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Entry version 222 (16 Jan 2019)
Sequence version 4 (11 Sep 2007)
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Protein

Complement factor H

Gene

CFH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces (PubMed:21285368, PubMed:25402769). Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop (PubMed:19503104). As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b (PubMed:18252712, PubMed:28671664). In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed (PubMed:9558116, PubMed:20008295).7 Publications

Caution

According to a report, Asn-217 is not glycosylated (PubMed:17591618). Another study observed glycosylation at this position (PubMed:19139490).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • heparan sulfate proteoglycan binding Source: BHF-UCL
  • heparin binding Source: BHF-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processComplement alternate pathway, Host-virus interaction, Immunity, Innate immunity

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-977606 Regulation of Complement cascade

SIGNOR Signaling Network Open Resource

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SIGNORi
P08603

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Complement factor H
Alternative name(s):
H factor 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CFH
Synonyms:HF, HF1, HF2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000000971.15

Human Gene Nomenclature Database

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HGNCi
HGNC:4883 CFH

Online Mendelian Inheritance in Man (OMIM)

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MIMi
134370 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P08603

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Basal laminar drusen (BLD)1 Publication
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionDrusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss.
See also OMIM:126700
Complement factor H deficiency (CFHD)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.
See also OMIM:609814
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_031978127R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031979224Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication1
Natural variantiVAR_031981431C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_019405536C → R in CFHD. 1 Publication1
Natural variantiVAR_031982673C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_019406959C → Y in CFHD; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_0258731076Q → E in CFHD. 2 Publications1
Natural variantiVAR_0258741119D → G in CFHD. 2 Publications1
Natural variantiVAR_0258811184T → R in CFHD. 2 Publications1
Natural variantiVAR_0258851210R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications1
Natural variantiVAR_0258871215R → Q in CFHD. 2 Publications1
Hemolytic uremic syndrome atypical 1 (AHUS1)8 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Disease descriptionAn 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.
See also OMIM:235400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02586478R → G in AHUS1. 1 Publication1
Natural variantiVAR_063648325C → Y in AHUS1. 1 Publication1
Natural variantiVAR_031980400Q → K in AHUS1. 1 Publication1
Natural variantiVAR_063649609V → I in AHUS1. 1 Publication1
Natural variantiVAR_025865630C → W in AHUS1. 1 Publication1
Natural variantiVAR_031983673C → Y in AHUS1. 1 Publication1
Natural variantiVAR_025866850E → K in AHUS1; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_031984893H → R in AHUS1. 1 Publication1
Natural variantiVAR_031985915C → S in AHUS1. 1 Publication1
Natural variantiVAR_025867950Q → H in AHUS1. 1 PublicationCorresponds to variant dbSNP:rs149474608EnsemblClinVar.1
Natural variantiVAR_025868951Y → H in AHUS1. 1 Publication1
Natural variantiVAR_025869956T → M in AHUS1. 2 PublicationsCorresponds to variant dbSNP:rs145975787EnsemblClinVar.1
Natural variantiVAR_025870978W → C in AHUS1. 1 Publication1
Natural variantiVAR_0258711021Y → F in AHUS1. 1 Publication1
Natural variantiVAR_0258721043C → R in AHUS1. 1 Publication1
Natural variantiVAR_0258751134V → G in AHUS1. 1 Publication1
Natural variantiVAR_0258761142Y → D in AHUS1. 1 Publication1
Natural variantiVAR_0258771157W → R in AHUS1. 1 Publication1
Natural variantiVAR_0258781163C → W in AHUS1. 1 Publication1
Natural variantiVAR_0636501169I → L in AHUS1. 1 Publication1
Natural variantiVAR_0636511183W → C in AHUS1. 1 Publication1
Natural variantiVAR_0258791183W → L in AHUS1. 3 Publications1
Natural variantiVAR_0258801183W → R in AHUS1. 2 Publications1
Natural variantiVAR_0194071189L → R in AHUS1. 2 Publications1
Natural variantiVAR_0194081191S → L in AHUS1. 2 PublicationsCorresponds to variant dbSNP:rs460897EnsemblClinVar.1
Natural variantiVAR_0258821194G → D in AHUS1. 1 Publication1
Natural variantiVAR_0258831197V → A in AHUS1. 2 PublicationsCorresponds to variant dbSNP:rs460184EnsemblClinVar.1
Natural variantiVAR_0258841198E → A in AHUS1. 1 Publication1
Natural variantiVAR_0319861199F → S in AHUS1. 1 Publication1
Natural variantiVAR_0258861215R → G in AHUS1. 2 Publications1
Natural variantiVAR_0194091225 – 1231YPTCAKR → FQS in AHUS1. 1 Publication7
Natural variantiVAR_0258881226P → S in AHUS1; atypical. 1 Publication1
Macular degeneration, age-related, 4 (ARMD4)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
See also OMIM:610698
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0258851210R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi337H → A: About 10% loss of heparin-binding. 1 Publication1
Mutagenesisi341R → A: About 20% loss of heparin-binding. 1 Publication1
Mutagenesisi1182R → A: About 50% loss of C3b binding. 1 Publication1
Mutagenesisi1183W → L: About 40% loss of C3b binding. 1 Publication1
Mutagenesisi1186K → A: About 20% loss of C3b binding. 1 Publication1
Mutagenesisi1188K → A: About 50% loss of C3b binding. 1 Publication1
Mutagenesisi1198E → A: About 30% loss of C3b binding. 1 Publication1

