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P15529

- MCP_HUMAN

UniProt

P15529 - MCP_HUMAN

Protein

Membrane cofactor protein

Gene

CD46

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (16 Jan 2004)
      Previous versions | rss
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    Functioni

    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 CD46.2 Publications

    GO - Molecular functioni

    1. cadherin binding Source: UniProt
    2. protein binding Source: IntAct
    3. receptor activity Source: ProtInc

    GO - Biological processi

    1. adaptive immune response Source: UniProt
    2. complement activation, classical pathway Source: UniProtKB-KW
    3. innate immune response Source: Reactome
    4. interleukin-10 production Source: UniProt
    5. negative regulation of complement activation Source: Ensembl
    6. negative regulation of gene expression Source: UniProt
    7. positive regulation of gene expression Source: UniProt
    8. positive regulation of interleukin-10 production Source: UniProt
    9. positive regulation of memory T cell differentiation Source: UniProt
    10. positive regulation of regulatory T cell differentiation Source: UniProt
    11. positive regulation of T cell proliferation Source: UniProt
    12. positive regulation of transforming growth factor beta production Source: UniProt
    13. proteolysis Source: Ensembl
    14. regulation of complement activation Source: Reactome
    15. regulation of Notch signaling pathway Source: UniProt
    16. sequestering of extracellular ligand from receptor Source: UniProt
    17. single fertilization Source: UniProtKB-KW
    18. T cell mediated immunity Source: UniProt
    19. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Complement pathway, Fertilization, Host-virus interaction, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane cofactor protein
    Alternative name(s):
    TLX
    Trophoblast leukocyte common antigen
    CD_antigen: CD46
    Gene namesi
    Name:CD46
    Synonyms:MCP, MIC10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6953. CD46.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicleacrosome inner membrane 3 Publications; Single-pass type I membrane protein 3 Publications
    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.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cell surface Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: Ensembl
    5. inner acrosomal membrane Source: UniProtKB-SubCell
    6. integral component of plasma membrane Source: ProtInc
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351C → Y in AHUS2. 1 Publication
    VAR_063656
    Natural varianti165 – 1651P → S in AHUS2; reduced cell surface expression. 1 Publication
    VAR_026569
    Natural varianti216 – 2161W → C in AHUS2. 1 Publication
    VAR_063657
    Natural varianti231 – 2311P → R in AHUS2. 1 Publication
    VAR_063658
    Natural varianti240 – 2401S → P in AHUS2; no change in cell surface expression but reduced activity.
    VAR_026570
    Natural varianti271 – 2722Missing in AHUS2; no cell surface expression.
    VAR_026571

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831N → Q: No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding. 3 Publications
    Mutagenesisi114 – 1141N → Q: Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding. 3 Publications
    Mutagenesisi273 – 2731N → Q: Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding. 3 Publications

