| UniProt ID | SPRL1_MOUSE | |
|---|---|---|
| UniProt AC | P70663 | |
| Protein Name | SPARC-like protein 1 | |
| Gene Name | Sparcl1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 650 | |
| Subcellular Localization | Secreted, extracellular space, extracellular matrix. | |
| Protein Description | ||
| Protein Sequence | MKAVLLLLCALGTAVAIPTSTRFLSDHSNPTTATLVTPEDATVPIAGVEATADIENHPSDKAEKPSALNSEEETHEQSTEQDKTYSFEVDLKDEEDGDGDLSVDPTEGTLTLDLQEGTSEPQQKSLPENGDFPATVSTSYVDPNQRANITKGKESQEQPVSDSHQQPNESSKQTQDLKAEESQTQDPDIPNEEEEEEEDEEEEEEEEPEDIGAPSDNQEEGKEPLEEQPTSKWEGNREQSDDTLEESSQPTQISKTEKHQSEQGNQGQESDSEAEGEDKAAGSKEHIPHTEQQDQEGKAGLEAIGNQKDTDEKAVSTEPTDAAVVPRSHGGAGDNGGGDDSKHGAGDDYFIPSQEFLEAERMHSLSYYLKYGGGEETTTGESENRREAADNQEAKKAESSPNAEPSDEGNSREHSAGSCTNFQCKRGHICKTDPQGKPHCVCQDPETCPPAKILDQACGTDNQTYASSCHLFATKCRLEGTKKGHQLQLDYFGACKSIPACTDFEVAQFPLRMRDWLKNILMQLYEPNPKHGGYLNEKQRSKVKKIYLDEKRLLAGDHPIELLLRDFKKNYHMYVYPVHWQFNELDQHPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKEEDIDENLLF | |
| 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 |
|---|---|---|---|---|---|
| 66 | Phosphorylation | SDKAEKPSALNSEEE CCCCCCCCCCCCCHH | 57.36 | 25521595 | |
| 70 | Phosphorylation | EKPSALNSEEETHEQ CCCCCCCCCHHHHHC | 47.43 | 25521595 | |
| 74 | Phosphorylation | ALNSEEETHEQSTEQ CCCCCHHHHHCCCCC | 33.71 | 24925903 | |
| 78 | Phosphorylation | EEETHEQSTEQDKTY CHHHHHCCCCCCCEE | 30.81 | 24925903 | |
| 79 | Phosphorylation | EETHEQSTEQDKTYS HHHHHCCCCCCCEEE | 37.04 | 24925903 | |
| 86 | Phosphorylation | TEQDKTYSFEVDLKD CCCCCEEEEEEECCC | 21.84 | - | |
| 148 | N-linked_Glycosylation | VDPNQRANITKGKES CCCCCCCCCCCCCCC | 44.65 | - | |
| 155 | Phosphorylation | NITKGKESQEQPVSD CCCCCCCCCCCCCCC | 42.37 | 25521595 | |
| 161 | Phosphorylation | ESQEQPVSDSHQQPN CCCCCCCCCCCCCCC | 39.83 | 23684622 | |
| 163 | Phosphorylation | QEQPVSDSHQQPNES CCCCCCCCCCCCCCC | 18.71 | 25521595 | |
| 168 | N-linked_Glycosylation | SDSHQQPNESSKQTQ CCCCCCCCCCCHHHH | 58.40 | - | |
| 170 | Phosphorylation | SHQQPNESSKQTQDL CCCCCCCCCHHHHHH | 49.85 | 22817900 | |
| 171 | Phosphorylation | HQQPNESSKQTQDLK CCCCCCCCHHHHHHH | 23.70 | 29899451 | |
| 270 | Phosphorylation | QGNQGQESDSEAEGE CCCCCCCCCHHHCCC | 38.25 | 22324799 | |
| 272 | Phosphorylation | NQGQESDSEAEGEDK CCCCCCCHHHCCCCC | 48.24 | 22324799 | |
| 283 | Phosphorylation | GEDKAAGSKEHIPHT CCCCCCCCCCCCCCH | 30.09 | 21930439 | |
| 290 | Phosphorylation | SKEHIPHTEQQDQEG CCCCCCCHHHHCHHC | 30.09 | 27742792 | |
| 316 | Phosphorylation | DTDEKAVSTEPTDAA CCCCCCCCCCCCCEE | 31.73 | 29899451 | |
| 317 | Phosphorylation | TDEKAVSTEPTDAAV CCCCCCCCCCCCEEE | 39.11 | 29899451 | |
| 320 | Phosphorylation | KAVSTEPTDAAVVPR CCCCCCCCCEEEECC | 31.85 | 27357545 | |
| 341 | Phosphorylation | DNGGGDDSKHGAGDD CCCCCCCCCCCCCCC | 31.15 | 19367708 | |
| 349 | Phosphorylation | KHGAGDDYFIPSQEF CCCCCCCCEECCHHH | 14.24 | 27180971 | |
| 353 | Phosphorylation | GDDYFIPSQEFLEAE CCCCEECCHHHHHHH | 37.21 | 27180971 | |
| 364 | Phosphorylation | LEAERMHSLSYYLKY HHHHHHHHHHEEECC | 15.07 | 21183079 | |
| 366 | Phosphorylation | AERMHSLSYYLKYGG HHHHHHHHEEECCCC | 18.10 | 21183079 | |
| 368 | Phosphorylation | RMHSLSYYLKYGGGE HHHHHHEEECCCCCC | 8.04 | 22817900 | |
| 378 | Phosphorylation | YGGGEETTTGESENR CCCCCCCCCCCCHHH | 35.76 | 21183079 | |
| 399 | Phosphorylation | QEAKKAESSPNAEPS HHHHHHHCCCCCCCC | 56.82 | 20415495 | |
| 400 | Phosphorylation | EAKKAESSPNAEPSD HHHHHHCCCCCCCCC | 17.43 | 20415495 | |
| 406 | Phosphorylation | SSPNAEPSDEGNSRE CCCCCCCCCCCCCCC | 39.54 | 25521595 | |
| 411 | Phosphorylation | EPSDEGNSREHSAGS CCCCCCCCCCCCCCC | 50.32 | 25521595 | |
| 415 | Phosphorylation | EGNSREHSAGSCTNF CCCCCCCCCCCCCCC | 29.58 | 23684622 | |
| 418 | Phosphorylation | SREHSAGSCTNFQCK CCCCCCCCCCCCEEC | 19.93 | 20415495 | |
| 420 | Phosphorylation | EHSAGSCTNFQCKRG CCCCCCCCCCEECCC | 40.54 | 29899451 | |
| 462 | N-linked_Glycosylation | DQACGTDNQTYASSC HHHCCCCCCHHHHHH | 35.61 | - | |
| 501 | S-nitrosylation | ACKSIPACTDFEVAQ CCCCCCCCCCCHHHC | 2.92 | 22588120 |
| 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 SPRL1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPRL1_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 SPRL1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of SPRL1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-411, AND MASSSPECTROMETRY. | |