UniProt ID | F10A1_DROME | |
---|---|---|
UniProt AC | C4NYP8 | |
Protein Name | Hsc70-interacting protein 1 {ECO:0000303|PubMed:19333534} | |
Gene Name | HIP {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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
80 | Phosphorylation | PANAPEDSEDEKSLS CCCCCCCCCCHHHCC | 45.33 | 21082442 | |
85 | Phosphorylation | EDSEDEKSLSDPESD CCCCCHHHCCCCCCC | 30.93 | 19429919 | |
87 | Phosphorylation | SEDEKSLSDPESDVE CCCHHHCCCCCCCCE | 59.20 | 19429919 | |
91 | Phosphorylation | KSLSDPESDVELDME HHCCCCCCCCEECCC | 52.96 | 19429919 | |
156 | Phosphorylation | YTKAIELSPGNALFH HHHCHHCCCCCHHHE | 20.26 | 19429919 | |
368 | Phosphorylation | EPKPKKDSADFVDDG CCCCCCCCCCCCCCC | 38.32 | 19429919 |
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 F10A1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of F10A1_DROME !! |
* 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 F10A1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GCYDB_DROME | Gyc-89Db | physical | 22036573 | |
Y5902_DROME | CG5902 | physical | 22036573 | |
VNNL1_DROME | vanin-like | physical | 22036573 | |
GCYDA_DROME | Gyc-89Da | physical | 22036573 | |
OTU1_DROME | CG4603 | physical | 22036573 | |
PANG1_DROME | pan | physical | 22036573 | |
PANG2_DROME | pan | physical | 22036573 | |
TAD2B_DROME | Ada2b | physical | 22036573 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |