| UniProt ID | F10A1_MOUSE | |
|---|---|---|
| UniProt AC | Q99L47 | |
| Protein Name | Hsc70-interacting protein | |
| Gene Name | St13 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 371 | |
| 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 | MDPRKVSELRAFVKMCRQDPSVLHTEEMRFLREWVESMGGKVPPATHKAKSEENTKEEKRDKTTEENIKTEELSSEESDLEIDNEGVIEPDTDAPQEMGDENAEITEEMMDEANEKKGAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALACKLDYDEDASAMLREVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHERAQREEEARRQSGSQYGSFPGGFPGGMPGNFPGGMPGMGGAMPGMAGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPSNMSKYQSNPKVMNLISKLSAKFGGQS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 14 | Malonylation | SELRAFVKMCRQDPS HHHHHHHHHHHCCCC | 26.31 | 26320211 | |
| 14 | Ubiquitination | SELRAFVKMCRQDPS HHHHHHHHHHHCCCC | 26.31 | - | |
| 74 | Phosphorylation | NIKTEELSSEESDLE HHHHHHHCCCCCCCC | 38.70 | 29899451 | |
| 75 | Phosphorylation | IKTEELSSEESDLEI HHHHHHCCCCCCCCC | 58.99 | 29899451 | |
| 78 | Phosphorylation | EELSSEESDLEIDNE HHHCCCCCCCCCCCC | 43.36 | 29899451 | |
| 117 | Malonylation | MDEANEKKGAAIEAL HHHHHHHCCHHHHHC | 47.83 | 26320211 | |
| 117 | Ubiquitination | MDEANEKKGAAIEAL HHHHHHHCCHHHHHC | 47.83 | - | |
| 141 | Ubiquitination | DLFTDAIKLNPRLAI HHHHHHHHHCHHHHH | 43.88 | - | |
| 152 | Ubiquitination | RLAILYAKRASVFVK HHHHHHHHHCCEEEE | 34.63 | - | |
| 152 | Malonylation | RLAILYAKRASVFVK HHHHHHHHHCCEEEE | 34.63 | 26320211 | |
| 152 | Succinylation | RLAILYAKRASVFVK HHHHHHHHHCCEEEE | 34.63 | 23806337 | |
| 152 | Acetylation | RLAILYAKRASVFVK HHHHHHHHHCCEEEE | 34.63 | 22826441 | |
| 155 | Phosphorylation | ILYAKRASVFVKLQK HHHHHHCCEEEECCC | 21.81 | 23684622 | |
| 159 | Malonylation | KRASVFVKLQKPNAA HHCCEEEECCCCCHH | 33.46 | 26320211 | |
| 159 | Ubiquitination | KRASVFVKLQKPNAA HHCCEEEECCCCCHH | 33.46 | - | |
| 159 | Acetylation | KRASVFVKLQKPNAA HHCCEEEECCCCCHH | 33.46 | 21728379 | |
| 162 | Ubiquitination | SVFVKLQKPNAAIRD CEEEECCCCCHHHCC | 51.15 | 27667366 | |
| 170 | Glutathionylation | PNAAIRDCDRAIEIN CCHHHCCCCCCEECC | 2.47 | 24333276 | |
| 180 | Phosphorylation | AIEINPDSAQPYKWR CEECCCCCCCCCCCC | 30.02 | 25338131 | |
| 185 | Ubiquitination | PDSAQPYKWRGKAHR CCCCCCCCCCCHHHH | 36.78 | 27667366 | |
| 185 | Acetylation | PDSAQPYKWRGKAHR CCCCCCCCCCCHHHH | 36.78 | 23236377 | |
| 208 | S-nitrosocysteine | AHDLALACKLDYDED HHHHHHHHCCCCCHH | 4.71 | - | |
| 208 | Glutathionylation | AHDLALACKLDYDED HHHHHHHHCCCCCHH | 4.71 | 24333276 | |
| 208 | S-palmitoylation | AHDLALACKLDYDED HHHHHHHHCCCCCHH | 4.71 | 28680068 | |
| 208 | S-nitrosylation | AHDLALACKLDYDED HHHHHHHHCCCCCHH | 4.71 | 20925432 | |
| 217 | Phosphorylation | LDYDEDASAMLREVQ CCCCHHHHHHHHHHH | 26.91 | 24759943 | |
| 348 | Phosphorylation | AQNPSNMSKYQSNPK HHCCCCHHHHHCCHH | 32.25 | - | |
| 349 | Ubiquitination | QNPSNMSKYQSNPKV HCCCCHHHHHCCHHH | 36.22 | - | |
| 352 | Phosphorylation | SNMSKYQSNPKVMNL CCHHHHHCCHHHHHH | 52.59 | - | |
| 355 | Acetylation | SKYQSNPKVMNLISK HHHHCCHHHHHHHHH | 59.37 | 23806337 | |
| 355 | Ubiquitination | SKYQSNPKVMNLISK HHHHCCHHHHHHHHH | 59.37 | 27667366 | |
| 361 | Phosphorylation | PKVMNLISKLSAKFG HHHHHHHHHHHHHHC | 30.61 | 26643407 | |
| 362 | Acetylation | KVMNLISKLSAKFGG HHHHHHHHHHHHHCC | 39.19 | 23806337 | |
| 362 | Ubiquitination | KVMNLISKLSAKFGG HHHHHHHHHHHHHCC | 39.19 | 27667366 | |
| 364 | Phosphorylation | MNLISKLSAKFGGQS HHHHHHHHHHHCCCC | 32.90 | 26643407 | |
| 366 | Ubiquitination | LISKLSAKFGGQS-- HHHHHHHHHCCCC-- | 40.96 | 27667366 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 348 | S | Phosphorylation | Kinase | GRK5 | Q8VEB1 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of F10A1_MOUSE !! | ||||||
* 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_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of F10A1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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