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P08603 (CFAH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor H
Alternative name(s):
H factor 1
Gene names
Name:CFH
Synonyms:HF, HF1, HF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Involvement in disease

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.
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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.32 Ref.38

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Ref.21 Ref.22 Ref.23 Ref.28 Ref.30 Ref.31 Ref.32 Ref.40

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.42

Sequence similarities

Contains 20 Sushi (CCP/SCR) domains.

Caution

According to a report, Asn-217 is not glycosylated (Ref.13). Another study observed glycosylation at this position (Ref.15).

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C3P010242EBI-1223708,EBI-6863106
ennXP169462EBI-1223708,EBI-6403567From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08603-1)

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.
Isoform 2 (identifier: P08603-2)

Also known as: FHL-1;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.8
Chain19 – 12311213Complement factor H
PRO_0000005894

Regions

Domain19 – 8264Sushi 1
Domain83 – 14361Sushi 2
Domain144 – 20764Sushi 3
Domain208 – 26457Sushi 4
Domain265 – 32258Sushi 5
Domain324 – 38663Sushi 6
Domain387 – 44458Sushi 7
Domain446 – 50762Sushi 8
Domain515 – 56652Sushi 9
Domain567 – 62559Sushi 10
Domain628 – 68659Sushi 11
Domain689 – 74658Sushi 12
Domain751 – 80555Sushi 13
Domain809 – 86658Sushi 14
Domain868 – 92861Sushi 15
Domain929 – 98658Sushi 16
Domain987 – 104559Sushi 17
Domain1046 – 110459Sushi 18
Domain1107 – 116559Sushi 19
Domain1170 – 123061Sushi 20

Amino acid modifications

Glycosylation2171N-linked (GlcNAc...) (complex) Ref.15
Glycosylation5291N-linked (GlcNAc...) Ref.1 Ref.12 Ref.13 Ref.14
Glycosylation7181N-linked (GlcNAc...) Ref.13
Glycosylation8021N-linked (GlcNAc...) Ref.13 Ref.14
Glycosylation8221N-linked (GlcNAc...) Ref.13
Glycosylation8821N-linked (GlcNAc...) (complex) Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Glycosylation9111N-linked (GlcNAc...) (complex) Ref.12 Ref.13 Ref.14 Ref.15
Glycosylation10291N-linked (GlcNAc...) (complex) Ref.13 Ref.14 Ref.15
Glycosylation10951N-linked (GlcNAc...) Ref.13
Disulfide bond21 ↔ 66 By similarity
Disulfide bond52 ↔ 80 By similarity
Disulfide bond85 ↔ 129 By similarity
Disulfide bond114 ↔ 141 By similarity
Disulfide bond146 ↔ 192 By similarity
Disulfide bond178 ↔ 205 By similarity
Disulfide bond210 ↔ 251 By similarity
Disulfide bond237 ↔ 262 By similarity
Disulfide bond267 ↔ 309 By similarity
Disulfide bond294 ↔ 320 By similarity
Disulfide bond325 ↔ 374 By similarity
Disulfide bond357 ↔ 385 By similarity
Disulfide bond389 ↔ 431 By similarity
Disulfide bond416 ↔ 442 By similarity
Disulfide bond448 ↔ 494 By similarity
Disulfide bond477 ↔ 505 By similarity
Disulfide bond509 ↔ 553 By similarity
Disulfide bond536 ↔ 564 By similarity
Disulfide bond569 ↔ 611 By similarity
Disulfide bond597 ↔ 623 By similarity
Disulfide bond630 ↔ 673 By similarity
Disulfide bond659 ↔ 684 By similarity
Disulfide bond691 ↔ 733 By similarity
Disulfide bond719 ↔ 744 By similarity
Disulfide bond753 ↔ 792 By similarity
Disulfide bond781 ↔ 803 By similarity
Disulfide bond811 ↔ 853 By similarity
Disulfide bond839 ↔ 864 By similarity
Disulfide bond870 ↔ 915 By similarity
Disulfide bond901 ↔ 926 By similarity
Disulfide bond931 ↔ 973 By similarity
Disulfide bond959 ↔ 984 By similarity
Disulfide bond989 ↔ 1032 By similarity
Disulfide bond1018 ↔ 1043 By similarity
Disulfide bond1048 ↔ 1091 By similarity
Disulfide bond1077 ↔ 1102 By similarity
Disulfide bond1109 ↔ 1152 By similarity
Disulfide bond1138 ↔ 1163 By similarity
Disulfide bond1167 ↔ 1218 By similarity
Disulfide bond1201 ↔ 1228 By similarity

