| 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 | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 104 | N-linked_Glycosylation | GRETIYPNASLLIQN CCCEECCCCEEEEEE | 25.78 | UniProtKB CARBOHYD | |
| 104 | N-linked_Glycosylation | GRETIYPNASLLIQN CCCEECCCCEEEEEE | 25.78 | 2341397 | |
| 111 | N-linked_Glycosylation | NASLLIQNVTQNDTG CCEEEEEECCCCCCC | 31.63 | UniProtKB CARBOHYD | |
| 111 | N-linked_Glycosylation | NASLLIQNVTQNDTG CCEEEEEECCCCCCC | 31.63 | 2341397 | |
| 115 | N-linked_Glycosylation | LIQNVTQNDTGFYTL EEEECCCCCCCEEEE | 39.17 | UniProtKB CARBOHYD | |
| 115 | N-linked_Glycosylation | LIQNVTQNDTGFYTL EEEECCCCCCCEEEE | 39.17 | 2341397 | |
| 152 | N-linked_Glycosylation | PKPSISSNNSNPVED CCCCCCCCCCCCCCC | 49.51 | 2341397 | |
| 152 | N-linked_Glycosylation | PKPSISSNNSNPVED CCCCCCCCCCCCCCC | 49.51 | UniProtKB CARBOHYD | |
| 173 | N-linked_Glycosylation | TCEPEVQNTTYLWWV EECCCCCCCEEEEEE | 39.29 | UniProtKB CARBOHYD | |
| 197 | N-linked_Glycosylation | RLQLSNGNMTLTLLS CEEECCCCEEEEEEE | 25.23 | 16740002 | |
| 204 | Phosphorylation | NMTLTLLSVKRNDAG CEEEEEEEEECCCCC | 28.80 | 24719451 | |
| 224 | N-linked_Glycosylation | IQNPASANRSDPVTL EECCCCCCCCCCEEE | 41.30 | 19159218 | |
| 243 | Phosphorylation | GPDGPTISPSKANYR CCCCCCCCCCCCCCC | 26.12 | 18318008 | |
| 245 | Phosphorylation | DGPTISPSKANYRPG CCCCCCCCCCCCCCC | 37.29 | 19690332 | |
| 256 | N-linked_Glycosylation | YRPGENLNLSCHAAS CCCCCCCCCEEECCC | 41.30 | 2341397 | |
| 256 | N-linked_Glycosylation | YRPGENLNLSCHAAS CCCCCCCCCEEECCC | 41.30 | 2341397 | |
| 274 | N-linked_Glycosylation | AQYSWFINGTFQQST CCEEEEECCEECCCC | 33.70 | 2341397 | |
| 274 | N-linked_Glycosylation | AQYSWFINGTFQQST CCEEEEECCEECCCC | 33.70 | 2341397 | |
| 288 | N-linked_Glycosylation | TQELFIPNITVNNSG CEEEECCCEEECCCC | 37.43 | 2341397 | |
| 288 | N-linked_Glycosylation | TQELFIPNITVNNSG CEEEECCCEEECCCC | 37.43 | 2341397 | |
| 292 | N-linked_Glycosylation | FIPNITVNNSGSYMC ECCCEEECCCCCEEE | 28.44 | 2341397 | |
| 292 | N-linked_Glycosylation | FIPNITVNNSGSYMC ECCCEEECCCCCEEE | 28.44 | 2341397 | |
| 304 | Phosphorylation | YMCQAHNSATGLNRT EEEEECCCCCCCCCC | 19.83 | - | |
| 309 | N-linked_Glycosylation | HNSATGLNRTTVTMI CCCCCCCCCCEEEEE | 40.37 | UniProtKB CARBOHYD | |
| 311 | Phosphorylation | SATGLNRTTVTMITV CCCCCCCCEEEEEEE | 25.25 | 22468782 | |
| 312 | Phosphorylation | ATGLNRTTVTMITVS CCCCCCCEEEEEEEC | 15.67 | 22468782 | |
| 314 | Phosphorylation | GLNRTTVTMITVSGS CCCCCEEEEEEECCC | 10.77 | 22468782 | |
| 317 | Phosphorylation | RTTVTMITVSGSAPV CCEEEEEEECCCCCH | 9.59 | 22468782 | |
| 319 | Phosphorylation | TVTMITVSGSAPVLS EEEEEEECCCCCHHH | 20.55 | 22468782 | |
| 320 | GPI-anchor | VTMITVSGSAPVLSA EEEEEECCCCCHHHH | 24.40 | - | |
| 321 | Phosphorylation | TMITVSGSAPVLSAV EEEEECCCCCHHHHH | 23.15 | 22468782 | |
| 326 | Phosphorylation | SGSAPVLSAVATVGI CCCCCHHHHHHHHCH | 22.41 | - | |
| 330 | Phosphorylation | PVLSAVATVGITIGV CHHHHHHHHCHHHHH | 16.80 | - |
| 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 !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CEAM6_HUMAN !! | ||||||
* 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 !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| A4_HUMAN | APP | physical | 21832049 | |
| CEAM8_HUMAN | CEACAM8 | physical | 21982860 | |
| CART_HUMAN | CARTPT | physical | 21982860 | |
| CEAM6_HUMAN | CEACAM6 | physical | 21982860 | |
| CEAM1_HUMAN | CEACAM1 | physical | 21982860 | |
| CEAM7_HUMAN | CEACAM7 | physical | 21982860 | |
| CEAM5_HUMAN | CEACAM5 | physical | 21982860 |
| 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. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "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 | |
| Reference | PubMed |
| "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. | |