FRP1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FRP1_SCHPO
• UniProt AC: Q04800
• Protein Name: Ferric reductase transmembrane component 1 {ECO:0000305}
• Gene Name: frp1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 564
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity)..
• Protein Sequence: MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNPYKDYSYLFLFAGGVGVSYILPIILDTIKKQSRTVHITFVWSARSSALLNIVHKSLCEAVRYTEMNINIFCHLTNSYPVEEVSSLNSQSARNYSLQYLNGRPDVNDYFKDFLHATGTQTAALASCGSDKLLRHLKSCVNTHSPSTVDLYQHYEEI

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
4	N-linked_Glycosylation	----MAINSSDKWTV ----CCCCCHHHHHH	26.39	-
111	N-linked_Glycosylation	TTQVSTGNWSKNAVA EEECCCCCCCHHHHH	39.68	-
268	N-linked_Glycosylation	RMLRSFLNRSKFDVV HHHHHHHCCCCCCEE	44.14	-
352	Phosphorylation	AKKVSSKSLSDVSDI HHHHCCCCHHCCCCC	34.74	21712547
354	Phosphorylation	KVSSKSLSDVSDINI HHCCCCHHCCCCCCC	42.95	25720772
357	Phosphorylation	SKSLSDVSDINISDE CCCHHCCCCCCCCHH	37.45	25720772
360	N-linked_Glycosylation	LSDVSDINISDEKIE HHCCCCCCCCHHHHH	32.47	-
362	Phosphorylation	DVSDINISDEKIEKN CCCCCCCCHHHHHHC	34.92	28889911
381	Phosphorylation	IEVMERHSLSQEDLV EEHHCCCCCCHHHHE	35.62	28889911
383	Phosphorylation	VMERHSLSQEDLVFE HHCCCCCCHHHHEEE	34.24	28889911
501	N-linked_Glycosylation	LNSQSARNYSLQYLN CCCHHHHHCCHHHHC	30.38	-

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

Oops, there are no upstream regulatory protein records of FRP1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FRP1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FRP1_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of FRP1_SCHPO !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-381 ANDSER-383, AND MASS SPECTROMETRY.
PubMed: 18257517