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P08603

- CFAH_HUMAN

UniProt

P08603 - CFAH_HUMAN

Protein

Complement factor H

Gene

CFH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 4 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.

    GO - Molecular functioni

    1. heparan sulfate proteoglycan binding Source: BHF-UCL
    2. heparin binding Source: BHF-UCL
    3. protein binding Source: IntAct

    GO - Biological processi

    1. complement activation Source: ProtInc
    2. complement activation, alternative pathway Source: UniProtKB-KW
    3. innate immune response Source: Reactome
    4. regulation of complement activation Source: Reactome

    Keywords - Biological processi

    Complement alternate pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement factor H
    Alternative name(s):
    H factor 1
    Gene namesi
    Name:CFH
    Synonyms:HF, HF1, HF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4883. CFH.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Basal laminar drusen (BLD) [MIM:126700]: Drusen 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.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis.
    Complement factor H deficiency (CFHD) [MIM:609814]: A 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.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031978
    Natural varianti224 – 2241Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication
    VAR_031979
    Natural varianti431 – 4311C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031981
    Natural varianti536 – 5361C → R in CFHD. 1 Publication
    VAR_019405
    Natural varianti673 – 6731C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031982
    Natural varianti959 – 9591C → Y in CFHD; variant confirmed at protein level. 2 Publications
    VAR_019406
    Natural varianti1076 – 10761Q → E in CFHD. 2 Publications
    VAR_025873
    Natural varianti1119 – 11191D → G in CFHD. 2 Publications
    VAR_025874
    Natural varianti1184 – 11841T → R in CFHD. 2 Publications
    VAR_025881
    Natural varianti1210 – 12101R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications
    VAR_025885
    Natural varianti1215 – 12151R → Q in CFHD. 2 Publications
    VAR_025887
    Hemolytic uremic syndrome atypical 1 (AHUS1) [MIM:235400]: 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.8 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti78 – 781R → G in AHUS1. 1 Publication
    VAR_025864
    Natural varianti325 – 3251C → Y in AHUS1. 1 Publication
    VAR_063648
    Natural varianti400 – 4001Q → K in AHUS1. 1 Publication
    VAR_031980
    Natural varianti609 – 6091V → I in AHUS1. 1 Publication
    VAR_063649
    Natural varianti630 – 6301C → W in AHUS1. 1 Publication
    VAR_025865
    Natural varianti673 – 6731C → Y in AHUS1. 1 Publication
    VAR_031983
    Natural varianti850 – 8501E → K in AHUS1; variant confirmed at protein level. 2 Publications
    VAR_025866
    Natural varianti893 – 8931H → R in AHUS1. 1 Publication
    VAR_031984
    Natural varianti915 – 9151C → S in AHUS1. 1 Publication
    VAR_031985
    Natural varianti950 – 9501Q → H in AHUS1. 1 Publication
    Corresponds to variant rs149474608 [ dbSNP | Ensembl ].
    VAR_025867
    Natural varianti951 – 9511Y → H in AHUS1. 1 Publication
    VAR_025868
    Natural varianti956 – 9561T → M in AHUS1. 2 Publications
    Corresponds to variant rs145975787 [ dbSNP | Ensembl ].
    VAR_025869
    Natural varianti978 – 9781W → C in AHUS1. 1 Publication
    VAR_025870
    Natural varianti1021 – 10211Y → F in AHUS1. 1 Publication
    VAR_025871
    Natural varianti1043 – 10431C → R in AHUS1. 1 Publication
    VAR_025872
    Natural varianti1134 – 11341V → G in AHUS1. 1 Publication
    VAR_025875
    Natural varianti1142 – 11421Y → D in AHUS1. 1 Publication
    VAR_025876
    Natural varianti1157 – 11571W → R in AHUS1. 1 Publication
    VAR_025877
    Natural varianti1163 – 11631C → W in AHUS1. 1 Publication
    VAR_025878
    Natural varianti1169 – 11691I → L in AHUS1. 1 Publication
    VAR_063650
    Natural varianti1183 – 11831W → C in AHUS1. 1 Publication
    VAR_063651
    Natural varianti1183 – 11831W → L in AHUS1. 3 Publications
    VAR_025879
    Natural varianti1183 – 11831W → R in AHUS1. 2 Publications
    VAR_025880
    Natural varianti1189 – 11891L → R in AHUS1. 2 Publications
    VAR_019407
    Natural varianti1191 – 11911S → L in AHUS1. 2 Publications
    Corresponds to variant rs460897 [ dbSNP | Ensembl ].
    VAR_019408
    Natural varianti1194 – 11941G → D in AHUS1. 1 Publication
    VAR_025882
    Natural varianti1197 – 11971V → A in AHUS1. 2 Publications
    Corresponds to variant rs460184 [ dbSNP | Ensembl ].
    VAR_025883
    Natural varianti1198 – 11981E → A in AHUS1. 1 Publication
    VAR_025884
    Natural varianti1199 – 11991F → S in AHUS1. 1 Publication
    VAR_031986
    Natural varianti1215 – 12151R → G in AHUS1. 2 Publications
    VAR_025886
    Natural varianti1225 – 12317YPTCAKR → FQS in AHUS1. 1 Publication
    VAR_019409
    Natural varianti1226 – 12261P → S in AHUS1; atypical. 1 Publication
    VAR_025888
    Macular degeneration, age-related, 4 (ARMD4) [MIM:610698]: A 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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti402 – 4021Y → H Polymorphism associated with ARMD4. 5 Publications
    Corresponds to variant rs1061170 [ dbSNP | Ensembl ].
    VAR_001979
    Natural varianti1210 – 12101R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications
    VAR_025885

