CERU_HUMAN - dbPTM
CERU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CERU_HUMAN
UniProt AC P00450
Protein Name Ceruloplasmin
Gene Name CP
Organism Homo sapiens (Human).
Sequence Length 1065
Subcellular Localization Secreted. Colocalizes with GCP1 in secretory intracellular compartments..
Protein Description Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity)..
Protein Sequence MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGPDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYHSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFHGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSYKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVDPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
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
46PhosphorylationHGEKKLISVDTEHSN
CCCCEEEEEECCCCC		25.1128122231
49PhosphorylationKKLISVDTEHSNIYL
CEEEEEECCCCCEEE		33.1828122231
52PhosphorylationISVDTEHSNIYLQNG
EEEECCCCCEEECCC		20.7726425664
55PhosphorylationDTEHSNIYLQNGPDR
ECCCCCEEECCCCHH		13.3928122231
72PhosphorylationRLYKKALYLQYTDET
HHHHHHHHHCCCCCC		9.16-
138N-linked_GlycosylationEGAIYPDNTTDFQRA
CCCCCCCCCCCCCCC		40.1315084671
138N-linked_GlycosylationEGAIYPDNTTDFQRA
CCCCCCCCCCCCCCC		40.1315084671
140O-linked_GlycosylationAIYPDNTTDFQRADD
CCCCCCCCCCCCCCC		40.86OGP
204PhosphorylationLIICKKDSLDKEKEK
EEEEECCCCCHHHHH		47.5522817900
209UbiquitinationKDSLDKEKEKHIDRE
CCCCCHHHHHCCCCE		77.22-
358N-linked_GlycosylationFFQVQECNKSSSKDN
HEEHHHCCCCCCCCC		46.6318638581
358N-linked_GlycosylationFFQVQECNKSSSKDN
HEEHHHCCCCCCCCC		46.6319838169
360PhosphorylationQVQECNKSSSKDNIR
EHHHCCCCCCCCCCC		26.3424505115
362PhosphorylationQECNKSSSKDNIRGK
HHCCCCCCCCCCCCH		51.6324505115
385PhosphorylationAEEIIWNYAPSGIDI
HHHHHHHCCCCCCEE		12.6126657352
388PhosphorylationIIWNYAPSGIDIFTK
HHHHCCCCCCEEEEC		39.9624505115
394PhosphorylationPSGIDIFTKENLTAP
CCCCEEEECCCCCCC		37.4726657352
397N-linked_GlycosylationIDIFTKENLTAPGSD
CEEEECCCCCCCCCC		44.2218514042
397N-linked_GlycosylationIDIFTKENLTAPGSD
CEEEECCCCCCCCCC		44.2217623646
399PhosphorylationIFTKENLTAPGSDSA
EEECCCCCCCCCCCE		42.2522210691
414PhosphorylationVFFEQGTTRIGGSYK
EEEECCCEEECCEEE		27.4122210691
419PhosphorylationGTTRIGGSYKKLVYR
CCEEECCEEEEEEEE		28.6822210691
428PhosphorylationKKLVYREYTDASFTN
EEEEEEEECCCCCCC		10.8322817900
429PhosphorylationKLVYREYTDASFTNR
EEEEEEECCCCCCCC		21.9722817900
432PhosphorylationYREYTDASFTNRKER
EEEECCCCCCCCCCC		35.1025072903
434PhosphorylationEYTDASFTNRKERGP
EECCCCCCCCCCCCC		31.4525072903
468GlycationIRVTFHNKGAYPLSI
EEEEEECCCCEEEEE		36.03-
471PhosphorylationTFHNKGAYPLSIEPI
EEECCCCEEEEEEEE		17.2424505115
474PhosphorylationNKGAYPLSIEPIGVR
CCCCEEEEEEEEEEE		22.0224505115
489PhosphorylationFNKNNEGTYYSPNYN
ECCCCCCCEECCCCC		17.0724505115
489O-linked_GlycosylationFNKNNEGTYYSPNYN
ECCCCCCCEECCCCC		17.07OGP
492O-linked_GlycosylationNNEGTYYSPNYNPQS
CCCCCEECCCCCCCC		9.0355832647
