SULF1_DROME - dbPTM
SULF1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SULF1_DROME
UniProt AC Q9VEX0
Protein Name Extracellular sulfatase SULF-1 homolog
Gene Name Sulf1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1114
Subcellular Localization Endoplasmic reticulum. Golgi apparatus, Golgi stack. Cell surface. Also localized on the cell surface..
Protein Description
Protein Sequence MMRHSSLRLIIGGLILLLFVLNVFSKEQGSHSHKRSHSAKRFSRDSNSARERRPNIILILTDDQDVELGSLNFMPRTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSSPQWQATHETRSYATYLSNAGYRTGYFGKYLNKYNGSYIPPGWREWGGLIMNSKYYNYSINLNGQKIKHGFDYAKDYYPDLIANDSIAFLRSSKQQNQRKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHHTPSYDHAPNPDKQWILRVTEPMQPVHKRFTNLLMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFDVRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRDNWPDSFLIESSGRRETAEQIAESRARLQIERRNMKLANSSLLEDFLEGAGESTTIVSSSSTAATLMSSTAQQPEDGEEEVETDNEEDDVDGDGAMDSSAAALEEDDLDDAAFEEGDEELDQEFQQNNDLPLAPYITKMMRLNSECSDPALLKNCLPGQKWKCVNEEGRWRKHKCKFHLQLEHQLAAMPRKQYQRNCACFTPDGVVYTKIRAPSAGLHRVNKRTHNGPGRRRNKREVFHTELPDEMEELLDLHQVVDQLVDHTHRSKRDLPASSNETIAQVIQQIQSTLEILELKFNEHELHASNSSGNSYERGEKYTKSGGHRCFVDATTAKVNCSNVIYDDEKTWRTSRTQIDMLIKLLKDKIGKLKEMKKQLRESNKQALAAGRRNDNRRRNDQSVLDSGAGPEFNMSYFTEISSTPRSNVVGQTEVFQGYGSASAFDSLEQTQSHRFTPRAECYCEPDVGENHADSKEMAREARRKLKEERQRKKERKRIKKARLEKECLSEKMNCFSHDNQHWRTAPLWNDSPFCFCMNANNNTYSCLRTINGTHNFLYCEFTTGLITFYNLTIDRFETINRAAGLTPGERSHMHDALDQLKSCRGRSCSIRRHQNHLEGGSSAPLLPINQVHRNNKRKHSPLAGAVGNYAFVGPRLDMEALPPIKRRKLSKYNRLTGSQQSHMKRRPWKQTPLQQSPRFLRTHSVTPAQA
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 Orthologous
Protein Cluster
983-oxoalanine (Cys)AYTTTPMCCPARSSL
EEECCCCCCCCCHHH
2.37-
98OxidationAYTTTPMCCPARSSL
EEECCCCCCCCCHHH
2.37-
122N-linked_GlycosylationMVFTNNDNCSSPQWQ
EEEECCCCCCCCCHH
29.69-
159N-linked_GlycosylationGKYLNKYNGSYIPPG
HHHHHHCCCCCCCCC
34.25-
181N-linked_GlycosylationIMNSKYYNYSINLNG
EEECCEEEEEEECCC
22.45-
208N-linked_GlycosylationYYPDLIANDSIAFLR
HCCHHHHCCHHHHHH
36.25-
251N-linked_GlycosylationQYSHLFFNVTTHHTP
CCEEEEEEEECCCCC
23.92-
387PhosphorylationLDMGGVPTPQHMDGR
CCCCCCCCCCCCCCC
32.9222817900
447N-linked_GlycosylationRRNMKLANSSLLEDF
HHCHHHCCCHHHHHH
42.44-
683N-linked_GlycosylationRDLPASSNETIAQVI
CCCCCCCHHHHHHHH
48.19-
713N-linked_GlycosylationEHELHASNSSGNSYE
CEEEEECCCCCCCCC
40.76-
743N-linked_GlycosylationDATTAKVNCSNVIYD
ECCCCEEECCCCEEC
23.8517893096
817N-linked_GlycosylationSGAGPEFNMSYFTEI
CCCCCCCCHHHEEEC
19.48-
945N-linked_GlycosylationCFCMNANNNTYSCLR
EEEEECCCCEEEEEE
39.55-
955N-linked_GlycosylationYSCLRTINGTHNFLY
EEEEEECCCCCCEEE
49.01-
974N-linked_GlycosylationTGLITFYNLTIDRFE
CCEEEEEEEEECCHH
26.90-

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 SULF1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SULF1_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 SULF1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DALY_DROMEdallygenetic
20637191
DALY_DROMEdallygenetic
21305649

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SULF1_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-743, AND MASSSPECTROMETRY.

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