) [UniParc].

Checksum: AE60F628C4DC271C
Show »

FASTA37842,193
Isoform H (del 9-13) [UniParc].

Checksum: 45FB279DC30B895E
Show »

FASTA38542,683
Isoform I (del 7-9) [UniParc].

Checksum: E48C0E7C0A616FF1
Show »

FASTA36340,693
Isoform J (del 7-9-13) [UniParc].

Checksum: CC2FD6E11C9A81E4
Show »

FASTA37041,183
Isoform K (del 7-8-9) [UniParc].

Checksum: A6F0D0E7C4203DDF
Show »

FASTA34839,313
Isoform L (del 7-8-9-13) [UniParc].

Checksum: 86C83A0D515EDF86
Show »

FASTA35539,804
Isoform M (del 7-12a-13) [UniParc].

Checksum: B09E917D96F2C0DC
Show »

FASTA36440,705
Isoform N (del 7-8-12-13) [UniParc].

Checksum: 8EFCEDA30D3C818E
Show »

FASTA34939,325
Isoform 2 [UniParc].

Checksum: 20E7721BB47CA27C
Show »

FASTA38743,286
Isoform 3 [UniParc].

Checksum: F57541078036A7EA
Show »

FASTA33636,826

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins."
Lublin D.M., Liszewski M.K., Post T.W., Arce M.A., le Beau M.M., Rebentisch M.B., Lemons R.S., Seya T., Atkinson J.P.
J. Exp. Med. 168:181-194(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), PROTEIN SEQUENCE OF 35-58, INTERACTION WITH C3B.
[2]"Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a regulator of complement activation."
Purcell D.F., Russell S.M., Deacon N.J., Brown M.A., Hooker D.J., McKenzie I.F.
Immunogenetics 33:335-344(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), ALTERNATIVE SPLICING.
[3]"Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype."
Post T.W., Liszewski M.K., Adams E.M., Tedja I., Miller E.A., Atkinson J.P.
J. Exp. Med. 174:93-102(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E AND F).
[4]"Characterization of a cDNA clone coding for human testis membrane cofactor protein (MCP, CD46)."
Cervoni F., Fenichel P., Akhoundi C., Hsi B.L., Rossi B.
Mol. Reprod. Dev. 34:107-113(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F).
Tissue: Testis.
[5]"Post-translational modification and intracellular localization of a splice product of CD46 cloned from human testis: role of the intracellular domains in O-glycosylation."
Hara T., Suzuki Y., Nakazawa T., Nishimura H., Nagasawa S., Nishiguchi M., Matsumoto M., Hatanaka M., Kitamura M., Seya T.
Immunology 93:546-555(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N).
Tissue: Testis.
[6]"Molecular cloning of human CD46 (membrane cofactor protein) CDS from cancer cell lines in a retroviral vector system."
Xue Z.T., Widegren B., Salford L.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; F AND L).
[7]"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] (ISOFORM D).
Tissue: Teratocarcinoma.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND E).
Tissue: Fetal kidney, Liver and Salivary gland.
[9]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), VARIANT PHE-13.
Tissue: Liver.
[10]SeattleSNPs variation discovery resource
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-266; LEU-324; VAL-353 AND GLY-355.
[11]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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 D).
Tissue: Testis.
[14]"Analysis of measles virus binding sites of the CD46 gene in patients with subacute sclerosing panencephalitis."
Kusuhara K., Sasaki Y., Nakao F., Ihara K., Hattori H., Yamashita S., Nihei K., Koide N., Aiba H., Takeshita K., Hara T.
J. Infect. Dis. 181:1447-1449(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-158, VARIANTS PHE-13 AND GLN-59.
[15]"Characterization of the promoter region of the membrane cofactor protein (CD46) gene of the human complement system and comparison to a membrane cofactor protein-like genetic element."
Cui W., Hourcade D., Post T.W., Greenlund A.C., Atkinson J.P., Kumar V.
J. Immunol. 151:4137-4146(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[16]"Homology of an acrosome-reacted sperm-specific antigen to CD46."
Okabe M., Ying X., Nagira M., Ikawa M., Kohama Y., Mimura T., Tanaka K.
J. Pharmacobio-Dyn. 15:455-459(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-60.
Tissue: Sperm.
[17]"Human non-lineage antigen, CD46 (HuLy-m5): purification and partial sequencing demonstrates structural homology with complement-regulating glycoproteins."
Purcell D.F., Deacon N.J., Andrew S.M., McKenzie I.F.
