| UniProt ID | CSTN1_HUMAN | |
|---|---|---|
| UniProt AC | O94985 | |
| Protein Name | Calsyntenin-1 | |
| Gene Name | CLSTN1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 981 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type I membrane protein . Golgi apparatus membrane . Cell projection . Cell junction, synapse, postsynaptic cell membrane Single-pass type I membrane protein. Nucleus . Neurite tips. Localized in the post |
|
| Protein Description | Induces KLC1 association with vesicles and functions as a cargo in axonal anterograde transport. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation. In complex with APBA2 and C99, a C-terminal APP fragment, abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably through stabilization of the direct interaction between APBA2 and APP. The intracellular fragment AlcICD suppresses APBB1-dependent transactivation stimulated by APP C-terminal intracellular fragment (AICD), most probably by competing with AICD for APBB1-binding. May modulate calcium-mediated postsynaptic signals (By similarity).. | |
| Protein Sequence | MLRRPAPALAPAARLLLAGLLCGGGVWAARVNKHKPWLEPTYHGIVTENDNTVLLDPPLIALDKDAPLRFAESFEVTVTKEGEICGFKIHGQNVPFDAVVVDKSTGEGVIRSKEKLDCELQKDYSFTIQAYDCGKGPDGTNVKKSHKATVHIQVNDVNEYAPVFKEKSYKATVIEGKQYDSILRVEAVDADCSPQFSQICSYEIITPDVPFTVDKDGYIKNTEKLNYGKEHQYKLTVTAYDCGKKRATEDVLVKISIKPTCTPGWQGWNNRIEYEPGTGALAVFPNIHLETCDEPVASVQATVELETSHIGKGCDRDTYSEKSLHRLCGAAAGTAELLPSPSGSLNWTMGLPTDNGHDSDQVFEFNGTQAVRIPDGVVSVSPKEPFTISVWMRHGPFGRKKETILCSSDKTDMNRHHYSLYVHGCRLIFLFRQDPSEEKKYRPAEFHWKLNQVCDEEWHHYVLNVEFPSVTLYVDGTSHEPFSVTEDYPLHPSKIETQLVVGACWQEFSGVENDNETEPVTVASAGGDLHMTQFFRGNLAGLTLRSGKLADKKVIDCLYTCKEGLDLQVLEDSGRGVQIQAHPSQLVLTLEGEDLGELDKAMQHISYLNSRQFPTPGIRRLKITSTIKCFNEATCISVPPVDGYVMVLQPEEPKISLSGVHHFARAASEFESSEGVFLFPELRIISTITREVEPEGDGAEDPTVQESLVSEEIVHDLDTCEVTVEGEELNHEQESLEVDMARLQQKGIEVSSSELGMTFTGVDTMASYEEVLHLLRYRNWHARSLLDRKFKLICSELNGRYISNEFKVEVNVIHTANPMEHANHMAAQPQFVHPEHRSFVDLSGHNLANPHPFAVVPSTATVVIVVCVSFLVFMIILGVFRIRAAHRRTMRDQDTGKENEMDWDDSALTITVNPMETYEDQHSSEEEEEEEEEEESEDGEEEDDITSAESESSEEEEGEQGDPQNATRQQQLEWDDSTLSY | |
| 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 |
|---|---|---|---|---|---|
| 41 | O-linked_Glycosylation | HKPWLEPTYHGIVTE CCCCCCCCCCEEECC | 20.83 | OGP | |
| 52 | O-linked_Glycosylation | IVTENDNTVLLDPPL EECCCCCEEEECCCE | 18.52 | OGP | |
| 112 | Phosphorylation | TGEGVIRSKEKLDCE CCCCEEECCCCCCCE | 33.76 | 26091039 | |
| 149 | O-linked_Glycosylation | VKKSHKATVHIQVND CCCCCEEEEEEEECC | 19.88 | OGP | |
| 167 (in isoform 2) | Ubiquitination | - | 60.73 | 21906983 | |
| 167 | Ubiquitination | YAPVFKEKSYKATVI CCCCCCCCCEEEEEE | 60.73 | - | |
| 170 | Ubiquitination | VFKEKSYKATVIEGK CCCCCCEEEEEECCC | 44.68 | - | |
| 177 (in isoform 1) | Ubiquitination | - | 32.66 | 21906983 | |
| 177 | Ubiquitination | KATVIEGKQYDSILR EEEEECCCCCCEEEE | 32.66 | 2190698 | |
| 181 | Phosphorylation | IEGKQYDSILRVEAV ECCCCCCEEEEEEEE | 20.70 | 24719451 | |
| 224 | Ubiquitination | GYIKNTEKLNYGKEH CCCCCCCCCCCCCCC | 39.74 | - | |
| 229 | Ubiquitination | TEKLNYGKEHQYKLT CCCCCCCCCCEEEEE | 41.48 | - | |
| 346 | N-linked_Glycosylation | PSPSGSLNWTMGLPT CCCCCCCEEEEECCC | 33.59 | UniProtKB CARBOHYD | |
| 366 | N-linked_Glycosylation | SDQVFEFNGTQAVRI CCCEEEECCEEEEEC | 45.46 | UniProtKB CARBOHYD | |
| 407 | Phosphorylation | KKETILCSSDKTDMN CCCEEEEECCCCCCC | 37.82 | - | |
| 408 | Phosphorylation | KETILCSSDKTDMNR CCEEEEECCCCCCCH | 41.97 | - | |
| 418 | Phosphorylation | TDMNRHHYSLYVHGC CCCCHHHHEEEEECE | 8.34 | - | |
| 421 | Phosphorylation | NRHHYSLYVHGCRLI CHHHHEEEEECEEEE | 5.62 | - | |
| 473 | Phosphorylation | EFPSVTLYVDGTSHE ECCEEEEEECCCCCC | 6.27 | 22468782 | |
| 515 | N-linked_Glycosylation | FSGVENDNETEPVTV HCCCCCCCCCCCEEE | 70.44 | UniProtKB CARBOHYD | |
| 553 | Acetylation | SGKLADKKVIDCLYT CCCCCCHHHHHHEEE | 44.99 | 24431067 | |
| 791 | Ubiquitination | SLLDRKFKLICSELN HHHHHHHHHHHHHHC | 39.72 | - | |
| 977 | Phosphorylation | QQLEWDDSTLSY--- HHHHCCCCCCCC--- | 28.86 | 28348404 | |
| 978 | Phosphorylation | QLEWDDSTLSY---- HHHCCCCCCCC---- | 27.07 | 24719451 | |
| 980 | Phosphorylation | EWDDSTLSY------ HCCCCCCCC------ | 100.00 | 28348404 | |
| 981 | Phosphorylation | WDDSTLSY------- CCCCCCCC------- | 100.00 | 28102081 |
| 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 CSTN1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSTN1_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 CSTN1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| APBA2_HUMAN | APBA2 | physical | 15037614 | |
| A4_HUMAN | APP | physical | 15037614 | |
| PSN1_HUMAN | PSEN1 | physical | 15037614 | |
| TRIPC_HUMAN | TRIP12 | physical | 12421765 | |
| SETB1_HUMAN | SETDB1 | physical | 12421765 | |
| SLK_HUMAN | SLK | physical | 12421765 | |
| GANP_HUMAN | MCM3AP | physical | 12421765 | |
| BAHC1_HUMAN | BAHCC1 | physical | 12421765 |
| 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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