Keywords - Diseasei

Age-related macular degeneration, Disease mutation, Hemolytic uremic syndrome

Organism-specific databases

DisGeNET

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DisGeNETi
3075

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
CFH

MalaCards human disease database

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MalaCardsi
CFH
MIMi126700 phenotype
235400 phenotype
609814 phenotype
610698 phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
93579 Atypical hemolytic-uremic syndrome with H factor anomaly
244275 De novo thrombotic microangiopathy after kidney transplantation
93571 Dense deposit disease
75376 Familial drusen
244242 HELLP syndrome
200421 Immunodeficiency with factor H anomaly
329903 Immunoglobulin-mediated membranoproliferative glomerulonephritis
279 NON RARE IN EUROPE: Age-related macular degeneration

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29261

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4629

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CFH

Domain mapping of disease mutations (DMDM)

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DMDMi
158517847

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 181 PublicationAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000589419 – 1231Complement factor HAdd BLAST1213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi21 ↔ 663 Publications
Disulfide bondi52 ↔ 803 Publications
Disulfide bondi85 ↔ 1293 Publications
Disulfide bondi114 ↔ 1413 Publications
Disulfide bondi146 ↔ 1922 Publications
Disulfide bondi178 ↔ 2052 Publications
Disulfide bondi210 ↔ 2512 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi217N-linked (GlcNAc...) (complex) asparagine1 Publication1
Disulfide bondi237 ↔ 2622 Publications
Disulfide bondi267 ↔ 309PROSITE-ProRule annotation
Disulfide bondi294 ↔ 3201 Publication
Disulfide bondi325 ↔ 3744 Publications
Disulfide bondi357 ↔ 3854 Publications
Disulfide bondi389 ↔ 4314 Publications
Disulfide bondi416 ↔ 4424 Publications
Disulfide bondi448 ↔ 4941 Publication
Disulfide bondi477 ↔ 5051 Publication
Disulfide bondi509 ↔ 5531 Publication
Glycosylationi529N-linked (GlcNAc...) asparagine4 Publications1
Disulfide bondi536 ↔ 5641 Publication
Disulfide bondi569 ↔ 6111 Publication
Disulfide bondi597 ↔ 6231 Publication
Disulfide bondi630 ↔ 6731 Publication
Disulfide bondi659 ↔ 6841 Publication
Disulfide bondi691 ↔ 7332 Publications
Glycosylationi718N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi719 ↔ 7442 Publications
Disulfide bondi753 ↔ 7921 Publication
Disulfide bondi781 ↔ 8031 Publication
Glycosylationi802N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi811 ↔ 853PROSITE-ProRule annotation
Glycosylationi822N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi839 ↔ 864PROSITE-ProRule annotation
Disulfide bondi870 ↔ 9151 Publication
Glycosylationi882N-linked (GlcNAc...) (complex) asparagine5 Publications1
Disulfide bondi901 ↔ 9261 Publication
Glycosylationi911N-linked (GlcNAc...) (complex) asparagine4 Publications1
Disulfide bondi931 ↔ 9732 Publications
Disulfide bondi959 ↔ 9842 Publications
Disulfide bondi989 ↔ 1032PROSITE-ProRule annotation
Disulfide bondi1018 ↔ 1043PROSITE-ProRule annotation
Glycosylationi1029N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi1048 ↔ 10911 Publication
Disulfide bondi1077 ↔ 11021 Publication
Glycosylationi1095N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi1109 ↔ 11527 Publications
Disulfide bondi1138 ↔ 11637 Publications
Disulfide bondi1167 ↔ 12187 Publications
Disulfide bondi1201 ↔ 12287 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P08603