Immunogenetics 31:21-28(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-58.
[18]"Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus."
Naniche D., Varior-Krishnan G., Cervoni F., Wild T.F., Rossi B., Rabourdin-Combe C., Gerlier D.
J. Virol. 67:6025-6032(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-49, BINDING TO MEASLES VIRUS.
[19]"Contribution of the repeating domains of membrane cofactor protein (CD46) of the complement system to ligand binding and cofactor activity."
Adams E.M., Brown M.C., Nunge M., Krych M., Atkinson J.P.
J. Immunol. 147:3005-3011(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C3B AND C4B.
[20]"Tissue-specific and allelic expression of the complement regulator CD46 is controlled by alternative splicing."
Russell S.M., Sparrow R.L., McKenzie I.F.C., Purcell D.F.J.
Eur. J. Immunol. 22:1513-1518(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[21]"The human CD46 molecule is a receptor for measles virus (Edmonston strain)."
Doerig R.E., Marcil A., Chopra A., Richardson C.D.
Cell 75:295-305(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO MEASLES VIRUS.
[22]"Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46)."
Manchester M., Valsamakis A., Kaufman R., Liszewski M.K., Alvarez J., Atkinson J.P., Lublin D.M., Oldstone M.B.
Proc. Natl. Acad. Sci. U.S.A. 92:2303-2307(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO MEASLES VIRUS.
[23]"Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus."
Okada N., Liszewski M.K., Atkinson J.P., Caparon M.
Proc. Natl. Acad. Sci. U.S.A. 92:2489-2493(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STREPTOCOCCUS PYOGENES M PROTEIN.
[24]"The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor."
Maisner A., Alvarez J., Liszewski M.K., Atkinson D.J., Atkinson J.P., Herrler G.
J. Virol. 70:4973-4977(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[25]"Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria."
Kaellstroem H., Liszewski M.K., Atkinson J.P., Jonsson A.-B.
Mol. Microbiol. 25:639-647(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEISSERIA TYPE IV PILI.
[26]"Membrane cofactor protein: importance of N- and O-glycosylation for complement regulatory function."
Liszewski M.K., Leung M.K., Atkinson J.P.
J. Immunol. 161:3711-3718(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[27]"CD46 is a cellular receptor for human herpesvirus 6."
Santoro F., Kennedy P.E., Locatelli G., Malnati M.S., Berger E.A., Lusso P.
Cell 99:817-827(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING OF HUMAN HERPESVIRUS 6.
[28]"Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine phosphorylation."
Wang G., Liszewski M.K., Chan A.C., Atkinson J.P.
J. Immunol. 164:1839-1846(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-384 (ISOFORM B); TYR-369 (ISOFORM D); TYR-354 (ISOFORM F); TYR-370 (ISOFORM H); TYR-355 (ISOFORM J); TYR-340 (ISOFORM L) AND TYR-321 (ISOFORM 3).
[29]"CD46, a new costimulatory molecule for T cells, that induces p120CBL and LAT phosphorylation."
Astier A., Trescol-Biemont M.-C., Azocar O., Lamouille B., Rabourdin-Combe C.
J. Immunol. 164:6091-6095(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"SLAM (CDw150) is a cellular receptor for measles virus."
Tatsuo H., Ono N., Tanaka K., Yanagi Y.
Nature 406:893-897(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEASLES VIRUS H PROTEIN.
[31]"Attachment of Neisseria gonorrhoeae to the cellular pilus receptor CD46: identification of domains important for bacterial adherence."
Kaellstroem H., Blackmer Gill D., Albiger B., Liszewski M.K., Atkinson J.P., Jonsson A.-B.
Cell. Microbiol. 3:133-143(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEISSERIA TYPE IV PILI, MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[32]"Human Herpesvirus 6 and Measles Virus employ distinct CD46 domains for receptor function."
Greenstone H.L., Santoro F., Lusso P., Berger E.A.
J. Biol. Chem. 277:39112-39118(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING OF HUMAN HERPESVIRUS 6.
[33]"CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae."
Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.
J. Cell Biol. 156:951-957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION (ISOFORMS B/D/F/H/J/L/3).
