CSTN1_HUMAN - dbPTM
CSTN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
41O-linked_GlycosylationHKPWLEPTYHGIVTE
CCCCCCCCCCEEECC
20.83OGP
52O-linked_GlycosylationIVTENDNTVLLDPPL
EECCCCCEEEECCCE
18.52OGP
112PhosphorylationTGEGVIRSKEKLDCE
CCCCEEECCCCCCCE
33.7626091039
149O-linked_GlycosylationVKKSHKATVHIQVND
CCCCCEEEEEEEECC
19.88OGP
167 (in isoform 2)Ubiquitination-60.7321906983
167UbiquitinationYAPVFKEKSYKATVI
CCCCCCCCCEEEEEE
60.73-
170UbiquitinationVFKEKSYKATVIEGK
CCCCCCEEEEEECCC
44.68-
177 (in isoform 1)Ubiquitination-32.6621906983
177UbiquitinationKATVIEGKQYDSILR
EEEEECCCCCCEEEE
32.662190698
181PhosphorylationIEGKQYDSILRVEAV
ECCCCCCEEEEEEEE
20.7024719451
224UbiquitinationGYIKNTEKLNYGKEH
CCCCCCCCCCCCCCC
39.74-
229UbiquitinationTEKLNYGKEHQYKLT
CCCCCCCCCCEEEEE
41.48-
346N-linked_GlycosylationPSPSGSLNWTMGLPT
CCCCCCCEEEEECCC
33.59UniProtKB CARBOHYD
366N-linked_GlycosylationSDQVFEFNGTQAVRI
CCCEEEECCEEEEEC
45.46UniProtKB CARBOHYD
407PhosphorylationKKETILCSSDKTDMN
CCCEEEEECCCCCCC
37.82-
408PhosphorylationKETILCSSDKTDMNR
CCEEEEECCCCCCCH
41.97-
418PhosphorylationTDMNRHHYSLYVHGC
CCCCHHHHEEEEECE
8.34-
421PhosphorylationNRHHYSLYVHGCRLI
CHHHHEEEEECEEEE
5.62-
473PhosphorylationEFPSVTLYVDGTSHE
ECCEEEEEECCCCCC
6.2722468782
515N-linked_GlycosylationFSGVENDNETEPVTV
HCCCCCCCCCCCEEE
70.44UniProtKB CARBOHYD
553AcetylationSGKLADKKVIDCLYT
CCCCCCHHHHHHEEE
44.9924431067
791UbiquitinationSLLDRKFKLICSELN
HHHHHHHHHHHHHHC
39.72-
977PhosphorylationQQLEWDDSTLSY---
HHHHCCCCCCCC---
28.8628348404
978PhosphorylationQLEWDDSTLSY----
HHHCCCCCCCC----
27.0724719451
980PhosphorylationEWDDSTLSY------
HCCCCCCCC------
100.0028348404
981PhosphorylationWDDSTLSY-------
CCCCCCCC-------
100.0028102081

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSTN1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APBA2_HUMANAPBA2physical
15037614
A4_HUMANAPPphysical
15037614
PSN1_HUMANPSEN1physical
15037614
TRIPC_HUMANTRIP12physical
12421765
SETB1_HUMANSETDB1physical
12421765
SLK_HUMANSLKphysical
12421765
GANP_HUMANMCM3APphysical
12421765
BAHC1_HUMANBAHCC1physical
12421765

Drug and Disease Associations
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.
Regulatory Network of CSTN1_HUMAN

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Related Literatures of Post-Translational Modification

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