Natural variations

Alternative sequence446 – 4494KTCS → SFTL in isoform 2.
VSP_001190
Alternative sequence450 – 1231782Missing in isoform 2.
VSP_001191
Natural variant621V → I Polymorphism confirmed at protein level. Ref.2 Ref.4 Ref.34 Ref.41
Corresponds to variant rs800292 [ dbSNP | Ensembl ].
VAR_023836
Natural variant781R → G in AHUS1. Ref.30
VAR_025864
Natural variant1271R → L in CFHD; with membranoproliferative glomerulonephritis. Ref.32
VAR_031978
Natural variant2241Missing in CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation. Ref.38
VAR_031979
Natural variant3251C → Y in AHUS1. Ref.40
VAR_063648
Natural variant4001Q → K in AHUS1. Ref.32
VAR_031980
Natural variant4021Y → H Polymorphism associated with ARMD4. Ref.1 Ref.3 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39
Corresponds to variant rs1061170 [ dbSNP | Ensembl ].
VAR_001979
Natural variant4311C → S in CFHD; with membranoproliferative glomerulonephritis. Ref.32
VAR_031981
Natural variant4931T → R. Ref.1
Corresponds to variant rs1061171 [ dbSNP | Ensembl ].
VAR_043892
Natural variant5361C → R in CFHD. Ref.20
VAR_019405
Natural variant5511I → T. Ref.2
Corresponds to variant rs35453854 [ dbSNP | Ensembl ].
VAR_025092
Natural variant5671R → G Associated with basal laminar drusen. Ref.39
VAR_043893
Natural variant6091V → I in AHUS1. Ref.40
VAR_063649
Natural variant6301C → W in AHUS1. Ref.31
VAR_025865
Natural variant6731C → S in CFHD; with membranoproliferative glomerulonephritis. Ref.32
VAR_031982
Natural variant6731C → Y in AHUS1. Ref.32
VAR_031983
Natural variant8501E → K in AHUS1; variant confirmed at protein level. Ref.31 Ref.41
VAR_025866
Natural variant8901S → I. Ref.2
Corresponds to variant rs515299 [ dbSNP | Ensembl ].
VAR_025093
Natural variant8931H → R in AHUS1. Ref.32
VAR_031984
Natural variant9151C → S in AHUS1. Ref.32
VAR_031985
Natural variant9361E → D Polymorphism associated with hemolytic uremic syndrome and basal laminar drusen. Ref.2 Ref.30 Ref.39 Ref.40
Corresponds to variant rs1065489 [ dbSNP | Ensembl ].
VAR_020261
Natural variant9501Q → H in AHUS1. Ref.30
Corresponds to variant rs149474608 [ dbSNP | Ensembl ].
VAR_025867
Natural variant9511Y → H in AHUS1. Ref.30
VAR_025868
Natural variant9561T → M in AHUS1. Ref.25 Ref.28
Corresponds to variant rs145975787 [ dbSNP | Ensembl ].
VAR_025869
Natural variant9591C → Y in CFHD; variant confirmed at protein level. Ref.20 Ref.41
VAR_019406
Natural variant9781W → C in AHUS1. Ref.31
VAR_025870
Natural variant9971N → T.
Corresponds to variant rs17575212 [ dbSNP | Ensembl ].
VAR_055683
Natural variant10071V → I. Ref.2
VAR_025094
Natural variant10071V → L.
Corresponds to variant rs534399 [ dbSNP | Ensembl ].
VAR_043894
Natural variant10101A → T.
Corresponds to variant rs11539862 [ dbSNP | Ensembl ].
VAR_055684
Natural variant10171T → I. Ref.2
Corresponds to variant rs34362004 [ dbSNP | Ensembl ].
VAR_025095
Natural variant10211Y → F in AHUS1. Ref.31
VAR_025871
Natural variant10431C → R in AHUS1. Ref.31
VAR_025872
Natural variant10501N → Y Polymorphism associated with basal laminar drusen. Ref.2 Ref.39
Corresponds to variant rs35274867 [ dbSNP | Ensembl ].
VAR_025096
Natural variant10591I → T. Ref.2
Corresponds to variant rs35343172 [ dbSNP | Ensembl ].
VAR_025097
Natural variant10761Q → E in CFHD. Ref.26 Ref.28
VAR_025873
Natural variant10781R → S Associated with basal laminar drusen. Ref.39
VAR_043895
Natural variant11191D → G in CFHD. Ref.26 Ref.28
VAR_025874
Natural variant11341V → G in AHUS1. Ref.31
VAR_025875
Natural variant11421Y → D in AHUS1. Ref.31
VAR_025876
Natural variant11431Q → E Polymorphism confirmed at protein level. Ref.41
Corresponds to variant rs34247141 [ dbSNP | Ensembl ].
VAR_043896
Natural variant11571W → R in AHUS1. Ref.31
VAR_025877
Natural variant11631C → W in AHUS1. Ref.30
VAR_025878
Natural variant11691I → L in AHUS1. Ref.40
VAR_063650
Natural variant11831W → C in AHUS1. Ref.40
VAR_063651
Natural variant11831W → L in AHUS1. Ref.25 Ref.28 Ref.32
VAR_025879
Natural variant11831W → R in AHUS1. Ref.29 Ref.31
VAR_025880
Natural variant11841T → R in CFHD. Ref.26 Ref.28
VAR_025881
Natural variant11891L → R in AHUS1. Ref.25 Ref.28
VAR_019407
Natural variant11911S → L in AHUS1. Ref.22 Ref.28
Corresponds to variant rs460897 [ dbSNP | Ensembl ].
VAR_019408
Natural variant11941G → D in AHUS1. Ref.28
VAR_025882
Natural variant11971V → A in AHUS1. Ref.25 Ref.28
Corresponds to variant rs460184 [ dbSNP | Ensembl ].
VAR_025883
Natural variant11981E → A in AHUS1. Ref.30
VAR_025884
Natural variant11991F → S in AHUS1. Ref.32
VAR_031986
Natural variant12101R → C in CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration. Ref.27 Ref.28 Ref.42
VAR_025885
Natural variant12151R → G in AHUS1. Ref.21 Ref.28
VAR_025886
Natural variant12151R → Q in CFHD. Ref.27 Ref.28
VAR_025887
Natural variant1225 – 12317YPTCAKR → FQS in AHUS1.
VAR_019409
Natural variant12261P → S in AHUS1; atypical. Ref.31
VAR_025888