    Keywords - Diseasei

    Disease mutation, Hemolytic uremic syndrome

    Organism-specific databases

    MIMi120920. gene+phenotype.
    612922. phenotype.
    Orphaneti93576. Atypical hemolytic uremic syndrome with MCP/CD46 anomaly.
    244242. HELLP syndrome.
    PharmGKBiPA30700.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 34344 PublicationsAdd
    BLAST
    Chaini35 – 392358Membrane cofactor proteinPRO_0000006008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 80PROSITE-ProRule annotation
    Disulfide bondi64 ↔ 94PROSITE-ProRule annotation
    Glycosylationi83 – 831N-linked (GlcNAc...)
    Disulfide bondi99 ↔ 141PROSITE-ProRule annotation
    Glycosylationi114 – 1141N-linked (GlcNAc...)
    Disulfide bondi127 ↔ 157PROSITE-ProRule annotation
    Disulfide bondi162 ↔ 210PROSITE-ProRule annotation
    Glycosylationi163 – 1631O-linked (GalNAc...)Sequence Analysis
    Disulfide bondi191 ↔ 223PROSITE-ProRule annotation
    Disulfide bondi228 ↔ 270PROSITE-ProRule annotation
    Disulfide bondi256 ↔ 283PROSITE-ProRule annotation
    Glycosylationi273 – 2731N-linked (GlcNAc...)
    Glycosylationi290 – 2901O-linked (GalNAc...)Sequence Analysis
    Glycosylationi291 – 2911O-linked (GalNAc...)Sequence Analysis
    Glycosylationi292 – 2921O-linked (GalNAc...)Sequence Analysis
    Glycosylationi298 – 2981O-linked (GalNAc...)Sequence Analysis
    Glycosylationi300 – 3001O-linked (GalNAc...)Sequence Analysis
    Glycosylationi302 – 3021O-linked (GalNAc...)Sequence Analysis
    Glycosylationi303 – 3031O-linked (GalNAc...)Sequence Analysis
    Glycosylationi304 – 3041O-linked (GalNAc...)Sequence Analysis
    Glycosylationi305 – 3051O-linked (GalNAc...)Sequence Analysis
    Glycosylationi306 – 3061O-linked (GalNAc...)Sequence Analysis
    Glycosylationi307 – 3071O-linked (GalNAc...)Sequence Analysis
    Glycosylationi309 – 3091O-linked (GalNAc...)Sequence Analysis
    Glycosylationi312 – 3121O-linked (GalNAc...)Sequence Analysis
    Glycosylationi313 – 3131O-linked (GalNAc...)Sequence Analysis
    Glycosylationi315 – 3151O-linked (GalNAc...)Sequence Analysis
    Glycosylationi320 – 3201O-linked (GalNAc...)Sequence Analysis
    Glycosylationi326 – 3261O-linked (GalNAc...)Sequence Analysis

    Post-translational modificationi

    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.
    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.
    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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP15529.
    PaxDbiP15529.
    PRIDEiP15529.

    PTM databases

    PhosphoSiteiP15529.

    Miscellaneous databases

    PMAP-CutDBP15529.

    Expressioni

    Tissue specificityi

    Expressed by all cells except erythrocytes.

    Gene expression databases

    ArrayExpressiP15529.
    BgeeiP15529.
    GenevestigatoriP15529.

    Organism-specific databases

    HPAiCAB010401.
    HPA016903.

    Interactioni

    Subunit structurei

    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.15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    JAG1P785045EBI-2623451,EBI-2847071

    Protein-protein interaction databases

    BioGridi110346. 11 interactions.
    DIPiDIP-41232N.
    IntActiP15529. 6 interactions.
    MINTiMINT-222279.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 487
    Beta strandi59 – 646
    Beta strandi68 – 703
    Beta strandi72 – 743
    Beta strandi77 – 804
    Beta strandi84 – 863
    Helixi91 – 933
    Beta strandi94 – 963
    Beta strandi108 – 1125
    Beta strandi115 – 1184
    Beta strandi122 – 1276
    Beta strandi131 – 1355
    Beta strandi137 – 14610
    Beta strandi148 – 1525
    Beta strandi156 – 1594
    Beta strandi171 – 1755
    Beta strandi186 – 1916
    Beta strandi195 – 1984
    Beta strandi201 – 2044
    Beta strandi206 – 2105
    Beta strandi214 – 2185
    Beta strandi222 – 2243
    Beta strandi236 – 2405
    Beta strandi251 – 2566
    Beta strandi260 – 2645
    Beta strandi266 – 2705
    Beta strandi276 – 2783
    Beta strandi282 – 2854

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP15529.
    SMRiP15529. Positions 35-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15529.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 343309ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini367 – 39226CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei344 – 36623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 9662Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 15963Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 22566Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini226 – 28560Sushi 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi302 – 32625Ser/Thr-richAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 4 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG151270.
    HOVERGENiHBG006335.
    KOiK04007.
    OMAiCKVVKCR.
    OrthoDBiEOG7XPZ64.
    PhylomeDBiP15529.
    TreeFamiTF334137.