    Keywords - Diseasei

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

    Organism-specific databases

    MIMi126700. phenotype.
    235400. phenotype.
    609814. phenotype.
    610698. phenotype.
    Orphaneti279. Age-related macular degeneration.
    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.
    PharmGKBiPA29261.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 12311213Complement factor HPRO_0000005894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 66PROSITE-ProRule annotation
    Disulfide bondi52 ↔ 80PROSITE-ProRule annotation
    Disulfide bondi85 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi114 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi146 ↔ 192PROSITE-ProRule annotation
    Disulfide bondi178 ↔ 205PROSITE-ProRule annotation
    Disulfide bondi210 ↔ 251PROSITE-ProRule annotation
    Glycosylationi217 – 2171N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi237 ↔ 262PROSITE-ProRule annotation
    Disulfide bondi267 ↔ 309PROSITE-ProRule annotation
    Disulfide bondi294 ↔ 320PROSITE-ProRule annotation
    Disulfide bondi325 ↔ 374PROSITE-ProRule annotation
    Disulfide bondi357 ↔ 385PROSITE-ProRule annotation
    Disulfide bondi389 ↔ 431PROSITE-ProRule annotation
    Disulfide bondi416 ↔ 442PROSITE-ProRule annotation
    Disulfide bondi448 ↔ 494PROSITE-ProRule annotation
    Disulfide bondi477 ↔ 505PROSITE-ProRule annotation
    Disulfide bondi509 ↔ 553PROSITE-ProRule annotation
    Glycosylationi529 – 5291N-linked (GlcNAc...)4 Publications
    Disulfide bondi536 ↔ 564PROSITE-ProRule annotation
    Disulfide bondi569 ↔ 611PROSITE-ProRule annotation
    Disulfide bondi597 ↔ 623PROSITE-ProRule annotation
    Disulfide bondi630 ↔ 673PROSITE-ProRule annotation
    Disulfide bondi659 ↔ 684PROSITE-ProRule annotation
    Disulfide bondi691 ↔ 733PROSITE-ProRule annotation
    Glycosylationi718 – 7181N-linked (GlcNAc...)1 Publication
    Disulfide bondi719 ↔ 744PROSITE-ProRule annotation
    Disulfide bondi753 ↔ 792PROSITE-ProRule annotation
    Disulfide bondi781 ↔ 803PROSITE-ProRule annotation
    Glycosylationi802 – 8021N-linked (GlcNAc...)2 Publications
    Disulfide bondi811 ↔ 853PROSITE-ProRule annotation
    Glycosylationi822 – 8221N-linked (GlcNAc...)1 Publication
    Disulfide bondi839 ↔ 864PROSITE-ProRule annotation
    Disulfide bondi870 ↔ 915PROSITE-ProRule annotation
    Glycosylationi882 – 8821N-linked (GlcNAc...) (complex)5 Publications
    Disulfide bondi901 ↔ 926PROSITE-ProRule annotation
    Glycosylationi911 – 9111N-linked (GlcNAc...) (complex)4 Publications
    Disulfide bondi931 ↔ 973PROSITE-ProRule annotation
    Disulfide bondi959 ↔ 984PROSITE-ProRule annotation
    Disulfide bondi989 ↔ 1032PROSITE-ProRule annotation
    Disulfide bondi1018 ↔ 1043PROSITE-ProRule annotation
    Glycosylationi1029 – 10291N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi1048 ↔ 1091PROSITE-ProRule annotation
    Disulfide bondi1077 ↔ 1102PROSITE-ProRule annotation
    Glycosylationi1095 – 10951N-linked (GlcNAc...)1 Publication
    Disulfide bondi1109 ↔ 1152PROSITE-ProRule annotation
    Disulfide bondi1138 ↔ 1163PROSITE-ProRule annotation
    Disulfide bondi1167 ↔ 1218PROSITE-ProRule annotation
    Disulfide bondi1201 ↔ 1228PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08603.
    PaxDbiP08603.
    PRIDEiP08603.

    PTM databases

    PhosphoSiteiP08603.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP08603.
    BgeeiP08603.
    GenevestigatoriP08603.

    Organism-specific databases

    HPAiCAB016385.
    CAB016769.
    HPA038922.
    HPA049176.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    C3P010242EBI-1223708,EBI-6863145
    ennXP169462EBI-1223708,EBI-6403567From a different organism.

    Protein-protein interaction databases

    BioGridi109324. 14 interactions.
    DIPiDIP-38303N.
    IntActiP08603. 13 interactions.