492PhosphorylationNNEGTYYSPNYNPQS
CCCCCEECCCCCCCC		9.0327251275
499PhosphorylationSPNYNPQSRSVPPSA
CCCCCCCCCCCCCCC		27.9927130503
499O-linked_GlycosylationSPNYNPQSRSVPPSA
CCCCCCCCCCCCCCC		27.99OGP
505O-linked_GlycosylationQSRSVPPSASHVAPT
CCCCCCCCCCCCCCC		36.01OGP
507O-linked_GlycosylationRSVPPSASHVAPTET
CCCCCCCCCCCCCCC		23.88OGP
528O-linked_GlycosylationVPKEVGPTNADPVCL
CCCCCCCCCCCHHHH		36.79OGP
539PhosphorylationPVCLAKMYYSAVDPT
HHHHHHHHHHCCCCC		8.12-
588N-linked_GlycosylationFPTVFDENESLLLED
CCEECCCCCCEEEEC		46.1016335952
622PhosphorylationQESNKMHSMNGFMYG
HHHHCHHHCCCCCCC		15.5024505115
722PhosphorylationVNQCRRQSEDSTFYL
HHHHHHCCCCCCEEE		41.3728355574
725PhosphorylationCRRQSEDSTFYLGER
HHHCCCCCCEEECCC		19.1627130503
726PhosphorylationRRQSEDSTFYLGERT
HHCCCCCCEEECCCE		28.7328857561
762N-linked_GlycosylationLHHLQEQNVSNAFLD
HHHHHHCCCCCHHHC		38.1317623646
762N-linked_GlycosylationLHHLQEQNVSNAFLD
HHHHHHCCCCCHHHC		38.1318638581
764PhosphorylationHLQEQNVSNAFLDKG
HHHHCCCCCHHHCCC		29.9527130503
784PhosphorylationSKYKKVVYRQYTDST
CCCEEEEEEECCCCC		8.5922817900
787PhosphorylationKKVVYRQYTDSTFRV
EEEEEEECCCCCEEE		11.9722817900
821AcetylationADVGDKVKIIFKNMA
CCCCCCEEEEEECCC		35.5127178108
829PhosphorylationIIFKNMATRPYSIHA
EEEECCCCCCCEEEE		22.7730108239
906UbiquitinationVCRRPYLKVFNPRRK
EECCCCHHHCCCCCC		38.65-
926N-linked_GlycosylationLFLVFDENESWYLDD
EEEEECCCCCEECCC		50.9016335952
1032PhosphorylationTLEMFPRTPGIWLLH
HHHCCCCCCCEEEEE		26.5524043423
1043PhosphorylationWLLHCHVTDHIHAGM
EEEEEEECCCCCCCC		9.7424043423
1052PhosphorylationHIHAGMETTYTVLQN
CCCCCCEEEEEEECC		19.0624043423
1053PhosphorylationIHAGMETTYTVLQNE
CCCCCEEEEEEECCC		12.1424043423
1054PhosphorylationHAGMETTYTVLQNED
CCCCEEEEEEECCCC		11.4124043423
1055PhosphorylationAGMETTYTVLQNEDT
CCCEEEEEEECCCCC		16.7924043423
1062PhosphorylationTVLQNEDTKSG----
EEECCCCCCCC----		22.4124043423
1064PhosphorylationLQNEDTKSG------
ECCCCCCCC------		52.4027130503
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
722SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CERU_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 CERU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRFL_HUMANLTFphysical
10666301
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604290Aceruloplasminemia (ACERULOP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CERU_HUMAN

loading...

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-138; ASN-358 AND ASN-397,STRUCTURE OF CARBOHYDRATES, 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-138; ASN-358; ASN-397 ANDASN-762, 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-138; ASN-358; ASN-397;ASN-588; ASN-762 AND ASN-926, AND MASS SPECTROMETRY.
"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-138; ASN-397 AND ASN-762,AND MASS SPECTROMETRY.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-787, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory