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P00751 (CFAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor B

EC=3.4.21.47
Alternative name(s):
C3/C5 convertase
Glycine-rich beta glycoprotein
Short name=GBG
PBF2
Properdin factor B
Gene names
Name:CFB
Synonyms:BF, BFD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.

Catalytic activity

Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.

Subunit structure

Monomer.

Subcellular location

Secreted.

Domain

The unliganded VWA domain has an inactive 'locked' conformation whereby the scissile Arg-259|Lys-260 bond is protected from proteolytic activation. Ref.23

Polymorphism

Two major variants, F and S, and 2 minor variants, as well as at least 14 very rare variants, have been identified. The variants His-9 and Gln-32 are associated with a reduced risk of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world.

Involvement in disease

Hemolytic uremic syndrome atypical 4 (AHUS4) [MIM:612924]: 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. Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. Ref.26 Ref.27

Complement factor B deficiency (CFBD) [MIM:615561]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 3 Sushi (CCP/SCR) domains.

Contains 1 VWFA domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00751-1)

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: P00751-2)

The sequence of this isoform differs from the canonical sequence as follows:
     543-621: GEKRDLEIEV...TTTCQQQKEE → KDATEGPGLH...LQEGRSGTWR
     622-764: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.12
Chain26 – 764739Complement factor B
PRO_0000027545
Chain26 – 259234Complement factor B Ba fragment
PRO_0000027546
Chain260 – 764505Complement factor B Bb fragment
PRO_0000027547

Regions

Domain35 – 10066Sushi 1
Domain101 – 16060Sushi 2
Domain163 – 22058Sushi 3
Domain270 – 469200VWFA
Domain477 – 757281Peptidase S1

Sites

Active site5261Charge relay system
Active site5761Charge relay system
Active site6991Charge relay system

Amino acid modifications

Glycosylation1221N-linked (GlcNAc...) Ref.12 Ref.19 Ref.20 Ref.23
Glycosylation1421N-linked (GlcNAc...) Ref.12 Ref.23 Ref.24
Glycosylation2851N-linked (GlcNAc...) Ref.12 Ref.19 Ref.20 Ref.23
Glycosylation2911N-linked (Glc) (glycation) Ref.12 Ref.18
Glycosylation3781N-linked (GlcNAc...) Ref.12 Ref.19 Ref.23 Ref.24
Disulfide bond37 ↔ 76 Ref.24
Disulfide bond62 ↔ 98 Ref.24
Disulfide bond103 ↔ 145 Ref.24
Disulfide bond131 ↔ 158 Ref.24
Disulfide bond165 ↔ 205 Ref.24
Disulfide bond191 ↔ 218 Ref.24
Disulfide bond478 ↔ 596 Ref.24
Disulfide bond511 ↔ 527 Ref.24
Disulfide bond599 ↔ 615 Ref.24
Disulfide bond656 ↔ 682 Ref.24
Disulfide bond695 ↔ 725 Ref.24

Natural variations

Alternative sequence543 – 62179GEKRD…QQKEE → KDATEGPGLHLCSPGNTSHF LQILHSTHPQCSPIPCTPDQ SGMGEDVKLGMTRGQRQEAA HKEVVPTLLLQEGRSGTWR in isoform 2.
VSP_005380
Alternative sequence622 – 764143Missing in isoform 2.
VSP_005381
Natural variant91L → H. Ref.7 Ref.25
Corresponds to variant rs4151667 [ dbSNP | Ensembl ].
VAR_016274
Natural variant281W → Q in allele FA; requires 2 nucleotide substitutions. Ref.1
VAR_006493
Natural variant281W → R in allele S. Ref.1 Ref.2 Ref.3 Ref.4
VAR_006492
Natural variant321R → Q in allele S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.25
Corresponds to variant rs641153 [ dbSNP | Ensembl ].
VAR_006494
Natural variant321R → W. Ref.7 Ref.8 Ref.10 Ref.11
Corresponds to variant rs12614 [ dbSNP | Ensembl ].
VAR_016275
Natural variant1661S → P in AHUS4. Ref.27
VAR_063659
Natural variant2031R → Q in AHUS4. Ref.27
VAR_063660
Natural variant2421I → L in AHUS4. Ref.27
VAR_063661
Natural variant2521G → S. Ref.7
Corresponds to variant rs4151651 [ dbSNP | Ensembl ].
VAR_016276
Natural variant2861F → L in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. Ref.26
VAR_063221
Natural variant3231K → E in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. Ref.26
VAR_063222
Natural variant3231K → Q in AHUS4. Ref.27
VAR_063662
Natural variant4581M → I in AHUS4. Ref.27
VAR_063663
Natural variant5331K → R in AHUS4. Ref.27
VAR_063664
Natural variant5651K → E. Ref.7 Ref.9
Corresponds to variant rs4151659 [ dbSNP | Ensembl ].
VAR_016277
Natural variant6511D → E. Ref.7
Corresponds to variant rs4151660 [ dbSNP | Ensembl ].
VAR_016278
Natural variant7361A → S in allele FA. Ref.1
VAR_006495

