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P00751

- CFAB_HUMAN

UniProt

P00751 - CFAB_HUMAN

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Protein

Complement factor B

Gene

CFB

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

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei526 – 5261Charge relay system
Active sitei576 – 5761Charge relay system
Active sitei699 – 6991Charge relay system

GO - Molecular functioni

  1. complement binding Source: UniProtKB
  2. serine-type endopeptidase activity Source: Reactome

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, alternative pathway Source: UniProtKB
  3. innate immune response Source: Reactome
  4. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement alternate pathway, Immunity, Innate immunity

Enzyme and pathway databases

BRENDAi3.4.21.47. 2681.
ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_7972. Activation of C3 and C5.
REACT_8001. Alternative complement activation.

Protein family/group databases

MEROPSiS01.196.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:CFB
Synonyms:BF, BFD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:1037. CFB.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
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.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661S → P in AHUS4. 1 Publication
VAR_063659
Natural varianti203 – 2031R → Q in AHUS4. 1 Publication
VAR_063660
Natural varianti242 – 2421I → L in AHUS4. 1 Publication
VAR_063661
Natural varianti286 – 2861F → L in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. 1 Publication
VAR_063221
Natural varianti323 – 3231K → E in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. 1 Publication
VAR_063222
Natural varianti323 – 3231K → Q in AHUS4. 1 Publication
VAR_063662
Natural varianti458 – 4581M → I in AHUS4. 1 Publication
VAR_063663
Natural varianti533 – 5331K → R in AHUS4. 1 Publication
VAR_063664
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Hemolytic uremic syndrome

Organism-specific databases

MIMi603075. phenotype.
612924. phenotype.
615561. phenotype.
Orphaneti279. Age-related macular degeneration.
93578. Atypical hemolytic-uremic syndrome with B factor anomaly.
PharmGKBiPA25341.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 764739Complement factor BPRO_0000027545Add
BLAST
Chaini26 – 259234Complement factor B Ba fragmentPRO_0000027546Add
BLAST
Chaini260 – 764505Complement factor B Bb fragmentPRO_0000027547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 761 Publication
Disulfide bondi62 ↔ 981 Publication
Disulfide bondi103 ↔ 1451 Publication
Glycosylationi122 – 1221N-linked (GlcNAc...)4 Publications
Disulfide bondi131 ↔ 1581 Publication
Glycosylationi142 – 1421N-linked (GlcNAc...)3 Publications
Disulfide bondi165 ↔ 2051 Publication
Disulfide bondi191 ↔ 2181 Publication
Glycosylationi285 – 2851N-linked (GlcNAc...)4 Publications
Glycosylationi291 – 2911N-linked (Glc) (glycation)1 Publication
Glycosylationi378 – 3781N-linked (GlcNAc...)4 Publications
Disulfide bondi478 ↔ 5961 Publication
Disulfide bondi511 ↔ 5271 Publication
Disulfide bondi599 ↔ 6151 Publication
Disulfide bondi656 ↔ 6821 Publication
Disulfide bondi695 ↔ 7251 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycation, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP00751.
PaxDbiP00751.
PeptideAtlasiP00751.
PRIDEiP00751.

2D gel databases

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

PTM databases

PhosphoSiteiP00751.

Expressioni

Gene expression databases

BgeeiP00751.
CleanExiHS_CFB.
ExpressionAtlasiP00751. baseline and differential.
GenevestigatoriP00751.

Organism-specific databases

HPAiCAB016381.
HPA001817.
HPA001832.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi107098. 8 interactions.
DIPiDIP-38319N.
IntActiP00751. 4 interactions.
MINTiMINT-3003542.
STRINGi9606.ENSP00000388516.

Structurei

Secondary structure

1
764
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 515Combined sources
Helixi53 – 553Combined sources
Beta strandi56 – 616Combined sources
Beta strandi66 – 705Combined sources
Beta strandi72 – 765Combined sources
Beta strandi80 – 823Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 943Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi112 – 1154Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi195 – 1995Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi217 – 2193Combined sources
Helixi227 – 23812Combined sources
Helixi240 – 2434Combined sources
Beta strandi269 – 2768Combined sources
Turni279 – 2813Combined sources
Helixi283 – 30119Combined sources
Turni302 – 3043Combined sources
Beta strandi308 – 32215Combined sources
Beta strandi324 – 3263Combined sources
Helixi327 – 3304Combined sources
Helixi332 – 3409Combined sources
Helixi344 – 3463Combined sources
Beta strandi348 – 3503Combined sources
Helixi355 – 36612Combined sources
Beta strandi369 – 3724Combined sources
Helixi377 – 3793Combined sources
Beta strandi381 – 3888Combined sources
Beta strandi394 – 3963Combined sources
Helixi399 – 40810Combined sources
Beta strandi412 – 4143Combined sources
Helixi420 – 4223Combined sources
Beta strandi423 – 4297Combined sources
Beta strandi431 – 4333Combined sources
Helixi436 – 4427Combined sources
Beta strandi452 – 4543Combined sources
Beta strandi455 – 4573Combined sources
Helixi461 – 4688Combined sources
Helixi471 – 4744Combined sources
Helixi489 – 4924Combined sources
Beta strandi496 – 5016Combined sources
Turni504 – 5063Combined sources
Beta strandi509 – 5157Combined sources
Beta strandi517 – 5237Combined sources
Helixi525 – 5273Combined sources
Helixi534 – 5363Combined sources
Beta strandi537 – 5415Combined sources
Beta strandi548 – 5558Combined sources
Turni561 – 5644Combined sources
Helixi565 – 5673Combined sources
Beta strandi578 – 5847Combined sources
Beta strandi598 – 6003Combined sources
Helixi601 – 6066Combined sources
Helixi615 – 6228Combined sources
Beta strandi625 – 63814Combined sources
Beta strandi640 – 6489Combined sources
Helixi653 – 6586Combined sources
Helixi659 – 6624Combined sources
Helixi666 – 6683Combined sources
Helixi672 – 6743Combined sources
Beta strandi680 – 68910Combined sources
Helixi696 – 6983Combined sources
Beta strandi702 – 7076Combined sources
Beta strandi710 – 72112Combined sources
Helixi725 – 7273Combined sources
Turni728 – 7303Combined sources
Helixi735 – 7373Combined sources
Beta strandi739 – 7446Combined sources
Helixi745 – 7484Combined sources
Helixi749 – 7557Combined sources
Turni756 – 7583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00751.
SMRiP00751. Positions 35-764.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 10066Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini101 – 16060Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini163 – 22058Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini270 – 469200VWFAPROSITE-ProRule annotationAdd
BLAST
Domaini477 – 757281Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Domaini

The unliganded VWA domain has an inactive 'locked' conformation whereby the scissile Arg-259|Lys-260 bond is protected from proteolytic activation.1 Publication

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 3 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG304026.
GeneTreeiENSGT00530000063826.
HOVERGENiHBG002567.
InParanoidiP00751.
KOiK01335.
OMAiFMYDTPA.
PhylomeDBiP00751.
TreeFamiTF330194.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR011360. 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]
PfamiPF00084. Sushi. 3 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFiPIRSF001154. Compl_C2_B. 1 hit.
PIRSF500181. Complement_B. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEiPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00751-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR
60 70 80 90 100
LLQEGQALEY VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA
110 120 130 140 150
IHCPRPHDFE NGEYWPRSPY YNVSDEISFH CYDGYTLRGS ANRTCQVNGR
160 170 180 190 200
WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ YRLEDSVTYH CSRGLTLRGS
210 220 230 240 250
QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE TIEGVDAEDG
260 270 280 290 300
HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV
310 320 330 340 350
ASYGVKPRYG LVTYATYPKI WVKVSEADSS NADWVTKQLN EINYEDHKLK
360 370 380 390 400
SGTNTKKALQ AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT
410 420 430 440 450
VIDEIRDLLY IGKDRKNPRE DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ
460 470 480 490 500
HVFKVKDMEN LEDVFYQMID ESQSLSLCGM VWEHRKGTDY HKQPWQAKIS
510 520 530 540 550
VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS VGGEKRDLEI
560 570 580 590 600
EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT
610 620 630 640 650
EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG
660 670 680 690 700
DKKGSCERDA QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG
710 720 730 740 750
GPLIVHKRSR FIQVGVISWG VVDVCKNQKR QKQVPAHARD FHINLFQVLP
760
WLKEKLQDED LGFL
Length:764
Mass (Da):85,533
Last modified:October 1, 1994 - v2
Checksum:i8BB6C101CC6AC200
GO
Isoform 2 (identifier: P00751-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:621
Mass (Da):68,872
Checksum:i181713F2D4D9EC1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971I → T AA sequence (PubMed:6342610)Curated
Sequence conflicti300 – 3001V → L in AAA36225. (PubMed:6546754)Curated
Sequence conflicti328 – 3281D → V in AAA36225. (PubMed:6546754)Curated
Sequence conflicti356 – 3572KK → EE in AAA36225. (PubMed:6546754)Curated
Sequence conflicti537 – 5371I → T in AAA36219. (PubMed:6957884)Curated
Sequence conflicti764 – 7641L → H in AAA36220. (PubMed:6957884)Curated

