SORC2_MOUSE - dbPTM
SORC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SORC2_MOUSE
UniProt AC Q9EPR5
Protein Name VPS10 domain-containing receptor SorCS2
Gene Name Sorcs2
Organism Mus musculus (Mouse).
Sequence Length 1159
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MAHRGPPSAPKRPGPTAPDRSFQALLPPCWPRSWPLLLLLLVLVAACGAMGRSPQPGRQGPGVQITRLLPAGRTESGDRKDPQARESEPSVPGLGPGSASGPSTDGAPAPGKGRRARAVPVAGAASASRAQVSLISTSFVLKGDATHNQAMVHWTGENSSVILILTKYYHADMGKVLESSLWRSSDFGTTYTKLTLQPGVTTVIDNFYICPANKRKIILVSSSLGDREQSLFLSTDEGATFQKYPVPFLVEMLLFHPKEEDKVLAYTKDSKLYVSSDLGKKWTLLQERVTKDHVFWAVSGVDDDPNLVHVEAQDLSGGYRYYTCLIYNCSAQPHIAPFSGPIDRGSLTVQDEYIFLKATSTNRTKYYVSYRRSDFVLMKLPKYALPKDLQIISTDEQQVFVAVQEWNQVDTYNLYQSDLRGVRYSLVLENVRSSRQAEENVVIDILEVRGVKGVFLANQKVDGKVTTVITYNKGRDWDYLRPPSTDMNGKPTNCQPPDCYLHLHLRWADNPYVSGTVHTKDTAPGLIMGAGNLGSQLVEYKEEMYITSDCGHTWRQVFEEEHHVLYLDHGGVIAAIKDTSIPLKILKFSVDEGHTWSTHNFTSTSVFVDGLLSEPGDETLVMTVFGHISFRSDWELVKVDFRPSFPRQCGEDDYSSWDLTDLQGDHCIMGQQRSYRKRKSTSWCVKGRSFTSALTSRVCKCRDSDFLCDYGFERSSSSESTANKCSANFWFNPLSPPEDCVLGQTYTSSLGYRKVVSNVCEGGVDLQQSPVQLQCPLQAPRGLQVSIRGEAVAVRPREDVLFVVRQEQGDVLTTKYQVDLGDGFKAMYVNLTLTGEPIRHHYESPGIYRVSVRAENMAGHDEAVLFVQVNSPLQALYLEVVPVIGVNQEVNLTAVLLPLNPNLTVFYWWIGHSLQPLLSLDNSVTTKFTDAGDVRVTVQAACGNSVLQDSRLVRVLDQFQVVPLRFSRELDTFNPNTPEWREDVGLVVTRLLSKETSIPEELLVTVVKPGLPTIADLYVLLPLPRPTRKRSLTSDKRLAAVQQALNSHRISFILRGGLRILVELRDTDTGPQRPGGSGGYWAVVVLFVIGLFAVGAFILYKFKRKRPGRTVYAQMHNEKEQEMTSPVSHSEDAQSTMQGNHSGVVLSINSREMHSYLVG
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
8PhosphorylationMAHRGPPSAPKRPGP
CCCCCCCCCCCCCCC
61.41-
16PhosphorylationAPKRPGPTAPDRSFQ
CCCCCCCCCCCCCHH
57.6523140645
21PhosphorylationGPTAPDRSFQALLPP
CCCCCCCCHHHHCCC
29.1423140645
133PhosphorylationSASRAQVSLISTSFV
CCCHHHEEEEEEEEE
14.12-
158N-linked_GlycosylationMVHWTGENSSVILIL
EEEEECCCCEEEEEE
40.7130061605
328N-linked_GlycosylationYYTCLIYNCSAQPHI
EEEEEEEECCCCCCC
13.2830061605
362N-linked_GlycosylationFLKATSTNRTKYYVS
EEEEECCCCEEEEEE
49.7630061605
366PhosphorylationTSTNRTKYYVSYRRS
ECCCCEEEEEEEECC
14.4229895711
600N-linked_GlycosylationGHTWSTHNFTSTSVF
CCCEECCCCCCEEEE
41.8130061605
830N-linked_GlycosylationGFKAMYVNLTLTGEP
CEEEEEEEEEECCCC
15.1530061605
891N-linked_GlycosylationIGVNQEVNLTAVLLP
ECCCCCEEEEEEEEE
30.8130061605
902N-linked_GlycosylationVLLPLNPNLTVFYWW
EEEECCCCCEEEEEE
47.4730061605
1110PhosphorylationKRKRPGRTVYAQMHN
HCCCCCCEEEEEECC
24.6326824392
1147O-linked_GlycosylationNHSGVVLSINSREMH
CCCCEEEEECCCCCH
14.2355414005

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 SORC2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SORC2_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 SORC2_MOUSE !!

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

Oops, there are no PPI records of SORC2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SORC2_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-830, AND MASSSPECTROMETRY.

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