dbPTM

CADM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CADM1_HUMAN
UniProt AC	Q9BY67
Protein Name	Cell adhesion molecule 1
Gene Name	CADM1 {ECO:0000312\|HGNC:HGNC:5951}
Organism	Homo sapiens (Human).
Sequence Length	442
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Cell junction, synapse . Localized to the basolateral plasma membrane of epithelial cells in gall bladder.
Protein Description	Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly (By similarity). May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa..
Protein Sequence	MASVVLPSGSQCAAAAAAAAPPGLRLRLLLLLFSAAALIPTGDGQNLFTKDVTVIEGEVATISCQVNKSDDSVIQLLNPNRQTIYFRDFRPLKDSRFQLLNFSSSELKVSLTNVSISDEGRYFCQLYTDPPQESYTTITVLVPPRNLMIDIQKDTAVEGEEIEVNCTAMASKPATTIRWFKGNTELKGKSEVEEWSDMYTVTSQLMLKVHKEDDGVPVICQVEHPAVTGNLQTQRYLEVQYKPQVHIQMTYPLQGLTREGDALELTCEAIGKPQPVMVTWVRVDDEMPQHAVLSGPNLFINNLNKTDNGTYRCEASNIVGKAHSDYMLYVYDPPTTIPPPTTTTTTTTTTTTTILTIITDSRAGEEGSIRAVDHAVIGGVVAVVVFAMLCLLIILGRYFARHKGTYFTHEAKGADDAADADTAIINAEGGQNNSEEKKEYFI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASVVLPSGS -----CCEEECCCHH	16.09	19362540
8	Phosphorylation	MASVVLPSGSQCAAA CCEEECCCHHHHHHH	47.09	19362540
10	Phosphorylation	SVVLPSGSQCAAAAA EEECCCHHHHHHHHH	26.82	19362540
67	N-linked_Glycosylation	ATISCQVNKSDDSVI EEEEEEECCCCCCEE	16.54	UniProtKB CARBOHYD
69	Phosphorylation	ISCQVNKSDDSVIQL EEEEECCCCCCEEEE	41.25	21659604
72	Phosphorylation	QVNKSDDSVIQLLNP EECCCCCCEEEECCC	26.55	21659604
95	Phosphorylation	DFRPLKDSRFQLLNF CCEECCCCCEEEEEC	33.15	28450419
101	N-linked_Glycosylation	DSRFQLLNFSSSELK CCCEEEEECCCCCEE	43.26	19159218
101	N-linked_Glycosylation	DSRFQLLNFSSSELK CCCEEEEECCCCCEE	43.26	16335952
103	Phosphorylation	RFQLLNFSSSELKVS CEEEEECCCCCEEEE	31.70	23025827
104	Phosphorylation	FQLLNFSSSELKVSL EEEEECCCCCEEEEE	24.56	28450419
105	Phosphorylation	QLLNFSSSELKVSLT EEEECCCCCEEEEEE	45.83	28450419
113	N-linked_Glycosylation	ELKVSLTNVSISDEG CEEEEEEEEECCCCC	30.72	16335952
113	N-linked_Glycosylation	ELKVSLTNVSISDEG CEEEEEEEEECCCCC	30.72	17623646
165	N-linked_Glycosylation	EGEEIEVNCTAMASK CCCEEEEEEEEEECC	12.48	UniProtKB CARBOHYD
220	Glutathionylation	DDGVPVICQVEHPAV CCCCEEEEEEECCCC	3.64	22555962
267	Glutathionylation	GDALELTCEAIGKPQ CCEEEEEHHHHCCCC	5.34	22555962
301	N-linked_Glycosylation	SGPNLFINNLNKTDN ECCCEEECCCCCCCC	39.33	19349973
301	N-linked_Glycosylation	SGPNLFINNLNKTDN ECCCEEECCCCCCCC	39.33	19349973
302	N-linked_Glycosylation	GPNLFINNLNKTDNG CCCEEECCCCCCCCC	39.93	19349973
302	N-linked_Glycosylation	GPNLFINNLNKTDNG CCCEEECCCCCCCCC	39.93	19349973
304	N-linked_Glycosylation	NLFINNLNKTDNGTY CEEECCCCCCCCCEE	47.51	19349973
304	N-linked_Glycosylation	NLFINNLNKTDNGTY CEEECCCCCCCCCEE	47.51	UniProtKB CARBOHYD
308	N-linked_Glycosylation	NNLNKTDNGTYRCEA CCCCCCCCCEEEEEE	50.35	UniProtKB CARBOHYD
324	Phosphorylation	NIVGKAHSDYMLYVY CEEEEECCCEEEEEE	34.98	-
326	Phosphorylation	VGKAHSDYMLYVYDP EEEECCCEEEEEECC	7.64	-
348	Phosphorylation	TTTTTTTTTTTTTIL CCEEEEEEEEEEEEE	21.76	-
406	Phosphorylation	FARHKGTYFTHEAKG HHHHCCCCEEECCCC	18.36	25884760
412	Ubiquitination	TYFTHEAKGADDAAD CCEEECCCCCCCCCC	52.20	-
422	Phosphorylation	DDAADADTAIINAEG CCCCCCCEEEEECCC	22.83	30266825
434	Phosphorylation	AEGGQNNSEEKKEYF CCCCCCCCHHHHHHC	55.47	30266825
437	Ubiquitination	GQNNSEEKKEYFI-- CCCCCHHHHHHCC--	47.02	-
438	Ubiquitination	QNNSEEKKEYFI--- CCCCHHHHHHCC---	62.01	-
440	Phosphorylation	NSEEKKEYFI----- CCHHHHHHCC-----	18.56	25884760

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 CADM1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
67	N	Glycosylation	-
Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and synapse induction.
101	N	Glycosylation	16335952
Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and synapse induction.

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 CADM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPP3_HUMAN	MPP3	physical	13679854
E41L3_HUMAN	EPB41L3	physical	12234973
CNBP_HUMAN	CNBP	physical	26344197
RS15_HUMAN	RPS15	physical	26344197

Drug and Disease Associations

Kegg Disease
H00054	Nasopharyngeal cancer
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 CADM1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-113; ASN-301 ANDASN-302, AND MASS SPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113, AND MASSSPECTROMETRY.	16335952 [Abstract]

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