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P08603

MaxQB - The MaxQuant DataBase

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MaxQBi
P08603

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P08603

PeptideAtlas

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PeptideAtlasi
P08603

PRoteomics IDEntifications database

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PRIDEi
P08603

ProteomicsDB human proteome resource

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ProteomicsDBi
52135
52136 [P08603-2]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P08603

GlyConnect protein glycosylation platform

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GlyConnecti
722

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08603

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P08603

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

CFH is one of the most abundant complement components in blood where the liver is the major source of CFH protein in vivo. in addition, CFH is secreted by additional cell types including monocytes, fibroblasts, or endothelial cells.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000000971 Expressed in 206 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P08603 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08603 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016385
CAB016769
HPA038922
HPA049176
HPA053326

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:18005991, PubMed:19505476). Forms also homooligomers (PubMed:19505476). Interacts with complement protein C3b; this interaction inhibits complement activation (PubMed:16601698, PubMed:19503104, PubMed:20378178, PubMed:21285368, PubMed:28671664). Interacts with complement protein C3d (PubMed:20378178, PubMed:21285368, PubMed:29190743). Interacts with CR3/ITGAM; this interaction mediates adhesion of neutrophils to pathogens leading to pathogen clearance (PubMed:9558116, PubMed:20008295). Interacts with complement factor I (PubMed:28671664).10 Publications
(Microbial infection) Interacts with West nile virus non-structural protein 1 (NS1); this interaction leads to the degradation of C3.1 Publication
(Microbial infection) Interacts with Neisseria meningitidis protein fHbp.2 Publications
(Microbial infection) Interacts with Borrelia burgdorferi outer surface protein E/OspE; this interaction recruits complement regulator factor H onto the bacterial surface to evade complement-mediated cell lysis.2 Publications
(Microbial infection) Interacts with Streptococcus pneumoniae protein virulence factor choline-binding protein A/CbpAN; this interaction enables Streptococcus pneumoniae to evade surveillance by human complement system.1 Publication
(Microbial infection) Interacts with Staphylococcus aureus surface protein serine-aspartate repeat protein E/SdrE; this interaction sequesters CFH on the surface of S. aureus for complement evasion.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109324, 18 interactors

Database of interacting proteins

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DIPi
DIP-38303N

Protein interaction database and analysis system

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IntActi
P08603, 19 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000356399