    Family and domain databases

    InterProiIPR017341. M_CF_CD46.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 4 hits.
    [Graphical view]
    PIRSFiPIRSF037971. TLX_CD46. 1 hit.
    SMARTiSM00032. CCP. 4 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 4 hits.
    PROSITEiPS50923. SUSHI. 4 hits.
    [Graphical view]

    Sequences (16)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 16 isoformsi produced by alternative splicing. Align

    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) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP    50
    KPYYEIGERV DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP 100
    YIRDPLNGQA VPANGTYEFG YQMHFICNEG YYLIGEEILY CELKGSVAIW 150
    SGKPPICEKV LCTPPPKIKN GKHTFSEVEV FEYLDAVTYS CDPAPGPDPF 200
    SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS GFGKKFYYKA 250
    TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 300
    VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI 350
    VIAIVVGVAV ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL 392
    Length:392
    Mass (Da):43,747
    Last modified:January 16, 2004 - v3
    Checksum:i85FE0CF100EA703E
    GO
    Isoform B (identifier: P15529-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:399
    Mass (Da):44,238
    Checksum:i8E4C641F2BD8AC15
    GO
    Isoform C (identifier: P15529-11) [UniParc]FASTAAdd to Basket

    Also known as: del 7, BC1

    The sequence of this isoform differs from the canonical sequence as follows:
         286-300: Missing.

    Show »
    Length:377
    Mass (Da):42,248
    Checksum:i2CA6F61752570B57
    GO
    Isoform D (identifier: P15529-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:384
    Mass (Da):42,738
    Checksum:iF45B03CBB466AA8C
    GO
    Isoform E (identifier: P15529-12) [UniParc]FASTAAdd to Basket

    Also known as: del 7-8, C1

    The sequence of this isoform differs from the canonical sequence as follows:
         286-315: Missing.

    Show »
    Length:362
    Mass (Da):40,868
    Checksum:iAA3F3F3110E8727D
    GO
    Isoform F (identifier: P15529-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:369
    Mass (Da):41,359
    Checksum:i3BD3000428BBA2EA
    GO
    Isoform G (identifier: P15529-13) [UniParc]FASTAAdd to Basket

    Also known as: del 9

    The sequence of this isoform differs from the canonical sequence as follows:
         316-329: Missing.

    Show »
    Length:378
    Mass (Da):42,193
    Checksum:iAE60F628C4DC271C
    GO
    Isoform H (identifier: P15529-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:385
    Mass (Da):42,683
    Checksum:i45FB279DC30B895E
    GO
    Isoform I (identifier: P15529-14) [UniParc]FASTAAdd to Basket

    Also known as: del 7-9

    The sequence of this isoform differs from the canonical sequence as follows:
         286-300: Missing.
         316-329: Missing.

    Show »
    Length:363
    Mass (Da):40,693
    Checksum:iE48C0E7C0A616FF1
    GO
    Isoform J (identifier: P15529-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:370
    Mass (Da):41,183
    Checksum:iCC2FD6E11C9A81E4
    GO
    Isoform K (identifier: P15529-15) [UniParc]FASTAAdd to Basket

    Also known as: del 7-8-9

    The sequence of this isoform differs from the canonical sequence as follows:
         286-329: Missing.

    Show »
    Length:348
    Mass (Da):39,313
    Checksum:iA6F0D0E7C4203DDF
    GO
    Isoform L (identifier: P15529-7) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:355
    Mass (Da):39,804
    Checksum:i86C83A0D515EDF86
    GO
    Isoform M (identifier: P15529-8) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:364
    Mass (Da):40,705
    Checksum:iB09E917D96F2C0DC
    GO
    Isoform N (identifier: P15529-9) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:349
    Mass (Da):39,325
    Checksum:i8EFCEDA30D3C818E
    GO
    Isoform 2 (identifier: P15529-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         301-305: Missing.

