CADM2_HUMAN - dbPTM
CADM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CADM2_HUMAN
UniProt AC Q8N3J6
Protein Name Cell adhesion molecule 2
Gene Name CADM2
Organism Homo sapiens (Human).
Sequence Length 435
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell junction, synapse . Cell projection, axon . Found in the axoplasm of myelinated axons.
Protein Description Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes..
Protein Sequence MIWKRSAVLRFYSVCGLLLQGSQGQFPLTQNVTVVEGGTAILTCRVDQNDNTSLQWSNPAQQTLYFDDKKALRDNRIELVRASWHELSISVSDVSLSDEGQYTCSLFTMPVKTSKAYLTVLGVPEKPQISGFSSPVMEGDLMQLTCKTSGSKPAADIRWFKNDKEIKDVKYLKEEDANRKTFTVSSTLDFRVDRSDDGVAVICRVDHESLNATPQVAMQVLEIHYTPSVKIIPSTPFPQEGQPLILTCESKGKPLPEPVLWTKDGGELPDPDRMVVSGRELNILFLNKTDNGTYRCEATNTIGQSSAEYVLIVHDVPNTLLPTTIIPSLTTATVTTTVAITTSPTTSATTSSIRDPNALAGQNGPDHALIGGIVAVVVFVTLCSIFLLGRYLARHKGTYLTNEAKGAEDAPDADTAIINAEGSQVNAEEKKEYFI
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
6Phosphorylation--MIWKRSAVLRFYS
--CCCCHHHHHHHHH
20.9923532336
31N-linked_GlycosylationGQFPLTQNVTVVEGG
CCCCCCCEEEEEECC
26.62UniProtKB CARBOHYD
51N-linked_GlycosylationCRVDQNDNTSLQWSN
EEECCCCCCCEEECC
38.83UniProtKB CARBOHYD
161UbiquitinationAADIRWFKNDKEIKD
CCEEEEECCCCCCCC
58.22-
181PhosphorylationEEDANRKTFTVSSTL
HHHCCCCEEEEEEEE
22.6929209046
183PhosphorylationDANRKTFTVSSTLDF
HCCCCEEEEEEEEEE
25.3929209046
185PhosphorylationNRKTFTVSSTLDFRV
CCCEEEEEEEEEEEE
17.9729209046
186PhosphorylationRKTFTVSSTLDFRVD
CCEEEEEEEEEEEEE
28.7529209046
187PhosphorylationKTFTVSSTLDFRVDR
CEEEEEEEEEEEEEC
23.8829209046
209PhosphorylationICRVDHESLNATPQV
EEEECHHHCCCCHHH
24.4124719451
291N-linked_GlycosylationLFLNKTDNGTYRCEA
EEEECCCCCEEEEEE
50.35UniProtKB CARBOHYD
423PhosphorylationAIINAEGSQVNAEEK
EEEECCCCCCCHHHH
23.5924719451
425PhosphorylationINAEGSQVNAEEKKE
EECCCCCCCHHHHHH
8.6324719451
433PhosphorylationNAEEKKEYFI-----
CHHHHHHHCC-----
18.5627196784

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 CADM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CADM2_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 CADM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CADM2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CADM2_HUMAN

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Related Literatures of Post-Translational Modification

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