Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08603

- CFAH_HUMAN

UniProt

P08603 - CFAH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Complement factor H

Gene

CFH

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

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

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
Complete GO annotation...

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
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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

BgeeiP08603.
ExpressionAtlasiP08603. baseline and differential.
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. 15 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

        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
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]
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 ]
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. 15 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

Bgeei P08603.
ExpressionAtlasi P08603. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 185 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