    Structurei

    Secondary structure

    1
    1231
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 233
    Beta strandi29 – 335
    Beta strandi47 – 526
    Beta strandi62 – 665
    Beta strandi68 – 747
    Beta strandi94 – 10512
    Beta strandi109 – 1146
    Beta strandi118 – 1236
    Beta strandi126 – 1294
    Beta strandi131 – 1344
    Beta strandi140 – 1434
    Beta strandi155 – 1584
    Beta strandi159 – 1624
    Beta strandi172 – 1754
    Beta strandi182 – 1865
    Beta strandi188 – 1925
    Beta strandi196 – 2005
    Beta strandi204 – 2074
    Beta strandi218 – 2225
    Beta strandi232 – 2376
    Beta strandi241 – 2455
    Beta strandi247 – 2526
    Beta strandi255 – 2584
    Beta strandi262 – 2643
    Beta strandi333 – 3353
    Helixi338 – 3414
    Helixi342 – 3443
    Beta strandi352 – 3576
    Beta strandi366 – 37510
    Beta strandi378 – 3836
    Beta strandi386 – 3905
    Turni400 – 4034
    Beta strandi405 – 4073
    Beta strandi411 – 4133
    Beta strandi415 – 4173
    Beta strandi420 – 4223
    Helixi423 – 4253
    Beta strandi428 – 4325
    Beta strandi435 – 4384
    Beta strandi447 – 4493
    Helixi450 – 4523
    Beta strandi456 – 4594
    Beta strandi465 – 4684
    Beta strandi472 – 4776
    Beta strandi484 – 4863
    Beta strandi488 – 4958
    Beta strandi498 – 5003
    Beta strandi508 – 5103
    Beta strandi515 – 5184
    Beta strandi524 – 5274
    Beta strandi531 – 5366
    Beta strandi547 – 5548
    Beta strandi557 – 5604
    Beta strandi578 – 5814
    Beta strandi585 – 5873
    Beta strandi592 – 5976
    Beta strandi602 – 6054
    Beta strandi607 – 6126
    Beta strandi615 – 6184
    Beta strandi622 – 6265
    Beta strandi637 – 6415
    Beta strandi654 – 6585
    Beta strandi663 – 6653
    Beta strandi669 – 6746
    Beta strandi675 – 6784
    Beta strandi684 – 6863
    Beta strandi700 – 7034
    Beta strandi714 – 7185
    Beta strandi723 – 7275
    Beta strandi729 – 7324
    Beta strandi737 – 7393
    Beta strandi743 – 7464
    Beta strandi757 – 7604
    Helixi765 – 7673
    Beta strandi769 – 7713
    Beta strandi790 – 7923
    Beta strandi797 – 7993
    Beta strandi870 – 8723
    Beta strandi879 – 8813
    Beta strandi883 – 8875
    Beta strandi889 – 8913
    Beta strandi895 – 90410
    Beta strandi906 – 9094
    Beta strandi911 – 9166
    Beta strandi925 – 9273
    Beta strandi940 – 9434
    Beta strandi950 – 9523
    Beta strandi957 – 9593
    Beta strandi965 – 9673
    Beta strandi971 – 9744
    Beta strandi977 – 9793
    Beta strandi1057 – 10593
    Beta strandi1065 – 10673
    Beta strandi1072 – 10776
    Beta strandi1082 – 10854
    Beta strandi1087 – 10926
    Beta strandi1101 – 11033
    Beta strandi1118 – 11225
    Beta strandi1126 – 11283
    Beta strandi1133 – 11386
    Beta strandi1143 – 11464
    Beta strandi1148 – 11536
    Beta strandi1162 – 11643
    Beta strandi1167 – 11704
    Helixi1171 – 11777
    Beta strandi1179 – 11813
    Turni1182 – 11865
    Beta strandi1189 – 11913
    Beta strandi1196 – 12016
    Turni1202 – 12043
    Beta strandi1205 – 12073
    Beta strandi1214 – 12174
    Beta strandi1228 – 12303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP08603.
    SMRiP08603. Positions 20-1230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08603.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 8264Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini83 – 14361Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 20764Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini208 – 26457Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini265 – 32258Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini324 – 38663Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 44458Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini446 – 50762Sushi 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini515 – 56652Sushi 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini567 – 62559Sushi 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini628 – 68659Sushi 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini689 – 74658Sushi 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini751 – 80555Sushi 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini809 – 86658Sushi 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini868 – 92861Sushi 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini929 – 98658Sushi 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini987 – 104559Sushi 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1046 – 110459Sushi 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini1107 – 116559Sushi 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini1170 – 123061Sushi 20PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 20 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG148800.
    HOVERGENiHBG005665.
    InParanoidiP08603.
    KOiK04004.
    OrthoDBiEOG75XGK1.
    PhylomeDBiP08603.
    TreeFamiTF326157.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 19 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 20 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 18 hits.
    PROSITEiPS50923. SUSHI. 19 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY     50
    KCRPGYRSLG NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG 100
    GNVFEYGVKA VYTCNEGYQL LGEINYRECD TDGWTNDIPI CEVVKCLPVT 150
    APENGKIVSS AMEPDREYHF GQAVRFVCNS GYKIEGDEEM HCSDDGFWSK 200
    EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG YEYSERGDAV 250
    CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP 300
    ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG 350
    KYYSYYCDEH FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ 400
    NYGRKFVQGK SIDVACHPGY ALPKAQTTVT CMENGWSPTP RCIRVKTCSK 450
    SSIDIENGFI SESQYTYALK EKAKYQCKLG YVTADGETSG SITCGKDGWS 500
    AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY ESNTGSTTGS 550
    IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG 600
    FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG 650
    HSEVVEYYCN PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG 700
    WAQLSSPPYY YGDSVEFNCS ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL 750
    KKCKSSNLII LEEHLKNKKE FDHNSNIRYR CRGKEGWIHT VCINGRWDPE 800
    VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ ENYLIQEGEE 850
    ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT 900
    CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ 950
    YGEEVTYKCF EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP 1000
    MGEKKDVYKA GEQVTYTCAT YYKMDGASNV TCINSRWTGR PTCRDTSCVN 1050
    PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP YEMFGDEEVM CLNGNWTEPP 1100
    QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN LYQLEGNKRI 1150
    TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV 1200
    CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R 1231
    Length:1,231
    Mass (Da):139,096
    Last modified:September 11, 2007 - v4
    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

