Details for: CFH

Gene ID: 3075

Symbol: CFH

Ensembl ID: ENSG00000000971

Description: complement factor H

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 4.68
    Marker Score: 15346
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 3.56
    Marker Score: 2341
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: 2.85
    Marker Score: 15310
  • Cell Name: fibroblast of lung (CL0002553)
    Fold Change: 2.76
    Marker Score: 7235
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 2.5
    Marker Score: 2873
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 2.47
    Marker Score: 794
  • Cell Name: alveolar type 2 fibroblast cell (CL4028006)
    Fold Change: 2.46
    Marker Score: 1367
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 2.36
    Marker Score: 1377
  • Cell Name: bronchus fibroblast of lung (CL2000093)
    Fold Change: 2.34
    Marker Score: 3221
  • Cell Name: keratocyte (CL0002363)
    Fold Change: 2.29
    Marker Score: 526
  • Cell Name: skin fibroblast (CL0002620)
    Fold Change: 2.2
    Marker Score: 570
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 2.1
    Marker Score: 13520
  • Cell Name: nasal mucosa goblet cell (CL0002480)
    Fold Change: 2.1
    Marker Score: 1405
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 2.03
    Marker Score: 8757
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 2
    Marker Score: 68119
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 1.99
    Marker Score: 1188
  • Cell Name: parietal epithelial cell (CL1000452)
    Fold Change: 1.98
    Marker Score: 718
  • Cell Name: preosteoblast (CL0007010)
    Fold Change: 1.97
    Marker Score: 559
  • Cell Name: inflammatory cell (CL0009002)
    Fold Change: 1.96
    Marker Score: 843.5
  • Cell Name: basal cell of epithelium of trachea (CL1000348)
    Fold Change: 1.96
    Marker Score: 14596
  • Cell Name: theca cell (CL0000503)
    Fold Change: 1.91
    Marker Score: 1368
  • Cell Name: fibroblast of breast (CL4006000)
    Fold Change: 1.9
    Marker Score: 1084
  • Cell Name: endocardial cell (CL0002350)
    Fold Change: 1.81
    Marker Score: 1024
  • Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
    Fold Change: 1.76
    Marker Score: 731
  • Cell Name: respiratory goblet cell (CL0002370)
    Fold Change: 1.68
    Marker Score: 486
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 1.68
    Marker Score: 2479
  • Cell Name: fibroblast (CL0000057)
    Fold Change: 1.64
    Marker Score: 1581
  • Cell Name: epicardial adipocyte (CL1000309)
    Fold Change: 1.54
    Marker Score: 748
  • Cell Name: adventitial cell (CL0002503)
    Fold Change: 1.49
    Marker Score: 369
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 1.49
    Marker Score: 1600
  • Cell Name: mural cell (CL0008034)
    Fold Change: 1.47
    Marker Score: 168448
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 1.47
    Marker Score: 2820
  • Cell Name: hepatic stellate cell (CL0000632)
    Fold Change: 1.46
    Marker Score: 552
  • Cell Name: tracheobronchial goblet cell (CL0019003)
    Fold Change: 1.43
    Marker Score: 392
  • Cell Name: fibroblast of connective tissue of prostate (CL1000299)
    Fold Change: 1.39
    Marker Score: 347
  • Cell Name: bronchial goblet cell (CL1000312)
    Fold Change: 1.39
    Marker Score: 687
  • Cell Name: prostate stromal cell (CL0002622)
    Fold Change: 1.38
    Marker Score: 347
  • Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
    Fold Change: 1.34
    Marker Score: 1140
  • Cell Name: mesothelial cell (CL0000077)
    Fold Change: 1.29
    Marker Score: 516
  • Cell Name: chondrocyte (CL0000138)
    Fold Change: 1.28
    Marker Score: 576
  • Cell Name: mucus secreting cell (CL0000319)
    Fold Change: 1.27
    Marker Score: 324
  • Cell Name: hepatocyte (CL0000182)
    Fold Change: 1.26
    Marker Score: 862
  • Cell Name: fat cell (CL0000136)
    Fold Change: 1.24
    Marker Score: 695
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 1.2
    Marker Score: 834
  • Cell Name: lung ciliated cell (CL1000271)
    Fold Change: 1.18
    Marker Score: 562
  • Cell Name: duct epithelial cell (CL0000068)
    Fold Change: 1.17
    Marker Score: 546
  • Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
    Fold Change: 1.14
    Marker Score: 9922
  • Cell Name: adipose microvascular endothelial cell (CL2000072)
    Fold Change: 1.1
    Marker Score: 328
  • Cell Name: myofibroblast cell (CL0000186)
    Fold Change: 1.1
    Marker Score: 1352
  • Cell Name: club cell (CL0000158)