    Show »
    Length:387
    Mass (Da):43,286
    Checksum:i20E7721BB47CA27C
    GO
    Isoform 3 (identifier: P15529-16) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:336
    Mass (Da):36,826
    Checksum:iF57541078036A7EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251V → A in CAE45719. (PubMed:17974005)Curated
    Sequence conflicti108 – 1081G → S in CAD97694. (PubMed:17974005)Curated
    Sequence conflicti159 – 1591K → S in CAD97694. (PubMed:17974005)Curated
    Sequence conflicti162 – 1621C → R in CAI45983. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131S → F.2 Publications
    Corresponds to variant rs138843816 [ dbSNP | Ensembl ].
    VAR_026567
    Natural varianti35 – 351C → Y in AHUS2. 1 Publication
    VAR_063656
    Natural varianti59 – 591R → Q.1 Publication
    VAR_026568
    Natural varianti165 – 1651P → S in AHUS2; reduced cell surface expression. 1 Publication
    VAR_026569
    Natural varianti216 – 2161W → C in AHUS2. 1 Publication
    VAR_063657
    Natural varianti228 – 2281C → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035828
    Natural varianti231 – 2311P → R in AHUS2. 1 Publication
    VAR_063658
    Natural varianti240 – 2401S → P in AHUS2; no change in cell surface expression but reduced activity.
    VAR_026570
    Natural varianti266 – 2661D → N.1 Publication
    Corresponds to variant rs17006830 [ dbSNP | Ensembl ].
    VAR_022262
    Natural varianti271 – 2722Missing in AHUS2; no cell surface expression.
    VAR_026571
    Natural varianti324 – 3241P → L.1 Publication
    Corresponds to variant rs41317833 [ dbSNP | Ensembl ].
    VAR_022263
    Natural varianti353 – 3531A → V.2 Publications
    Corresponds to variant rs35366573 [ dbSNP | Ensembl ].
    VAR_022264
    Natural varianti355 – 3551V → G.1 Publication
    VAR_022265

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei33 – 331D → G in isoform 3. CuratedVSP_019005
    Alternative sequencei34 – 9663Missing in isoform 3. CuratedVSP_019006Add
    BLAST
    Alternative sequencei286 – 32944Missing in isoform K and isoform L. 1 PublicationVSP_009176Add
    BLAST
    Alternative sequencei286 – 31530Missing in isoform E, isoform F and isoform N. 5 PublicationsVSP_009175Add
    BLAST
    Alternative sequencei286 – 30015Missing in isoform C, isoform D, isoform I, isoform J and isoform M. 7 PublicationsVSP_009174Add
    BLAST
    Alternative sequencei301 – 3055Missing in isoform 2. CuratedVSP_001201
    Alternative sequencei316 – 32914Missing in isoform G, isoform H, isoform I and isoform J. CuratedVSP_009177Add
    BLAST
    Alternative sequencei355 – 39238VVGVA…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform N. 1 PublicationVSP_009178Add
    BLAST
    Alternative sequencei355 – 36713Missing in isoform M. CuratedVSP_001202Add
    BLAST
    Alternative sequencei368 – 39225YLQRR…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform M. CuratedVSP_001203Add
    BLAST
    Alternative sequencei377 – 39216TYLTD…KFTSL → KADGGAEYATYQTKSTTPAE QRG in isoform B, isoform D, isoform F, isoform H, isoform J, isoform L and isoform 3. 8 PublicationsVSP_001204Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1479.1. [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]
    PIRiG02913.
    I54479.
    I57998.
    S01896.
    RefSeqiNP_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]
    UniGeneiHs.510402.