    Sequence cautioni

    The sequence CAB41739.1 differs from that shown. Reason: Frameshift at position 341.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211C → Q AA sequence (PubMed:6215918)Curated
    Sequence conflicti30 – 301T → V AA sequence (PubMed:6215918)Curated
    Sequence conflicti34 – 341T → Q AA sequence (PubMed:6215918)Curated
    Sequence conflicti53 – 542RP → IL in CAB41739. (PubMed:2946589)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621V → I Polymorphism confirmed at protein level. 4 Publications
    Corresponds to variant rs800292 [ dbSNP | Ensembl ].
    VAR_023836
    Natural varianti78 – 781R → G in AHUS1. 1 Publication
    VAR_025864
    Natural varianti127 – 1271R → L in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031978
    Natural varianti224 – 2241Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. 1 Publication
    VAR_031979
    Natural varianti325 – 3251C → Y in AHUS1. 1 Publication
    VAR_063648
    Natural varianti400 – 4001Q → K in AHUS1. 1 Publication
    VAR_031980
    Natural varianti402 – 4021Y → H Polymorphism associated with ARMD4. 5 Publications
    Corresponds to variant rs1061170 [ dbSNP | Ensembl ].
    VAR_001979
    Natural varianti431 – 4311C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031981
    Natural varianti493 – 4931T → R.1 Publication
    Corresponds to variant rs1061171 [ dbSNP | Ensembl ].
    VAR_043892
    Natural varianti536 – 5361C → R in CFHD. 1 Publication
    VAR_019405
    Natural varianti551 – 5511I → T.1 Publication
    Corresponds to variant rs35453854 [ dbSNP | Ensembl ].
    VAR_025092
    Natural varianti567 – 5671R → G Associated with basal laminar drusen. 1 Publication
    VAR_043893
    Natural varianti609 – 6091V → I in AHUS1. 1 Publication
    VAR_063649
    Natural varianti630 – 6301C → W in AHUS1. 1 Publication
    VAR_025865
    Natural varianti673 – 6731C → S in CFHD; with membranoproliferative glomerulonephritis. 1 Publication
    VAR_031982
    Natural varianti673 – 6731C → Y in AHUS1. 1 Publication
    VAR_031983
    Natural varianti850 – 8501E → K in AHUS1; variant confirmed at protein level. 2 Publications
    VAR_025866
    Natural varianti890 – 8901S → I.1 Publication
    Corresponds to variant rs515299 [ dbSNP | Ensembl ].
    VAR_025093
    Natural varianti893 – 8931H → R in AHUS1. 1 Publication
    VAR_031984
    Natural varianti915 – 9151C → S in AHUS1. 1 Publication
    VAR_031985
    Natural varianti936 – 9361E → D Polymorphism associated with hemolytic uremic syndrome and basal laminar drusen. 4 Publications
    Corresponds to variant rs1065489 [ dbSNP | Ensembl ].
    VAR_020261
    Natural varianti950 – 9501Q → H in AHUS1. 1 Publication
    Corresponds to variant rs149474608 [ dbSNP | Ensembl ].
    VAR_025867
    Natural varianti951 – 9511Y → H in AHUS1. 1 Publication
    VAR_025868
    Natural varianti956 – 9561T → M in AHUS1. 2 Publications
    Corresponds to variant rs145975787 [ dbSNP | Ensembl ].
    VAR_025869
    Natural varianti959 – 9591C → Y in CFHD; variant confirmed at protein level. 2 Publications
    VAR_019406
    Natural varianti978 – 9781W → C in AHUS1. 1 Publication
