CPLX2_HUMAN - dbPTM
CPLX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPLX2_HUMAN
UniProt AC Q6PUV4
Protein Name Complexin-2
Gene Name CPLX2
Organism Homo sapiens (Human).
Sequence Length 134
Subcellular Localization Cytoplasm, cytosol. Enriched at synaptic-releasing sites in mature neurons..
Protein Description Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis (By similarity)..
Protein Sequence MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK
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
6Ubiquitination--MDFVMKQALGGAT
--CCHHHHHHCCCCC
27.4133845483
13PhosphorylationKQALGGATKDMGKML
HHHCCCCCHHHHHHC
30.7428348404
14AcetylationQALGGATKDMGKMLG
HHCCCCCHHHHHHCC
45.2219608861
18UbiquitinationGATKDMGKMLGGEEE
CCCHHHHHHCCCCCC
25.0633845483
26UbiquitinationMLGGEEEKDPDAQKK
HCCCCCCCCCHHHHH
77.2533845483
32UbiquitinationEKDPDAQKKEEERQE
CCCCHHHHHHHHHHH
64.9733845483
70PhosphorylationRQQIRDKYGLKKKEE
HHHHHHHHCCCHHHH
31.7922817900
83UbiquitinationEEKEAEEKAALEQPC
HHHHHHHHHHHCCCC
30.3933845483
93PhosphorylationLEQPCEGSLTRPKKA
HCCCCCCCCCCCCCC
12.3227422710
95PhosphorylationQPCEGSLTRPKKAIP
CCCCCCCCCCCCCCC
46.7729116813
98UbiquitinationEGSLTRPKKAIPAGC
CCCCCCCCCCCCCCC
52.0933845483
99UbiquitinationGSLTRPKKAIPAGCG
CCCCCCCCCCCCCCC
54.9833845483
133UbiquitinationGPLQDMFKK------
CCHHHHHCC------
51.4333845483

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 CPLX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPLX2_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 CPLX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AN13C_HUMANANKRD13Cphysical
28514442
WAC2A_HUMANFAM21Aphysical
28514442
RAP1A_HUMANRAP1Aphysical
28514442
DEGS1_HUMANDEGS1physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442

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 CPLX2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND MASS SPECTROMETRY.

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