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P08603

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FHCmodel-A1105-1231[»]
1HAQX-ray-A19-1231[»]
1HCCNMR-A927-985[»]
1HFHNMR-A866-985[»]
1HFINMR-A866-927[»]
1KOVmodel-A321-443[»]
2BZMNMR-A1107-1231[»]
2G7IX-ray1.75A1107-1231[»]
2IC4X-ray-A321-506[»]
2JGWNMR-A386-446[»]
2JGXNMR-A386-446[»]
2KMSNMR-A690-804[»]
2QFGX-ray-A19-322[»]
2QFHX-ray-A928-1231[»]
2RLPNMR-A20-142[»]
2RLQNMR-A84-206[»]
2UWNX-ray2.35A322-506[»]
2V8EX-ray2.50A322-506[»]
2W80X-ray2.35A/B/E/G321-443[»]
2W81X-ray2.35A/B/E321-443[»]
2WIIX-ray2.70C18-264[»]
2XQWX-ray2.31C1103-1231[»]
3GAUX-ray-A19-1231[»]
3GAVX-ray-A19-1231[»]
3GAWX-ray-A19-1231[»]
3KXVX-ray2.00A1103-1231[»]
3KZJX-ray1.65A1103-1231[»]
3OXUX-ray2.10D/E/F1107-1231[»]
3R62X-ray1.52A/B1107-1231[»]
3RJ3X-ray2.35D/E/F1107-1231[»]
3SW0X-ray1.80X1046-1231[»]
4AYDX-ray2.40A/B/E321-443[»]
4AYEX-ray2.80A/B/E321-443[»]
4AYIX-ray2.31A/E321-443[»]
4AYMX-ray3.00A/B/E/F321-443[»]
4B2RNMR-A566-687[»]
4B2SNMR-A627-747[»]
4J38X-ray2.83B1103-1231[»]
4K12X-ray1.08A508-567[»]
4ONTX-ray2.15D/E/F1107-1231[»]
4ZH1X-ray2.24D/E/F1107-1231[»]
5NBQX-ray3.18D/E/F1104-1230[»]
5O32X-ray4.21C/G19-387[»]
5O35X-ray4.20C19-388[»]
5WTBX-ray3.30E/F/G/H1206-1226[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P08603

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P08603

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P08603

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini19 – 82Sushi 1PROSITE-ProRule annotationAdd BLAST64
Domaini83 – 143Sushi 2PROSITE-ProRule annotationAdd BLAST61
Domaini144 – 207Sushi 3PROSITE-ProRule annotationAdd BLAST64
Domaini208 – 264Sushi 4PROSITE-ProRule annotationAdd BLAST57
Domaini265 – 322Sushi 5PROSITE-ProRule annotationAdd BLAST58
Domaini324 – 386Sushi 6PROSITE-ProRule annotationAdd BLAST63
Domaini387 – 444Sushi 7PROSITE-ProRule annotationAdd BLAST58
Domaini446 – 507Sushi 8PROSITE-ProRule annotationAdd BLAST62
Domaini515 – 566Sushi 9PROSITE-ProRule annotationAdd BLAST52
Domaini567 – 625Sushi 10PROSITE-ProRule annotationAdd BLAST59
Domaini628 – 686Sushi 11PROSITE-ProRule annotationAdd BLAST59
Domaini689 – 746Sushi 12PROSITE-ProRule annotationAdd BLAST58
Domaini751 – 805Sushi 13PROSITE-ProRule annotationAdd BLAST55
Domaini809 – 866Sushi 14PROSITE-ProRule annotationAdd BLAST58
Domaini868 – 928Sushi 15PROSITE-ProRule annotationAdd BLAST61
Domaini929 – 986Sushi 16PROSITE-ProRule annotationAdd BLAST58
Domaini987 – 1045Sushi 17PROSITE-ProRule annotationAdd BLAST59
Domaini1046 – 1104Sushi 18PROSITE-ProRule annotationAdd BLAST59
Domaini1107 – 1165Sushi 19PROSITE-ProRule annotationAdd BLAST59
Domaini1170 – 1230Sushi 20PROSITE-ProRule annotationAdd BLAST61