    VAR_025870
    Natural varianti997 – 9971N → T.
    Corresponds to variant rs17575212 [ dbSNP | Ensembl ].
    VAR_055683
    Natural varianti1007 – 10071V → I.1 Publication
    VAR_025094
    Natural varianti1007 – 10071V → L.
    Corresponds to variant rs534399 [ dbSNP | Ensembl ].
    VAR_043894
    Natural varianti1010 – 10101A → T.
    Corresponds to variant rs11539862 [ dbSNP | Ensembl ].
    VAR_055684
    Natural varianti1017 – 10171T → I.1 Publication
    Corresponds to variant rs34362004 [ dbSNP | Ensembl ].
    VAR_025095
    Natural varianti1021 – 10211Y → F in AHUS1. 1 Publication
    VAR_025871
    Natural varianti1043 – 10431C → R in AHUS1. 1 Publication
    VAR_025872
    Natural varianti1050 – 10501N → Y Polymorphism associated with basal laminar drusen. 2 Publications
    Corresponds to variant rs35274867 [ dbSNP | Ensembl ].
    VAR_025096
    Natural varianti1059 – 10591I → T.1 Publication
    Corresponds to variant rs35343172 [ dbSNP | Ensembl ].
    VAR_025097
    Natural varianti1076 – 10761Q → E in CFHD. 2 Publications
    VAR_025873
    Natural varianti1078 – 10781R → S Associated with basal laminar drusen. 1 Publication
    VAR_043895
    Natural varianti1119 – 11191D → G in CFHD. 2 Publications
    VAR_025874
    Natural varianti1134 – 11341V → G in AHUS1. 1 Publication
    VAR_025875
    Natural varianti1142 – 11421Y → D in AHUS1. 1 Publication
    VAR_025876
    Natural varianti1143 – 11431Q → E Polymorphism confirmed at protein level. 1 Publication
    Corresponds to variant rs34247141 [ dbSNP | Ensembl ].
    VAR_043896
    Natural varianti1157 – 11571W → R in AHUS1. 1 Publication
    VAR_025877
    Natural varianti1163 – 11631C → W in AHUS1. 1 Publication
    VAR_025878
    Natural varianti1169 – 11691I → L in AHUS1. 1 Publication
    VAR_063650
    Natural varianti1183 – 11831W → C in AHUS1. 1 Publication
    VAR_063651
    Natural varianti1183 – 11831W → L in AHUS1. 3 Publications
    VAR_025879
    Natural varianti1183 – 11831W → R in AHUS1. 2 Publications
    VAR_025880
    Natural varianti1184 – 11841T → R in CFHD. 2 Publications
    VAR_025881
    Natural varianti1189 – 11891L → R in AHUS1. 2 Publications
    VAR_019407
    Natural varianti1191 – 11911S → L in AHUS1. 2 Publications
    Corresponds to variant rs460897 [ dbSNP | Ensembl ].
    VAR_019408
    Natural varianti1194 – 11941G → D in AHUS1. 1 Publication
    VAR_025882
    Natural varianti1197 – 11971V → A in AHUS1. 2 Publications
    Corresponds to variant rs460184 [ dbSNP | Ensembl ].
    VAR_025883
    Natural varianti1198 – 11981E → A in AHUS1. 1 Publication
    VAR_025884
    Natural varianti1199 – 11991F → S in AHUS1. 1 Publication
    VAR_031986
    Natural varianti1210 – 12101R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. 3 Publications
    VAR_025885
    Natural varianti1215 – 12151R → G in AHUS1. 2 Publications
    VAR_025886
    Natural varianti1215 – 12151R → Q in CFHD. 2 Publications
    VAR_025887
    Natural varianti1225 – 12317YPTCAKR → FQS in AHUS1. 1 Publication
    VAR_019409
    Natural varianti1226 – 12261P → S in AHUS1; atypical. 1 Publication
    VAR_025888

