KRI1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KRI1_DROME
• UniProt AC: Q9VTU0
• Protein Name: Protein KRI1 homolog
• Gene Name: CG5645
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 855
• Protein Sequence: MNNNLFEGSDDDGEDLQLSTNKDYAKTYNILRKKELLQKYKDRGLDVSESEFDSDSSSSEEDEVDPKFDQDFFKTLSSLKSKDPCIYDKGTKFFSESSGDEDDKDGEAPKKKKKAKPVTLKDYERKVILEHNGKFESSDEEQQEKEHEELQRAQSPSAVEEERRLKAEFRKVMNKEDDSEDEEFGGIFKKRSKTKEQTAAEEADFAKWLAGKQAEIQETDKKQLEPLKQYWSSNKLTQGESFLRDYILNKGYANTDESAIPTYDEIVGEAAPLSEDEQELEKQAEFEHKYNFRFEEPDADFIKRYPRTIEQSLRRTDDKRKEKRKELKERKDQEKQQKMKELELVKEMKRKEIDEKIRKLKAVTGNDELGFRDEELEEDFDPAAHDRRMQELFDDEYYNVDEGEEKPECPSDIDELVLEDWDNYDPRQHANGGGEDYEGHCEDDDFNMDCDYDPSTAKEQLQQELIENTRGRKGRKGRRNRFMEMIQAEKPAFNPEDEKTYSEYIDEYYQMDCEDIIGDQPCRFKYVETTPNDFGLTIEEILLAKNKELNQWASLKKAVQNRPEHVEKKEQRLYKMKAKNEDLKRKIFKSLYGEGSDDEEQPAEEKPEVTPAEATAPAENGQVSTEGLSKSKRKRLKRKAAAAAASAPKVLKEESDSKDPKEADGSTEDVQAESSKKKVDTPSKKGKDDANQETKNSPQSTEKTKNNNALKNNKKEPKNVQNGFQKPQNQANKSAKTKSNQPFKTTESAPAKAEKSNGNNPFNKPQSKSQQRQELPPIHKNQGGNKKGPRNANGTNPFKKSNQKPSAPFPAKKTNNFKAKNKQNNNSGITDDRLKAYGINPRKFHKREKYGKKDN

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
9	Phosphorylation	NNNLFEGSDDDGEDL CCCCCCCCCCCCCCC	30.57	19429919
95	Phosphorylation	DKGTKFFSESSGDED CCCCCEECCCCCCCC	39.44	19429919
97	Phosphorylation	GTKFFSESSGDEDDK CCCEECCCCCCCCCC	38.12	19429919
98	Phosphorylation	TKFFSESSGDEDDKD CCEECCCCCCCCCCC	46.33	19429919
137	Phosphorylation	EHNGKFESSDEEQQE HCCCCCCCCHHHHHH	46.34	19429919
138	Phosphorylation	HNGKFESSDEEQQEK CCCCCCCCHHHHHHH	41.67	19429919
155	Phosphorylation	EELQRAQSPSAVEEE HHHHHCCCHHHHHHH	21.60	19429919
157	Phosphorylation	LQRAQSPSAVEEERR HHHCCCHHHHHHHHH	50.63	19429919
179	Phosphorylation	VMNKEDDSEDEEFGG HHCCCCCCCCCCCCH	60.30	21082442
252	Phosphorylation	DYILNKGYANTDESA HHHHHCCCCCCCCCC	9.78	23607784
255	Phosphorylation	LNKGYANTDESAIPT HHCCCCCCCCCCCCC	32.73	23607784
258	Phosphorylation	GYANTDESAIPTYDE CCCCCCCCCCCCHHH	34.02	23607784
262	Phosphorylation	TDESAIPTYDEIVGE CCCCCCCCHHHHHCC	37.18	23607784
263	Phosphorylation	DESAIPTYDEIVGEA CCCCCCCHHHHHCCC	13.26	23607784
274	Phosphorylation	VGEAAPLSEDEQELE HCCCCCCCCCHHHHH	41.78	19429919
590	Phosphorylation	LKRKIFKSLYGEGSD HHHHHHHHHHCCCCC	18.97	27794539
596	Phosphorylation	KSLYGEGSDDEEQPA HHHHCCCCCCCCCCC	37.27	19429919
697	Phosphorylation	ANQETKNSPQSTEKT CCHHCCCCCCHHHHH	26.35	21082442
795	Phosphorylation	GPRNANGTNPFKKSN CCCCCCCCCCCCCCC	39.25	22817900

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

Oops, there are no upstream regulatory protein records of KRI1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KRI1_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 KRI1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

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-95; SER-97; SER-98;SER-137 AND SER-138, AND MASS SPECTROMETRY.
PubMed: 18327897

"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-179, AND MASSSPECTROMETRY.
PubMed: 17372656