P00751 (CFAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Cleaved into the following 2 chains:

1. Complement factor B Ba fragment
2. Complement factor B Bb fragment

Gene names

Name:	CFB
Synonyms:	BF, BFD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	764 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.22 Ref.23
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. Contains 3 Sushi (CCP/SCR) domains. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Complement alternate pathway Immunity Innate immunity
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hemolytic uremic syndrome
Domain	Repeat Signal Sushi
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycation Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, alternative pathway Non-traceable author statement Ref.3. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of complement activation Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	complement binding Traceable author statement PubMed 11367526. Source: UniProtKB serine-type endopeptidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.10

Chain

26 – 764

739

Complement factor B

PRO_0000027545

Chain

26 – 259

234

Complement factor B Ba fragment

PRO_0000027546

Chain

260 – 764

505

Complement factor B Bb fragment

PRO_0000027547

Regions

Domain

35 – 100

66

Sushi 1

Domain

101 – 160

60

Sushi 2

Domain

163 – 220

58

Sushi 3

Domain

270 – 469

200

VWFA

Domain

477 – 757

281

Peptidase S1

Sites

Active site

526

1

Charge relay system

Active site

576

1

Charge relay system

Active site

699

1

Charge relay system

Amino acid modifications

Glycosylation

122

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18

Glycosylation

142

1

N-linked (GlcNAc...) Ref.10 Ref.20

Glycosylation

285

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18

Glycosylation

291

1

N-linked (Glc) (glycation) Ref.10 Ref.16

Glycosylation

378

1

N-linked (GlcNAc...) Ref.10 Ref.17 Ref.20

Disulfide bond

37 ↔ 76

Ref.20

Disulfide bond

62 ↔ 98

Ref.20

Disulfide bond

103 ↔ 145

Ref.20

Disulfide bond

131 ↔ 158

Ref.20

Disulfide bond

165 ↔ 205

Ref.20

Disulfide bond

191 ↔ 218

Ref.20

Disulfide bond

478 ↔ 596

Ref.20

Disulfide bond

511 ↔ 527

Ref.20

Disulfide bond

599 ↔ 615

Ref.20

Disulfide bond

656 ↔ 682

Ref.20

Disulfide bond

695 ↔ 725

Ref.20

Natural variations

Alternative sequence

543 – 621

79

GEKRD…QQKEE → KDATEGPGLHLCSPGNTSHF LQILHSTHPQCSPIPCTPDQ SGMGEDVKLGMTRGQRQEAA HKEVVPTLLLQEGRSGTWR in isoform 2.

VSP_005380

Alternative sequence

622 – 764

143

Missing in isoform 2.

VSP_005381

Natural variant

9

1

L → H. Ref.7 Ref.21
Corresponds to variant rs4151667 [ dbSNP | Ensembl ].

VAR_016274

Natural variant

28

1

W → Q in allele FA; requires 2 nucleotide substitutions. Ref.1

VAR_006493

Natural variant

28

1

W → R in allele S. Ref.1 Ref.2 Ref.3 Ref.4

VAR_006492

Natural variant

32

1

R → Q in allele S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.21
Corresponds to variant rs641153 [ dbSNP | Ensembl ].

VAR_006494

Natural variant

32

1

R → W. Ref.7 Ref.9
Corresponds to variant rs12614 [ dbSNP | Ensembl ].

VAR_016275

Natural variant

166

1

S → P in AHUS4. Ref.23

VAR_063659

Natural variant

203

1

R → Q in AHUS4. Ref.23

VAR_063660

Natural variant

242

1

I → L in AHUS4. Ref.23

VAR_063661

Natural variant

252

1

G → S. Ref.7
Corresponds to variant rs4151651 [ dbSNP | Ensembl ].

VAR_016276

Natural variant

286

1

F → L in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. Ref.22

VAR_063221

Natural variant

323

1

K → E in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. Ref.22

VAR_063222

Natural variant

323

1

K → Q in AHUS4. Ref.23

VAR_063662

Natural variant

458

1

M → I in AHUS4. Ref.23

VAR_063663

Natural variant

533

1

K → R in AHUS4. Ref.23

VAR_063664

Natural variant

565

1

K → E. Ref.7 Ref.8
Corresponds to variant rs4151659 [ dbSNP | Ensembl ].

