dbPTM

EYS_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EYS_DROME
UniProt AC	A0A1F4
Protein Name	Protein eyes shut
Gene Name	eys {ECO:0000312\|EMBL:ABJ09588.1, ECO:0000312\|FlyBase:FBgn0031414}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	2176
Subcellular Localization	Membrane Single-pass membrane protein . Secreted . Secreted by photoreceptor cells, through the stalk membrane into the interrhabdomeral space (IRS). Although secreted, lacks a canonical signal sequence and contains a predicted transmembrane domain
Protein Description	Essential for the formation of matrix-filled interrhabdomeral space: critical for the formation of epithelial lumina in the retina. Acts together with prominin (prom) and the cell adhesion molecule chaoptin (chp) to choreograph the partitioning of rhabdomeres into an open system..
Protein Sequence	MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLAAYACACPMGYTGINCEEEILICADNPCQNNALCLMEEGVPTCYCVPDYHGEKCEFQYDECQLGPRCMNGGVCIDGVDTFSCSCPPLLTGMLCECLMVGEESLDCNYTAPATQSPPRRTTTTSTMAPPTVRPVTPPETTVSPSRASEEVEIIVVTTSAPAEVVTSVLSPSSSSSSSEEGVSVEIKTPTVAPPESGSHSISVEQTTAVPAQPEPESEQEPESKPHPESESASESETETEEEIIPGTTARPPTSRSSSSSEESPSIFTTLPPLPGKPQTSASSESSGEVVTSEEYTTVPHFEVSGSKSESGSEEVTTVRPTAAPSITISVDITSSGSSSSSSESVEVFTTPAPVFVQRVTTIETSISIDYVTPTPLPETTTPRVVPVPRPTFAPEPPLDVVETTASTHHLWTEVPTTAAPFFTEYPAEVLITTHRTSAGRFTTVQPPAGVTTTSPTEDSSVELPTPHTPQIVVTILDSNEVIPSLITTTGSPTTHHHHHHHPHHEAEGTTLQPLEEDEHHHHHHHDEFTTPQPVEITTGHPLQTEDLIGVQEPAVVTTESPFAPAETTVVPVVVPATIAPLGTAAPPATPAPVPPATTTPPPSPPSLATETPTLPPTLPPVTLPPVTQPPPTIPPTPPSTQSAQTLPPPTSAINVYTTPDGPPTASQTKPSVTESSEEVEGTNTVSTGGRGSGGVPEEKAGDVDCIKLGCYNGGTCVTTSEGSRCVCRFDRQGPLCELPIIIRNAAFSGDSYVSHRIYKDIGGHESLDAVLPMHIQLKVRTRATNGLIMLAAAQGTKGGHYMALFLQKGLMQFQFSCGLQTMLLSELETPVNTGHEITIRAELDFSRNYTHCNASLLVNDTLAMSGDQPTWLKLLPPRLHTPEAILNTWLHLGGAPQAPIGLIIELPPAQSGSGFTGCLHTLRINGQAREIFGDALDGFGITECGSLACLSSPCRNGAACIKIETNDLDENGEKAEKWKCKCPTGYMGPTCEISVCEDNPCQYGGTCVQFPGSGYLCLCPLGKHGHYCEHNLEVALPSFSGSVNGLSSFVAYTVPIPLEYSLELSFKILPQTMSQISLLAFFGQSGYHDEKSDHLAVSFIQGYIMLTWNLGAGPRRIFTQKPIDFRLDAPRVPYEIKVGRIGRQAWLSVDGKFNITGRSPGSGSRMDVLPILYLGGHEIANFNTLPHDLPLHSGFQGCIYDVQLKAGQVTVPLQETRGVRGRGVGQCGTRECHRHACQHDGACLQHGATFTCICQEGWYGPLCAQPTNPCDSFNNKCYEDATCVPLVNGYECDCPVGRTGKNCEEVIRSLSDVSLTGRRSYLAVRWPYLYDGGDKLGAKRSQMVSYRNFTKKLMPPKPITTPSSHFVMKLLNEVEKQRSFSPVPLMGSKSFEEHHRVQFFFIEFQLRPLSERGLLLYFGTLNNNQDKKIGFVSLSLQGGVVEFRISGPSNHVTVVRSVRMLAIGEWHKIKMAQRGRWLTLWVEGSASSALAPSAEVLVEPDSLLYIGGLKDVSKLPHNAISGFPIPFRGCVRGLVVSGTRIVLNETNIVESRNIRDCDGTACGGDSCESGGHCWLDEKLQPHCICPEYAKGDRCEYSETCKLIPCKNNGRCLRSGRCSCPNGWGGFYCEIAMSKPTTPSFRGNSYLILPPPRIPMKDKRRGPSLYVRPREAIQVSLNFSTIEPDGLLLWSEHERSKFLGLGLEAGHLKLASNLLGSTNDTVRAPASGFIADGAWHWTSVLLDRSRLELQLDGEVIFTERLPEGGRSLGSTTPRSTLAGRRKNSSKEPTISYEDVFYLGGFPNSDSVSRRTKGRFFDPFKGCLQDIQFGAEPTAIISDFSTYQGENIGSCDLHGDEPLTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
163	N-linked_Glycosylation	GVCIDGLNSSYSCYC EEEECCCCCCCEEEE	34.14	-
205	N-linked_Glycosylation	VDGVAYYNCTCPEGF ECCEEEEECCCCCCC	11.27	-
425	N-linked_Glycosylation	GEESLDCNYTAPATQ CCCCCCCCCCCCCCC	36.54	-
1165	N-linked_Glycosylation	AELDFSRNYTHCNAS EEEECCCCCCCCCEE	44.87	-
1170	N-linked_Glycosylation	SRNYTHCNASLLVND CCCCCCCCEEEEECC	25.59	-
1176	N-linked_Glycosylation	CNASLLVNDTLAMSG CCEEEEECCEEHHCC	36.20	-
1471	N-linked_Glycosylation	LSVDGKFNITGRSPG EEECCEEEECCCCCC	34.10	17893096
1665	N-linked_Glycosylation	SQMVSYRNFTKKLMP HHCCCCCCCCCCCCC	40.48	-
1861	N-linked_Glycosylation	SGTRIVLNETNIVES ECCEEEECCCCCCCC	43.05	-
1994	N-linked_Glycosylation	EAIQVSLNFSTIEPD HEEEEEEECCCCCCC	22.71	-
2035	N-linked_Glycosylation	SNLLGSTNDTVRAPA HHHHCCCCCCEECCC	44.65	-
2099	N-linked_Glycosylation	TLAGRRKNSSKEPTI HHCCCCCCCCCCCCC	50.10	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of EYS_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EYS_DROME !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EYS_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CRB_DROME	crb	genetic	24705015

Drug and Disease Associations

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

Regulatory Network of EYS_DROME

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster."; Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.; Glycobiology 17:1388-1403(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1471, AND MASSSPECTROMETRY.	17893096 [Abstract]