dbPTM

SYEP_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYEP_DROME
UniProt AC	P28668
Protein Name	Bifunctional glutamate/proline--tRNA ligase
Gene Name	GluProRS {ECO:0000303\|PubMed:9063462, ECO:0000312\|FlyBase:FBgn0005674}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1714
Subcellular Localization
Protein Description	Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA..
Protein Sequence	MSIKLKANLNNPPISGLATAHLINGTVPVEIVWSKEETSLQFPDNRLLVCHSNNDVLRALARAAPDYKLYGETAIERTQIDHWLSFSLTCEDDISWALSFLDKSIAPVTYLVANKLTIADFALFNEMHSRYEFLAAKGIPQHVQRWYDLITAQPLIQKVLQSLPEDAKVKRSPQSSKEQTPAKTGERKQEGKFVDLPGAEMGKVVVRFPPEASGYLHIGHAKAALLNQYYALAFQGTLIMRFDDTNPAKETVEFENVILGDLEQLQIKPDVFTHTSNYFDLMLDYCVRLIKESKAYVDDTPPEQMKLEREQRVESANRSNSVEKNLSLWEEMVKGSEKGQKYCVRAKIDMSSPNGCMRDPTIYRCKNEPHPRTGTKYKVYPTYDFACPIVDAIENVTHTLRTTEYHDRDDQFYWFIDALKLRKPYIWSYSRLNMTNTVLSKRKLTWFVDSGLVDGWDDPRFPTVRGIIRRGMTVEGLKEFIIAQGSSKSVVFMNWDKIWAFNKKVIDPIAPRYTALEKEKRVIVNVAGAKVERIQVSVHPKDESLGKKTVLLGPRIYIDYVDAEALKEGENATFINWGNILIRKVNKDASGNITSVDAALNLENKDFKKTLKLTWLAVEDDPSAYPPTFCVYFDNIISKAVLGKDEDFKQFIGHKTRDEVPMLGDPELKKCKKGDIIQLQRRGFFKVDVAYAPPSGYTNVPSPIVLFSIPDGHTKDVPTSGLKVNAPDAKATKKASSPVSSSGQASELDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQTSASSAPVPAASSSSANDAVSVNASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGTVPTTAAPSASAAPSVGVNDSVAQILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGTTAPAPAAAPVKVKQEKNPDPASVLTVNTLLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVAPAPTTVNVIDLTGGDSGSDVGSVLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKSEPAVVKKEASPVSMASPAKDELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFPVAGRGGGGGGGSAKKAPKEAQPKPAKPVKKEPAADASGAVKKQTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISASGRAIQGATSHHLGQNFSKMFEIVYEDPETQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPCGITVNTKDDERAQLLDACKALEKRLVGGGVRCEGDYRDNYSPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQEDMTSHTKKVTNWTDFCGFLEQKNILLAPFCGEISCEDKIKADSARGEEAEPGAPAMGAKSLCIPFDQPAPIAASDKCINPSCTNKPKFYTLFGRSY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
172	Phosphorylation	EDAKVKRSPQSSKEQ CCCCCCCCCCCCCCC	22.90	19429919
175	Phosphorylation	KVKRSPQSSKEQTPA CCCCCCCCCCCCCCC	46.92	25749252
176	Phosphorylation	VKRSPQSSKEQTPAK CCCCCCCCCCCCCCC	34.66	22817900
180	Phosphorylation	PQSSKEQTPAKTGER CCCCCCCCCCCCCCC	26.72	27626673
306	Acetylation	DTPPEQMKLEREQRV CCCHHHHHHHHHHHH	47.06	21791702
503	Acetylation	DKIWAFNKKVIDPIA HHHHEEEHHHCCCCC	41.80	21791702
504	Acetylation	KIWAFNKKVIDPIAP HHHEEEHHHCCCCCC	45.59	21791702
783	Acetylation	VKKLLALKADYKSAT HHHHHHHHCCHHHCC	33.34	21791702
882	Ubiquitination	AAPSASAAPSVGVND CCCCCCCCCCCCCCH	8.39	31113955
1110	Phosphorylation	AVVKKEASPVSMASP CEEECCCCCCCCCCC	27.25	21082442
1113	Phosphorylation	KKEASPVSMASPAKD ECCCCCCCCCCCCHH	16.41	23607784
1116	Phosphorylation	ASPVSMASPAKDELT CCCCCCCCCCHHHHH	19.42	29892262
1123	Phosphorylation	SPAKDELTQEINAQG CCCHHHHHHHHHHHH	23.31	30478224
1181	Phosphorylation	GGGGGGGSAKKAPKE CCCCCCCCCCCCCCC	39.94	30478224
1599	Acetylation	IPLADVEKKIPALLE EEHHHHHHHHHHHHH	56.71	21791702
1600	Ubiquitination	PLADVEKKIPALLET EHHHHHHHHHHHHHH	40.18	31113955

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 SYEP_DROME !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYQ_DROME	Aats-gln	physical	22036573
NFS1_DROME	CG12264	physical	22036573
IDH3A_DROME	l(1)G0156	physical	22036573
SYRC_DROME	Aats-arg	physical	22036573
2AAA_DROME	Pp2A-29B	physical	22036573
CCD1P_DROME	Cyp12d1-p	physical	22036573
AIMP2_DROME	CG12304	physical	22036573
TCPG_DROME	Cctgamma	physical	22036573
COPB_DROME	betaCOP	physical	22036573
KRH2_DROME	Kr-h2	physical	22036573
ACADM_DROME	CG12262	physical	22036573
TERA_DROME	TER94	physical	22036573

Drug and Disease Associations

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

Regulatory Network of SYEP_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-1110, AND MASSSPECTROMETRY.	18327897 [Abstract]