Polymorphismi

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) [MIMi:603075]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91L → H.2 Publications
Corresponds to variant rs4151667 [ dbSNP | Ensembl ].
VAR_016274
Natural varianti28 – 281W → Q in allele FA; requires 2 nucleotide substitutions. 1 Publication
VAR_006493
Natural varianti28 – 281W → R in allele S. 4 Publications
VAR_006492
Natural varianti32 – 321R → Q in allele S. 6 Publications
Corresponds to variant rs641153 [ dbSNP | Ensembl ].
VAR_006494
Natural varianti32 – 321R → W.4 Publications
Corresponds to variant rs12614 [ dbSNP | Ensembl ].
VAR_016275
Natural varianti166 – 1661S → P in AHUS4. 1 Publication
VAR_063659
Natural varianti203 – 2031R → Q in AHUS4. 1 Publication
VAR_063660
Natural varianti242 – 2421I → L in AHUS4. 1 Publication
VAR_063661
Natural varianti252 – 2521G → S.1 Publication
Corresponds to variant rs4151651 [ dbSNP | Ensembl ].
VAR_016276
Natural varianti286 – 2861F → L in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. 1 Publication
VAR_063221
Natural varianti323 – 3231K → E in AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb. 1 Publication
VAR_063222
Natural varianti323 – 3231K → Q in AHUS4. 1 Publication
VAR_063662
Natural varianti458 – 4581M → I in AHUS4. 1 Publication
VAR_063663
Natural varianti533 – 5331K → R in AHUS4. 1 Publication
VAR_063664
Natural varianti565 – 5651K → E.2 Publications
Corresponds to variant rs4151659 [ dbSNP | Ensembl ].
VAR_016277
Natural varianti651 – 6511D → E.1 Publication
Corresponds to variant rs4151660 [ dbSNP | Ensembl ].
VAR_016278
Natural varianti736 – 7361A → S in allele FA. 1 Publication
VAR_006495

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei543 – 62179GEKRD…QQKEE → KDATEGPGLHLCSPGNTSHF LQILHSTHPQCSPIPCTPDQ SGMGEDVKLGMTRGQRQEAA HKEVVPTLLLQEGRSGTWR in isoform 2. 1 PublicationVSP_005380Add
BLAST
Alternative sequencei622 – 764143Missing in isoform 2. 1 PublicationVSP_005381Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4729.1. [P00751-1]
PIRiS34075. BBHU.
RefSeqiNP_001701.2. NM_001710.5. [P00751-1]
UniGeneiHs.69771.

Genome annotation databases

EnsembliENST00000399981; 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]
GeneIDi629.
KEGGihsa:629.
UCSCiuc003nyi.2. human. [P00751-2]
uc003nyj.4. human. [P00751-1]

Polymorphism databases

DMDMi584908.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4729.1. [P00751-1 ]
PIRi S34075. BBHU.
RefSeqi NP_001701.2. NM_001710.5. [P00751-1 ]
UniGenei Hs.69771.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P00751.
SMRi P00751. Positions 35-764.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107098. 8 interactions.
DIPi DIP-38319N.
IntActi P00751. 4 interactions.
MINTi MINT-3003542.
STRINGi 9606.ENSP00000388516.

Chemistry

BindingDBi P00751.
ChEMBLi CHEMBL5731.

Protein family/group databases

MEROPSi S01.196.

PTM databases

PhosphoSitei P00751.

Polymorphism databases

DMDMi 584908.

2D gel databases

DOSAC-COBS-2DPAGE P00751.
REPRODUCTION-2DPAGE P00751.
SWISS-2DPAGE P00751.

Proteomic databases

MaxQBi P00751.
PaxDbi P00751.
PeptideAtlasi P00751.
PRIDEi P00751.

Protocols and materials databases

DNASUi 629.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399981 ; 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 ]
GeneIDi 629.
KEGGi hsa:629.
UCSCi uc003nyi.2. human. [P00751-2 ]
uc003nyj.4. human. [P00751-1 ]

Organism-specific databases

CTDi 629.
GeneCardsi GC06P031931.
GC06Pj31900.
GC06Pk31895.
GC06Pm31989.
GC06Pn31885.
GC06Po31905.
GeneReviewsi CFB.
H-InvDB HIX0038706.
HGNCi HGNC:1037. CFB.
HPAi CAB016381.
HPA001817.
HPA001832.
MIMi 138470. gene.
603075. phenotype.
612924. phenotype.
615561. phenotype.
neXtProti NX_P00751.
Orphaneti 279. Age-related macular degeneration.
93578. Atypical hemolytic-uremic syndrome with B factor anomaly.
PharmGKBi PA25341.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304026.
GeneTreei ENSGT00530000063826.
HOVERGENi HBG002567.
InParanoidi P00751.
KOi K01335.
OMAi FMYDTPA.
PhylomeDBi P00751.
TreeFami TF330194.

Enzyme and pathway databases

BRENDAi 3.4.21.47. 2681.
Reactomei REACT_118707. Regulation of Complement cascade.
REACT_7972. Activation of C3 and C5.
REACT_8001. Alternative complement activation.

Miscellaneous databases

ChiTaRSi CFB. human.
EvolutionaryTracei P00751.
GeneWikii Complement_factor_B.
GenomeRNAii 629.
NextBioi 2546.
PROi P00751.
SOURCEi Search...

Gene expression databases

Bgeei P00751.
CleanExi HS_CFB.
ExpressionAtlasi P00751. baseline and differential.
Genevestigatori P00751.

Family and domain databases

Gene3Di 3.40.50.410. 1 hit.
InterProi IPR011360. 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 ]
Pfami PF00084. Sushi. 3 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view ]
PIRSFi PIRSF001154. Compl_C2_B. 1 hit.
PIRSF500181. Complement_B. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiCFAB_HUMAN
AccessioniPrimary (citable) accession number: P00751
Secondary accession number(s): B0QZQ6
, O15006, Q29944, Q53F89, Q5JP67, Q5ST50, Q96HX6, Q9BTF5, Q9BX92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 198 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3