[34]"Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46)."
Giannakis E., Jokiranta T.S., Ormsby R.J., Duthy T.G., Male D.A., Christiansen D., Fischetti V.A., Bagley C., Loveland B.E., Gordon D.L.
J. Immunol. 168:4585-4592(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STREPTOCOCCUS PYOGENES M PROTEIN.
[35]"Characterization of human membrane cofactor protein (MCP; CD46) on spermatozoa."
Riley R.C., Kemper C., Leung M., Atkinson J.P.
Mol. Reprod. Dev. 62:534-546(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[36]"Interaction of glycoprotein H of human herpesvirus 6 with the cellular receptor CD46."
Santoro F., Greenstone H.L., Insinga A., Liszewski M.K., Atkinson J.P., Lusso P., Berger E.A.
J. Biol. Chem. 278:25964-25969(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN HERPESVIRUS 6 GH PROTEIN.
[37]"Down-regulation of CD46 by piliated Neisseria gonorrhoeae."
Gill D.B., Koomey M., Cannon J.G., Atkinson J.P.
J. Exp. Med. 198:1313-1322(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[38]"Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-glycoprotein Q complex associates with human CD46."
Mori Y., Yang X., Akkapaiboon P., Okuno T., Yamanishi K.
J. Virol. 77:4992-4999(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN HERPESVIRUS 6 GH PROTEIN.
[39]"Adenovirus type 11 uses CD46 as a cellular receptor."
Segerman A., Atkinson J.P., Marttila M., Dennerquist V., Wadell G., Arnberg N.
J. Virol. 77:9183-9191(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 11 PIV/FIBER PROTEIN.
[40]"Familial haemolytic uraemic syndrome and an MCP mutation."
Noris M., Brioschi S., Caprioli J., Todeschini M., Bresin E., Porrati F., Gamba S., Remuzzi G.
Lancet 362:1542-1547(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[41]"Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype."
Kemper C., Chan A.C., Green J.M., Brett K.A., Murphy K.M., Atkinson J.P.
Nature 421:388-392(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[42]"CD46 is a cellular receptor for group B adenoviruses."
Gaggar A., Shayakhmetov D.M., Lieber A.
Nat. Med. 9:1408-1412(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS B PIV/FIBER PROTEIN, IDENTIFICATION BY MASS SPECTROMETRY.
[43]"Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form."
Hakulinen J., Junnikkala S., Sorsa T., Meri S.
Eur. J. Immunol. 34:2620-2629(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[44]"Membrane cofactor protein is a receptor for adenoviruses associated with epidemic keratoconjunctivitis."
Wu E., Trauger S.A., Pache L., Mullen T.-M., von Seggern D.J., Siuzdak G., Nemerow G.R.
J. Virol. 78:3897-3905(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS D TYPE 37 PIV/FIBER PROTEIN, IDENTIFICATION BY MASS SPECTROMETRY.
[45]"The human membrane cofactor CD46 is a receptor for species B adenovirus serotype 3."
Sirena D., Lilienfeld B., Eisenhut M., Kaelin S., Boucke K., Beerli R.R., Vogt L., Ruedl C., Bachmann M.F., Greber U.F., Hemmi S.
J. Virol. 78:4454-4462(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 3 PIV/FIBER PROTEIN.
[46]"Localization of regions in CD46 that interact with adenovirus."
Gaggar A., Shayakhmetov D.M., Liszewski M.K., Atkinson J.P., Lieber A.
J. Virol. 79:7503-7513(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 35 PIV/FIBER PROTEIN.
[47]"CD46 is a cellular receptor for all species B adenoviruses except types 3 and 7."
Marttila M., Persson D., Gustafsson D., Liszewski M.K., Atkinson J.P., Wadell G., Arnberg N.
J. Virol. 79:14429-14436(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS B PIV/FIBER PROTEIN.
[48]"Crystal structure of two CD46 domains reveals an extended measles virus-binding surface."
Casasnovas J.M., Larvie M., Stehle T.
EMBO J. 18:2911-2922(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 35-160.
[49]"Mutations in human complement regulator, membrane cofactor protein (CD46), predispose to development of familial hemolytic uremic syndrome."
Richards A., Kemp E.J., Liszewski M.K., Goodship J.A., Lampe A.K., Decorte R., Muesluemanoglu M.H., Kavukcu S., Filler G., Pirson Y., Wen L.S., Atkinson J.P., Goodship T.H.J.
Proc. Natl. Acad. Sci. U.S.A. 100:12966-12971(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS AHUS2 PRO-240 AND 271-ASP-SER-272 DEL.
