APOH_MOUSE - dbPTM
APOH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APOH_MOUSE
UniProt AC Q01339
Protein Name Beta-2-glycoprotein 1
Gene Name Apoh
Organism Mus musculus (Mouse).
Sequence Length 345
Subcellular Localization Secreted.
Protein Description Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells..
Protein Sequence MVSPVLALFSAFLCHVAIAGRICPKPDDLPFATVVPLKTSYDPGEQIVYSCKPGYVSRGGMRRFTCPLTGMWPINTLRCVPRVCPFAGILENGIVRYTSFEYPKNISFACNPGFFLNGTSSSKCTEEGKWSPDIPACARITCPPPPVPKFALLKDYRPSAGNNSLYQDTVVFKCLPHFAMIGNDTVMCTEQGNWTRLPECLEVKCPFPPRPENGYVNYPAKPVLLYKDKATFGCHETYKLDGPEEAECTKTGTWSFLPTCRESCKLPVKKATVLYQGMRVKIQEQFKNGMMHGDKIHFYCKNKEKKCSYTVEAHCRDGTIEIPSCFKEHSSLAFWKTDASELTPC
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
23S-palmitoylationVAIAGRICPKPDDLP
HHHHCCCCCCCCCCC
3.2328526873
33O-linked_GlycosylationPDDLPFATVVPLKTS
CCCCCCEEEEEECCC
23.55-
55PhosphorylationVYSCKPGYVSRGGMR
EEEECCCEECCCCCC
12.0923737553
57PhosphorylationSCKPGYVSRGGMRRF
EECCCEECCCCCCEE
19.4123737553
79S-palmitoylationWPINTLRCVPRVCPF
CCCCCCCCCCCCCCC
5.7826165157
84S-palmitoylationLRCVPRVCPFAGILE
CCCCCCCCCCCCHHH
2.1226165157
105N-linked_GlycosylationTSFEYPKNISFACNP
CCEECCCCEEEEECC
30.5417330941
117N-linked_GlycosylationCNPGFFLNGTSSSKC
ECCCEECCCCCCCCC
46.6816944957
162N-linked_GlycosylationDYRPSAGNNSLYQDT
CCCCCCCCCCCCCCE
34.3316944957
183N-linked_GlycosylationPHFAMIGNDTVMCTE
CCEEEECCCEEEECC
30.7517330941
193N-linked_GlycosylationVMCTEQGNWTRLPEC
EEECCCCCEEECCCC
36.3217330941
260S-palmitoylationTWSFLPTCRESCKLP
CEEECCCCHHHCCCC
4.2528526873
319PhosphorylationEAHCRDGTIEIPSCF
EEEECCCEEECCCCC
21.52-
324PhosphorylationDGTIEIPSCFKEHSS
CCEEECCCCCCCCCC
37.54-

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 APOH_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APOH_MOUSE !!

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 APOH_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of APOH_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APOH_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105; ASN-117; ASN-162;ASN-183 AND ASN-193, AND MASS SPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117 AND ASN-162, AND MASSSPECTROMETRY.

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