Experimental info

Sequence conflict2971I → T AA sequence Ref.13
Sequence conflict3001V → L in AAA36225. Ref.12
Sequence conflict3281D → V in AAA36225. Ref.12
Sequence conflict356 – 3572KK → EE in AAA36225. Ref.12
Sequence conflict5371I → T in AAA36219. Ref.15
Sequence conflict7641L → H in AAA36220. Ref.15

Secondary structure

........................................................................................................................................................ 764
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1994. Version 2.
Checksum: 8BB6C101CC6AC200

FASTA76485,533
        10         20         30         40         50         60 
MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY 

        70         80         90        100        110        120 
VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY 

       130        140        150        160        170        180 
YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ 

       190        200        210        220        230        240 
YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE 

       250        260        270        280        290        300 
TIEGVDAEDG HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV 

       310        320        330        340        350        360 
ASYGVKPRYG LVTYATYPKI WVKVSEADSS NADWVTKQLN EINYEDHKLK SGTNTKKALQ 

       370        380        390        400        410        420 
AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT VIDEIRDLLY IGKDRKNPRE 

       430        440        450        460        470        480 
DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ HVFKVKDMEN LEDVFYQMID ESQSLSLCGM 

       490        500        510        520        530        540 
VWEHRKGTDY HKQPWQAKIS VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS 

       550        560        570        580        590        600 
VGGEKRDLEI EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT 

       610        620        630        640        650        660 
EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG DKKGSCERDA 

       670        680        690        700        710        720 
QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG GPLIVHKRSR FIQVGVISWG 

       730        740        750        760 
VVDVCKNQKR QKQVPAHARD FHINLFQVLP WLKEKLQDED LGFL 

« Hide

Isoform 2 [UniParc].

Checksum: 181713F2D4D9EC1E
Show »

FASTA62168,872

References

« Hide 'large scale' references
[1]"Molecular characterization of human complement factor B subtypes."
Davrinche C., Abbal M., Clerc A.
Immunogenetics 32:309-312(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-28; GLN-28; GLN-32 AND SER-736.
[2]"Human factor B. Complete cDNA sequence of the BF*S allele."
Mejia J.E., Jahn I., de la Salle H., Hauptmann G.
Hum. Immunol. 39:49-53(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-28 AND GLN-32.
Tissue: Liver.
[3]"Human complement factor B: functional properties of a recombinant zymogen of the alternative activation pathway convertase."
Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H., Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.
Immunobiology 188:221-232(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-28 AND GLN-32.
Tissue: Liver.
[4]"Human complement factor B: cDNA cloning, nucleotide sequencing, phenotypic conversion by site-directed mutagenesis and expression."
Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S., Volanakis J.E.
Mol. Immunol. 30:1587-1592(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-28 AND GLN-32.
[5]"Expression and alternative splicing of human factor B gene in leukemic mononuclear cells."
Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U., Lokki M.-L.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[6]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]SeattleSNPs variation discovery resource
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-9; GLN-32; TRP-32; SER-252; GLU-565 AND GLU-651.
[8]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TRP-32.
[9]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-565.
[10]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-32.
[11]"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] (ISOFORM 1), VARIANT TRP-32.
Tissue: Colon.
[12]"Complete primary structure for the zymogen of human complement factor B."
Mole J.E., Anderson J.K., Davison E.A., Woods D.E.
J. Biol. Chem. 259:3407-3412(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-764, PARTIAL NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
[13]"Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment."
Christie D.L., Gagnon J.
Biochem. J. 209:61-70(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 260-764.
[14]"Molecular cloning and characterization of the gene coding for human complement protein factor B."
Campbell R.D., Porter R.R.
Proc. Natl. Acad. Sci. U.S.A. 80:4464-4468(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 339-764.
[15]"Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product."
Woods D.E., Markham A.F., Ricker A.T., Goldberger G., Colten H.R.
Proc. Natl. Acad. Sci. U.S.A. 79:5661-5665(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 467-595 AND 752-764.
[16]"Internal homologies of the Ba fragment from human complement component Factor B, a class III MHC antigen."
Morley B.J., Campbell R.D.
EMBO J. 3:153-157(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-259.
[17]"Cell-specific expression of the human complement protein factor B gene: evidence for the role of two distinct 5'-flanking elements."
Wu L.C., Morley B.J., Campbell R.D.
Cell 48:331-342(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
Tissue: Blood.
[18]"The principal site of glycation of human complement factor B."
Niemann M.A., Bhown A.S., Miller E.J.
Biochem. J. 274:473-480(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-291.
[19]"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-122; ASN-285 AND ASN-378.
Tissue: Plasma.
[20]"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-122 AND ASN-285.
Tissue: Liver.
[21]"Deficiency in complement factor B."
Slade C., Bosco J., Unglik G., Bleasel K., Nagel M., Winship I.
N. Engl. J. Med. 369:1667-1669(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CFBD.
[22]"New structural motifs on the chymotrypsin fold and their potential roles in complement factor B."
Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E., Narayana S.V.L.
EMBO J. 19:164-173(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 467-764.
[23]"Factor B structure provides insights into activation of the central protease of the complement system."
Milder F.J., Gomes L., Schouten A., Janssen B.J., Huizinga E.G., Romijn R.A., Hemrika W., Roos A., Daha M.R., Gros P.
Nat. Struct. Mol. Biol. 14:224-228(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-764, DOMAIN ARCHITECTURE, GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
[24]"Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex."
Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J., Fritzinger D.C., Vogel C.-W., Gros P.
EMBO J. 28:2469-2478(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-764 IN COMPLEX WITH COBRA VENOM FACTOR, GLYCOSYLATION AT ASN-142 AND ASN-378, DISULFIDE BONDS.
[25]"Variation in factor B (BF) and complement component 2 (C2) genes is associated with age-related macular degeneration."
Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K., Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T., Hageman G.S., Dean M., Allikmets R.
Nat. Genet. 38:458-462(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-9 AND GLN-32, INVOLVEMENT IN REDUCED RISK OF ARMD.
[26]"Gain-of-function mutations in complement factor B are associated with atypical hemolytic uremic syndrome."
Goicoechea de Jorge E., Harris C.L., Esparza-Gordillo J., Carreras L., Arranz E.A., Garrido C.A., Lopez-Trascasa M., Sanchez-Corral P., Morgan B.P., Rodriguez de Cordoba S.
Proc. Natl. Acad. Sci. U.S.A. 104:240-245(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AHUS4 LEU-286 AND GLU-323, CHARACTERIZATION OF VARIANTS AHUS4 LEU-286 AND GLU-323.
[27]"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 AHUS4 PRO-166; GLN-203; LEU-242; GLN-323; ILE-458 AND ARG-533.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72875 mRNA. Translation: CAA51389.1.
S67310 mRNA. Translation: AAD13989.1.
L15702 mRNA. Translation: AAA16820.1.
X00284 mRNA. Translation: CAA25077.1.
AF349679 mRNA. Translation: AAK30167.1.
AF019413 Genomic DNA. Translation: AAB67977.1.
AF551848 Genomic DNA. Translation: AAN71991.1.
AL844853 Genomic DNA. Translation: CAI41860.1.
AL662849 Genomic DNA. Translation: CAI17456.1.
BX005143 Genomic DNA. Translation: CAM25864.1.
CR759782 Genomic DNA. Translation: CAQ07113.1.
CR388219 Genomic DNA. Translation: CAQ07483.1.
AK223400 mRNA. Translation: BAD97120.1.
AL645922 Genomic DNA. Translation: CAQ09274.1.
CH471081 Genomic DNA. Translation: EAX03550.1.
BC004143 mRNA. Translation: AAH04143.1.
BC007990 mRNA. Translation: AAH07990.1.
K01566 mRNA. Translation: AAA36225.2.
J00125 Genomic DNA. No translation available.
J00126 mRNA. Translation: AAA36226.1.
J00185 mRNA. Translation: AAA36219.1. Sequence problems.
J00186 mRNA. Translation: AAA36220.1.
M15082 Genomic DNA. Translation: AAA59625.1.
CCDSCCDS4729.1. [P00751-1]
PIRBBHU. S34075.
RefSeqNP_001701.2. NM_001710.5. [P00751-1]
UniGeneHs.69771.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLEX-ray2.10A/B470-764[»]
1Q0PX-ray1.80A254-476[»]
1RRKX-ray2.00A268-764[»]
1RS0X-ray2.60A268-764[»]
1RTKX-ray2.30A268-764[»]
2OK5X-ray2.30A26-764[»]
2WINX-ray3.90I/J/K/L260-764[»]
2XWBX-ray3.49F/H35-764[»]
2XWJX-ray4.00I/J/K/L26-764[»]
3HRZX-ray2.20D26-764[»]
3HS0X-ray3.00D/I26-764[»]
ProteinModelPortalP00751.
SMRP00751. Positions 35-764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107098. 6 interactions.
DIPDIP-38319N.
IntActP00751. 4 interactions.
MINTMINT-3003542.
STRING9606.ENSP00000388516.

