FRRS1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FRRS1_MOUSE
• UniProt AC: Q8K385
• Protein Name: Ferric-chelate reductase 1
• Gene Name: FRRS1
• Organism: Mus musculus (Mouse).
• Sequence Length: 592
• Subcellular Localization: Membrane ; Multi-pass membrane protein .
• Protein Description: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm..
• Protein Sequence: MAAPQITLSVLVIALLTCSVTAYPNGKVPMSCGGMIPQHNHSPQSEPIHQITVSQTTFKPGDQIEVTLSGPPFRGFLLEARDAENLSGPPIGSFTLIDSEESQLLTCTDVQGLAVSHTRSSKKTEIKVYWDAPSPAPDHIRFLATVVQKFKIYWVKIPSPVISQPNAPPFTTPKATTQPLTTPPSVSHLTKPFSAFECGNKKFCVRSPLNCDPEKEPACVFLSFTRDNQSVMVEMSGPSDGYVSFAFSHDQWMGDDDAYLCIREDQTVDIQPSYLTGRSYPVMDSRGTLEDMAWRLADGVIQCSFRRNITLPEAKNRFVLNESYYIFFAEGPSHDGRIFRHSQQPLITYEKYNVTDTPKSVGGSRSSPLLKAHGALMFVAWMTTVSIGVLVARFFRSVWSKAFFLREAAWFQVHRMLMVATSLLTCVAFVLPFVYRGGWSWRAGYHPYLGCTVMTLAVLQPLLATFRPPLHDPRRQVFNWTHWSVGTAARIIAVAAMFLGMDLPGLNLPSPQKTYAMMGFVVWHIGTEVILEIHAYRLSRKVEILDNDRIQILQSLTVAEAEGHVFKKVVLAVYICGNVIFLSIFLSAINHI

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
85	N-linked_Glycosylation	LEARDAENLSGPPIG EEEECHHHCCCCCCE	41.02	-
99	Phosphorylation	GSFTLIDSEESQLLT EEEEEECCCCCEEEE	35.95	-
107	Glutathionylation	EESQLLTCTDVQGLA CCCEEEEEECCCCEE	2.85	24333276
303	Glutathionylation	LADGVIQCSFRRNIT HHCCEEEEEEECCCC	2.59	24333276
308	N-linked_Glycosylation	IQCSFRRNITLPEAK EEEEEECCCCCCHHH	27.60	-
321	N-linked_Glycosylation	AKNRFVLNESYYIFF HHHCEEECCEEEEEE	30.76	19349973
353	N-linked_Glycosylation	LITYEKYNVTDTPKS CEEEEECCCCCCCCC	41.08	19349973
510	Phosphorylation	LPGLNLPSPQKTYAM CCCCCCCCCHHHHHH	43.03	28059163

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of FRRS1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FRRS1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FRRS1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of FRRS1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-321 AND ASN-353, AND MASSSPECTROMETRY.
PubMed: 19349973