[50]"Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical presentation, response to treatment, and outcome."
The international registry of recurrent and familial HUS/TTP
Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F., Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F., Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K., Kavanagh D., Atkinson J.P., Remuzzi G.
Blood 108:1267-1279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AHUS2 TYR-35.
[51]"Insights into hemolytic uremic syndrome: segregation of three independent predisposition factors in a large, multiple affected pedigree."
Esparza-Gordillo J., Jorge E.G., Garrido C.A., Carreras L., Lopez-Trascasa M., Sanchez-Corral P., de Cordoba S.R.
Mol. Immunol. 43:1769-1775(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AHUS2 SER-165.
[52]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-228 AND VAL-353.
[53]"Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome."
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.
Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS2 CYS-216 AND ARG-231.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00651 mRNA. Translation: CAA68675.1.
M58050 mRNA. Translation: AAA62833.1.
X59405 mRNA. No translation available.
X59406 mRNA. No translation available.
X59407 mRNA. No translation available.
X59408 mRNA. No translation available.
X59409 mRNA. No translation available.
X59410 mRNA. No translation available.
S51940 mRNA. Translation: AAB24802.1.
D84105 mRNA. Translation: BAA12224.1.
EF076055 mRNA. Translation: ABK81635.1.
EF076056 mRNA. Translation: ABK81636.1.
EF076057 mRNA. Translation: ABK81637.1.
EF076058 mRNA. Translation: ABK81638.1.
AK291227 mRNA. Translation: BAF83916.1.
BX537451 mRNA. Translation: CAD97694.1.
BX640613 mRNA. Translation: CAE45719.1.
BX649050 mRNA. Translation: CAI45983.1.
AK222822 mRNA. Translation: BAD96542.1.
AY916779 Genomic DNA. Translation: AAW82433.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73947.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73948.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73949.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73950.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73951.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73952.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73953.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73954.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18804.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18805.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18806.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18807.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18808.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18809.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18810.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18811.1.
CH471100 Genomic DNA. Translation: EAW93465.1.
CH471100 Genomic DNA. Translation: EAW93470.1.
CH471100 Genomic DNA. Translation: EAW93476.1.
BC030594 mRNA. Translation: AAH30594.1.
AF209712 mRNA. Translation: AAF73844.1.
AF209713 mRNA. Translation: AAF73845.1.
AF209714 mRNA. Translation: AAF73846.1.
S65879 Genomic DNA. Translation: AAD13968.1.
CCDSCCDS1479.1. [P15529-9]
CCDS1480.1. [P15529-3]
CCDS1481.1. [P15529-4]
CCDS1482.1. [P15529-2]
CCDS1484.1. [P15529-7]
CCDS1485.1. [P15529-1]
CCDS31008.1. [P15529-11]
CCDS31009.1. [P15529-12]
PIRG02913.
I54479.
I57998.
S01896.
RefSeqNP_002380.3. NM_002389.4. [P15529-1]
NP_722548.1. NM_153826.3. [P15529-3]
NP_758860.1. NM_172350.2. [P15529-9]
NP_758861.1. NM_172351.2. [P15529-11]
NP_758862.1. NM_172352.2. [P15529-12]
NP_758863.1. NM_172353.2. [P15529-4]
NP_758869.1. NM_172359.2. [P15529-2]
NP_758871.1. NM_172361.2. [P15529-7]
UniGeneHs.510402.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CKLX-ray3.10A/B/C/D/E/F35-160[»]
1HR4model-A159-284[»]
2O39X-ray2.85C/D35-160[»]
3INBX-ray3.10C/D35-160[»]
3L89X-ray3.50M/N/O/P/Q/R/S/T/U/V/W/X35-160[»]
3O8EX-ray2.84B/D35-286[»]
ProteinModelPortalP15529.
SMRP15529. Positions 35-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110346. 11 interactions.
DIPDIP-41232N.
IntActP15529. 6 interactions.
MINTMINT-222279.

PTM databases

PhosphoSiteP15529.

Polymorphism databases

DMDM41019474.

Proteomic databases

MaxQBP15529.
PaxDbP15529.
PRIDEP15529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322875; ENSP00000313875; ENSG00000117335. [P15529-2]
ENST00000322918; ENSP00000314664; ENSG00000117335. [P15529-9]
ENST00000354848; ENSP00000346912; ENSG00000117335. [P15529-3]
ENST00000357714; ENSP00000350346; ENSG00000117335. [P15529-4]
ENST00000358170; ENSP00000350893; ENSG00000117335. [P15529-1]
ENST00000360212; ENSP00000353342; ENSG00000117335. [P15529-7]
ENST00000361067; ENSP00000354358; ENSG00000117335. [P15529-5]
ENST00000367041; ENSP00000356008; ENSG00000117335. [P15529-12]
ENST00000367042; ENSP00000356009; ENSG00000117335. [P15529-11]
ENST00000367047; ENSP00000356014; ENSG00000117335. [P15529-16]
ENST00000441839; ENSP00000413543; ENSG00000117335. [P15529-8]
ENST00000480003; ENSP00000418471; ENSG00000117335. [P15529-6]
GeneID4179.
KEGGhsa:4179.
UCSCuc001hgc.3. human. [P15529-1]
uc001hgg.3. human. [P15529-9]
uc001hgh.3. human. [P15529-7]
uc001hgi.3. human. [P15529-11]
uc001hgj.3. human. [P15529-2]
uc001hgl.3. human. [P15529-12]
uc001hgm.3. human. [P15529-3]
uc001hgp.3. human. [P15529-4]

Organism-specific databases

CTD4179.
GeneCardsGC01P207925.
GeneReviewsCD46.
HGNCHGNC:6953. CD46.
HPACAB010401.
HPA016903.
MIM120920. gene+phenotype.
612922. phenotype.
neXtProtNX_P15529.
Orphanet93576. Atypical hemolytic uremic syndrome with MCP/CD46 anomaly.
244242. HELLP syndrome.
PharmGKBPA30700.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG151270.
HOVERGENHBG006335.
KOK04007.
OMACKVVKCR.
OrthoDBEOG7XPZ64.
PhylomeDBP15529.
TreeFamTF334137.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP15529.
BgeeP15529.
GenevestigatorP15529.

Family and domain databases

InterProIPR017341. M_CF_CD46.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 4 hits.
[Graphical view]
PIRSFPIRSF037971. TLX_CD46. 1 hit.
SMARTSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 4 hits.
PROSITEPS50923. SUSHI. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD46. human.
EvolutionaryTraceP15529.
GeneWikiCD46.
GenomeRNAi4179.
NextBio16458.
PMAP-CutDBP15529.
PROP15529.
SOURCESearch...

Entry information

Entry nameMCP_HUMAN
AccessionPrimary (citable) accession number: P15529
Secondary accession number(s): A0T1T0 expand/collapse secondary AC list , A0T1T1, A0T1T2, Q15429, Q53GV9, Q5HY94, Q5VWS6, Q5VWS7, Q5VWS8, Q5VWS9, Q5VWT0, Q5VWT1, Q5VWT2, Q6N0A1, Q7Z3R5, Q9NNW2, Q9NNW3, Q9NNW4, Q9UCJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 16, 2004
Last modified: July 9, 2014
This is version 169 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries