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P00751

- CFAB_HUMAN

UniProt

P00751 - CFAB_HUMAN

Protein

Complement factor B

Gene

CFB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 196 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    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

    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

    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: UniProt
    5. plasma membrane Source: Reactome

    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

    ArrayExpressiP00751.
    BgeeiP00751.
    CleanExiHS_CFB.
    GenevestigatoriP00751.

    Organism-specific databases

    HPAiCAB016381.
    HPA001817.
    HPA001832.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi107098. 6 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 – 515
    Helixi53 – 553
    Beta strandi56 – 616
    Beta strandi66 – 705
    Beta strandi72 – 765
    Beta strandi80 – 823
    Beta strandi88 – 903
    Beta strandi92 – 943
    Beta strandi97 – 1004
    Beta strandi112 – 1154
    Beta strandi119 – 1224
    Beta strandi126 – 1316
    Beta strandi136 – 1394
    Beta strandi141 – 1455
    Beta strandi151 – 1533
    Beta strandi157 – 1593
    Beta strandi163 – 1653
    Beta strandi174 – 1774
    Beta strandi186 – 1916
    Beta strandi195 – 1995
    Beta strandi201 – 2055
    Beta strandi209 – 2135
    Beta strandi217 – 2193
    Helixi227 – 23812
    Helixi240 – 2434
    Beta strandi269 – 2768
    Turni279 – 2813
    Helixi283 – 30119
    Turni302 – 3043
    Beta strandi308 – 32215
    Beta strandi324 – 3263
    Helixi327 – 3304
    Helixi332 – 3409
    Helixi344 – 3463
    Beta strandi348 – 3503
    Helixi355 – 36612
    Beta strandi369 – 3724
    Helixi377 – 3793
    Beta strandi381 – 3888
    Beta strandi394 – 3963
    Helixi399 – 40810
    Beta strandi412 – 4143
    Helixi420 – 4223
    Beta strandi423 – 4297
    Beta strandi431 – 4333
    Helixi436 – 4427
    Beta strandi452 – 4543
    Beta strandi455 – 4573
    Helixi461 – 4688
    Helixi471 – 4744
    Helixi489 – 4924
    Beta strandi496 – 5016
    Turni504 – 5063
    Beta strandi509 – 5157
    Beta strandi517 – 5237
    Helixi525 – 5273
    Helixi534 – 5363
    Beta strandi537 – 5415
    Beta strandi548 – 5558
    Turni561 – 5644
    Helixi565 – 5673
    Beta strandi578 – 5847
    Beta strandi598 – 6003
    Helixi601 – 6066
    Helixi615 – 6228
    Beta strandi625 – 63814
    Beta strandi640 – 6489
    Helixi653 – 6586
    Helixi659 – 6624
    Helixi666 – 6683
    Helixi672 – 6743
    Beta strandi680 – 68910
    Helixi696 – 6983
    Beta strandi702 – 7076
    Beta strandi710 – 72112
    Helixi725 – 7273
    Turni728 – 7303
    Helixi735 – 7373
    Beta strandi739 – 7446
    Helixi745 – 7484
    Helixi749 – 7557
    Turni756 – 7583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR    50
    LLQEGQALEY VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA 100
    IHCPRPHDFE NGEYWPRSPY YNVSDEISFH CYDGYTLRGS ANRTCQVNGR 150
    WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ YRLEDSVTYH CSRGLTLRGS 200
    QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE TIEGVDAEDG 250
    HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV 300
    ASYGVKPRYG LVTYATYPKI WVKVSEADSS NADWVTKQLN EINYEDHKLK 350
    SGTNTKKALQ AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT 400
    VIDEIRDLLY IGKDRKNPRE DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ 450
    HVFKVKDMEN LEDVFYQMID ESQSLSLCGM VWEHRKGTDY HKQPWQAKIS 500
    VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS VGGEKRDLEI 550
    EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT 600
    EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG 650
    DKKGSCERDA QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG 700
    GPLIVHKRSR FIQVGVISWG VVDVCKNQKR QKQVPAHARD FHINLFQVLP 750
    WLKEKLQDED LGFL 764
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 6 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 GC06P031917.
    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.
    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

    ArrayExpressi P00751.
    Bgeei P00751.
    CleanExi HS_CFB.
    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

    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: October 1, 2014
    This is version 196 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