C4BPB_HUMAN - dbPTM
C4BPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C4BPB_HUMAN
UniProt AC P20851
Protein Name C4b-binding protein beta chain
Gene Name C4BPB
Organism Homo sapiens (Human).
Sequence Length 252
Subcellular Localization Secreted.
Protein Description Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. It also interacts with anticoagulant protein S and with serum amyloid P component. The beta chain binds protein S..
Protein Sequence MFFWCACCLMVAWRVSASDAEHCPELPPVDNSIFVAKEVEGQILGTYVCIKGYHLVGKKTLFCNASKEWDNTTTECRLGHCPDPVLVNGEFSSSGPVNVSDKITFMCNDHYILKGSNRSQCLEDHTWAPPFPICKSRDCDPPGNPVHGYFEGNNFTLGSTISYYCEDRYYLVGVQEQQCVDGEWSSALPVCKLIQEAPKPECEKALLAFQESKNLCEAMENFMQQLKESGMTMEELKYSLELKKAELKAKLL
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
57UbiquitinationIKGYHLVGKKTLFCN
EECEEEECCEEEEEC		31.9122817900
58UbiquitinationKGYHLVGKKTLFCNA
ECEEEECCEEEEECC		34.8021963094
59UbiquitinationGYHLVGKKTLFCNAS
CEEEECCEEEEECCC		44.5221963094
64N-linked_GlycosylationGKKTLFCNASKEWDN
CCEEEEECCCCCCCC		39.6618638581
64N-linked_GlycosylationGKKTLFCNASKEWDN
CCEEEEECCCCCCCC		39.6616335952
66UbiquitinationKTLFCNASKEWDNTT
EEEEECCCCCCCCCC		19.6721963094
67UbiquitinationTLFCNASKEWDNTTT
EEEECCCCCCCCCCC		61.4921963094
71N-linked_GlycosylationNASKEWDNTTTECRL
CCCCCCCCCCCEEEC		40.1614760718
71N-linked_GlycosylationNASKEWDNTTTECRL
CCCCCCCCCCCEEEC		40.1618638581
98N-linked_GlycosylationFSSSGPVNVSDKITF
ECCCCCCCCCCEEEE		30.6116335952
98N-linked_GlycosylationFSSSGPVNVSDKITF
ECCCCCCCCCCEEEE		30.6118638581
101UbiquitinationSGPVNVSDKITFMCN
CCCCCCCCEEEEEEC		41.9321963094
102UbiquitinationGPVNVSDKITFMCND
CCCCCCCEEEEEECC		35.8221963094
113UbiquitinationMCNDHYILKGSNRSQ
EECCEEEECCCCHHH		3.9721963094
114UbiquitinationCNDHYILKGSNRSQC
ECCEEEECCCCHHHH		51.2221963094
117N-linked_GlycosylationHYILKGSNRSQCLED
EEEECCCCHHHHCCC		57.18UniProtKB CARBOHYD
134UbiquitinationWAPPFPICKSRDCDP
CCCCCCEECCCCCCC		3.1321963094
135UbiquitinationAPPFPICKSRDCDPP
CCCCCEECCCCCCCC		49.6021963094
154N-linked_GlycosylationHGYFEGNNFTLGSTI
CEEEECCCEECCCEE		41.98UniProtKB CARBOHYD
160O-linked_GlycosylationNNFTLGSTISYYCED
CCEECCCEEEEEECC		16.49OGP
191UbiquitinationWSSALPVCKLIQEAP
HHHHHHHHHHHHHCC		2.5421963094
192UbiquitinationSSALPVCKLIQEAPK
HHHHHHHHHHHHCCC		49.1921963094
198UbiquitinationCKLIQEAPKPECEKA
HHHHHHCCCHHHHHH		52.5621963094
199UbiquitinationKLIQEAPKPECEKAL
HHHHHCCCHHHHHHH		61.5721963094
203UbiquitinationEAPKPECEKALLAFQ
HCCCHHHHHHHHHHH		39.4421963094
204UbiquitinationAPKPECEKALLAFQE
CCCHHHHHHHHHHHH		56.8621963094
226UbiquitinationMENFMQQLKESGMTM
HHHHHHHHHHCCCCH		3.6029967540
227UbiquitinationENFMQQLKESGMTME
HHHHHHHHHCCCCHH		45.5629967540
236UbiquitinationSGMTMEELKYSLELK
CCCCHHHHHHHHHHH		3.9329967540
237UbiquitinationGMTMEELKYSLELKK
CCCHHHHHHHHHHHH		35.7529967540
239PhosphorylationTMEELKYSLELKKAE
CHHHHHHHHHHHHHH		17.49-
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 C4BPB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C4BPB_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 C4BPB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN655_HUMANZNF655physical
26186194
DCTN4_HUMANDCTN4physical
26186194
PROS_HUMANPROS1physical
26186194
MTO1_HUMANMTO1physical
26186194
RTL8C_HUMANFAM127Aphysical
26186194
VPS52_HUMANVPS52physical
26186194
GDC_HUMANSLC25A16physical
26186194
DCTN6_HUMANDCTN6physical
26186194
ORNT1_HUMANSLC25A15physical
26186194
KMCP1_HUMANSLC25A30physical
26186194
NEK4_HUMANNEK4physical
26186194
DCTN3_HUMANDCTN3physical
26186194
MP2K7_HUMANMAP2K7physical
26186194
ZN655_HUMANZNF655physical
28514442
PROS_HUMANPROS1physical
28514442
RTL8C_HUMANFAM127Aphysical
28514442
ORNT1_HUMANSLC25A15physical
28514442
VPS52_HUMANVPS52physical
28514442
MP2K7_HUMANMAP2K7physical
28514442
DCTN4_HUMANDCTN4physical
28514442
DCTN6_HUMANDCTN6physical
28514442
RM10_HUMANMRPL10physical
28514442
ACTY_HUMANACTR1Bphysical
28514442
NEK4_HUMANNEK4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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 C4BPB_HUMAN

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Related Literatures of Post-Translational Modification
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-98, 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-64 AND ASN-98, 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-64; ASN-71 AND ASN-98, ANDMASS SPECTROMETRY.

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