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Sushi 1-3 domain represents the minimal unit capable of cofactor activity (PubMed:18252712). The property to discriminate self surfaces from non-self surfaces depends on the C-terminal region made of Sushis 19-20 (PubMed:21285368).2 Publications

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IVQ9 Eukaryota
ENOG410YBAR LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005665

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08603

KEGG Orthology (KO)

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KOi
K04004

Database of Orthologous Groups

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OrthoDBi
296899at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P08603

TreeFam database of animal gene trees

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TreeFami
TF326157

Family and domain databases

Conserved Domains Database

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CDDi
cd00033 CCP, 16 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00084 Sushi, 19 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00032 CCP, 20 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57535 SSF57535, 18 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50923 SUSHI, 19 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P08603-1) [UniParc]FASTAAdd to basket

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
MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY
60 70 80 90 100
KCRPGYRSLG NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG
110 120 130 140 150
GNVFEYGVKA VYTCNEGYQL LGEINYRECD TDGWTNDIPI CEVVKCLPVT
160 170 180 190 200
APENGKIVSS AMEPDREYHF GQAVRFVCNS GYKIEGDEEM HCSDDGFWSK
210 220 230 240 250
EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG YEYSERGDAV
260 270 280 290 300
CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP
310 320 330 340 350
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG
360 370 380 390 400
KYYSYYCDEH FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ
410 420 430 440 450
NYGRKFVQGK SIDVACHPGY ALPKAQTTVT CMENGWSPTP RCIRVKTCSK
460 470 480 490 500
SSIDIENGFI SESQYTYALK EKAKYQCKLG YVTADGETSG SITCGKDGWS
510 520 530 540 550
AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY ESNTGSTTGS
560 570 580 590 600
IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG
610 620 630 640 650
FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG
660 670 680 690 700
HSEVVEYYCN PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG
710 720 730 740 750
WAQLSSPPYY YGDSVEFNCS ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL
760 770 780 790 800
KKCKSSNLII LEEHLKNKKE FDHNSNIRYR CRGKEGWIHT VCINGRWDPE
810 820 830 840 850
VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ ENYLIQEGEE
860 870 880 890 900
ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT
910 920 930 940 950
CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ
960 970 980 990 1000
YGEEVTYKCF EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP
1010 1020 1030 1040 1050
MGEKKDVYKA GEQVTYTCAT YYKMDGASNV TCINSRWTGR PTCRDTSCVN
1060 1070 1080 1090 1100
PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP YEMFGDEEVM CLNGNWTEPP
1110 1120 1130 1140 1150
QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN LYQLEGNKRI
1160 1170 1180 1190 1200
TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV
1210 1220 1230
CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R
Length:1,231
Mass (Da):139,096
Last modified:September 11, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3C26D62A2BF9BFEE
GO
Isoform 2 (identifier: P08603-2) [UniParc]FASTAAdd to basket
Also known as: FHL-1

The sequence of this isoform differs from the canonical sequence as follows:
     446-449: KTCS → SFTL
     450-1231: Missing.