Experimental info

Sequence conflict211C → Q AA sequence Ref.8
Sequence conflict301T → V AA sequence Ref.8
Sequence conflict341T → Q AA sequence Ref.8
Sequence conflict53 – 542RP → IL in CAB41739. Ref.5

Secondary structure

.............................................................................................................................................................................................................. 1231
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 11, 2007. Version 4.
Checksum: 3C26D62A2BF9BFEE

FASTA1,231139,096
        10         20         30         40         50         60 
MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY KCRPGYRSLG 

        70         80         90        100        110        120 
NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG GNVFEYGVKA VYTCNEGYQL 

       130        140        150        160        170        180 
LGEINYRECD TDGWTNDIPI CEVVKCLPVT APENGKIVSS AMEPDREYHF GQAVRFVCNS 

       190        200        210        220        230        240 
GYKIEGDEEM HCSDDGFWSK EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG 

       250        260        270        280        290        300 
YEYSERGDAV CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP 

       310        320        330        340        350        360 
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG KYYSYYCDEH 

       370        380        390        400        410        420 
FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ NYGRKFVQGK SIDVACHPGY 

       430        440        450        460        470        480 
ALPKAQTTVT CMENGWSPTP RCIRVKTCSK SSIDIENGFI SESQYTYALK EKAKYQCKLG 

       490        500        510        520        530        540 
YVTADGETSG SITCGKDGWS AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY 

       550        560        570        580        590        600 
ESNTGSTTGS IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG 

       610        620        630        640        650        660 
FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG HSEVVEYYCN 

       670        680        690        700        710        720 
PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG WAQLSSPPYY YGDSVEFNCS 

       730        740        750        760        770        780 
ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL KKCKSSNLII LEEHLKNKKE FDHNSNIRYR 

       790        800        810        820        830        840 
CRGKEGWIHT VCINGRWDPE VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ 

       850        860        870        880        890        900 
ENYLIQEGEE ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT 

       910        920        930        940        950        960 
CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ YGEEVTYKCF 

       970        980        990       1000       1010       1020 
EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP MGEKKDVYKA GEQVTYTCAT 

      1030       1040       1050       1060       1070       1080 
YYKMDGASNV TCINSRWTGR PTCRDTSCVN PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP 

      1090       1100       1110       1120       1130       1140 
YEMFGDEEVM CLNGNWTEPP QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN 

      1150       1160       1170       1180       1190       1200 
LYQLEGNKRI TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV 

      1210       1220       1230 
CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R 

« Hide

Isoform 2 (FHL-1) [UniParc].

