DAF_HUMAN - dbPTM
DAF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAF_HUMAN
UniProt AC P08174
Protein Name Complement decay-accelerating factor
Gene Name CD55
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cell membrane
Lipid-anchor, GPI-anchor.
Isoform 3: Secreted .
Isoform 4: Secreted .
Isoform 5: Secreted .
Isoform 6: Cell membrane
Lipid-anchor, GPI-anchor .
Isoform 7: Cel
Protein Description This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. [PubMed: 7525274 Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage]
Protein Sequence MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT
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
64UbiquitinationEDTVITYKCEESFVK
CCCEEEEECCCCEEE		26.90-
71UbiquitinationKCEESFVKIPGEKDS
ECCCCEEECCCCCCE		40.97-
76UbiquitinationFVKIPGEKDSVICLK
EEECCCCCCEEEEEE		62.31-
95N-linked_GlycosylationSDIEEFCNRSCEVPT
HHHHHHHCCCCCCCC		44.1917660510
110UbiquitinationRLNSASLKQPYITQN
CCCCCCCCCCEECCC		46.89-
138PhosphorylationPGYRREPSLSPKLTC
CCCCCCCCCCCCEEH		36.4024719451
140PhosphorylationYRREPSLSPKLTCLQ
CCCCCCCCCCEEHHH		25.0720068231
142AcetylationREPSLSPKLTCLQNL
CCCCCCCCEEHHHHC		53.7226051181
142UbiquitinationREPSLSPKLTCLQNL
CCCCCCCCEEHHHHC		53.72-
159AcetylationSTAVEFCKKKSCPNP
HHHHHHHHHCCCCCC		69.4326051181
161SuccinylationAVEFCKKKSCPNPGE
HHHHHHHCCCCCCCC		42.6727452117
162PhosphorylationVEFCKKKSCPNPGEI
HHHHHHCCCCCCCCC		43.62-
245PhosphorylationGERDHYGYRQSVTYA
CCCCCCCCCHHHEEE		9.79-
251PhosphorylationGYRQSVTYACNKGFT
CCCHHHEEEECCCEE		13.65-
266PhosphorylationMIGEHSIYCTVNNDE
EEEECEEEEEEECCC		5.77-
290PhosphorylationCRGKSLTSKVPPTVQ
CCCCCCCCCCCCCCC		36.6329116813
291UbiquitinationRGKSLTSKVPPTVQK
CCCCCCCCCCCCCCC		54.23-
295PhosphorylationLTSKVPPTVQKPTTV
CCCCCCCCCCCCCEE		29.5129116813
298UbiquitinationKVPPTVQKPTTVNVP
CCCCCCCCCCEEECC		39.74-
300PhosphorylationPPTVQKPTTVNVPTT
CCCCCCCCEEECCCC		50.8722210691
301PhosphorylationPTVQKPTTVNVPTTE
CCCCCCCEEECCCCE		20.7129116813
306O-linked_GlycosylationPTTVNVPTTEVSPTS
CCEEECCCCEECCCC		31.16OGP
306PhosphorylationPTTVNVPTTEVSPTS
CCEEECCCCEECCCC		31.1625627689
307O-linked_GlycosylationTTVNVPTTEVSPTSQ
CEEECCCCEECCCCC		28.46OGP
310PhosphorylationNVPTTEVSPTSQKTT
ECCCCEECCCCCCEE		19.0725159151
312O-linked_GlycosylationPTTEVSPTSQKTTTK
CCCEECCCCCCEECC		35.96OGP
312PhosphorylationPTTEVSPTSQKTTTK
CCCEECCCCCCEECC		35.9622210691
313PhosphorylationTTEVSPTSQKTTTKT
CCEECCCCCCEECCC		32.8222210691
315UbiquitinationEVSPTSQKTTTKTTT
EECCCCCCEECCCCC		47.83-
319UbiquitinationTSQKTTTKTTTPNAQ
CCCCEECCCCCCCCC		41.61-
334PhosphorylationATRSTPVSRTTKHFH
CCCCCCCCCCCCEEE		25.72-
338UbiquitinationTPVSRTTKHFHETTP
CCCCCCCCEEEECCC		43.59-
343O-linked_GlycosylationTTKHFHETTPNKGSG
CCCEEEECCCCCCCC		38.7055827263
344O-linked_GlycosylationTKHFHETTPNKGSGT
CCEEEECCCCCCCCC		23.1455827267
347UbiquitinationFHETTPNKGSGTTSG
EEECCCCCCCCCCCC		56.51-
351O-linked_GlycosylationTPNKGSGTTSGTTRL
CCCCCCCCCCCCEEE		21.34OGP
352O-linked_GlycosylationPNKGSGTTSGTTRLL
CCCCCCCCCCCEEEC		28.78OGP
353GPI-anchorNKGSGTTSGTTRLLS
CCCCCCCCCCEEECC		33.701824699
353O-linked_GlycosylationNKGSGTTSGTTRLLS
CCCCCCCCCCEEECC		33.70OGP
360PhosphorylationSGTTRLLSGHTCFTL
CCCEEECCCCHHHHH		32.8724719451
360 (in isoform 2)Phosphorylation-32.8719664995
362 (in isoform 2)Phosphorylation-18.9827282143
363PhosphorylationTRLLSGHTCFTLTGL
EEECCCCHHHHHHHH		16.9124719451
366 (in isoform 2)Phosphorylation-26.0919664995
372 (in isoform 6)Phosphorylation-23.2628634298
372 (in isoform 7)Phosphorylation-23.2628634298
373 (in isoform 6)Phosphorylation-20.3028634298
373 (in isoform 7)Phosphorylation-20.3028634298
376PhosphorylationGLLGTLVTMGLLT--
HHHHHHHHHCCCC--		14.5024719451
