| UniProt ID | CABP1_HUMAN | |
|---|---|---|
| UniProt AC | Q9NZU7 | |
| Protein Name | Calcium-binding protein 1 | |
| Gene Name | CABP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 370 | |
| Subcellular Localization |
Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell membrane Lipid-anchor Cytoplasmic side. Golgi apparatus . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . L-CaBP1 is associated most likely with the cytoskel |
|
| Protein Description | Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs)(PubMed:14570872). Inhibits agonist-induced intracellular calcium signaling. [PubMed: 15980432 Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels] | |
| Protein Sequence | MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR | |
| 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 |
|---|---|---|---|---|---|
| 2 | Myristoylation | ------MGGGDGAAF ------CCCCCCCCC | 49.11 | - | |
| 2 (in isoform 1) | Myristoylation | - | 49.11 | 10625670 | |
| 2 (in isoform 2) | Myristoylation | - | 49.11 | 10625670 | |
| 4 (in isoform 1) | S-palmitoylation | - | 25.17 | 10625670 | |
| 4 (in isoform 2) | S-palmitoylation | - | 25.17 | 10625670 | |
| 31 | Methylation | LGSRREPRSLPAGGP CCCCCCCCCCCCCCC | 46.18 | - | |
| 70 | Phosphorylation | AKSESKTSLLKAAAA HCCCCHHHHHHHHHH | 35.13 | 24719451 | |
| 87 | Dimethylation | SGGSRAPRHGPARDP HCCCCCCCCCCCCCC | 46.54 | - | |
| 92 | Dimethylation | APRHGPARDPGLPSR CCCCCCCCCCCCCCC | 54.51 | - | |
| 98 | Phosphorylation | ARDPGLPSRRLPGSC CCCCCCCCCCCCCCC | 34.77 | - | |
| 176 | Phosphorylation | DGEERGLSPALGLRG CCCCCCCCHHHCHHH | 15.79 | 28857561 | |
| 180 | Phosphorylation | RGLSPALGLRGSLRA CCCCHHHCHHHHHHH | 18.55 | 14685260 | |
| 190 | Methylation | GSLRARGRGDSVPAA HHHHHCCCCCCCCHH | 39.94 | - | |
| 323 | Phosphorylation | TNGDGEISTSELREA CCCCCCCCHHHHHHH | 22.90 | 10625670 |
| 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 CABP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CABP1_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 CABP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CAC1C_HUMAN | CACNA1C | physical | 15140941 | |
| CAC1A_HUMAN | CACNA1A | physical | 14570872 | |
| CAC1A_HUMAN | CACNA1A | physical | 11865310 | |
| GRK5_HUMAN | GRK5 | physical | 10625670 | |
| ITPR1_HUMAN | ITPR1 | physical | 12032348 | |
| UBP4_HUMAN | USP4 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Regulation of InsP3 receptor activity by neuronal Ca2+-bindingproteins."; Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D.,Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J.,Holmes A.B., Berridge M.J., Roderick H.L.; EMBO J. 23:312-321(2004). Cited for: PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULARLOCATION, AND INTERACTION WITH ITPR1. | |