PRIO_HUMAN - dbPTM
PRIO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRIO_HUMAN
UniProt AC P04156
Protein Name Major prion protein
Gene Name PRNP
Organism Homo sapiens (Human).
Sequence Length 253
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 under
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 (By similarity)..
Protein Sequence MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG
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
36O-linked_GlycosylationGGWNTGGSRYPGQGS
CCCCCCCCCCCCCCC		29.95OGP
38PhosphorylationWNTGGSRYPGQGSPG
CCCCCCCCCCCCCCC		17.2624719451
43PhosphorylationSRYPGQGSPGGNRYP
CCCCCCCCCCCCCCC		16.6924719451
44HydroxylationRYPGQGSPGGNRYPP
CCCCCCCCCCCCCCC		62.6311032800
95O-linked_GlycosylationGWGQGGGTHSQWNKP
CCCCCCCCCCCCCCC		22.9455828625
107PhosphorylationNKPSKPKTNMKHMAG
CCCCCCCCCHHHHHH		49.4222210691
109SulfoxidationPSKPKTNMKHMAGAA
CCCCCCCHHHHHHHH		3.6919172188
112SulfoxidationPKTNMKHMAGAAAAG
CCCCHHHHHHHHHHH		2.8419172188
128PhosphorylationVVGGLGGYMLGSAMS
HHCHHHHHHHHHHHC		6.3322210691
129SulfoxidationVGGLGGYMLGSAMSR
HCHHHHHHHHHHHCC		3.7519172188
134SulfoxidationGYMLGSAMSRPIIHF
HHHHHHHHCCCEEEC		3.6019172188
135O-linked_GlycosylationYMLGSAMSRPIIHFG
HHHHHHHCCCEEECC		34.32OGP
145PhosphorylationIIHFGSDYEDRYYRE
EEECCCCHHHHHHHH		22.79-
154SulfoxidationDRYYRENMHRYPNQV
HHHHHHHHHHCCCCC		1.3119172188
166SulfoxidationNQVYYRPMDEYSNQN
CCCEECCHHHCCCCC		4.5319172188
181N-linked_GlycosylationNFVHDCVNITIKQHT
CCCEECEEEEEEECE		31.8312356908
181N-linked_GlycosylationNFVHDCVNITIKQHT
CCCEECEEEEEEECE		31.8312356908
193O-linked_GlycosylationQHTVTTTTKGENFTE
ECEEEEECCCCCCCH		34.6555835733
194UbiquitinationHTVTTTTKGENFTET
CEEEEECCCCCCCHH		63.23-
197N-linked_GlycosylationTTTTKGENFTETDVK
EEECCCCCCCHHHHH		58.7812356908
197N-linked_GlycosylationTTTTKGENFTETDVK
EEECCCCCCCHHHHH		58.7817660510
213SulfoxidationMERVVEQMCITQYER
HHHHHHHHHHHHHHH		0.8319172188
230GPI-anchorQAYYQRGSSMVLFSS
HHHHHCCCCCEECCC		19.90-
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
43SPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRIO_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 PRIO_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_HUMANBAG6physical
16169070
PIMRE_HUMANFAM64Aphysical
18482256
HXA1_HUMANHOXA1physical
18482256
CASK_HUMANCSN3physical
18482256
BAZ2B_HUMANBAZ2Bphysical
18482256
CG050_HUMANC7orf50physical
18482256
SURF2_HUMANSURF2physical
18482256
SCNM1_HUMANSCNM1physical
18482256
TYMOS_HUMANTYMSOSphysical
18482256
PLK3_HUMANPLK3physical
18482256
RBM22_HUMANRBM22physical
18482256
CC149_HUMANCCDC149physical
18482256
3MG_HUMANMPGphysical
18482256
ZKSC8_HUMANZKSCAN8physical
18482256
TSLP_HUMANTSLPphysical
18482256
DDX47_HUMANDDX47physical
18482256
MARK4_HUMANMARK4physical
18482256
ZN408_HUMANZNF408physical
18482256
TBPL1_HUMANTBPL1physical
18482256
ABT1_HUMANABT1physical
18482256
RL41_HUMANRPL41physical
18482256
ZN740_HUMANZNF740physical
18482256
CWC15_HUMANCWC15physical
18482256
FHL1_HUMANFHL1physical
18482256
TM237_HUMANTMEM237physical
18482256
IEX1_HUMANIER3physical
18482256
P33MX_HUMANKIAA1191physical
18482256
PTH_HUMANPTRH1physical
18482256
MYOME_HUMANPDE4DIPphysical
18482256
RHG15_HUMANARHGAP15physical
18482256
MTG1_HUMANMTG1physical
18482256
UTP4_HUMANCIRH1Aphysical
18482256
AGO1_HUMANAGO1physical
18482256
WDR5_HUMANWDR5physical
18482256
ADAP2_HUMANADAP2physical
18482256
PP14A_HUMANPPP1R14Aphysical
18482256
CIRBP_HUMANCIRBPphysical
18482256
LST2_HUMANZFYVE28physical
18482256
PYM1_HUMANWIBGphysical
18482256
NHP2_HUMANNHP2physical
18482256
LIPB2_HUMANPPFIBP2physical
18482256
FGF13_HUMANFGF13physical
18482256
AIFM3_HUMANAIFM3physical
18482256
CN37_HUMANCNPphysical
18482256
NOB1_HUMANNOB1physical
18482256
RBM40_HUMANRNPC3physical
18482256
DYRK3_HUMANDYRK3physical
18482256
T22D4_HUMANTSC22D4physical
16713569
PSA3_HUMANPSMA3physical
16713569
CLUS_HUMANCLUphysical
18786636
GRP78_HUMANHSPA5physical
10970892
DPP6_MOUSEDpp6physical
24225951
ARF1_HUMANARF1physical
25896910
CSK21_HUMANCSNK2A1physical
28900035
ZBED3_HUMANZBED3physical
28900035
1433T_HUMANYWHAQphysical
28900035
PABP1_HUMANPABPC1physical
28900035
PABP4_HUMANPABPC4physical
28900035
CH60_HUMANHSPD1physical
28900035
CYLD_HUMANCYLDphysical
28900035
HS90A_HUMANHSP90AA1physical
28900035
RSSA_HUMANRPSAphysical
28900035
PSMD2_HUMANPSMD2physical
28900035
RSSA_HUMANRPSAphysical
28759037
Drug and Disease Associations
Kegg Disease
H00061 Prion diseases; Creutzfeldt-Jacob disease (CJD); Gerstmann-Straussler disease (GSD); Gerstmann-Strau
H01243 Huntington's disease-like syndrome
OMIM Disease
Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humansNote=PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like
scrapie in sheep and goat
bovine spongiform encephalopathy (BSE) in cattle
transmissible mink encephalopathy (TME)
chronic wasting disease (CWD) of mule deer and elk
(1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs. feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration
123400
600072Fatal familial insomnia (FFI)
137440Gerstmann-Straussler disease (GSD)
603218Huntington disease-like 1 (HDL1)
245300Kuru (KURU)
606688Spongiform encephalopathy with neuropsychiatric features (SENF)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRIO_HUMAN

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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-197, AND MASSSPECTROMETRY.

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