379 (in isoform 7)Phosphorylation-3.1128634298
379 (in isoform 6)Phosphorylation-3.1128634298
382 (in isoform 6)Phosphorylation-28634298
382 (in isoform 7)Phosphorylation-28634298
383 (in isoform 6)Phosphorylation-28634298
383 (in isoform 7)Phosphorylation-28634298
415 (in isoform 7)Phosphorylation-25627689
415 (in isoform 6)Phosphorylation-25627689
427 (in isoform 6)Phosphorylation-30206219
427 (in isoform 7)Phosphorylation-30206219
429 (in isoform 7)Phosphorylation-30206219
429 (in isoform 6)Phosphorylation-30206219
429 (in isoform 5)Phosphorylation--
430 (in isoform 7)Phosphorylation-30206219
430 (in isoform 6)Phosphorylation-30206219
430 (in isoform 2)Phosphorylation--
432 (in isoform 7)Phosphorylation-30206219
432 (in isoform 6)Phosphorylation-30206219
434 (in isoform 7)Phosphorylation-30206219
434 (in isoform 6)Phosphorylation-30206219
442 (in isoform 7)Phosphorylation-30206219
442 (in isoform 6)Phosphorylation-30206219
445 (in isoform 6)Phosphorylation-30206219
445 (in isoform 7)Phosphorylation-30206219
447 (in isoform 7)Phosphorylation-30206219
447 (in isoform 6)Phosphorylation-30206219
450 (in isoform 7)Phosphorylation-30206219
450 (in isoform 6)Phosphorylation-30206219
452 (in isoform 7)Phosphorylation-30206219
452 (in isoform 6)Phosphorylation-30206219
478 (in isoform 7)Phosphorylation-25627689
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 DAF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DAF_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 DAF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAF_HUMANCD55physical
12499389
NDUB7_HUMANNDUFB7physical
22939629
MPV17_HUMANMPV17physical
22939629
MA2A1_HUMANMAN2A1physical
22939629
RAB31_HUMANRAB31physical
22939629
PTCD3_HUMANPTCD3physical
22939629
GTR1_HUMANSLC2A1physical
22939629
RM04_HUMANMRPL4physical
22939629
GNAI3_HUMANGNAI3physical
22939629
INF2_HUMANINF2physical
22939629
FACE1_HUMANZMPSTE24physical
22939629
PTH2_HUMANPTRH2physical
22939629
S10AA_HUMANS100A10physical
22939629
SYJ2B_HUMANSYNJ2BPphysical
22939629
TIM50_HUMANTIMM50physical
22939629
S12A4_HUMANSLC12A4physical
22939629
NDUS7_HUMANNDUFS7physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
SCMC1_HUMANSLC25A24physical
22939629
PICAL_HUMANPICALMphysical
22939629
CH3L1_HUMANCHI3L1physical
26186194
CF120_HUMANC6orf120physical
26186194
CH3L1_HUMANCHI3L1physical
28514442
Drug and Disease Associations
Kegg Disease
H00106 Complement regulatory protein defects, including the following six diseases: C1 inhibitor deficiency
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAF_HUMAN

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Related Literatures of Post-Translational Modification
GPI-anchor
ReferencePubMed
"Modification-specific proteomics of plasma membrane proteins:identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment.";
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,Brodbeck U., Peck S.C., Jensen O.N.;
J. Proteome Res. 5:935-943(2006).
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
"Proteomic analysis of glycosylphosphatidylinositol-anchored membraneproteins.";
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,Jensen O.N.;
Mol. Cell. Proteomics 2:1261-1270(2003).
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
"Glycophospholipid membrane anchor attachment. Molecular analysis ofthe cleavage/attachment site.";
Moran P., Raab H., Kohr W.J., Caras I.W.;
J. Biol. Chem. 266:1250-1257(1991).
Cited for: GPI-ANCHOR AT SER-353.
N-linked Glycosylation
ReferencePubMed
"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-95, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.

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