    Fold Change: 1.09
    Marker Score: 1273
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 1.05
    Marker Score: 1123
  • Cell Name: retinal blood vessel endothelial cell (CL0002585)
    Fold Change: 1.03
    Marker Score: 247
  • Cell Name: skeletal muscle satellite cell (CL0000594)
    Fold Change: 1.03
    Marker Score: 687
  • Cell Name: epithelial cell of urethra (CL1000296)
    Fold Change: 1.02
    Marker Score: 805
  • Cell Name: cerebral cortex GABAergic interneuron (CL0010011)
    Fold Change: 1
    Marker Score: 71761
  • Cell Name: forebrain radial glial cell (CL0013000)
    Fold Change: 1
    Marker Score: 47986
  • Cell Name: multi-ciliated epithelial cell (CL0005012)
    Fold Change: 0.99
    Marker Score: 1882
  • Cell Name: papillary tips cell (CL1000597)
    Fold Change: 0.99
    Marker Score: 199
  • Cell Name: lung secretory cell (CL1000272)
    Fold Change: 0.98
    Marker Score: 875
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30404
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.95
    Marker Score: 2411
  • Cell Name: stromal cell (CL0000499)
    Fold Change: 0.95
    Marker Score: 1109.5
  • Cell Name: stromal cell of lamina propria of small intestine (CL0009022)
    Fold Change: 0.92
    Marker Score: 207
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 0.91
    Marker Score: 14653
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.91
    Marker Score: 2727
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 0.91
    Marker Score: 339
  • Cell Name: Leydig cell (CL0000178)
    Fold Change: 0.9
    Marker Score: 974
  • Cell Name: glandular cell of esophagus (CL0002657)
    Fold Change: 0.89
    Marker Score: 281
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 0.88
    Marker Score: 922
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5296
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.87
    Marker Score: 4973
  • Cell Name: cell of skeletal muscle (CL0000188)
    Fold Change: 0.86
    Marker Score: 656
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 0.84
    Marker Score: 1528
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 0.81
    Marker Score: 811
  • Cell Name: early T lineage precursor (CL0002425)
    Fold Change: 0.81
    Marker Score: 616.5
  • Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
    Fold Change: 0.8
    Marker Score: 221
  • Cell Name: pancreatic stellate cell (CL0002410)
    Fold Change: 0.8
    Marker Score: 502.5
  • Cell Name: muscle precursor cell (CL0000680)
    Fold Change: 0.79
    Marker Score: 204
  • Cell Name: reticular cell (CL0000432)
    Fold Change: 0.78
    Marker Score: 284
  • Cell Name: ciliated cell (CL0000064)
    Fold Change: 0.78
    Marker Score: 2675
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.76
    Marker Score: 1242
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 0.76
    Marker Score: 1855.5
  • Cell Name: muscle cell (CL0000187)
    Fold Change: 0.76
    Marker Score: 214
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 0.75
    Marker Score: 673
  • Cell Name: Cajal-Retzius cell (CL0000695)
    Fold Change: 0.75
    Marker Score: 388
  • Cell Name: brush cell (CL0002204)
    Fold Change: 0.75
    Marker Score: 681
  • Cell Name: cardiac neuron (CL0010022)
    Fold Change: 0.73
    Marker Score: 912
  • Cell Name: lung goblet cell (CL1000143)
    Fold Change: 0.73
    Marker Score: 209
  • Cell Name: connective tissue cell (CL0002320)
    Fold Change: 0.72
    Marker Score: 188
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: 0.72
    Marker Score: 4350
  • Cell Name: osteoblast (CL0000062)
    Fold Change: 0.72
    Marker Score: 385
  • Cell Name: epithelial cell of stratum germinativum of esophagus (CL1000447)
    Fold Change: 0.7
    Marker Score: 168
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 0.7
    Marker Score: 418
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: 0.69
    Marker Score: 177
  • Cell Name: CD8-positive, alpha-beta cytotoxic T cell (CL0000794)
    Fold Change: 0.69
    Marker Score: 606
  • Cell Name: blood vessel smooth muscle cell (CL0019018)
    Fold Change: 0.68
    Marker Score: 180
  • Cell Name: tendon cell (CL0000388)
    Fold Change: 0.68
    Marker Score: 168
  • Cell Name: hematopoietic stem cell (CL0000037)
    Fold Change: 0.68
    Marker Score: 359
  • Cell Name: pericyte (CL0000669)
    Fold Change: 0.68
    Marker Score: 395
  • Cell Name: cardiac mesenchymal cell (CL0000569)
    Fold Change: 0.67
    Marker Score: 166

