PRIO_MOUSE - dbPTM
PRIO_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRIO_MOUSE
UniProt AC P04925
Protein Name Major prion protein
Gene Name Prnp
Organism Mus musculus (Mouse).
Sequence Length 254
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor. Golgi apparatus . Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to. vesicles in para- and perinuclear regions, where both proteins unde
Protein Description Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains. [PubMed: 12732622]
Protein Sequence MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG
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
33PhosphorylationPKPGGWNTGGSRYPG
CCCCCCCCCCCCCCC		36.0924719451
36PhosphorylationGGWNTGGSRYPGQGS
CCCCCCCCCCCCCCC		29.9523684622
38PhosphorylationWNTGGSRYPGQGSPG
CCCCCCCCCCCCCCC		17.2624719451
43PhosphorylationSRYPGQGSPGGNRYP
CCCCCCCCCCCCCCC		16.6922817900
44HydroxylationRYPGQGSPGGNRYPP
CCCCCCCCCCCCCCC		62.6311032800
106PhosphorylationNKPSKPKTNLKHVAG
CCCCCCCCCHHHHHH		55.0729109428
180N-linked_GlycosylationNFVHDCVNITIKQHT
CCCEEEEEEEEEECE		31.83-
187PhosphorylationNITIKQHTVTTTTKG
EEEEEECEEEEECCC		19.6330635358
189PhosphorylationTIKQHTVTTTTKGEN
EEEECEEEEECCCCC		21.4130635358
190PhosphorylationIKQHTVTTTTKGENF
EEECEEEEECCCCCC		28.2930635358
196N-linked_GlycosylationTTTTKGENFTETDVK
EEECCCCCCCHHHHH		58.7819349973
198PhosphorylationTTKGENFTETDVKMM
ECCCCCCCHHHHHHH		49.9430635358
200PhosphorylationKGENFTETDVKMMER
CCCCCCHHHHHHHHH		42.9330635358
203UbiquitinationNFTETDVKMMERVVE
CCCHHHHHHHHHHHH		35.0322790023
205SulfoxidationTETDVKMMERVVEQM
CHHHHHHHHHHHHHH		2.1722654104
212SulfoxidationMERVVEQMCVTQYQK
HHHHHHHHHHHHHHH		0.9522654104
230GPI-anchorAYYDGRRSSSTVLFS
HHCCCCCCCCCCCCC		27.55-
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 PRIO_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRIO_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 PRIO_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT2B2_MOUSEAtp2b2physical
15146195
CSTN1_MOUSEClstn1physical
15146195
APLP2_MOUSEAplp2physical
15146195
CLUS_MOUSECluphysical
15146195
SPRL1_MOUSESparcl1physical
15146195
PDIA1_MOUSEP4hbphysical
15146195
ADA23_MOUSEAdam23physical
15146195
GRP78_MOUSEHspa5physical
15146195
APBB1_MOUSEApbb1physical
15146195
DYN1_MOUSEDnm1physical
15146195
CNTN1_MOUSECntn1physical
15146195
NCAM2_MOUSENcam2physical
15146195
A4_MOUSEAppphysical
15146195
LSAMP_MOUSELsampphysical
15146195
MOG_MOUSEMogphysical
15146195
IGSF8_MOUSEIgsf8physical
15146195
CADM3_MOUSECadm3physical
15146195
APOE_MOUSEApoephysical
15146195
NCAM1_MOUSENcam1physical
15146195
DPP6_MOUSEDpp6physical
15146195
MAG_MOUSEMagphysical
15146195
1433Z_MOUSEYwhazphysical
15146195
1433E_MOUSEYwhaephysical
15146195
AT1A3_MOUSEAtp1a3physical
15146195
AT1A1_MOUSEAtp1a1physical
15146195
AT1B1_MOUSEAtp1b1physical
15146195
MBP_MOUSEMbpphysical
15146195
MYPR_MOUSEPlp1physical
15146195
GBB1_MOUSEGnb1physical
15146195
DPYL2_MOUSEDpysl2physical
15146195
PDE10_MOUSEPde10aphysical
15146195
STXB1_MOUSEStxbp1physical
15146195
DPP6_MOUSEDpp6physical
24225951
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRIO_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, AND MASSSPECTROMETRY.

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