| UniProt ID | JSPR1_HUMAN | |
|---|---|---|
| UniProt AC | Q96MG2 | |
| Protein Name | Junctional sarcoplasmic reticulum protein 1 | |
| Gene Name | JSRP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 331 | |
| Subcellular Localization | Sarcoplasmic reticulum membrane. Endoplasmic reticulum membrane. Colocalizes with ryanodine receptors at the sarcoplasmic reticulum triad membranes.. | |
| Protein Description | Involved in skeletal muscle excitation/contraction coupling (EC), probably acting as a regulator of the voltage-sensitive calcium channel CACNA1S. EC is a physiological process whereby an electrical signal (depolarization of the plasma membrane) is converted into a chemical signal, a calcium gradient, by the opening of ryanodine receptor calcium release channels. May regulate CACNA1S membrane targeting and activity.. | |
| Protein Sequence | MSMTTRAWEELDGGLGSCQALEDHSALAETQEDRASATPRLADSGSVPHDSQVAEGPSVDTRPKKMEKEPAARGTPGTGKERLKAGASPRSVPARKKAQTAPPLQPPPPPPALSEELPWGDLSLNKCLVLASLVALLGSAFQLCRDAVPGEAALQARVPEPWVPPSSAPREPSSPLPKFEAQAPPSAPPAPRAEAEVRPKIPGSREAAENDEEEPGEATGEAVREDRVTLADRGPKERPRREGKPRKEKPRKEERPKKERPRKEERPRAAREPREALPQRWESREGGHRPWARDSRDAEPRKKQAWVSPRRPDEEQRPGSRQKLRAGKGRD | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | ATPRLADSGSVPHDS CCCCCCCCCCCCCCC | 27.62 | 22673903 | |
| 46 | Phosphorylation | PRLADSGSVPHDSQV CCCCCCCCCCCCCCC | 36.11 | 26437602 | |
| 51 | Phosphorylation | SGSVPHDSQVAEGPS CCCCCCCCCCCCCCC | 24.42 | 26437602 | |
| 132 | Phosphorylation | NKCLVLASLVALLGS HHHHHHHHHHHHHHH | 21.15 | 28842319 | |
| 139 | Phosphorylation | SLVALLGSAFQLCRD HHHHHHHHHHHHHHH | 26.36 | 28842319 | |
| 166 | Phosphorylation | PEPWVPPSSAPREPS CCCCCCCCCCCCCCC | 32.82 | 26437602 | |
| 167 | Phosphorylation | EPWVPPSSAPREPSS CCCCCCCCCCCCCCC | 48.33 | - | |
| 173 | Phosphorylation | SSAPREPSSPLPKFE CCCCCCCCCCCCCCC | 39.57 | 26657352 | |
| 174 | Phosphorylation | SAPREPSSPLPKFEA CCCCCCCCCCCCCCC | 40.97 | 26437602 | |
| 178 | Ubiquitination | EPSSPLPKFEAQAPP CCCCCCCCCCCCCCC | 64.62 | - | |
| 186 | Phosphorylation | FEAQAPPSAPPAPRA CCCCCCCCCCCCCCC | 52.96 | - | |
| 204 | Phosphorylation | VRPKIPGSREAAEND CCCCCCCCHHHHHCC | 22.92 | 26437602 | |
| 302 | Acetylation | SRDAEPRKKQAWVSP CCCCCHHHCCCCCCC | 61.01 | 7692215 | |
| 320 | Phosphorylation | DEEQRPGSRQKLRAG CCHHCCCHHHHHHCC | 33.93 | 26437602 |
| 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 JSPR1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of JSPR1_HUMAN !! | ||||||
* 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 JSPR1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| AHNK2_HUMAN | AHNAK2 | physical | 26186194 | |
| AHNK_HUMAN | AHNAK | physical | 26186194 | |
| GNAO_HUMAN | GNAO1 | physical | 26186194 | |
| YES_HUMAN | YES1 | physical | 26186194 | |
| KPCA_HUMAN | PRKCA | physical | 26186194 | |
| RRAS_HUMAN | RRAS | physical | 26186194 | |
| SIAH1_HUMAN | SIAH1 | physical | 26186194 | |
| SIAH1_HUMAN | SIAH1 | physical | 28514442 | |
| AHNK_HUMAN | AHNAK | physical | 28514442 | |
| AHNK2_HUMAN | AHNAK2 | physical | 28514442 | |
| GNAO_HUMAN | GNAO1 | physical | 28514442 | |
| RRAS_HUMAN | RRAS | physical | 28514442 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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