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Other Information

**Key characteristics:** - Type: Protein - Ensembl ID: ENSG00000000971 - Molecular weight: 180 kDa - Function: Complement activation, Complement activation, alternative pathway, Complement cascade **Pathways and functions:** - **Complement activation:** CFH binds to complement proteins and facilitates the assembly of the alternative pathway complex. - **Complement activation, alternative pathway:** The alternative pathway is activated by the binding of C3b to its receptor on the surface of infected cells, leading to the formation of the C3 convertase complex and the activation of downstream complement proteins. - **Regulation of complement activation:** CFH and other regulators of the complement system help to control the inflammatory response by inhibiting excessive complement activation. **Clinical significance:** - CFH gene is commonly mutated in human genetic disorders, including C3, C4, C5, C6, and C7 deficiencies, resulting in severe immune disorders known as complement deficiencies. - Mutations in CFH are also associated with autoimmune disorders, where the immune system mistakenly attacks healthy tissues. - CFH is a potential therapeutic target for diseases characterized by excessive complement activation, such as autoimmune disorders and infections.

Genular Protein ID: 397786447

Symbol: CFAH_HUMAN

Name: Complement factor H

UniProtKB Accession Codes:

P08603 A5PL14 P78435 Q14570 Q2TAZ5 Q38G77 Q5TFM3 Q8N708 Q9NU86

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 1 CPTAC 1 CTD 1 CarbonylDB 1 ChEMBL 1 ChiTaRS 1 ComplexPortal 2 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 5 EMBL 12 EPD 1 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 16 Gene3D 1 GeneCards 1 GeneReviews 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 2 KEGG 1 MANE-Select 1 MIM 9 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 Orphanet 8 OrthoDB 1 PANTHER 2 PDB 65 PDBsum 47 PIR 2 PRO 1 PROSITE 1 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 2 Pumba 1 RNAct 1 Reactome 1 RefSeq 1 SIGNOR 1 SMART 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 UniProtKB 5 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 2963625

Title: The complete amino acid sequence of human complement factor H.

PubMed ID: 2963625

DOI: 10.1042/bj2490593

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2946589

Title: Human complement factor H: isolation of cDNA clones and partial cDNA sequence of the 38-kDa tryptic fragment containing the binding site for C3b.

PubMed ID: 2946589

DOI: 10.1002/eji.1830161107

PubMed ID: 2937845

Title: Structural analysis of human complement protein H: homology with C4b binding protein, beta 2-glycoprotein I, and the Ba fragment of B2.

PubMed ID: 2937845

PubMed ID: 1826708

Title: Cloning of the 1.4-kb mRNA species of human complement factor H reveals a novel member of the short consensus repeat family related to the carboxy terminal of the classical 150-kDa molecule.

PubMed ID: 1826708

PubMed ID: 6215918

Title: Purification and structural studies on the complement-system control protein beta 1H (Factor H).

PubMed ID: 6215918

DOI: 10.1042/bj2050285

PubMed ID: 6444659

Title: Biosynthesis of the complement components and the regulatory proteins of the alternative complement pathway by human peripheral blood monocytes.

PubMed ID: 6444659

DOI: 10.1084/jem.151.3.501

PubMed ID: 2968404

Title: Synthesis and regulation of complement protein factor H in human skin fibroblasts.

PubMed ID: 2968404

PubMed ID: 2139673

Title: Differential regulation of complement factor H and C3 production in human umbilical vein endothelial cells by IFN-gamma and IL-1.

PubMed ID: 2139673

PubMed ID: 9558116

Title: Human polymorphonuclear leukocytes adhere to complement factor H through an interaction that involves alphaMbeta2 (CD11b/CD18).

PubMed ID: 9558116

PubMed ID: 14760718

Title: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 17591618

Title: Site-specific N-glycan characterization of human complement factor H.

PubMed ID: 17591618

DOI: 10.1093/glycob/cwm060

PubMed ID: 19112495

Title: The Staphylococcus aureus protein Sbi acts as a complement inhibitor and forms a tripartite complex with host complement Factor H and C3b.

PubMed ID: 19112495

DOI: 10.1371/journal.ppat.1000250

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19139490

Title: A strategy for precise and large scale identification of core fucosylated glycoproteins.

PubMed ID: 19139490

DOI: 10.1074/mcp.m800504-mcp200

PubMed ID: 19838169

Title: Enrichment of glycopeptides for glycan structure and attachment site identification.

PubMed ID: 19838169

DOI: 10.1038/nmeth.1392

PubMed ID: 20008295

Title: Factor H and factor H-related protein 1 bind to human neutrophils via complement receptor 3, mediate attachment to Candida albicans, and enhance neutrophil antimicrobial activity.

PubMed ID: 20008295

DOI: 10.4049/jimmunol.0901702

PubMed ID: 23332154

Title: Malaria parasites co-opt human factor H to prevent complement-mediated lysis in the mosquito midgut.

PubMed ID: 23332154

DOI: 10.1016/j.chom.2012.11.013

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25136834

Title: Complement factor H, vitronectin, and opticin are tyrosine-sulfated proteins of the retinal pigment epithelium.

PubMed ID: 25136834

DOI: 10.1371/journal.pone.0105409

PubMed ID: 26700768

Title: Recruitment of Factor H as a Novel Complement Evasion Strategy for Blood-Stage Plasmodium falciparum Infection.

PubMed ID: 26700768

DOI: 10.4049/jimmunol.1501581

PubMed ID: 1829116

Title: Three-dimensional structure of a complement control protein module in solution.

PubMed ID: 1829116

DOI: 10.1016/0022-2836(91)90666-t

PubMed ID: 1533152

Title: Solution structure of the fifth repeat of factor H: a second example of the complement control protein module.

PubMed ID: 1533152

DOI: 10.1021/bi00129a011

PubMed ID: 8331663

Title: Solution structure of a pair of complement modules by nuclear magnetic resonance.

PubMed ID: 8331663

DOI: 10.1006/jmbi.1993.1381

PubMed ID: 9312129

Title: Human factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolism.

PubMed ID: 9312129

DOI: 10.1074/jbc.272.40.25168

PubMed ID: 9551389

Title: Genetic studies into inherited and sporadic hemolytic uremic syndrome.

PubMed ID: 9551389

DOI: 10.1111/j.1523-1755.1998.00824.x

PubMed ID: 10577907

Title: Complement factor H gene mutation associated with autosomal recessive atypical hemolytic uremic syndrome.

PubMed ID: 10577907

DOI: 10.1086/302673

PubMed ID: 10762557

Title: Complement factor H gene mutation associated with autosomal recessive atypical hemolytic uremic syndrome.

PubMed ID: 10762557

DOI: 10.1086/302877

PubMed ID: 10803850

Title: Molecular basis for factor H and FHL-1 deficiency in an Italian family.

PubMed ID: 10803850

DOI: 10.1007/s002510050631

PubMed ID: 11170895

Title: Clustering of missense mutations in the C-terminal region of factor H in atypical hemolytic uremic syndrome.

PubMed ID: 11170895

DOI: 10.1086/318201

PubMed ID: 11170896

Title: Factor H mutations in hemolytic uremic syndrome cluster in exons 18-20, a domain important for host cell recognition.

PubMed ID: 11170896

DOI: 10.1086/318203

PubMed ID: 11158219

Title: The molecular basis of familial hemolytic uremic syndrome: mutation analysis of factor H gene reveals a hot spot in short consensus repeat 20.

PubMed ID: 11158219

DOI: 10.1681/asn.v122297

PubMed ID: 11851332

Title: Molecular modelling of the C-terminal domains of factor H of human complement: a correlation between haemolytic uraemic syndrome and a predicted heparin binding site.

PubMed ID: 11851332

DOI: 10.1006/jmbi.2001.5337

PubMed ID: 12020532

Title: Combined kidney and liver transplantation for familial haemolytic uraemic syndrome.

PubMed ID: 12020532

DOI: 10.1016/s0140-6736(02)08560-4

PubMed ID: 14583443

Title: Complement factor H mutations and gene polymorphisms in haemolytic uraemic syndrome: the C-257T, the A2089G and the G2881T polymorphisms are strongly associated with the disease.

PubMed ID: 14583443

DOI: 10.1093/hmg/ddg363

PubMed ID: 12960213

Title: Haemolytic uraemic syndrome and mutations of the factor H gene: a registry-based study of German speaking countries.

PubMed ID: 12960213

DOI: 10.1136/jmg.40.9.676

PubMed ID: 14978182

Title: Heterozygous and homozygous factor H deficiencies associated with hemolytic uremic syndrome or membranoproliferative glomerulonephritis: report and genetic analysis of 16 cases.

PubMed ID: 14978182

DOI: 10.1097/01.asn.0000115702.28859.a7

PubMed ID: 15895326

Title: Strong association of the Y402H variant in complement factor H at 1q32 with susceptibility to age-related macular degeneration.

PubMed ID: 15895326

DOI: 10.1086/431426

PubMed ID: 15870199

Title: A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration.

PubMed ID: 15870199

DOI: 10.1073/pnas.0501536102

PubMed ID: 15761122

Title: Complement factor H polymorphism in age-related macular degeneration.

PubMed ID: 15761122

DOI: 10.1126/science.1109557

PubMed ID: 15761120

Title: Complement factor H variant increases the risk of age-related macular degeneration.

PubMed ID: 15761120

DOI: 10.1126/science.1110359

PubMed ID: 15761121

Title: Complement factor H polymorphism and age-related macular degeneration.

PubMed ID: 15761121

DOI: 10.1126/science.1110189

PubMed ID: 16612335

Title: Deletion of Lys224 in regulatory domain 4 of factor H reveals a novel pathomechanism for dense deposit disease (MPGN II).

PubMed ID: 16612335

DOI: 10.1038/sj.ki.5000269

PubMed ID: 17132743

Title: West Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.

PubMed ID: 17132743

DOI: 10.1073/pnas.0605668103

PubMed ID: 18252232

Title: Basal laminar drusen caused by compound heterozygous variants in the CFH gene.

PubMed ID: 18252232

DOI: 10.1016/j.ajhg.2007.11.007

PubMed ID: 20513133

Title: Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome.

PubMed ID: 20513133

DOI: 10.1002/humu.21256

PubMed ID: 22028381

Title: Quantitative detection of single amino acid polymorphisms by targeted proteomics.

PubMed ID: 22028381

DOI: 10.1093/jmcb/mjr024

PubMed ID: 22019782

Title: A rare penetrant mutation in CFH confers high risk of age-related macular degeneration.

PubMed ID: 22019782

DOI: 10.1038/ng.976

PubMed ID: 16601698

Title: Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.

PubMed ID: 16601698

DOI: 10.1038/sj.emboj.7601052

PubMed ID: 17360715

Title: Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism.

PubMed ID: 17360715

DOI: 10.1074/jbc.m609636200

PubMed ID: 17893204

Title: Structural basis for complement factor H linked age-related macular degeneration.

PubMed ID: 17893204

DOI: 10.1084/jem.20071069

PubMed ID: 18252712

Title: Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations.

PubMed ID: 18252712

DOI: 10.1074/jbc.m709587200

PubMed ID: 18005991

Title: The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties.

PubMed ID: 18005991

DOI: 10.1016/j.jmb.2007.09.026

PubMed ID: 19505476

Title: Electrostatic interactions contribute to the folded-back conformation of wild type human factor H.

PubMed ID: 19505476

DOI: 10.1016/j.jmb.2009.06.010

PubMed ID: 19503104

Title: Structure of complement fragment C3b-factor H and implications for host protection by complement regulators.

PubMed ID: 19503104

DOI: 10.1038/ni.1755

PubMed ID: 19225461

Title: Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates.

PubMed ID: 19225461

DOI: 10.1038/nature07769

PubMed ID: 19835885

Title: The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module.

PubMed ID: 19835885

DOI: 10.1016/j.jmb.2009.10.010

PubMed ID: 20378178

Title: Both domain 19 and domain 20 of factor H are involved in binding to complement C3b and C3d.

PubMed ID: 20378178

DOI: 10.1016/j.molimm.2010.03.007

PubMed ID: 21285368

Title: Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement.

PubMed ID: 21285368

DOI: 10.1073/pnas.1017087108

PubMed ID: 23133374

Title: Design and evaluation of meningococcal vaccines through structure-based modification of host and pathogen molecules.

PubMed ID: 23133374

DOI: 10.1371/journal.ppat.1002981

PubMed ID: 23017427

Title: Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H.

PubMed ID: 23017427

DOI: 10.1016/j.jmb.2012.09.013

PubMed ID: 22389686

Title: Structural analysis of the C-terminal region (modules 18-20) of complement regulator factor H (FH).

PubMed ID: 22389686

DOI: 10.1371/journal.pone.0032187

PubMed ID: 23658013

Title: Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi.

PubMed ID: 23658013

DOI: 10.1074/jbc.m113.459040

PubMed ID: 23204165

Title: Glycerol-3-phosphate dehydrogenase 2 is a novel factor H-, factor H-like protein 1-, and plasminogen-binding surface protein of Candida albicans.

PubMed ID: 23204165

DOI: 10.1093/infdis/jis718

PubMed ID: 25330773

Title: Structural determinants of host specificity of complement Factor H recruitment by Streptococcus pneumoniae.

PubMed ID: 25330773

DOI: 10.1042/bj20141069

PubMed ID: 25402769

Title: Structural basis for sialic acid-mediated self-recognition by complement factor H.

PubMed ID: 25402769

DOI: 10.1038/nchembio.1696

PubMed ID: 28258151

Title: Staphylococcus aureus SdrE captures complement factor H's C-terminus via a novel 'close, dock, lock and latch' mechanism for complement evasion.

PubMed ID: 28258151

DOI: 10.1042/bcj20170085

PubMed ID: 28671664

Title: Regulator-dependent mechanisms of C3b processing by factor I allow differentiation of immune responses.

PubMed ID: 28671664

DOI: 10.1038/nsmb.3427

PubMed ID: 29190743

Title: Crystal structure of a tripartite complex between C3dg, C-terminal domains of factor H and OspE of Borrelia burgdorferi.

PubMed ID: 29190743

DOI: 10.1371/journal.pone.0188127

PubMed ID: 34986357

Title: Estrogen promotes innate immune evasion of Candida albicans through inactivation of the alternative complement system.

PubMed ID: 34986357

DOI: 10.1016/j.celrep.2021.110183

Sequence Information:

  • Length: 1231
  • Mass: 139096
  • Checksum: 3C26D62A2BF9BFEE
  • Sequence:
    • MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY KCRPGYRSLG 
NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG GNVFEYGVKA VYTCNEGYQL 
LGEINYRECD TDGWTNDIPI CEVVKCLPVT APENGKIVSS AMEPDREYHF GQAVRFVCNS 
GYKIEGDEEM HCSDDGFWSK EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG 
YEYSERGDAV CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP 
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG KYYSYYCDEH 
FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ NYGRKFVQGK SIDVACHPGY 
ALPKAQTTVT CMENGWSPTP RCIRVKTCSK SSIDIENGFI SESQYTYALK EKAKYQCKLG 
YVTADGETSG SITCGKDGWS AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY 
ESNTGSTTGS IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG 
FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG HSEVVEYYCN 
PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG WAQLSSPPYY YGDSVEFNCS 
ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL KKCKSSNLII LEEHLKNKKE FDHNSNIRYR 
CRGKEGWIHT VCINGRWDPE VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ 
ENYLIQEGEE ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT 
CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ YGEEVTYKCF 
EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP MGEKKDVYKA GEQVTYTCAT 
YYKMDGASNV TCINSRWTGR PTCRDTSCVN PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP 
YEMFGDEEVM CLNGNWTEPP QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN 
LYQLEGNKRI TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV 
CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R

Genular Protein ID: 3465716094

Symbol: A0A0D9SG88_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A0D9SG88

Database IDs:

ARBA 3 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CDD 1 CTD 1 ChiTaRS 1 DNASU 1 EMBL 3 Ensembl 2 ExpressionAtlas 1 Gene3D 1 GeneTree 1 GenomeRNAi 1 HGNC 1 InterPro 2 MassIVE 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 2 PROSITE-ProRule 1 PeptideAtlas 1 Pfam 1 Proteomes 2 RefSeq 1 SAM 1 SMART 1 SMR 1 SUPFAM 1 VEuPathDB 1

Citations:

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

Sequence Information:

  • Length: 449
  • Mass: 51008
  • Checksum: A9C77F0F155343F7
  • Sequence:
    • MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY KCRPGYRSLG 
NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG GNVFEYGVKA VYTCNEGYQL 
LGEINYRECD TDGWTNDIPI CEVVKCLPVT APENGKIVSS AMEPDREYHF GQAVRFVCNS 
GYKIEGDEEM HCSDDGFWSK EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG 
YEYSERGDAV CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP 
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG KYYSYYCDEH 
FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ NHGRKFVQGK SIDVACHPGY 
ALPKAQTTVT CMENGWSPTP RCIRVSFTL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.