FRE4_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FRE4_YEAST
• UniProt AC: P53746
• Protein Name: Ferric reductase transmembrane component 4
• Gene Name: FRE4
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 719
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid. 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..
• Protein Sequence: MLLVHIISFLLFFQLSAAKAPPSKTSLINTHERRSIYSCYVGLRKETWGFNGSAICRYEPAIQSMLYCLYEDTHEKGYSNKTLEKGFEEMRQFCYTPKFLNMTDAEFYTSLDNGTYYIQDQPKAGINITYPIRLNTTLRKAYYDAYYGYYYNHDIPYYFGGIICAYFVGVMLLAGLIRFLNYTPIKKIMFQQKLVNYVRGYTTLPTLYEKHAEPFSYLKVITGYLPTRFETLVILGYLILHTIFMAYKYQYDPYHIIFAAHRAEVAHFVAYRSGILSFAHLPLIVLFAGRNNFLQLISGLKHTSFIVFHKWLGRMMFLDAIIHAAGFTNYYLYYKKWNTVRLRVYWKFGIATTCLAGMLIFFSIAAFRRHYYETFMALHIVFAALFLYTCWEHVTNFSGIEWIYAAIAIWGVDRIVRITRIALLGFPKADLQLVGSDLVRVTVKKPKKFWKAKPGQYVFVSFLRPLCFWQSHPFTVMDSCVNDRELVIVLKAKKGVTKLVRNFVERKGGKASMRLAIEGPYGSKSTAHRFDNVLLLAGGSGLPGPISHALELGKTTAASGKNFVQLVIAVRGLDMLNACKKELMALKGLNVQVHIYNSKQELASAEKISSNEVKNGETTAEKAPSSLSNSEKAPSESENTELPLSLNDTSISDLEFATFHVGRPNVEEILNESVNHSGSLAVVCCGPPIFVDTARNQTAKAVIRNPSRMIEYLEEYQAW

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
51	N-linked_Glycosylation	RKETWGFNGSAICRY CCCCCCCCCHHHHCC	39.30	-
80	N-linked_Glycosylation	THEKGYSNKTLEKGF CCCCCCCCHHHHHHH	32.61	-
101	N-linked_Glycosylation	CYTPKFLNMTDAEFY HCCHHHCCCCCCCCE	34.15	-
113	N-linked_Glycosylation	EFYTSLDNGTYYIQD CCEEECCCCEEEECC	50.42	-
127	N-linked_Glycosylation	DQPKAGINITYPIRL CCCCCCEEEEEEEEC	21.45	-
135	N-linked_Glycosylation	ITYPIRLNTTLRKAY EEEEEECCCHHHHHH	22.59	-
609	Phosphorylation	LASAEKISSNEVKNG HHHCCCCCCCCCCCC	37.87	25521595
628	Phosphorylation	EKAPSSLSNSEKAPS HHCCCCCCCCCCCCC	40.01	25521595
707	Phosphorylation	KAVIRNPSRMIEYLE HHHHHCHHHHHHHHH	37.72	17563356

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

Oops, there are no upstream regulatory protein records of FRE4_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FRE4_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FRE4_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSC1_YEAST	CSC1	physical	16093310
MGA2_YEAST	MGA2	genetic	19325107
DPB3_YEAST	DPB3	genetic	27708008
SED1_YEAST	SED1	genetic	27708008
YCFI_YEAST	YCF1	genetic	27708008

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND MASSSPECTROMETRY.
PubMed: 17563356