    Genome annotation databases

    EnsembliENST00000322875; 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]
    ENST00000367041; ENSP00000356008; ENSG00000117335. [P15529-12]
    ENST00000367042; ENSP00000356009; ENSG00000117335. [P15529-11]
    ENST00000367047; ENSP00000356014; ENSG00000117335. [P15529-16]
    ENST00000480003; ENSP00000418471; ENSG00000117335. [P15529-6]
    GeneIDi4179.
    KEGGihsa:4179.
    UCSCiuc001hgc.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]

    Polymorphism databases

    DMDMi41019474.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1479.1. [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 ]
    PIRi G02913.
    I54479.
    I57998.
    S01896.
    RefSeqi NP_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 ]
    UniGenei Hs.510402.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CKL X-ray 3.10 A/B/C/D/E/F 35-160 [» ]
    1HR4 model - A 159-284 [» ]
    2O39 X-ray 2.85 C/D 35-160 [» ]
    3INB X-ray 3.10 C/D 35-160 [» ]
    3L89 X-ray 3.50 M/N/O/P/Q/R/S/T/U/V/W/X 35-160 [» ]
    3O8E X-ray 2.84 B/D 35-286 [» ]
    ProteinModelPortali P15529.
    SMRi P15529. Positions 35-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110346. 11 interactions.
    DIPi DIP-41232N.
    IntActi P15529. 6 interactions.
    MINTi MINT-222279.

    PTM databases

    PhosphoSitei P15529.

    Polymorphism databases

    DMDMi 41019474.

    Proteomic databases

    MaxQBi P15529.
    PaxDbi P15529.
    PRIDEi P15529.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322875 ; 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 ]
    ENST00000367041 ; ENSP00000356008 ; ENSG00000117335 . [P15529-12 ]
    ENST00000367042 ; ENSP00000356009 ; ENSG00000117335 . [P15529-11 ]
    ENST00000367047 ; ENSP00000356014 ; ENSG00000117335 . [P15529-16 ]
    ENST00000480003 ; ENSP00000418471 ; ENSG00000117335 . [P15529-6 ]
    GeneIDi 4179.
    KEGGi hsa:4179.
    UCSCi uc001hgc.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

    CTDi 4179.
    GeneCardsi GC01P207925.
    GeneReviewsi CD46.
    HGNCi HGNC:6953. CD46.
    HPAi CAB010401.
    HPA016903.
    MIMi 120920. gene+phenotype.
    612922. phenotype.
    neXtProti NX_P15529.
    Orphaneti 93576. Atypical hemolytic uremic syndrome with MCP/CD46 anomaly.
    244242. HELLP syndrome.
    PharmGKBi PA30700.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG151270.
    HOVERGENi HBG006335.
    KOi K04007.
    OMAi CKVVKCR.
    OrthoDBi EOG7XPZ64.
    PhylomeDBi P15529.
    TreeFami TF334137.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.

    Miscellaneous databases

    ChiTaRSi CD46. human.
    EvolutionaryTracei P15529.
    GeneWikii CD46.
    GenomeRNAii 4179.
    NextBioi 16458.
    PMAP-CutDB P15529.
    PROi P15529.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15529.
    Bgeei P15529.
    Genevestigatori P15529.

    Family and domain databases

    InterProi IPR017341. M_CF_CD46.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF037971. TLX_CD46. 1 hit.
    SMARTi SM00032. CCP. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 4 hits.
    PROSITEi PS50923. SUSHI. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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. 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. Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 11 PIV/FIBER PROTEIN.
    40. 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. 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. 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.

    Entry informationi

    Entry nameiMCP_HUMAN
    AccessioniPrimary (citable) accession number: P15529
    Secondary accession number(s): A0T1T0
    , A0T1T1, A0T1T2, Q15429, Q53GV9, Q5HY94, Q5VWS6, Q5VWS7, Q5VWS8, Q5VWS9, Q5VWT0, Q5VWT1, Q5VWT2, Q6N0A1, Q7Z3R5, Q9NNW2, Q9NNW3, Q9NNW4, Q9UCJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3