PPN_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PPN_DROME
• UniProt AC: Q868Z9
• Protein Name: Papilin
• Gene Name: Ppn
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2898
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane .
• Protein Description: Essential extracellular matrix (ECM) protein that influences cell rearrangements. May act by modulating metalloproteinases action during organogenesis. Able to non-competitively inhibit procollagen N-proteinase, an ADAMTS metalloproteinase..
• Protein Sequence: MDLSRRLCSTALVAFIVLASIHDSQSRFPGLRQKRQYGANMYLPESSVTPGGEGNDPDEWTPWSSPSDCSRTCGGGVSYQTRECLRRDDRGEAVCSGGSRRYFSCNTQDCPEEESDFRAQQCSRFDRQQFDGVFYEWVPYTNAPNPCELNCMPKGERFYYRQREKVVDGTRCNDKDLDVCVNGECMPVGCDMMLGSDAKEDKCRKCGGDGSTCKTIRNTITTKDLAPGYNDLLLLPEGATNIRIEETVPSSNYLACRNHSGHYYLNGDWRIDFPRPMFFANSWWNYQRKPMGFAAPDQLTCSGPISESLFIVMLVQEKNISLDYEYSIPESLSHSQQDTHTWTHHQFNACSASCGGGSQSRKVTCNNRITLAEVNPSLCDQKSKPVEEQACGTEPCAPHWVEGEWSKCSKGCGSDGFQNRSITCERISSSGEHTVEEDAVCLKEVGNKPATKQECNRDVKNCPKYHLGPWTPCDKLCGDGKQTRKVTCFIEENGHKRVLPEEDCVEEKPETEKSCLLTPCEGVDWIISQWSGCNACGQNTETRTAICGNKEGKVYPEEFCEPEVPTLSRPCKSPKCEAQWFSSEWSKCSAPCGKGVKSRIVICGEFDGKTVTPADDDSKCNKETKPESEQDCEGEEKVCPGEWFTGPWGKCSKPCGGGERVREVLCLSNGTKSVNCDEEKVEPLSEKCNSEACTEDEILPLTSTDKPIEDDEEDCDEDGIELISDGLSDDEKSEDVIDLEGTAKTETTPEAEDLMQSDSPTPYDEFESTGTTFEGSGYDSESTTDSGISTEGSGDDEETSEASTDLSSSTDSGSTSSDSTSSDSSSSISSDATSEAPASSVSDSSDSTDASTETTGVSDDSTDVSSSTEASASESTDVSGASDSTGSTNASDSTPESSTEASSSTDDSTDSSDNSSNVSESSTEASSSSVSDSNDSSDGSTDGVSSTTENSSDSTSDATSDSTASSDSTDSTSDQTTETTPESSTDSTESSTLDASSTTDASSTSESSSESSTDGSSTTSNSASSETTGLSSDGSTTDATTAASDNTDITTDGSTDESTDGSSNASTEGSTEGASEDTTISTESSGSTESTDAIASDGSTTEGSTVEDLSSSTSSDVTSDSTITDSSPSTEVSGSTDSSSSTDGSSTDASSTEASSTDVTESTDSTVSGGTSDTTESGPTEESTTEGSTESTTEGSTDSTQSTDLDSTTSDIWSTSDKDDESESSTPYSFDSEVTKSKPRKCKPKKSTCAKSEYGCCPDGKSTPKGPFDEGCPIAKTCADTKYGCCLDGVSPAKGKNNKGCPKSQCAETLFGCCPDKFTAADGENDEGCPETTTVPPTTTTEETQPETTTEIEGSGQDSTTSEPDTKKSCSFSEFGCCPDAETSAKGPDFEGCGLASPVAKGCAESENGCCPDGQTPASGPNGEGCSGCTRERFGCCPDSQTPAHGPNKEGCCLDTQFGCCPDNILAARGPNNEGCECHYTPYGCCPDNKSAATGYNQEGCACETTQYGCCPDKITAAKGPKHEGCPCETTQFGCCPDGLTFAKGPHHHGCHCTQTEFKCCDDEKTPAKGPNGDGCTCVESKFGCCPDGVTKATDEKFGGCENVQEPPQKACGLPKETGTCNNYSVKYYFDTSYGGCARFWYGGCDGNDNRFESEAECKDTCQDYTGKHVCLLPKSAGPCTGFTKKWYFDVDRNRCEEFQYGGCYGTNNRFDSLEQCQGTCAASENLPTCEQPVESGPCAGNFERWYYDNETDICRPFTYGGCKGNKNNYPTEHACNYNCRQPGVLKDRCALPKQTGDCSEKLAKWHFSESEKRCVPFYYSGCGGNKNNFPTLESCEDHCPRQVAKDICEIPAEVGECANYVTSWYYDTQDQACRQFYYGGCGGNENRFPTEESCLARCDRKPEPTTTTPATRPQPSRQDVCDEEPAPGECSTWVLKWHFDRKIGACRQFYYGNCGGNGNRFETENDCQQRCLSQEPPAPTPPRAPAPTRQPDPAPTVAQCSQPADPGQCDKWALHWNYNETEGRCQSFYYGGCGGNDNRFATEEECSARCSVNIDIRIGADPVEHDTSKCFLAFEPGNCYNNVTRWFYNSAEGLCDEFVYTGCGGNANNYATEEECQNECNDAQTTCALPPVRGRCSDLSRRWYFDERSGECHEFEFTGCRGNRNNFVSQSDCLNFCIGEPVVEPSAPTYSVCAEPPEAGECDNRTTAWFYDSENMACTAFTYTGCGGNGNRFETRDQCERQCGEFKGVDVCNEPVTTGPCTDWQTKYYFNTASQACEPFTYGGCDGTGNRFSDLFECQTVCLAGREPRVGSAKEICLLPVATGRCNGPSVHERRWYYDDEAGNCVSFIYAGCSGNQNNFRSFEACTNQCRPEPNKQDNEIGQNPCDTFDAECQELRCPYGVRRVAARSQPECTQCICENPCEGYSCPEGQQCAIDVASSDDRQFAPVCRDIYKPGECPALSANASGCARECYTDADCRGDNKCCSDGCGQLCVHPARPTQPPRTQAPVVSYPGDARAALEPKEAHELDVQTAIGGIAVLRCFATGNPAPNITWSLKNLVINTNKGRYVLTANGDLTIVQVRQTDDGTYVCVASNGLGEPVRREVALQVTEPVSQPAYIYGDKNVTQIVELNRPAVIRCPAGGFPEPHVSWWRNGQMFGLKNNLMARDYSLVFNSIQLSDLGLYTCEVYNQRRPVSLRVTLKAVGPVRPLSPEEEQYMQYVLNPATRPVTQRPSYPYRPTRPAYVPEPTVNVHAVLALEPKNSYTPGSTIVMSCSVQGYPEPNVTWIKDDVPLYNNERVQITYQPHRLVLSDVTSADSGKYTCRASNAYTYANGEANVSIQSVVPVSPECVDNPYFANCKLIVKGRYCSNPYYTQFCCRSCTLAGQVASPPLHPNAV

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
258	N-linked_Glycosylation	SNYLACRNHSGHYYL CCEEEEECCCCCEEE	33.29	-
319	N-linked_Glycosylation	VMLVQEKNISLDYEY EEEEECCCEECEEEE	28.47	-
419	N-linked_Glycosylation	CGSDGFQNRSITCER CCCCCCCCCCEEEEE	37.09	-
669	N-linked_Glycosylation	REVLCLSNGTKSVNC EEEEEECCCCEECCC	49.56	17893096
889	N-linked_Glycosylation	SDSTGSTNASDSTPE CCCCCCCCCCCCCCC	38.86	-
914	N-linked_Glycosylation	DSTDSSDNSSNVSES CCCCCCCCCCCCCCC	49.65	-
917	N-linked_Glycosylation	DSSDNSSNVSESSTE CCCCCCCCCCCCCCC	40.95	-
950	N-linked_Glycosylation	GVSSTTENSSDSTSD CCCCCCCCCCCCCCC	44.73	-
1064	N-linked_Glycosylation	ESTDGSSNASTEGST CCCCCCCCCCCCCCC	39.34	-
1489	N-linked_Glycosylation	PYGCCPDNKSAATGY CCCCCCCCCCCCCCC	25.89	-
1623	N-linked_Glycosylation	KETGTCNNYSVKYYF CCCCCCCCCEEEEEE	32.38	-
1750	N-linked_Glycosylation	FERWYYDNETDICRP CEEEEECCCCCCCCC	37.64	-
2020	N-linked_Glycosylation	WALHWNYNETEGRCQ EEEEECCCCCCCCEE	46.64	-
2083	N-linked_Glycosylation	EPGNCYNNVTRWFYN CCCCCCCHHHHHHHH	15.29	-
2205	N-linked_Glycosylation	PEAGECDNRTTAWFY CCCCCCCCCCEEEEE	55.65	-
2465	N-linked_Glycosylation	ECPALSANASGCARE CCCCCCCCCCCCCCC	31.12	-
2552	N-linked_Glycosylation	ATGNPAPNITWSLKN HCCCCCCCCEEEEEE	46.56	-
2625	N-linked_Glycosylation	AYIYGDKNVTQIVEL EEEECCCCEEEEEEE	46.97	-
2784	N-linked_Glycosylation	VQGYPEPNVTWIKDD ECCCCCCCEEEEECC	42.04	-
2838	N-linked_Glycosylation	TYANGEANVSIQSVV EECCCEECEEEEEEE	24.62	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PPN_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 PPN_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BICC_DROME	BicC	physical	14605208
RS3_DROME	RpS3	physical	14605208
PYG_DROME	GlyP	physical	14605208
AXN_DROME	Axn	physical	14605208
AKIRN_DROME	akirin	physical	14605208
NUP54_DROME	Nup54	physical	14605208

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-669, AND MASSSPECTROMETRY.
PubMed: 17893096