Checksum: C2AAD47F155343E3
Show »

FASTA44951,034

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
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]"Genetic studies into inherited and sporadic hemolytic uremic syndrome."
Warwicker P., Goodship T.H.J., Donne R.L., Pirson Y., Nicholls A., Ward R.M., Turnpenny P., Goodship J.A.
Kidney Int. 53:836-844(1998) [PubMed] [Europe PMC] [Abstract]
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]"A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration."
Hageman G.S., Anderson D.H., Johnson L.V., Hancox L.S., Taiber A.J., Hardisty L.I., Hageman J.L., Stockman H.A., Borchardt J.D., Gehrs K.M., Smith R.J.H., Silvestri G., Russell S.R., Klaver C.C.W., Barbazetto I., Chang S., Yannuzzi L.A., Barile G.R. expand/collapse author list , Merriam J.C., Smith R.T., Olsh A.K., Bergeron J., Zernant J., Merriam J.E., Gold B., Dean M., Allikmets R.
Proc. Natl. Acad. Sci. U.S.A. 102:7227-7232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-62 AND HIS-402, ASSOCIATION WITH ARMD.
[35]"Complement factor H polymorphism in age-related macular degeneration."
Klein R.J., Zeiss C., Chew E.Y., Tsai J.-Y., Sackler R.S., Haynes C., Henning A.K., SanGiovanni J.P., Mane S.M., Mayne S.T., Bracken M.B., Ferris F.L., Ott J., Barnstable C., Hoh J.
Science 308:385-389(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
[36]"Complement factor H variant increases the risk of age-related macular degeneration."
Haines J.L., Hauser M.A., Schmidt S., Scott W.K., Olson L.M., Gallins P., Spencer K.L., Kwan S.Y., Noureddine M., Gilbert J.R., Schnetz-Boutaud N., Agarwal A., Postel E.A., Pericak-Vance M.A.
Science 308:419-421(2005) [PubMed] [Europe PMC] [Abstract]
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]"Basal laminar drusen caused by compound heterozygous variants in the CFH gene."
Boon C.J.F., Klevering B.J., Hoyng C.B., Zonneveld-Vrieling M.N., Nabuurs S.B., Blokland E., Cremers F.P.M., den Hollander A.I.
Am. J. Hum. Genet. 82:516-523(2008) [PubMed] [Europe PMC] [Abstract]
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]"A rare penetrant mutation in CFH confers high risk of age-related macular degeneration."
Raychaudhuri S., Iartchouk O., Chin K., Tan P.L., Tai A.K., Ripke S., Gowrisankar S., Vemuri S., Montgomery K., Yu Y., Reynolds R., Zack D.J., Campochiaro B., Campochiaro P., Katsanis N., Daly M.J., Seddon J.M.
Nat. Genet. 43:1232-1236(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARMD4 CYS-1210.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRNBHUH. S00254.
NBHUHS. S03013.
RefSeqNP_000177.2. NM_000186.3.
UniGeneHs.363396.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP08603.
SMRP08603. Positions 20-1230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109324. 14 interactions.
DIPDIP-38303N.
IntActP08603. 12 interactions.

Chemistry

BindingDBP08603.
ChEMBLCHEMBL4629.

PTM databases

PhosphoSiteP08603.

Polymorphism databases

DMDM158517847.

Proteomic databases

PaxDbP08603.
PRIDEP08603.

Protocols and materials databases

DNASU3075.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367429; ENSP00000356399; ENSG00000000971.
GeneID3075.
KEGGhsa:3075.
UCSCuc001gtj.4. human. [P08603-1]

Organism-specific databases

CTD3075.
GeneCardsGC01P196621.
HGNCHGNC:4883. CFH.
HPACAB016385.
CAB016769.
HPA038922.
HPA049176.
MIM126700. phenotype.
134370. gene.
235400. phenotype.
609814. phenotype.
610698. phenotype.
neXtProtNX_P08603.
Orphanet279. 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.
PharmGKBPA29261.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148800.
HOVERGENHBG005665.
InParanoidP08603.
KOK04004.
OrthoDBEOG75XGK1.
PhylomeDBP08603.
TreeFamTF326157.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP08603.
BgeeP08603.
GenevestigatorP08603.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 19 hits.
[Graphical view]
SMARTSM00032. CCP. 20 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 18 hits.
PROSITEPS50923. SUSHI. 19 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCFH. human.
EvolutionaryTraceP08603.
GeneWikiFactor_H.
GenomeRNAi3075.
NextBio12163.
PROP08603.
SOURCESearch...

Entry information

Entry nameCFAH_HUMAN
AccessionPrimary (citable) accession number: P08603
Secondary accession number(s): A5PL14 expand/collapse secondary AC list , P78435, Q14570, Q2TAZ5, Q38G77, Q5TFM3, Q8N708, Q9NU86
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 179 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM