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P15529

- MCP_HUMAN

UniProt

P15529 - MCP_HUMAN

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Protein

Membrane cofactor protein

Gene

CD46

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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. focal adhesion Source: UniProtKB
  5. Golgi apparatus Source: Ensembl
  6. inner acrosomal membrane Source: Ensembl
  7. integral component of plasma membrane Source: ProtInc
  8. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP15529.
ExpressionAtlasiP15529. baseline and differential.
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.
GeneTreeiENSGT00760000118803.
HOVERGENiHBG006335.
InParanoidiP15529.
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

        10         20         30         40         50
MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP
60 70 80 90 100
KPYYEIGERV DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP
110 120 130 140 150
YIRDPLNGQA VPANGTYEFG YQMHFICNEG YYLIGEEILY CELKGSVAIW
160 170 180 190 200
SGKPPICEKV LCTPPPKIKN GKHTFSEVEV FEYLDAVTYS CDPAPGPDPF
210 220 230 240 250
SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS GFGKKFYYKA
260 270 280 290 300
TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS
310 320 330 340 350
VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI
360 370 380 390
VIAIVVGVAV ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL
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.
GeneTreei ENSGT00760000118803.
HOVERGENi HBG006335.
InParanoidi P15529.
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

Bgeei P15529.
ExpressionAtlasi P15529. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 172 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