CEAM6_HUMAN - dbPTM
CEAM6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEAM6_HUMAN
UniProt AC P40199
Protein Name Carcinoembryonic antigen-related cell adhesion molecule 6
Gene Name CEACAM6
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor . Apical cell membrane . Cell surface . Localized to the apical glycocalyx surface.
Protein Description Cell surface glycoprotein that plays a role in cell adhesion and tumor progression. [PubMed: 2803308]
Protein Sequence MGPPSAPPCRLHVPWKEVLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLAHNLPQNRIGYSWYKGERVDGNSLIVGYVIGTQQATPGPAYSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPEVQNTTYLWWVNGQSLPVSPRLQLSNGNMTLTLLSVKRNDAGSYECEIQNPASANRSDPVTLNVLYGPDGPTISPSKANYRPGENLNLSCHAASNPPAQYSWFINGTFQQSTQELFIPNITVNNSGSYMCQAHNSATGLNRTTVTMITVSGSAPVLSAVATVGITIGVLARVALI
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
104N-linked_GlycosylationGRETIYPNASLLIQN
CCCEECCCCEEEEEE
25.78UniProtKB CARBOHYD
104N-linked_GlycosylationGRETIYPNASLLIQN
CCCEECCCCEEEEEE
25.782341397
111N-linked_GlycosylationNASLLIQNVTQNDTG
CCEEEEEECCCCCCC
31.63UniProtKB CARBOHYD
111N-linked_GlycosylationNASLLIQNVTQNDTG
CCEEEEEECCCCCCC
31.632341397
115N-linked_GlycosylationLIQNVTQNDTGFYTL
EEEECCCCCCCEEEE
39.17UniProtKB CARBOHYD
115N-linked_GlycosylationLIQNVTQNDTGFYTL
EEEECCCCCCCEEEE
39.172341397
152N-linked_GlycosylationPKPSISSNNSNPVED
CCCCCCCCCCCCCCC
49.512341397
152N-linked_GlycosylationPKPSISSNNSNPVED
CCCCCCCCCCCCCCC
49.51UniProtKB CARBOHYD
173N-linked_GlycosylationTCEPEVQNTTYLWWV
EECCCCCCCEEEEEE
39.29UniProtKB CARBOHYD
197N-linked_GlycosylationRLQLSNGNMTLTLLS
CEEECCCCEEEEEEE
25.2316740002
204PhosphorylationNMTLTLLSVKRNDAG
CEEEEEEEEECCCCC
28.8024719451
224N-linked_GlycosylationIQNPASANRSDPVTL
EECCCCCCCCCCEEE
41.3019159218
243PhosphorylationGPDGPTISPSKANYR
CCCCCCCCCCCCCCC
26.1218318008
245PhosphorylationDGPTISPSKANYRPG
CCCCCCCCCCCCCCC
37.2919690332
256N-linked_GlycosylationYRPGENLNLSCHAAS
CCCCCCCCCEEECCC
41.302341397
256N-linked_GlycosylationYRPGENLNLSCHAAS
CCCCCCCCCEEECCC
41.302341397
274N-linked_GlycosylationAQYSWFINGTFQQST
CCEEEEECCEECCCC
33.702341397
274N-linked_GlycosylationAQYSWFINGTFQQST
CCEEEEECCEECCCC
33.702341397
288N-linked_GlycosylationTQELFIPNITVNNSG
CEEEECCCEEECCCC
37.432341397
288N-linked_GlycosylationTQELFIPNITVNNSG
CEEEECCCEEECCCC
37.432341397
292N-linked_GlycosylationFIPNITVNNSGSYMC
ECCCEEECCCCCEEE
28.442341397
292N-linked_GlycosylationFIPNITVNNSGSYMC
ECCCEEECCCCCEEE
28.442341397
304PhosphorylationYMCQAHNSATGLNRT
EEEEECCCCCCCCCC
19.83-
309N-linked_GlycosylationHNSATGLNRTTVTMI
CCCCCCCCCCEEEEE
40.37UniProtKB CARBOHYD
311PhosphorylationSATGLNRTTVTMITV
CCCCCCCCEEEEEEE
25.2522468782
312PhosphorylationATGLNRTTVTMITVS
CCCCCCCEEEEEEEC
15.6722468782
314PhosphorylationGLNRTTVTMITVSGS
CCCCCEEEEEEECCC
10.7722468782
317PhosphorylationRTTVTMITVSGSAPV
CCEEEEEEECCCCCH
9.5922468782
319PhosphorylationTVTMITVSGSAPVLS
EEEEEEECCCCCHHH
20.5522468782
320GPI-anchorVTMITVSGSAPVLSA
EEEEEECCCCCHHHH
24.40-
321PhosphorylationTMITVSGSAPVLSAV
EEEEECCCCCHHHHH
23.1522468782
326PhosphorylationSGSAPVLSAVATVGI
CCCCCHHHHHHHHCH
22.41-
330PhosphorylationPVLSAVATVGITIGV
CHHHHHHHHCHHHHH
16.80-

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 CEAM6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEAM6_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 CEAM6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CEAM8_HUMANCEACAM8physical
21982860
CART_HUMANCARTPTphysical
21982860
CEAM6_HUMANCEACAM6physical
21982860
CEAM1_HUMANCEACAM1physical
21982860
CEAM7_HUMANCEACAM7physical
21982860
CEAM5_HUMANCEACAM5physical
21982860

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
D02977 Arcitumomab (USAN/INN); Cea-Scan (TN)
D06028 Technetium Tc 99m arcitumomab (USP)
D06350 Yttrium Y 90 labetuzumab (USAN); CES-Cide (TN)
D06351 Yttrium Y 90 labetuzumab tetraxetan (USAN)
D08936 Labetuzumab (INN/USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CEAM6_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-224, AND MASSSPECTROMETRY.
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASSSPECTROMETRY.

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