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei446 – 4494KTCS → SFTL in isoform 2. 2 PublicationsVSP_001190
    Alternative sequencei450 – 1231782Missing in isoform 2. 2 PublicationsVSP_001191Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00716 mRNA. Translation: CAA68704.1.
    DQ233256 Genomic DNA. Translation: ABB02180.1.
    AL049744 Genomic DNA. Translation: CAI19672.1.
    BC037285 mRNA. Translation: AAH37285.1.
    BC110643 mRNA. Translation: AAI10644.1.
    BC142699 mRNA. Translation: AAI42700.1.
    X04697 mRNA. Translation: CAB41739.1. Frameshift.
    X07523 mRNA. Translation: CAA30403.1.
    M12383 mRNA. Translation: AAA52013.1.
    M65294 mRNA. Translation: AAA35948.1.
    U56979 Genomic DNA. Translation: AAB01987.1.
    Z29665 Genomic DNA. Translation: CAA82763.1.
    CCDSiCCDS1385.1. [P08603-1]
    CCDS53452.1. [P08603-2]
    PIRiS00254. NBHUH.
    S03013. NBHUHS.
    RefSeqiNP_000177.2. NM_000186.3.
    UniGeneiHs.363396.

    Genome annotation databases

    EnsembliENST00000367429; ENSP00000356399; ENSG00000000971.
    GeneIDi3075.
    KEGGihsa:3075.
    UCSCiuc001gtj.4. human. [P08603-1]

    Polymorphism databases

    DMDMi158517847.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    CFHbase

    CFH mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00716 mRNA. Translation: CAA68704.1 .
    DQ233256 Genomic DNA. Translation: ABB02180.1 .
    AL049744 Genomic DNA. Translation: CAI19672.1 .
    BC037285 mRNA. Translation: AAH37285.1 .
    BC110643 mRNA. Translation: AAI10644.1 .
    BC142699 mRNA. Translation: AAI42700.1 .
    X04697 mRNA. Translation: CAB41739.1 . Frameshift.
    X07523 mRNA. Translation: CAA30403.1 .
    M12383 mRNA. Translation: AAA52013.1 .
    M65294 mRNA. Translation: AAA35948.1 .
    U56979 Genomic DNA. Translation: AAB01987.1 .
    Z29665 Genomic DNA. Translation: CAA82763.1 .
    CCDSi CCDS1385.1. [P08603-1 ]
    CCDS53452.1. [P08603-2 ]
    PIRi S00254. NBHUH.
    S03013. NBHUHS.
    RefSeqi NP_000177.2. NM_000186.3.
    UniGenei Hs.363396.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHC model - A 1105-1231 [» ]
    1HAQ X-ray - A 19-1231 [» ]
    1HCC NMR - A 927-985 [» ]
    1HFH NMR - A 866-985 [» ]
    1HFI NMR - A 866-927 [» ]
    1KOV model - A 321-443 [» ]
    2BZM NMR - A 1107-1231 [» ]
    2G7I X-ray 1.75 A 1107-1231 [» ]
    2IC4 X-ray - A 321-506 [» ]
    2JGW NMR - A 386-446 [» ]
    2JGX NMR - A 386-446 [» ]
    2KMS NMR - A 690-804 [» ]
    2QFG X-ray - A 19-322 [» ]
    2QFH X-ray - A 928-1231 [» ]
    2RLP NMR - A 20-142 [» ]
    2RLQ NMR - A 84-206 [» ]
    2UWN X-ray 2.35 A 322-506 [» ]
    2V8E X-ray 2.50 A 322-506 [» ]
    2W80 X-ray 2.35 A/B/E/G 321-443 [» ]
    2W81 X-ray 2.35 A/B/E 321-443 [» ]
    2WII X-ray 2.70 C 18-264 [» ]
    2XQW X-ray 2.31 C 1103-1231 [» ]
    3GAU X-ray - A 19-1231 [» ]
    3GAV X-ray - A 19-1231 [» ]
    3GAW X-ray - A 19-1231 [» ]
    3KXV X-ray 2.00 A 1103-1231 [» ]
    3KZJ X-ray 1.65 A 1103-1231 [» ]
    3OXU X-ray 2.10 D/E/F 1107-1231 [» ]
    3R62 X-ray 1.52 A/B 1107-1231 [» ]
    3RJ3 X-ray 2.35 D/E/F 1107-1231 [» ]
    3SW0 X-ray 1.80 X 1046-1231 [» ]
    4AYD X-ray 2.40 A/B/E 321-443 [» ]
    4AYE X-ray 2.80 A/B/E 321-443 [» ]
    4AYI X-ray 2.31 A/E 321-443 [» ]
    4AYM X-ray 3.00 A/B/E/F 321-443 [» ]
    4B2R NMR - A 566-687 [» ]
    4B2S NMR - A 627-747 [» ]
    4J38 X-ray 2.83 B 1103-1231 [» ]
    4K12 X-ray 1.08 A 508-567 [» ]
    ProteinModelPortali P08603.
    SMRi P08603. Positions 20-1230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109324. 14 interactions.
    DIPi DIP-38303N.
    IntActi P08603. 13 interactions.

    Chemistry

    BindingDBi P08603.
    ChEMBLi CHEMBL4629.

    PTM databases

    PhosphoSitei P08603.

    Polymorphism databases

    DMDMi 158517847.

    Proteomic databases

    MaxQBi P08603.
    PaxDbi P08603.
    PRIDEi P08603.

    Protocols and materials databases

    DNASUi 3075.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367429 ; ENSP00000356399 ; ENSG00000000971 .
    GeneIDi 3075.
    KEGGi hsa:3075.
    UCSCi uc001gtj.4. human. [P08603-1 ]

    Organism-specific databases

    CTDi 3075.
    GeneCardsi GC01P196621.
    GeneReviewsi CFH.
    HGNCi HGNC:4883. CFH.
    HPAi CAB016385.
    CAB016769.
    HPA038922.
    HPA049176.
    MIMi 126700. phenotype.
    134370. gene.
    235400. phenotype.
    609814. phenotype.
    610698. phenotype.
    neXtProti NX_P08603.
    Orphaneti 279. Age-related macular degeneration.
    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.
    PharmGKBi PA29261.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148800.
    HOVERGENi HBG005665.
    InParanoidi P08603.
    KOi K04004.
    OrthoDBi EOG75XGK1.
    PhylomeDBi P08603.
    TreeFami TF326157.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.

