KRI1_DROME - dbPTM
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
Subcellular Localization
Protein Description
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 Orthologous
Protein Cluster
9PhosphorylationNNNLFEGSDDDGEDL
CCCCCCCCCCCCCCC
30.5719429919
95PhosphorylationDKGTKFFSESSGDED
CCCCCEECCCCCCCC
39.4419429919
97PhosphorylationGTKFFSESSGDEDDK
CCCEECCCCCCCCCC
38.1219429919
98PhosphorylationTKFFSESSGDEDDKD
CCEECCCCCCCCCCC
46.3319429919
137PhosphorylationEHNGKFESSDEEQQE
HCCCCCCCCHHHHHH
46.3419429919
138PhosphorylationHNGKFESSDEEQQEK
CCCCCCCCHHHHHHH
41.6719429919
155PhosphorylationEELQRAQSPSAVEEE
HHHHHCCCHHHHHHH
21.6019429919
157PhosphorylationLQRAQSPSAVEEERR
HHHCCCHHHHHHHHH
50.6319429919
179PhosphorylationVMNKEDDSEDEEFGG
HHCCCCCCCCCCCCH
60.3021082442
252PhosphorylationDYILNKGYANTDESA
HHHHHCCCCCCCCCC
9.7823607784
255PhosphorylationLNKGYANTDESAIPT
HHCCCCCCCCCCCCC
32.7323607784
258PhosphorylationGYANTDESAIPTYDE
CCCCCCCCCCCCHHH
34.0223607784
262PhosphorylationTDESAIPTYDEIVGE
CCCCCCCCHHHHHCC
37.1823607784
263PhosphorylationDESAIPTYDEIVGEA
CCCCCCCHHHHHCCC
13.2623607784
274PhosphorylationVGEAAPLSEDEQELE
HCCCCCCCCCHHHHH
41.7819429919
590PhosphorylationLKRKIFKSLYGEGSD
HHHHHHHHHHCCCCC
18.9727794539
596PhosphorylationKSLYGEGSDDEEQPA
HHHHCCCCCCCCCCC
37.2719429919
697PhosphorylationANQETKNSPQSTEKT
CCHHCCCCCCHHHHH
26.3521082442
795PhosphorylationGPRNANGTNPFKKSN
CCCCCCCCCCCCCCC
39.2522817900

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 KRI1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KRI1_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 KRI1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

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