Show »
Length:449
Mass (Da):51,034
Checksum:iC2AAD47F155343E3
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0D9SG88A0A0D9SG88_HUMAN
Complement factor H
CFH
449Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5TFM2Q5TFM2_HUMAN
Complement factor H
CFH
385Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAB41739 differs from that shown. Reason: Frameshift at position 341.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21C → Q AA sequence (PubMed:6215918).Curated1
Sequence conflicti30T → V AA sequence (PubMed:6215918).Curated1
Sequence conflicti34T → Q AA sequence (PubMed:6215918).Curated1
Sequence conflicti53 – 54RP → IL in CAB41739 (PubMed:2946589).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02383662V → I Polymorphism; confirmed at protein level. 4 PublicationsCorresponds to variant dbSNP:rs800292EnsemblClinVar.1
Natural variantiVAR_02586478R → G in AHUS1. 1 Publication1
Natural variantiVAR_031978127R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031979224Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication1
Natural variantiVAR_063648325C → Y in AHUS1. 1 Publication1
Natural variantiVAR_031980400Q → K in AHUS1. 1 Publication1
Natural variantiVAR_001979402Y → H Polymorphism associated with ARMD4. 5 PublicationsCorresponds to variant dbSNP:rs1061170Ensembl.1
Natural variantiVAR_031981431C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_043892493T → R1 PublicationCorresponds to variant dbSNP:rs1061171Ensembl.1
Natural variantiVAR_019405536C → R in CFHD. 1 Publication1
Natural variantiVAR_025092551I → T1 PublicationCorresponds to variant dbSNP:rs35453854EnsemblClinVar.1
Natural variantiVAR_043893567R → G Associated with basal laminar drusen. 1 Publication1
Natural variantiVAR_063649609V → I in AHUS1. 1 Publication1
Natural variantiVAR_025865630C → W in AHUS1. 1 Publication1
Natural variantiVAR_031982673C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication1
Natural variantiVAR_031983673C → Y in AHUS1. 1 Publication1
Natural variantiVAR_025866850E → K in AHUS1; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_025093890S → I1 PublicationCorresponds to variant dbSNP:rs515299EnsemblClinVar.1
Natural variantiVAR_031984893H → R in AHUS1. 1 Publication1
Natural variantiVAR_031985915C → S in AHUS1. 1 Publication1
Natural variantiVAR_020261936E → D Polymorphism associated with hemolytic uremic syndrome and basal laminar drusen. 4 PublicationsCorresponds to variant dbSNP:rs1065489EnsemblClinVar.1
Natural variantiVAR_025867950Q → H in AHUS1. 1 PublicationCorresponds to variant dbSNP:rs149474608EnsemblClinVar.1
Natural variantiVAR_025868951Y → H in AHUS1. 1 Publication1
Natural variantiVAR_025869956T → M in AHUS1. 2 PublicationsCorresponds to variant dbSNP:rs145975787EnsemblClinVar.1
Natural variantiVAR_019406959C → Y in CFHD; variant confirmed at protein level. 2 Publications1
Natural variantiVAR_025870978W → C in AHUS1. 1 Publication1
Natural variantiVAR_055683997N → T. Corresponds to variant dbSNP:rs17575212Ensembl.1
Natural variantiVAR_0250941007V → I1 Publication1
Natural variantiVAR_0438941007V → L. Corresponds to variant dbSNP:rs534399EnsemblClinVar.1
Natural variantiVAR_0556841010A → T. Corresponds to variant dbSNP:rs11539862EnsemblClinVar.1
Natural variantiVAR_0250951017T → I1 PublicationCorresponds to variant dbSNP:rs34362004EnsemblClinVar.1
Natural variantiVAR_0258711021Y → F in AHUS1. 1 Publication1
Natural variantiVAR_0258721043C → R in AHUS1. 1 Publication1
Natural variantiVAR_0250961050N → Y Polymorphism associated with basal laminar drusen. 2 PublicationsCorresponds to variant dbSNP:rs35274867EnsemblClinVar.1
Natural variantiVAR_0250971059I → T1 PublicationCorresponds to variant dbSNP:rs35343172EnsemblClinVar.1
Natural variantiVAR_0258731076Q → E in CFHD. 2 Publications1
Natural variantiVAR_0438951078R → S Associated with basal laminar drusen. 1 Publication1
Natural variantiVAR_0258741119D → G in CFHD. 2 Publications1
Natural variantiVAR_0258751134V → G in AHUS1. 1 Publication1
Natural variantiVAR_0258761142Y → D in AHUS1. 1 Publication1
Natural variantiVAR_0438961143Q → E Polymorphism; confirmed at protein level. 1 PublicationCorresponds to variant dbSNP:rs15809EnsemblClinVar.1
Natural variantiVAR_0258771157W → R in AHUS1. 1 Publication