FOI_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FOI_DROME
• UniProt AC: Q9VSL7
• Protein Name: Zinc transporter foi
• Gene Name: foi {ECO:0000312|EMBL:AAF50401.3}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 706
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Required for the normal migration of longitudinal and peripheral glial cells. During larval development, required for the migration of the subretinal glia into the eye disk. During embryonic development, also controls the migration of muscle cells toward their attachment sites. Required in the mesoderm for the correct morphogenesis of embryonic gonad and for tracheal branch fusion during tracheal development. Shg may be cooperating with foi to mediate a common mechanism for gonad and tracheal morphogenesis. Acts as a zinc transporter in both yeast and mammalian cells..
• Protein Sequence: MARHIMAVCVVCLLCAHRLHCQDHIESLLGPARVTTHNSQDQLNARVYTNLSPSSETTDRRQQRSASGDDDTFNYSISPPSRREKRHAGHEHGPTSESRVPQITQYYLEKLMAQDELMNSSGFDGLLQQLSLHSLASGASEGTCVPGSRLVHHVQPHDHHHAHHHEEEDHSLQLNNCTLIQNGTTSNVICPSLPNNNTHPLGKEAKNFTLSDKDLLHLCPILLYELKAQSGGCIEPAILSDIDTTEELLEAEKDKDIFYVWIYAFISVFACGILGLVGVAIIPFMGSRYYKYIIQYLVALAVGTMTGDALLHLLPHSLAGQDERGMIMKGLGCLGGIIFFYVMEHALTMISEWRKSVEKKETKKPSRAKVMRDPDSSVNNSVAGDKICKQKYSSYPYCYDEITMNNKQSEWMHLPFDVAAGAGGDAPSVAELRNGVGDHDGSNDMAAAAESLISPLHTNCVEMNHHNHNHKHNSHQQNHEGQDSNTIVTDLDGNAVYAVNKAKDKDSRNDHVTVILREHESSHHGHSHRHGHVHSPPETLSAVAWMIIMGDGLHNFTDGMAIGAAFAENIAGGFSTSLAVFCHELPHELGDFAILIKAGMSVKSAVYYNLLTGVLSFIGMIFGIAFGQSQDVAQWMFAVAAGLFIYIALVDMMPEISASHKSLGQFLLQILGMLSGVGIMLLIALYEGDLMSAFGTAGAASHQHAH

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
74	N-linked_Glycosylation	SGDDDTFNYSISPPS CCCCCCCCCCCCCCC	31.56	-
119	N-linked_Glycosylation	MAQDELMNSSGFDGL HHCHHHHHCCCHHHH	45.72	-
176	N-linked_Glycosylation	DHSLQLNNCTLIQNG CCCEEECCCEECCCC	28.83	-
182	N-linked_Glycosylation	NNCTLIQNGTTSNVI CCCEECCCCCCCCEE	42.67	-
196	N-linked_Glycosylation	ICPSLPNNNTHPLGK ECCCCCCCCCCCCCH	53.49	-
207	N-linked_Glycosylation	PLGKEAKNFTLSDKD CCCHHCCCCCCCHHH	42.03	-
376	Phosphorylation	KVMRDPDSSVNNSVA HHHCCCCCCCCCCCC	41.39	22817900
377	Phosphorylation	VMRDPDSSVNNSVAG HHCCCCCCCCCCCCC	35.92	22817900
381	Phosphorylation	PDSSVNNSVAGDKIC CCCCCCCCCCCHHHH	14.24	22817900

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PNT1_DROME	pnt	genetic	9895324
PNT2_DROME	pnt	genetic	9895324
CADE_DROME	shg	genetic	16481356

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 Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-377 ANDSER-381, AND MASS SPECTROMETRY.
PubMed: 18327897