CFAH_HUMAN - dbPTM
CFAH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CFAH_HUMAN
UniProt AC P08603
Protein Name Complement factor H
Gene Name CFH
Organism Homo sapiens (Human).
Sequence Length 1231
Subcellular Localization Secreted.
Protein Description Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway..
Protein Sequence MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCSKSSIDIENGFISESQYTYALKEKAKYQCKLGYVTADGETSGSITCGKDGWSAQPTCIKSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPICYERECELPKIDVHLVPDRKKDQYKVGEVLKFSCKPGFTIVGPNSVQCYHFGLSPDLPICKEQVQSCGPPPELLNGNVKEKTKEEYGHSEVVEYYCNPRFLMKGPNKIQCVDGEWTTLPVCIVEESTCGDIPELEHGWAQLSSPPYYYGDSVEFNCSESFTMIGHRSITCIHGVWTQLPQCVAIDKLKKCKSSNLIILEEHLKNKKEFDHNSNIRYRCRGKEGWIHTVCINGRWDPEVNCSMAQIQLCPPPPQIPNSHNMTTTLNYRDGEKVSVLCQENYLIQEGEEITCKDGRWQSIPLCVEKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCIKTDCLSLPSFENAIPMGEKKDVYKAGEQVTYTCATYYKMDGASNVTCINSRWTGRPTCRDTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR
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
150PhosphorylationVVKCLPVTAPENGKI
EEEEEEEECCCCCEE		34.26-
159PhosphorylationPENGKIVSSAMEPDR
CCCCEEEECCCCCCC		18.8227130503
160PhosphorylationENGKIVSSAMEPDRE
CCCEEEECCCCCCCC		22.2727130503
193PhosphorylationGDEEMHCSDDGFWSK
CCCCEECCCCCCCCC		24.8627130503
199PhosphorylationCSDDGFWSKEKPKCV
CCCCCCCCCCCCCEE		28.7724505115
204AcetylationFWSKEKPKCVEISCK
CCCCCCCCEEEEEEC		63.087675159
217N-linked_GlycosylationCKSPDVINGSPISQK
ECCCCCCCCCCCCEE		44.7517623646
217N-linked_GlycosylationCKSPDVINGSPISQK
ECCCCCCCCCCCCEE		44.7518638581
219PhosphorylationSPDVINGSPISQKII
CCCCCCCCCCCEEEE		17.9925627689
266PhosphorylationLPSCEEKSCDNPYIP
CCCCCCCCCCCCCCC		29.9524505115
411PhosphorylationRKFVQGKSIDVACHP
CCCCCCCEEEEEECC		30.7423312004
427PhosphorylationYALPKAQTTVTCMEN
CCCCCCCEEEEECCC		28.2625072903
428PhosphorylationALPKAQTTVTCMENG
CCCCCCEEEEECCCC		11.1825072903
430PhosphorylationPKAQTTVTCMENGWS
CCCCEEEEECCCCCC		12.2125072903
437PhosphorylationTCMENGWSPTPRCIR
EECCCCCCCCCCEEE		21.9425072903
439PhosphorylationMENGWSPTPRCIRVK
CCCCCCCCCCEEEEE		20.1825072903
451PhosphorylationRVKTCSKSSIDIENG
EEEECCCCCEECCCC		19.07-
452PhosphorylationVKTCSKSSIDIENGF
EEECCCCCEECCCCE		28.19-
529N-linked_GlycosylationDFTWFKLNDTLDYEC
CCCEEECCCCCCEEE		40.592963625
583AcetylationVHLVPDRKKDQYKVG
EEECCCCCCCCCCHH		68.9918529005
587PhosphorylationPDRKKDQYKVGEVLK
CCCCCCCCCHHCEEE		20.13-
588AcetylationDRKKDQYKVGEVLKF
CCCCCCCCHHCEEEE		37.8218529011
718N-linked_GlycosylationYGDSVEFNCSESFTM
CCCCEEEECCCCEEE		18.2017591618
802N-linked_GlycosylationGRWDPEVNCSMAQIQ
CEECCCCCEEEEEEE		15.5217591618
822N-linked_GlycosylationPQIPNSHNMTTTLNY
CCCCCCCCCEEEEEC		29.3517591618
882N-linked_GlycosylationQIEHGTINSSRSSQE
CCCCCCCCCCCCCCC		33.5018638581
882N-linked_GlycosylationQIEHGTINSSRSSQE
CCCCCCCCCCCCCCC		33.5019838169
911N-linked_GlycosylationGFRISEENETTCYMG
CEEECCCCCCEEECC		48.1118638581
911N-linked_GlycosylationGFRISEENETTCYMG
CEEECCCCCCEEECC		48.1117623646
987PhosphorylationHPPSCIKTDCLSLPS
CCCCCCCCCCCCCCC		16.4222210691
991PhosphorylationCIKTDCLSLPSFENA
CCCCCCCCCCCCCCC		44.5622210691
994PhosphorylationTDCLSLPSFENAIPM
CCCCCCCCCCCCCCC		50.9522210691
1008PhosphorylationMGEKKDVYKAGEQVT
CCCCCCHHHCCCEEE		12.78-
1029N-linked_GlycosylationYKMDGASNVTCINSR
EECCCCCCEEEEECC		32.3617623646
1029N-linked_GlycosylationYKMDGASNVTCINSR
EECCCCCCEEEEECC		32.3618638581
1047PhosphorylationRPTCRDTSCVNPPTV
CCCCCCCCCCCCCCC		21.9824505115
1095N-linked_GlycosylationEVMCLNGNWTEPPQC
EEEEECCCCCCCCCC		41.2317591618
1170PhosphorylationCLHPCVISREIMENY
CCCCEEECHHHHHHC		11.9427130503
1190PhosphorylationWTAKQKLYSRTGESV
EEHHHHHHHCCCCCE		11.8026074081
1191PhosphorylationTAKQKLYSRTGESVE
EHHHHHHHCCCCCEE		33.5324719451
1193PhosphorylationKQKLYSRTGESVEFV
HHHHHHCCCCCEEEE		39.0826074081
1196PhosphorylationLYSRTGESVEFVCKR
HHHCCCCCEEEEECC		28.4324505115
1205PhosphorylationEFVCKRGYRLSSRSH
EEEECCCCCCCCCCE		16.6526074081
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 CFAH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CFAH_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
1205Phosphorylation1210 (5)R ⇒ Crs121913059
  • Advanced age-related macular degeneration
26691988
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO3_HUMANC3physical
9291131
EP300_HUMANEP300physical
21988832
SMAD3_HUMANSMAD3physical
21988832
VDR_HUMANVDRphysical
21988832
ZBT16_HUMANZBTB16physical
21988832
YTDC1_HUMANYTHDC1physical
21988832
KLH18_HUMANKLHL18physical
28514442
MUTA_HUMANMUTphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
126700Basal laminar drusen (BLD)
609814Complement factor H deficiency (CFHD)
235400Hemolytic uremic syndrome atypical 1 (AHUS1)
610698Macular degeneration, age-related, 4 (ARMD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CFAH_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"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-529; ASN-802; ASN-882;ASN-911 AND ASN-1029, AND MASS SPECTROMETRY.
"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-529 AND ASN-911, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882, AND MASSSPECTROMETRY.
"The complete amino acid sequence of human complement factor H.";
Ripoche J., Day A.J., Harris T.J.R., Sim R.B.;
Biochem. J. 249:593-602(1988).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), GLYCOSYLATION ATASN-529, AND VARIANTS HIS-402 AND ARG-493.

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