2LEJ

human prion protein mutant HuPrP(90-231, M129, V210I)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0051260	biological_process	protein homooligomerization

Functional Information from PROSITE/UniProt

site_id	PS00291
Number of Residues	16
Details	PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY

Chain	Residue	Details
A	ALA113-TYR128

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site_id	PS00706
Number of Residues	19
Details	PRION_2 Prion protein signature 2. EtDvKMMeRVIeQMCitQY

Chain	Residue	Details
A	GLU200-TYR218

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	LIPID: GPI-anchor amidated serine => ECO:0000250|UniProtKB:P04273

Chain	Residue	Details
A	SER230

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site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12214108

Chain	Residue	Details
A	ASN181

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973

Chain	Residue	Details
A	ASN197

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