EPCAM_HUMAN - dbPTM
EPCAM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPCAM_HUMAN
UniProt AC P16422
Protein Name Epithelial cell adhesion molecule
Gene Name EPCAM
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Lateral cell membrane
Single-pass type I membrane protein . Cell junction, tight junction . Colocalizes with CLDN7 at the lateral cell membrane and tight junction.
Protein Description May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E..
Protein Sequence MAPPQVLAFGLLLAAATATFAAAQEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMNGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSMCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTRYQLDPKFITSILYENNVITIDLVQNSSQKTQNDVDIADVAYYFEKDVKGESLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKAGVIAVIVVVVIAVVAGIVVLVISRKKRMAKYEKAEIKEMGEMHRELNA
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
24Pyrrolidone_carboxylic_acidTATFAAAQEECVCEN
HHHHHHHHHHHHCCC		42.15-
74N-linked_GlycosylationLVMKAEMNGSKLGRR
HHHHHHHCCCCCCCC		42.9918508581
74N-linked_GlycosylationLVMKAEMNGSKLGRR
HHHHHHHCCCCCCCC		42.9911080501
111N-linked_GlycosylationLFKAKQCNGTSMCWC
CEEEEECCCCCEEEE		55.0418508581
111N-linked_GlycosylationLFKAKQCNGTSMCWC
CEEEEECCCCCEEEE		55.0411080501
168UbiquitinationSLRTALQKEITTRYQ
HHHHHHHHHHHHHHC		52.5121906983
171O-linked_GlycosylationTALQKEITTRYQLDP
HHHHHHHHHHHCCCH		13.3055831383
172O-linked_GlycosylationALQKEITTRYQLDPK
HHHHHHHHHHCCCHH		32.8055831389
198N-linked_GlycosylationITIDLVQNSSQKTQN
EEEEEECCCCCCCCC		35.8318508581
214PhosphorylationVDIADVAYYFEKDVK
CCHHHHHHHHHCCCC		14.45-
215PhosphorylationDIADVAYYFEKDVKG
CHHHHHHHHHCCCCC		8.77-
218UbiquitinationDVAYYFEKDVKGESL
HHHHHHHCCCCCCCC		58.9021906983
231SulfoxidationSLFHSKKMDLTVNGE
CCEECCEEEEEECCE		6.1628465586
234PhosphorylationHSKKMDLTVNGEQLD
ECCEEEEEECCEEEC		13.9923403867
247PhosphorylationLDLDPGQTLIYYVDE
ECCCCCCEEEEEECC		22.4923403867
291UbiquitinationVVLVISRKKRMAKYE
HHHHHCCHHHHHHHH		37.6323503661
292UbiquitinationVLVISRKKRMAKYEK
HHHHCCHHHHHHHHH		46.4223503661
296UbiquitinationSRKKRMAKYEKAEIK
CCHHHHHHHHHHHHH		44.6023503661
297PhosphorylationRKKRMAKYEKAEIKE
CHHHHHHHHHHHHHH		17.0828152594
299UbiquitinationKRMAKYEKAEIKEMG
HHHHHHHHHHHHHHH		48.5121906983
303UbiquitinationKYEKAEIKEMGEMHR
HHHHHHHHHHHHHHH		32.9027667366
303NeddylationKYEKAEIKEMGEMHR
HHHHHHHHHHHHHHH		32.9032015554
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 EPCAM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
198NGlycosylation

18508581
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 EPCAM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPCAM_HUMANEPCAMphysical
11058587
Drug and Disease Associations
Kegg Disease
H00876 Mismatch repair deficiency, including: Hereditary non-polyposis colorectal cancer (HNPCC); Lynch syn
H01174 Congenital diarrhea, including: Congenital chloride diarrhea (DIAR1); Microvillus inclusion disease
OMIM Disease
613217Diarrhea 5, with tufting enteropathy, congenital (DIAR5)
613244Hereditary non-polyposis colorectal cancer 8 (HNPCC8)
Kegg Drug
D03958 Edrecolomab (USAN/INN); Panorex (TN)
D09027 Tucotuzumab celmoleukin (USAN/INN)
D09207 Catumaxomab (INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPCAM_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-198, AND MASSSPECTROMETRY.
"Glycosylation is crucial for stability of tumour and cancer stem cellantigen EpCAM.";
Munz M., Fellinger K., Hofmann T., Schmitt B., Gires O.;
Front. Biosci. 13:5195-5201(2008).
Cited for: GLYCOSYLATION AT ASN-74; ASN-111 AND ASN-198, AND MUTAGENESIS OFASN-74; ASN-111 AND ASN-198.
"Determination of disulfide bond assignments and N-glycosylation sitesof the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP,KS1-4, KSA, and Ep-CAM).";
Chong J.M., Speicher D.W.;
J. Biol. Chem. 276:5804-5813(2001).
Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-74 AND ASN-111.

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