GEK_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GEK_DROME
• UniProt AC: Q9W1B0
• Protein Name: Serine/threonine-protein kinase Genghis Khan
• Gene Name: gek
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1637
• Protein Description: Acts as a downstream effector for the regulation of actin polymerization by Cdc42..
• Protein Sequence: MEYESSEISDITTGSCKKRLTFLKCILSDTTSDQKWAAEFGEDTEGHQFSLDYLLDTFIVLYDECSNSSLRREKGVSDFLKLSKPFVHIVRKLRLSRDDFDILKIIGRGAFGEVCVVQMISTEKVYAMKILNKWEMLKRAETACFREERDVLVFGDRQWITNLHYAFQDNINLYLVMDYYCGGDLLTLLSKFEDKLPEDMAKFYITEMILAINSIHQIRYVHRDIKPDNVLLDKRGHVRLADFGSCLRLDKDGTVQSNVAVGTPDYISPEILRAMEDGKGRYGTECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHQNCFNLPSQETLNYKVSETSQDLLCKLICIPENRLGQNGIQDFMDHPWFVGIDWKNIRQGPAPYVPEVSSPTDTSNFDVDDNDVRLTDSIPPSANPAFSGFHLPFIGFTFSLTSSSTLDSKKNQSSGFGDDTLDTISSPQLAILPSNNSETPVDSVQLKALNDQLAALKQEKAELSKQHNEVFERLKTQDSELQDAISQRNIAMMEYSEVTEKLSELRNQKQKLSRQVRDKEEELDGAMQKNDSLRNELRKSDKTRRELELHIEDAVIEAAKEKKLREHAEDCCRQLQMELRKGSSSVETTMPLSISSEMSSYEIERLELQFSEKLSHQQTRHNMELEALREQFSELENANLALTKELQQTQERLKYTQMESITDSAETLLELKKQHDLEKSSWFEEKQRLSSEVNLKSKSLKELQAEDDEIFKELRMKREAITLWERQMAEIIQWVSDEKDARGYLQALATKMTEELEYLKHVGTFNNNGVDNKNWRNRRSQKLDKMELLNLQSALQREIQAKNMISDELSQTRSDLISTQKEVRDYKKRYDSILHDFQKKETELRDLQKGGLEYSESFLNKSTHHGLSSAFFRDMSKNSEIIDSAESFGNESGDNFTPNFFQSGNSGMLFNYEPKYAGKNNKDHSSMKEASVSDLSREESDQLVKESQKKVPGNTAIHQFLVRTFSSPTKCNHCTSLMVGLTRQGVVCEICGFACHTICCQKVPTTCPVPMDQTKRPLGIDPTRGIGTAYEGYVKVPKSGVIKRGWIRQFVVVCDFKLFLYDISPDRCALPSVSVSQVLDMRDPEFSVGSVRESDVIHAAKKDVPCIFKIKTALIDGGLSLNTLMLADNESEKSKWVIALGELHRILKRNSLPNTAIFKVNEILDNTLSLIRNALCSVIIYPNQILLGTEDGLFYINLDQYEIARIGESKKILQLWYIEEEQILVILCGKQRNLRLLPIRALEASDVEWIKVVESKNCISACTGIIRRFPNIVYSFIIALKRPNNHTQIVVYEINRTRTRHQKTCEFTIGYMAQHLQILSDMRLVVAHQSGFTAYFLRGEATAMSLVHPENQLCAFLNYSGVDAVRVIEILCPSGGNFGEYLLVFQTLAIYVDLQGRKSRDREIMYPAFPTYITFCDGHLLVFSDTHLDIFNTQTAEWVQSIGLKQSLPLNNLGNVVLSSVNDTPLIVYLSNIHTKGLLQYRDGNRKGLPSIKRRFSIREINKTIKSDRRSKMISAPTNFNHISHMGPGDGIQNQRLLDLPTTLETADQACSPIIHSLSCIPQSRKSNFLEQVDANSDDYGNDNIISRTPSPMASSFMDGLSNND

