PROP_HUMAN - dbPTM
PROP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PROP_HUMAN
UniProt AC P27918
Protein Name Properdin
Gene Name CFP
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization Secreted.
Protein Description A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes..
Protein Sequence MITEGAQAPRLLLPPLLLLLTLPATGSDPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCRSPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCPTHGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCPVDGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCPLKGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACKDPEEEEL
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
39PhosphorylationCFTQYEESSGKCKGL
EEEEEECCCCCCCCC
32.24-
40PhosphorylationFTQYEESSGKCKGLL
EEEEECCCCCCCCCC
45.62-
83C-linked_GlycosylationRSPRWSLWSTWAPCS
CCCCCCEECCCCCCE
6.5431507604
86C-linked_GlycosylationRWSLWSTWAPCSVTC
CCCEECCCCCCEEEE
7.8431507604
92O-linked_GlycosylationTWAPCSVTCSEGSQL
CCCCCEEEECCCCEE
8.2712096136
139C-linked_GlycosylationCCPEMGGWSGWGPWE
CCCCCCCCCCCCCCC
6.4831507604
142C-linked_GlycosylationEMGGWSGWGPWEPCS
CCCCCCCCCCCCCCE
12.2631507604
145C-linked_GlycosylationGWSGWGPWEPCSVTC
CCCCCCCCCCCEEEE
20.4431507604
151O-linked_GlycosylationPWEPCSVTCSKGTRT
CCCCCEEEECCCCHH
8.5112096136
196C-linked_GlycosylationVCPTHGAWATWGPWT
CCCCCCCCCCCCCCC
9.9831507604
199C-linked_GlycosylationTHGAWATWGPWTPCS
CCCCCCCCCCCCCCC
11.7831507604
202C-linked_GlycosylationAWATWGPWTPCSASC
CCCCCCCCCCCCCCC
14.7231507604
208O-linked_GlycosylationPWTPCSASCHGGPHE
CCCCCCCCCCCCCCC
7.1412096136
260C-linked_GlycosylationPCPVAGGWGPWGPVS
CCCCCCCCCCCCCCC
14.5731507604
263C-linked_GlycosylationVAGGWGPWGPVSPCP
CCCCCCCCCCCCCCC
21.5631507604
272O-linked_GlycosylationPVSPCPVTCGLGQTM
CCCCCCCCCCCCCCC
5.9912096136
278PhosphorylationVTCGLGQTMEQRTCN
CCCCCCCCCCCEECC
22.3728787133
321C-linked_GlycosylationVDGEWDSWGEWSPCI
CCCCCCCCCCCCHHH
13.2731507604
324C-linked_GlycosylationEWDSWGEWSPCIRRN
CCCCCCCCCHHHHHH
12.0231507604
325PhosphorylationWDSWGEWSPCIRRNM
CCCCCCCCHHHHHHC
12.9422468782
334PhosphorylationCIRRNMKSISCQEIP
HHHHHCCCCCCEECC
14.6822468782
336PhosphorylationRRNMKSISCQEIPGQ
HHHCCCCCCEECCCC
19.4822468782
382C-linked_GlycosylationHCPLKGSWSEWSTWG
CCCCCCCHHHCCCCE
14.6731507604
385C-linked_GlycosylationLKGSWSEWSTWGLCM
CCCCHHHCCCCEEEC
8.7831507604
388C-linked_GlycosylationSWSEWSTWGLCMPPC
CHHHCCCCEEECCCC
7.7031507604
400PhosphorylationPPCGPNPTRARQRLC
CCCCCCHHHHHHHHC
43.5330257219
428N-linked_GlycosylationVEGQGEKNVTFWGRP
ECCCCCCCEEEECEE
33.4916335952

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 PROP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PROP_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 PROP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
B3GLT_HUMANB3GALTLphysical
28514442
D19L3_HUMANDPY19L3physical
28514442
CRAC1_HUMANCRTAC1physical
28514442
CRBN_HUMANCRBNphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
312060Properdin deficiency (PFD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PROP_HUMAN

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Related Literatures of Post-Translational Modification
C-linked Glycosylation
ReferencePubMed
"Properdin, the positive regulator of complement, is highly C-mannosylated.";
Hartmann S., Hofsteenge J.;
J. Biol. Chem. 275:28569-28574(2000).
Cited for: GLYCOSYLATION AT TRP-83; TRP-86; TRP-139; TRP-142; TRP-145; TRP-196;TRP-199; TRP-260; TRP-263; TRP-321; TRP-324; TRP-382; TRP-385 ANDTRP-388.
N-linked Glycosylation
ReferencePubMed
"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-428, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"C-mannosylation and O-fucosylation of thrombospondin type 1repeats.";
Gonzalez de Peredo A., Klein D., Macek B., Hess D.,Peter-Katalinic J., Hofsteenge J.;
Mol. Cell. Proteomics 1:11-18(2002).
Cited for: GLYCOSYLATION AT THR-92; THR-151; SER-208 AND THR-272.

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