Chemistry

BindingDBP00751.
ChEMBLCHEMBL5731.

Protein family/group databases

MEROPSS01.196.

PTM databases

PhosphoSiteP00751.

Polymorphism databases

DMDM584908.

2D gel databases

DOSAC-COBS-2DPAGEP00751.
REPRODUCTION-2DPAGEP00751.
SWISS-2DPAGEP00751.

Proteomic databases

MaxQBP00751.
PaxDbP00751.
PeptideAtlasP00751.
PRIDEP00751.

Protocols and materials databases

DNASU629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399981; ENSP00000382862; ENSG00000241253.
ENST00000417261; ENSP00000414889; ENSG00000239754. [P00751-1]
ENST00000419411; ENSP00000391902; ENSG00000242335. [P00751-1]
ENST00000419920; ENSP00000411474; ENSG00000241253.
ENST00000424727; ENSP00000401719; ENSG00000243570. [P00751-1]
ENST00000425368; ENSP00000416561; ENSG00000243649. [P00751-1]
ENST00000426239; ENSP00000413351; ENSG00000242335. [P00751-1]
ENST00000427888; ENSP00000411515; ENSG00000239754. [P00751-1]
ENST00000433503; ENSP00000388352; ENSG00000241534. [P00751-1]
ENST00000436692; ENSP00000389604; ENSG00000243570. [P00751-1]
ENST00000455591; ENSP00000414341; ENSG00000241534. [P00751-1]
GeneID629.
KEGGhsa:629.
UCSCuc003nyi.2. human. [P00751-2]
uc003nyj.4. human. [P00751-1]

Organism-specific databases

CTD629.
GeneCardsGC06P031917.
GC06Pj31900.
GC06Pk31895.
GC06Pm31989.
GC06Pn31885.
GC06Po31905.
GeneReviewsCFB.
H-InvDBHIX0038706.
HGNCHGNC:1037. CFB.
HPACAB016381.
HPA001817.
HPA001832.
MIM138470. gene.
603075. phenotype.
612924. phenotype.
615561. phenotype.
neXtProtNX_P00751.
Orphanet279. Age-related macular degeneration.
93578. Atypical hemolytic uremic syndrome with B factor anomaly.
PharmGKBPA25341.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304026.
HOVERGENHBG002567.
InParanoidP00751.
KOK01335.
OMAFMYDTPA.
PhylomeDBP00751.
TreeFamTF330194.

Enzyme and pathway databases

BRENDA3.4.21.47. 2681.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP00751.
BgeeP00751.
CleanExHS_CFB.
GenevestigatorP00751.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR011360. Compl_C2_B.
IPR028341. Complement_B.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
IPR002035. VWF_A.
[Graphical view]
PfamPF00084. Sushi. 3 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF001154. Compl_C2_B. 1 hit.
PIRSF500181. Complement_B. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCFB. human.
EvolutionaryTraceP00751.
GeneWikiComplement_factor_B.
GenomeRNAi629.
NextBio2546.
PROP00751.
SOURCESearch...

Entry information

Entry nameCFAB_HUMAN
AccessionPrimary (citable) accession number: P00751
Secondary accession number(s): B0QZQ6 expand/collapse secondary AC list , O15006, Q29944, Q53F89, Q5JP67, Q5ST50, Q96HX6, Q9BTF5, Q9BX92
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 194 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

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 6

Human chromosome 6: entries, gene names and cross-references to MIM