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
21	Phosphorylation	GSCKKRLTFLKCILS CCHHHHEEEHHHHHC	30.84	22817900
458	Phosphorylation	DTLDTISSPQLAILP CCCCCCCCCCEEECC	16.89	30478224
712	Phosphorylation	KQHDLEKSSWFEEKQ HHHCCHHCCHHHHHH	24.35	27794539
713	Phosphorylation	QHDLEKSSWFEEKQR HHCCHHCCHHHHHHH	47.02	27794539
722	Phosphorylation	FEEKQRLSSEVNLKS HHHHHHHHHHHCCCC	27.00	19429919
723	Phosphorylation	EEKQRLSSEVNLKSK HHHHHHHHHHCCCCC	50.59	19429919
838	Phosphorylation	IQAKNMISDELSQTR HHHHHCCCHHHHHHH	17.79	19429919
842	Phosphorylation	NMISDELSQTRSDLI HCCCHHHHHHHHHHH	27.71	19429919
844	Phosphorylation	ISDELSQTRSDLIST CCHHHHHHHHHHHHH	28.85	19429919
846	Phosphorylation	DELSQTRSDLISTQK HHHHHHHHHHHHHHH	39.91	19429919
850	Phosphorylation	QTRSDLISTQKEVRD HHHHHHHHHHHHHHH	31.89	19429919
851	Phosphorylation	TRSDLISTQKEVRDY HHHHHHHHHHHHHHH	36.34	19429919
864	Phosphorylation	DYKKRYDSILHDFQK HHHHHHHHHHHHHHH	20.36	19429919
886	Phosphorylation	LQKGGLEYSESFLNK HHHCCCCCCHHHHCC	23.84	19429919
887	Phosphorylation	QKGGLEYSESFLNKS HHCCCCCCHHHHCCC	19.86	19429919
894	Phosphorylation	SESFLNKSTHHGLSS CHHHHCCCCCCCCCH	31.72	19429919
895	Phosphorylation	ESFLNKSTHHGLSSA HHHHCCCCCCCCCHH	21.36	18327897
900	Phosphorylation	KSTHHGLSSAFFRDM CCCCCCCCHHHHHCC	24.98	21082442
963	Phosphorylation	HSSMKEASVSDLSRE CCHHCHHCHHHHCHH	24.20	22817900
1071	Phosphorylation	GYVKVPKSGVIKRGW EEEECCCCCEECCCC	32.02	22817900
1183	Phosphorylation	HRILKRNSLPNTAIF HHHHHHCCCCCCEEE	49.60	19429919
1374	Phosphorylation	YFLRGEATAMSLVHP EEECCCCHHHHHCCC	20.70	22668510
1377	Phosphorylation	RGEATAMSLVHPENQ CCCCHHHHHCCCHHC	25.44	22668510
1391	Phosphorylation	QLCAFLNYSGVDAVR CEEHHCCCCCCCEEE	14.67	22668510
1392	Phosphorylation	LCAFLNYSGVDAVRV EEHHCCCCCCCEEEE	31.13	22668510
1543	Phosphorylation	TIKSDRRSKMISAPT HHCCCHHHCCCCCCC	27.72	21082442
1578	Phosphorylation	DLPTTLETADQACSP CCCCHHHHHHHHHHH	38.35	22817900
1584	Phosphorylation	ETADQACSPIIHSLS HHHHHHHHHHHHHHH	23.34	22817900
1589	Phosphorylation	ACSPIIHSLSCIPQS HHHHHHHHHHCCCCC	16.15	21082442
1591	Phosphorylation	SPIIHSLSCIPQSRK HHHHHHHHCCCCCHH	17.02	21082442
1609	Phosphorylation	LEQVDANSDDYGNDN HHHHCCCCCCCCCCC	33.31	25749252
1612	Phosphorylation	VDANSDDYGNDNIIS HCCCCCCCCCCCCCC	23.87	19429919
1619	Phosphorylation	YGNDNIISRTPSPMA CCCCCCCCCCCCCCH	26.72	19429919
1621	Phosphorylation	NDNIISRTPSPMASS CCCCCCCCCCCCHHH	22.71	19429919
1623	Phosphorylation	NIISRTPSPMASSFM CCCCCCCCCCHHHHH	27.05	22668510

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GEK_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 GEK_DROME !!

Protein-Protein Interaction

Oops, there are no PPI records of GEK_DROME !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-1584, AND MASSSPECTROMETRY.
PubMed: 17372656

"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 THR-895, AND MASSSPECTROMETRY.
PubMed: 18327897