    Miscellaneous databases

    ChiTaRSi CFH. human.
    EvolutionaryTracei P08603.
    GeneWikii Factor_H.
    GenomeRNAii 3075.
    NextBioi 12163.
    PROi P08603.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08603.
    Bgeei P08603.
    Genevestigatori P08603.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 19 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 20 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 18 hits.
    PROSITEi PS50923. SUSHI. 19 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino acid sequence of human complement factor H."
      Ripoche J., Day A.J., Harris T.J.R., Sim R.B.
      Biochem. J. 249:593-602(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), GLYCOSYLATION AT ASN-529, VARIANTS HIS-402 AND ARG-493.
      Tissue: Liver.
    2. SeattleSNPs variation discovery resource
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-62; THR-551; ILE-890; ASP-936; ILE-1007; ILE-1017; TYR-1050 AND THR-1059.
    3. "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], VARIANT HIS-402.
    4. "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] (ISOFORMS 1 AND 2), VARIANT ILE-62.
      Tissue: Testis and Urinary bladder.
    5. "Human complement factor H: isolation of cDNA clones and partial cDNA sequence of the 38-kDa tryptic fragment containing the binding site for C3b."
      Schulz T.F., Schwaeble W., Stanley K.K., Weiss E., Dierich M.P.
      Eur. J. Immunol. 16:1351-1355(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-445.
    6. "Structural analysis of human complement protein H: homology with C4b binding protein, beta 2-glycoprotein I, and the Ba fragment of B2."
      Kristensen T., Wetsel R.A., Tack B.F.
      J. Immunol. 136:3407-3411(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-449, PROTEIN SEQUENCE OF 205-216; 237-246; 320-331; 425-435; 508-518; 645-662; 667-717; 858-885; 907-972; 1163-1182 AND 1193-1203.
    7. "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."
      Estaller C., Koistinen V., Schwaeble W., Dierich M.P., Weiss E.H.
      J. Immunol. 146:3190-3196(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1047-1231.
    8. "Purification and structural studies on the complement-system control protein beta 1H (Factor H)."
      Sim R.B., Discipio R.G.
      Biochem. J. 205:285-293(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-35.
    9. Vik D.P., Williams S.A.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
    10. Dominguez O.
      Thesis (1993), Hospital Trias I Pujol, Spain
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    11. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882.
      Tissue: Plasma.
    12. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529 AND ASN-911.
      Tissue: Plasma.
    13. "Site-specific N-glycan characterization of human complement factor H."
      Fenaille F., Le Mignon M., Groseil C., Ramon C., Riande S., Siret L., Bihoreau N.
      Glycobiology 17:932-944(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-529; ASN-718; ASN-802; ASN-822; ASN-882; ASN-911; ASN-1029 AND ASN-1095.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529; ASN-802; ASN-882; ASN-911 AND ASN-1029.
      Tissue: Liver.
    15. Cited for: GLYCOSYLATION AT ASN-217; ASN-882; ASN-911 AND ASN-1029.
    16. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    17. "Three-dimensional structure of a complement control protein module in solution."
      Norman D.G., Barlow P.N., Baron M., Day A.J., Sim B., Campbell I.D.
      J. Mol. Biol. 219:717-725(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 927-985 (SUSHI 16).
    18. "Solution structure of the fifth repeat of factor H: a second example of the complement control protein module."
      Barlow P.N., Norman D.G., Steinkasserer A., Horne T.J., Pearce J., Driscoll P.C., Sim B., Campbell I.D.
      Biochemistry 31:3626-3634(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 264-322 (SUSHI 5).
    19. "Solution structure of a pair of complement modules by nuclear magnetic resonance."
      Barlow P.N., Steinkasserer A., Norman D.G., Kieffer B., Wiles A.P., Sim B., Campbell I.D.
      J. Mol. Biol. 232:268-284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 866-985 (SUSHIS 15 AND 16).
    20. "Human factor H deficiency. Mutations in framework cysteine residues and block in H protein secretion and intracellular catabolism."
      Ault B.H., Schmidt B.Z., Fowler N.L., Kashtan C.E., Ahmed A.E., Vogt B.A., Colten H.R.
      J. Biol. Chem. 272:25168-25175(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFHD ARG-536 AND TYR-959.
    21. Cited for: VARIANT AHUS1 GLY-1215.
    22. "Complement factor H gene mutation associated with autosomal recessive atypical hemolytic uremic syndrome."
      Ying L., Katz Y., Schlesinger M., Carmi R., Shalev H., Haider N., Beck G., Sheffield V.C., Landau D.
      Am. J. Hum. Genet. 65:1538-1546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AHUS1 LEU-1191.
    23. "Complement factor H gene mutation associated with autosomal recessive atypical hemolytic uremic syndrome."
      Buddles M.R.H., Donne R.L., Richards A., Goodship J., Goodship T.H.J.
      Am. J. Hum. Genet. 66:1721-1722(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AHUS1 1225-TYR--ARG-1231 DELINS PHE-GLN-SER.
    24. "Molecular basis for factor H and FHL-1 deficiency in an Italian family."
      Sanchez-Corral P., Bellavia D., Amico L., Brai M., Rodriguez de Cordoba S.
      Immunogenetics 51:366-369(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CFHD.
    25. "Clustering of missense mutations in the C-terminal region of factor H in atypical hemolytic uremic syndrome."
      Perez-Caballero D., Gonzalez-Rubio C., Gallardo M.E., Vera M., Lopez-Trascasa M., Rodriguez de Cordoba S., Sanchez-Corral P.
      Am. J. Hum. Genet. 68:478-484(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFHD MET-956; LEU-1183; ARG-1189 AND ALA-1197.
    26. "Factor H mutations in hemolytic uremic syndrome cluster in exons 18-20, a domain important for host cell recognition."
      Richards A., Buddles M.R., Donne R.L., Kaplan B.S., Kirk E., Venning M.C., Tielemans C.L., Goodship J.A., Goodship T.H.J.
      Am. J. Hum. Genet. 68:485-490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFHD GLU-1076; GLY-1119 AND ARG-1184.
    27. "The molecular basis of familial hemolytic uremic syndrome: mutation analysis of factor H gene reveals a hot spot in short consensus repeat 20."
      Italian registry of familial and recurrent HUS/TTP
      Caprioli J., Bettinaglio P., Zipfel P.F., Amadei B., Daina E., Gamba S., Skerka C., Marziliano N., Remuzzi G., Noris M.
      J. Am. Soc. Nephrol. 12:297-307(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFHD CYS-1210 AND GLN-1215.
    28. "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."
      Perkins S.J., Goodship T.H.J.
      J. Mol. Biol. 316:217-224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHUS1 MET-956; GLU-1076; GLY-1119; LEU-1183; ARG-1184; ARG-1189; LEU-1191; ASP-1194; ALA-1197; CYS-1210; GLY-1215 AND GLN-1215.
    29. "Combined kidney and liver transplantation for familial haemolytic uraemic syndrome."
      Remuzzi G., Ruggenenti P., Codazzi D., Noris M., Caprioli J., Locatelli G., Gridelli B.
      Lancet 359:1671-1672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CFHD ARG-1183.
    30. "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."
      International registry of recurrent and familial HUS/TTP
      Caprioli J., Castelletti F., Bucchioni S., Bettinaglio P., Bresin E., Pianetti G., Gamba S., Brioschi S., Daina E., Remuzzi G., Noris M.
      Hum. Mol. Genet. 12:3385-3395(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHUS1 GLY-78; HIS-950; HIS-951; TRP-1163 AND ALA-1198, VARIANT ASP-936.
    31. "Haemolytic uraemic syndrome and mutations of the factor H gene: a registry-based study of German speaking countries."
      Neumann H.P.H., Salzmann M., Bohnert-Iwan B., Mannuelian T., Skerka C., Lenk D., Bender B.U., Cybulla M., Riegler P., Koenigsrainer A., Neyer U., Bock A., Widmer U., Male D.A., Franke G., Zipfel P.F.
      J. Med. Genet. 40:676-681(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AHUS1 TRP-630; LYS-850; CYS-978; PHE-1021; ARG-1043; GLY-1134; ASP-1142; ARG-1157; ARG-1183 AND SER-1226.
    32. "Heterozygous and homozygous factor H deficiencies associated with hemolytic uremic syndrome or membranoproliferative glomerulonephritis: report and genetic analysis of 16 cases."
      Dragon-Durey M.-A., Fremeaux-Bacchi V., Loirat C., Blouin J., Niaudet P., Deschenes G., Coppo P., Herman Fridman W., Weiss L.
      J. Am. Soc. Nephrol. 15:787-795(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CFHD LEU-127; SER-431 AND SER-673, VARIANTS AHUS1 LYS-400; TYR-673; ARG-893; SER-915; LEU-1183 AND SER-1199.
    33. "Strong association of the Y402H variant in complement factor H at 1q32 with susceptibility to age-related macular degeneration."
      Zareparsi S., Branham K.E.H., Li M., Shah S., Klein R.J., Ott J., Hoh J., Abecasis G.R., Swaroop A.
      Am. J. Hum. Genet. 77:149-153(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIS-402.
    34. Cited for: VARIANTS ILE-62 AND HIS-402, ASSOCIATION WITH ARMD.
    35. Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
    36. Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
    37. "Complement factor H polymorphism and age-related macular degeneration."
      Edwards A.O., Ritter R. III, Abel K.J., Manning A., Panhuysen C., Farrer L.A.
      Science 308:421-424(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
    38. "Deletion of Lys224 in regulatory domain 4 of factor H reveals a novel pathomechanism for dense deposit disease (MPGN II)."
      Licht C., Heinen S., Jozsi M., Loeschmann I., Saunders R.E., Perkins S.J., Waldherr R., Skerka C., Kirschfink M., Hoppe B., Zipfel P.F.
      Kidney Int. 70:42-50(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CFHD LYS-224 DEL, CHARACTERIZATION OF VARIANT CFHD LYS-224 DEL.
    39. Cited for: INVOLVEMENT IN BASAL LAMINAR DRUSEN, VARIANTS HIS-402; GLY-567; ASP-936; TYR-1050 AND SER-1078.
    40. "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 AHUS1 TYR-325; ILE-609; LEU-1169 AND CYS-1183, VARIANT ASP-936.
    41. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
      Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
      J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-62; LYS-850; TYR-959 AND GLU-1143, IDENTIFICATION BY MASS SPECTROMETRY.
    42. Cited for: VARIANT ARMD4 CYS-1210.

    Entry informationi

    Entry nameiCFAH_HUMAN
    AccessioniPrimary (citable) accession number: P08603
    Secondary accession number(s): A5PL14
    , P78435, Q14570, Q2TAZ5, Q38G77, Q5TFM3, Q8N708, Q9NU86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 184 of the entry and version 4 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

    Caution

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

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3