F10A2_DROME - dbPTM
F10A2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F10A2_DROME
UniProt AC Q86DS1
Protein Name Hsc70-interacting protein 2 {ECO:0000250|UniProtKB:P50503, ECO:0000312|EMBL:AAP31294.1}
Gene Name HIP-R {ECO:0000303|PubMed:19333534}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 377
Subcellular Localization Cytoplasm .
Protein Description One HIP oligomer binds the ATPase domains of at least two Hsc70 molecules dependent on activation of the Hsc70 ATPase by Hsp40. Stabilizes the ADP state of Hsc70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of Hsc70 with various target proteins (By similarity)..
Protein Sequence MAFTMQTGDLKKLKYFIDFALENPTFLNMPQLQFVKDFVEKFGGTVPPGQFNGGSAGGKCPFGGVAGAKANEPANAPEDSEDEKSLSDPESDVELDMEGVIEADSDPAQPMGNYSKKATEEEVEQASELRAQAASAYGQQKFDEAIALYTKAIELSPGNALFHAKRGQAFLKLKKPNACIRDCDVALELNSDLAAGYKFRGRARRLLGDFELAAHDLRQACKLDFDEETDEWLKEVTPNAKKIEQHRLKQERRQAERKIKERQRDQRRARKEQEKHNASSGGSSGEFSGGNPGNGNMSDILGAMSDPEVSAAIQDILSNPGNITKYASNPKIYNLIKKIVPGGDVGAAFGQAGEKAGKPSEPKPKKDSADFVDDGLD
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
80PhosphorylationPANAPEDSEDEKSLS
CCCCCCCCCCHHHCC
45.3321082442
85PhosphorylationEDSEDEKSLSDPESD
CCCCCHHHCCCCCCC
30.9319429919
87PhosphorylationSEDEKSLSDPESDVE
CCCHHHCCCCCCCCE
59.2019429919
91PhosphorylationKSLSDPESDVELDME
HHCCCCCCCCEECCC
52.9619429919
156PhosphorylationYTKAIELSPGNALFH
HHHCHHCCCCCHHHE
20.2619429919
368PhosphorylationEPKPKKDSADFVDDG
CCCCCCCCCCCCCCC
38.3219429919

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 F10A2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F10A2_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 F10A2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCYDB_DROMEGyc-89Dbphysical
22036573
Y5902_DROMECG5902physical
22036573
VNNL1_DROMEvanin-likephysical
22036573
GCYDA_DROMEGyc-89Daphysical
22036573
OTU1_DROMECG4603physical
22036573
PANG1_DROMEpanphysical
22036573
PANG2_DROMEpanphysical
22036573
TAD2B_DROMEAda2bphysical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F10A2_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-80, AND MASSSPECTROMETRY.

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