VAR_016277

Natural variant

651

1

D → E. Ref.7
Corresponds to variant rs4151660 [ dbSNP | Ensembl ].

VAR_016278

Natural variant

736

1

A → S in allele FA. Ref.1

VAR_006495

Experimental info

Sequence conflict

297

1

I → T AA sequence Ref.11

Sequence conflict

300

1

V → L in AAA36225. Ref.10

Sequence conflict

328

1

D → V in AAA36225. Ref.10

Sequence conflict

356 – 357

2

KK → EE in AAA36225. Ref.10

Sequence conflict

537

1

I → T in AAA36219. Ref.13

Sequence conflict

764

1

L → H in AAA36220. Ref.13

Secondary structure

1

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764

Helix Strand Turn

Details...

Beta strand

47 – 51

5

Helix

53 – 55

3

Beta strand

56 – 61

6

Beta strand

66 – 70

5

Beta strand

72 – 76

5

Beta strand

80 – 82

3

Beta strand

88 – 90

3

Beta strand

92 – 94

3

Beta strand

97 – 100

4

Beta strand

112 – 115

4

Beta strand

119 – 122

4

Beta strand

126 – 131

6

Beta strand

136 – 139

4

Beta strand

141 – 145

5

Beta strand

151 – 153

3

Beta strand

157 – 159

3

Beta strand

163 – 165

3

Beta strand

174 – 177

4

Beta strand

186 – 191

6

Beta strand

195 – 199

5

Beta strand

201 – 205

5

Beta strand

209 – 213

5

Beta strand

217 – 219

3

Helix

227 – 238

12

Helix

240 – 243

4

Beta strand

269 – 276

8

Turn

279 – 281

3

Helix

283 – 301

19

Turn

302 – 304

3

Beta strand

308 – 322

15

Beta strand

324 – 326

3

Helix

327 – 330

4

Helix

332 – 340

9

Helix

344 – 346

3

Beta strand

348 – 350

3

Helix

355 – 366

12

Beta strand

369 – 372

4

Helix

377 – 379

3

Beta strand

381 – 388

8

Beta strand

394 – 396

3

Helix

399 – 408

10

Beta strand

412 – 414

3

Helix

420 – 422

3

Beta strand

423 – 429

7

Beta strand

431 – 433

3

Helix

436 – 442

7

Beta strand

452 – 454

3

Beta strand

455 – 457

3

Helix

458 – 468

11

Helix

471 – 474

4

Helix

489 – 492

4

Beta strand

496 – 501

6

Turn

504 – 506

3

Beta strand

509 – 515

7

Beta strand

517 – 523

7

Helix

525 – 527

3

Helix

534 – 536

3

Beta strand

537 – 541

5

Beta strand

548 – 555

8

Turn

561 – 564

4

Helix

565 – 567

3

Beta strand

578 – 584

7

Beta strand

598 – 600

3

Helix

601 – 606

6

Helix

615 – 622

8

Beta strand

625 – 638

14

Beta strand

640 – 648

9

Helix

653 – 658

6

Helix

659 – 662

4

Helix

666 – 668

3

Helix

672 – 674

3

Beta strand

680 – 689

10

Helix

696 – 698

3

Beta strand

702 – 707

6

Beta strand

710 – 721

12

Helix

725 – 727

3

Turn

728 – 730

3

Helix

735 – 737

3

Beta strand

739 – 744

6

Helix

745 – 748

4

Helix

749 – 755

7

Turn

756 – 758

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 8BB6C101CC6AC200	FASTA	764	85,533
	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
	Isoform 2 [UniParc]. Checksum: 181713F2D4D9EC1E	FASTA	621	68,872
	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 VGKDATEGPG LHLCSPGNTS HFLQILHSTH PQCSPIPCTP DQSGMGEDVK LGMTRGQRQE 610 620 AAHKEVVPTL LLQEGRSGTW R

References

	« Hide 'large scale' referencesShow '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]	"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. , 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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"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, MASS SPECTROMETRY. Tissue: Liver.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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

GeneReviews

SeattleSNPs

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.
AL645922 Genomic DNA. Translation: CAQ09274.1.
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.

IPI

IPI00218508.
IPI00921523.

PIR

BBHU. S34075.

RefSeq

NP_001701.2. NM_001710.5.

UniGene

Hs.69771.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DLE	X-ray	2.10	A/B	470-764	[»]
1Q0P	X-ray	1.80	A	254-476	[»]
1RRK	X-ray	2.00	A	268-764	[»]
1RS0	X-ray	2.60	A	268-764	[»]
1RTK	X-ray	2.30	A	268-764	[»]
2OK5	X-ray	2.30	A	26-764	[»]
2WIN	X-ray	3.90	I/J/K/L	260-764	[»]
2XWB	X-ray	3.49	F/H	35-764	[»]
2XWJ	X-ray	4.00	I/J/K/L	26-764	[»]
3HRZ	X-ray	2.20	D	26-764	[»]
3HS0	X-ray	3.00	D/I	26-764	[»]

ProteinModelPortal

P00751.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38319N.

IntAct

P00751. 3 interactions.

STRING

9606.ENSP00000388516.

Protein family/group databases

MEROPS

S01.196.

PTM databases

PhosphoSite

P00751.

Polymorphism databases

DMDM

584908.

2D gel databases

DOSAC-COBS-2DPAGE

P00751.

REPRODUCTION-2DPAGE

P00751.

SWISS-2DPAGE

P00751.

Proteomic databases

PaxDb

P00751.

PeptideAtlas

P00751.

PRIDE

P00751.

Protocols and materials databases

DNASU

629.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399981; ENSP00000382862; ENSG00000241253.
ENST00000417261; ENSP00000414889; ENSG00000239754.
ENST00000419411; ENSP00000391902; ENSG00000242335.
ENST00000419920; ENSP00000411474; ENSG00000241253.
ENST00000424727; ENSP00000401719; ENSG00000243570.
ENST00000425368; ENSP00000416561; ENSG00000243649.
ENST00000426239; ENSP00000413351; ENSG00000242335.
ENST00000427888; ENSP00000411515; ENSG00000239754.
ENST00000433503; ENSP00000388352; ENSG00000241534.
ENST00000436692; ENSP00000389604; ENSG00000243570.
ENST00000455591; ENSP00000414341; ENSG00000241534.

GeneID

629.

KEGG

hsa:629.

UCSC

uc003nyi.2. human.
uc003nyj.4. human.

Organism-specific databases

CTD

629.

GeneCards

GC06P031917.

H-InvDB

HIX0038706.

HGNC

HGNC:1037. CFB.

HPA

CAB016381.
HPA001817.
HPA001832.

MIM

138470. gene.
603075. phenotype.
612924. phenotype.

neXtProt

NX_P00751.

Orphanet

279. Age-related macular degeneration.
93578. Atypical hemolytic uremic syndrome with B factor anomaly.

PharmGKB

PA25341.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304026.

HOVERGEN

HBG002567.

InParanoid

P00751.

KO

K01335.

OrthoDB

EOG4DV5KF.

PhylomeDB

P00751.

Enzyme and pathway databases

BRENDA

3.4.21.47. 2681.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P00751.

Bgee

P00751.

CleanEx

HS_CFB.

Genevestigator

P00751.

GermOnline

ENSG00000204359. Homo sapiens.

Family and domain databases

InterPro

IPR011360. Compl_C2_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]

Pfam

PF00084. Sushi. 3 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

PIRSF

PIRSF001154. Compl_C2_B. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 3 hits.
SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00751.

ChEMBL

CHEMBL5731.

ChiTaRS

CFB. human.

EvolutionaryTrace

P00751.

GenomeRNAi

629.

NextBio

2546.

SOURCE

Search...

Entry information

Entry name

CFAB_HUMAN

Accession

Primary (citable) accession number: P00751
Secondary accession number(s): B0QZQ6 , O15006, Q29944, Q5JP67, Q5ST50, Q96HX6, Q9BTF5, Q9BX92

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 181 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.