KELC_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KELC_DROME
• UniProt AC: Q04652
• Protein Name: Ring canal kelch protein
• Gene Name: kel
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1477
• Subcellular Localization: Cytoplasm, cytoskeleton . Inner surface of cytoplasmic bridges or ring canals present in egg chambers. Subcortically in imaginal disk epithelia.
• Protein Description: Component of ring canals that regulates the flow of cytoplasm between cells. May be involved in the regulation of cytoplasm flow from nurse cells to the oocyte during oogenesis. Binds actin..
• Protein Sequence: MIALSALLTKYTIGIMSNLSNGNSNNNNQQQQQQQQGQNPQQPAQNEGGAGAEFVAPPPGLGAAVGVAAMQQRNRLLQQQQQQHHHHQNPAAEGSGLERGSCLLRYASQNSLDESSQKHVQRPNGKERGTVGQYSNEQHTARSFDAMNEMRKQKQLCDVILVADDVEIHAHRMVLASCSPYFYAMFTSFEESRQARITLQSVDARALELLIDYVYTATVEVNEDNVQVLLTAANLLQLTDVRDACCDFLQTQLDASNCLGIREFADIHACVELLNYAETYIEQHFNEVIQFDEFLNLSHEQVISLIGNDRISVPNEERVYECVIAWLRYDVPMREQFTSLLMEHVRLPFLSKEYITQRVDKEILLEGNIVCKNLIIEALTYHLLPTETKSARTVPRKPVGMPKILLVIGGQAPKAIRSVEWYDLREEKWYQAAEMPNRRCRSGLSVLGDKVYAVGGFNGSLRVRTVDVYDPATDQWANCSNMEARRSTLGVAVLNGCIYAVGGFDGTTGLSSAEMYDPKTDIWRFIASMSTRRSSVGVGVVHGLLYAVGGYDGFTRQCLSSVERYNPDTDTWVNVAEMSSRRSGAGVGVLNNILYAVGGHDGPMVRRSVEAYDCETNSWRSVADMSYCRRNAGVVAHDGLLYVVGGDDGTSNLASVEVYCPDSDSWRILPALMTIGRSYAGVCMIDKPMUMEEQGALARQAASLAIALLDDENSQAEGTMEGAIGGAIYGNLAPAGGAAAAAAPAAPAQAPQPNHPHYENIYAPIGQPSNNNNNSGSNSNQAAAIANANAPANAEEIQQQQQPAPTEPNANNNPQPPTAAAPAPSQQQQQQQAQPQQPQRILPMNNYRNDLYDRSAAGGVCSAYDVPRAVRSGLGYRRNFRIDMQNGNRCGSGLRCTPLYTNSRSNCQRQRSFDDTESTDGYNLPYAGAGTMRYENIYEQIRDEPLYRTSAANRVPLYTRLDVLGHGIGRIERHLSSSCGNIDHYNLGGHYAVLGHSHFGTVGHIRLNANGSGVAAPGVAGTGTCNVPNCQGYMTAAGSTVPVEYANVKVPVKNSASSFFSCLHGENSQSMTNIYKTSGTAAAMAAHNSPLTPNVSMERASRSASAGAAGSAAAAVEEHSAADSIPSSSNINANRTTGAIPKVKTANKPAKESGGSSTAASPILDKTTSTGSGKSVTLAKKTSTAAARSSSSGDTNGNGTLNRISKSSLQWLLVNKWLPLWIGQGPDCKVIDFNFMFSRDCVSCDTASVASQMSNPYGTPRLSGLPQDMVRFQSSCAGACAAAGAASTIRRDANASARPLHSTLSRLRNGEKRNPNRVAGNYQYEDPSYENVHVQWQNGFEFGRSRDYDPNSTYHQQRPLLQRARSESPTFSNQQRRLQRQGAQAQQQSQQPKPPGSPDPYKNYKLNADNNTFKPKPIAADELEGAVGGAVAEIALPEVDIEVVDPVSLSDNETETTSSQNNLPSTTNSNNLNEHND

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
106	Phosphorylation	RGSCLLRYASQNSLD CHHHHHHHHHCCCCC	15.58	29892262
108	Phosphorylation	SCLLRYASQNSLDES HHHHHHHHCCCCCHH	22.44	29892262
111	Phosphorylation	LRYASQNSLDESSQK HHHHHCCCCCHHHHH	29.57	25749252
627	Phosphorylation	RSVADMSYCRRNAGV CHHHCHHHHHHCCCE	5.37	11854310
1366	Phosphorylation	PLLQRARSESPTFSN HHHHHHHHCCCCCHH	41.25	25749252
1368	Phosphorylation	LQRARSESPTFSNQQ HHHHHHCCCCCHHHH	30.41	25749252

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KELC_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 KELC_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KELC_DROME	kel	physical	20065088
ACT4_DROME	Act79B	physical	11854310

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-108 AND SER-111, ANDMASS SPECTROMETRY.
PubMed: 18327897