CFAB_HUMAN - dbPTM
CFAB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CFAB_HUMAN
UniProt AC P00751
Protein Name Complement factor B
Gene Name CFB
Organism Homo sapiens (Human).
Sequence Length 764
Subcellular Localization Secreted.
Protein Description 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..
Protein Sequence MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
20PhosphorylationPFILGLLSGGVTTTP
HHHHHHHHCCCCCCC		38.2524719451
24PhosphorylationGLLSGGVTTTPWSLA
HHHHCCCCCCCHHHC		28.3824719451
25O-linked_GlycosylationLLSGGVTTTPWSLAR
HHHCCCCCCCHHHCC		28.58OGP
25PhosphorylationLLSGGVTTTPWSLAR
HHHCCCCCCCHHHCC		28.5830624053
26O-linked_GlycosylationLSGGVTTTPWSLARP
HHCCCCCCCHHHCCC		17.25OGP
26PhosphorylationLSGGVTTTPWSLARP
HHCCCCCCCHHHCCC		17.2530624053
29PhosphorylationGVTTTPWSLARPQGS
CCCCCCHHHCCCCCC		17.2330624053
36PhosphorylationSLARPQGSCSLEGVE
HHCCCCCCCEEECEE		8.6924505115
38PhosphorylationARPQGSCSLEGVEIK
CCCCCCCEEECEEEC		31.0224505115
60PhosphorylationQEGQALEYVCPSGFY
ECCCEEEEECCCCCC		14.2725332170
64PhosphorylationALEYVCPSGFYPYPV
EEEEECCCCCCCCCC		36.0925332170
122N-linked_GlycosylationWPRSPYYNVSDEISF
CCCCCCCCCCCCEEE		22.4517310251
136PhosphorylationFHCYDGYTLRGSANR
EEEECCEEEECCCCC		18.6024719451
142N-linked_GlycosylationYTLRGSANRTCQVNG
EEEECCCCCEEEECC		41.3017310251
152PhosphorylationCQVNGRWSGQTAICD
EEECCEECCCEEECC		21.4722210691
155PhosphorylationNGRWSGQTAICDNGA
CCEECCCEEECCCCC		22.8622210691
174PhosphorylationNPGIPIGTRKVGSQY
CCCCCCCCEECCCEE		28.2122210691
179PhosphorylationIGTRKVGSQYRLEDS
CCCEECCCEEEECCC		27.33-
181PhosphorylationTRKVGSQYRLEDSVT
CEECCCEEEECCCEE		20.89-
278PhosphorylationIYLVLDGSDSIGASN
EEEEEECCCCCCCCC		28.05-
285N-linked_GlycosylationSDSIGASNFTGAKKC
CCCCCCCCCCCHHHH		37.6617310251
285N-linked_GlycosylationSDSIGASNFTGAKKC
CCCCCCCCCCCHHHH		37.6616335952
291GlycationSNFTGAKKCLVNLIE
CCCCCHHHHHHHHHH		32.06-
291N-linked_GlycosylationSNFTGAKKCLVNLIE
CCCCCHHHHHHHHHH		32.066546754
306UbiquitinationKVASYGVKPRYGLVT
HHHHCCCCCCCCEEE		21.29-
309PhosphorylationSYGVKPRYGLVTYAT
HCCCCCCCCEEEEEE		24.2826074081
313PhosphorylationKPRYGLVTYATYPKI
CCCCCEEEEEECCEE		16.6926074081
314PhosphorylationPRYGLVTYATYPKIW
CCCCEEEEEECCEEE		6.8926074081
316PhosphorylationYGLVTYATYPKIWVK
CCEEEEEECCEEEEE		29.9126074081
329PhosphorylationVKVSEADSSNADWVT
EEECHHCCCCHHHHH		32.3224505115
330PhosphorylationKVSEADSSNADWVTK
EECHHCCCCHHHHHH		36.2624505115
337UbiquitinationSNADWVTKQLNEINY
CCHHHHHHHHHHCCC		43.07-
351PhosphorylationYEDHKLKSGTNTKKA
CCCCCCCCCCCHHHH		62.3823403867
353PhosphorylationDHKLKSGTNTKKALQ
CCCCCCCCCHHHHHH		46.9723403867
355PhosphorylationKLKSGTNTKKALQAV
CCCCCCCHHHHHHHH		33.4923403867
378N-linked_GlycosylationDVPPEGWNRTRHVII
CCCCCCCCCCCEEEE		46.4317310251
380PhosphorylationPPEGWNRTRHVIILM
CCCCCCCCCEEEEEE		23.1624043423
388PhosphorylationRHVIILMTDGLHNMG
CEEEEEECCCHHHCC		24.3824043423
400PhosphorylationNMGGDPITVIDEIRD
HCCCCCEEHHHHHHH		19.4524043423
500PhosphorylationQPWQAKISVIRPSKG
CCCEEEEEEECCCCC		15.7024719451
588PhosphorylationKLKNKLKYGQTIRPI
EECCCCCCCCCCCCE		25.5425884760
629UbiquitinationLLPAQDIKALFVSEE
HCCHHHHHHHCCCHH		47.53-
634PhosphorylationDIKALFVSEEEKKLT
HHHHHCCCHHHHHCC		31.7726852163
652AcetylationVYIKNGDKKGSCERD
EEEECCCCCCCCHHH		61.5019811501
653AcetylationYIKNGDKKGSCERDA
EEECCCCCCCCHHHH		61.8819811509
655PhosphorylationKNGDKKGSCERDAQY
ECCCCCCCCHHHHCC		22.99-
673PhosphorylationYDKVKDISEVVTPRF
CCHHCCHHHCCCCCE		34.1829449344
677PhosphorylationKDISEVVTPRFLCTG
CCHHHCCCCCEEECC		17.5829449344
687PhosphorylationFLCTGGVSPYADPNT
EEECCCCCCCCCCCC		18.57-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CFAB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CFAB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CFAB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PROP_HUMANCFPphysical
10861231
RFA2_HUMANRPA2physical
21988832
LAMC3_HUMANLAMC3physical
21988832
NDKB_HUMANNME2physical
28514442
OAF_HUMANOAFphysical
28514442
RSPRY_HUMANRSPRY1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612924Hemolytic uremic syndrome atypical 4 (AHUS4)
615561Complement factor B deficiency (CFBD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CFAB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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).
Cited for: GLYCATION AT LYS-291.
"Complete primary structure for the zymogen of human complement factorB.";
Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
J. Biol. Chem. 259:3407-3412(1984).
Cited for: PROTEIN SEQUENCE OF 26-764, PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ANDGLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
"Insights into complement convertase formation based on the structureof 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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-764 IN COMPLEX WITH COBRAVENOM FACTOR, GLYCOSYLATION AT ASN-142 AND ASN-378, AND DISULFIDEBONDS.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122 AND ASN-285, AND MASSSPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-285 AND ASN-378,AND MASS SPECTROMETRY.

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