dbPTM

TTC14_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTC14_DROME
UniProt AC	Q9VGU5
Protein Name	Tetratricopeptide repeat protein 14 homolog
Gene Name	CG6621
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	872
Subcellular Localization
Protein Description
Protein Sequence	MNFDYIGQALGYHGQPLQKIWDDERGVDDLRLMGLTQVNYGVYQERQKYFTFQERAKRLKMHQFLARKATDLYDRTLVANVMEDSLLAQGNTYMTQMAPFEFFLNVKDKRKGWAHRLSALKQGDIIYTQVTRLASGNRLIVKPLCTAEPKHAYLADIPIKAVILQDFWGPLPLDKQGNPRSFVQNDILRCEINNISADTERLSLNMIGMFNKVPDLKFGLCDFKELPKYYSKIHNLDHPSASHYEDELNKALEFENPNYDLLFQMNGLQPNENLSLMSYLRAGFPEEENAAELRQKQASQWAFRSVADGIEHFKNGQQVEAFQCLNKALNIDPRNVEALVARGALYANRGSFLKGLQDFEKALHLNKYHVNARKYMGETLVALGRSYEEENRIAEAVKAYSDCLNLLPLHEEARQSLDALHRSGDGKRRISTEPSNMTGGQSSDESSSSSASDSECEDSAGKPKSNISQPFYAQHKLKQSGDEKLAVIDAHKANEFRLDDDETVSSVRKLLREASKHKKAKKKGKKKKDKKERRRSRTKSETEDPIELLKKIDFQEALRQDNKLMNSTRSDEERKAKIKSYLKEGGKESPPPPPPMKKTAVSSRKSSFDNVGPSTSRHAASVVGFGGAQPPPAPKFLGQKKHPEPAPKLSFQIKKRPLQMDKLGMLRLAAPAEPLKGGRSSSSRSRSRSRSRSRSRSRNRRLGRSTRSSLRSRRSGSRSRSISRSRSRRRRTYSRSRSPSPRSYGNRFVIGRYRNRRTRRSRSFHRRRSPSPILKRRSPSPFVPRRTPSPASRYRRSRSRSRSRSRSRSPRRFQSRYMPRDRGSVNRSRYSWHNPHKRSVSRTVEPNGKDERAATPPKKGVADDRSGREERA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
536	Phosphorylation	DKKERRRSRTKSETE CHHHHHHHHCCCCCC	42.35	19429919
538	Phosphorylation	KERRRSRTKSETEDP HHHHHHHCCCCCCCH	39.92	19429919
540	Phosphorylation	RRRSRTKSETEDPIE HHHHHCCCCCCCHHH	49.49	19429919
542	Phosphorylation	RSRTKSETEDPIELL HHHCCCCCCCHHHHH	53.42	22668510
589	Phosphorylation	LKEGGKESPPPPPPM HHHCCCCCCCCCCCC	46.31	22817900
606	Phosphorylation	TAVSSRKSSFDNVGP CCCCCCCCCCCCCCC	34.82	18327897
607	Phosphorylation	AVSSRKSSFDNVGPS CCCCCCCCCCCCCCC	39.39	19429919
761	Phosphorylation	RNRRTRRSRSFHRRR CCCCCHHCHHCCCCC	29.05	25749252
763	Phosphorylation	RRTRRSRSFHRRRSP CCCHHCHHCCCCCCC	27.01	25749252
769	Phosphorylation	RSFHRRRSPSPILKR HHCCCCCCCCCCCCC	28.11	19429919
771	Phosphorylation	FHRRRSPSPILKRRS CCCCCCCCCCCCCCC	26.31	19429919
778	Phosphorylation	SPILKRRSPSPFVPR CCCCCCCCCCCCCCC	33.49	19429919
780	Phosphorylation	ILKRRSPSPFVPRRT CCCCCCCCCCCCCCC	32.01	19429919
787	Phosphorylation	SPFVPRRTPSPASRY CCCCCCCCCCHHHHH	29.42	22817900
789	Phosphorylation	FVPRRTPSPASRYRR CCCCCCCCHHHHHHH	32.27	22817900
805	Phosphorylation	RSRSRSRSRSRSPRR HCCCCCCCCCCCCHH	35.54	19429919
807	Phosphorylation	RSRSRSRSRSPRRFQ CCCCCCCCCCCHHHH	38.05	19429919
809	Phosphorylation	RSRSRSRSPRRFQSR CCCCCCCCCHHHHHC	24.81	19429919
824	Phosphorylation	YMPRDRGSVNRSRYS CCCCCCCCCCHHHCC	19.67	25749252
841	Phosphorylation	NPHKRSVSRTVEPNG CCCCCCCCCEECCCC	24.39	25749252
843	Phosphorylation	HKRSVSRTVEPNGKD CCCCCCCEECCCCCC	23.01	25749252
849	Acetylation	RTVEPNGKDERAATP CEECCCCCCCCCCCC	64.16	21791702
855	Phosphorylation	GKDERAATPPKKGVA CCCCCCCCCCCCCCC	38.86	22817900

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 TTC14_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TTC14_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 TTC14_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions

Drug and Disease Associations

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

Regulatory Network of TTC14_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-536; THR-538; SER-540;SER-606; SER-607; SER-769; SER-771; SER-778 AND SER-780, AND MASSSPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538 AND SER-540, ANDMASS SPECTROMETRY.	17372656 [Abstract]