CEAM5_HUMAN - dbPTM
CEAM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEAM5_HUMAN
UniProt AC P06731
Protein Name Carcinoembryonic antigen-related cell adhesion molecule 5
Gene Name CEACAM5
Organism Homo sapiens (Human).
Sequence Length 702
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, intracellular signaling and tumor progression. [PubMed: 2803308]
Protein Sequence MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNKLSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI
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_GlycosylationGREIIYPNASLLIQN
CCEEECCCHHHHHHH		25.78UniProtKB CARBOHYD
115N-linked_GlycosylationLIQNIIQNDTGFYTL
HHHHHHHCCCCEEEE		38.10UniProtKB CARBOHYD
152N-linked_GlycosylationPKPSISSNNSKPVED
CCCCCCCCCCCCCCC		50.43UniProtKB CARBOHYD
182N-linked_GlycosylationTYLWWVNNQSLPVSP
EEEEEECCCCCCCCC		24.17UniProtKB CARBOHYD
197N-linked_GlycosylationRLQLSNGNRTLTLFN
CEEEECCCEEEEEEE		37.70UniProtKB CARBOHYD
199PhosphorylationQLSNGNRTLTLFNVT
EEECCCEEEEEEEEE		28.26-
201PhosphorylationSNGNRTLTLFNVTRN
ECCCEEEEEEEEECC		28.79-
204N-linked_GlycosylationNRTLTLFNVTRNDTA
CEEEEEEEEECCCCC		37.05UniProtKB CARBOHYD
206PhosphorylationTLTLFNVTRNDTASY
EEEEEEEECCCCCCE		25.51-
208N-linked_GlycosylationTLFNVTRNDTASYKC
EEEEEECCCCCCEEE		41.44UniProtKB CARBOHYD
213PhosphorylationTRNDTASYKCETQNP
ECCCCCCEEEECCCC		19.73-
226PhosphorylationNPVSARRSDSVILNV
CCCCCCCCCEEEEEE		28.78-
246N-linked_GlycosylationAPTISPLNTSYRSGE
CCCCCCCCCCCCCCC		30.2919159218
256N-linked_GlycosylationYRSGENLNLSCHAAS
CCCCCCCCCEEEECC		41.30UniProtKB CARBOHYD
274N-linked_GlycosylationAQYSWFVNGTFQQST
CCEEEEECCEECCCC		34.02UniProtKB CARBOHYD
288N-linked_GlycosylationTQELFIPNITVNNSG
CEEEECCCEEECCCC		37.43UniProtKB CARBOHYD
292N-linked_GlycosylationFIPNITVNNSGSYTC
ECCCEEECCCCCEEE		28.44UniProtKB CARBOHYD
309N-linked_GlycosylationHNSDTGLNRTTVTTI
CCCCCCCCCCEEEEE		40.37UniProtKB CARBOHYD
330N-linked_GlycosylationPKPFITSNNSNPVED
CCCCCCCCCCCCCCC		47.50UniProtKB CARBOHYD
351N-linked_GlycosylationTCEPEIQNTTYLWWV
EECCEEECCEEEEEE		39.80UniProtKB CARBOHYD
360N-linked_GlycosylationTYLWWVNNQSLPVSP
EEEEEECCCCCCCCC		24.17UniProtKB CARBOHYD
375N-linked_GlycosylationRLQLSNDNRTLTLLS
CEEECCCCCEEEEEE		42.99UniProtKB CARBOHYD
404PhosphorylationNKLSVDHSDPVILNV
CCCCCCCCCCEEEEE		38.86-
419PhosphorylationLYGPDDPTISPSYTY
EECCCCCCCCCCCEE		40.87-
421PhosphorylationGPDDPTISPSYTYYR
CCCCCCCCCCCEEEC		15.40-
432N-linked_GlycosylationTYYRPGVNLSLSCHA
EEECCCCCEEEEEEC		29.81UniProtKB CARBOHYD
466N-linked_GlycosylationTQELFISNITEKNSG
HEEEEEECCCCCCCC		40.14UniProtKB CARBOHYD
476PhosphorylationEKNSGLYTCQANNSA
CCCCCEEEEECCCCC		11.8127251275
480N-linked_GlycosylationGLYTCQANNSASGHS
CEEEEECCCCCCCCC		19.67UniProtKB CARBOHYD
508N-linked_GlycosylationPKPSISSNNSKPVED
CCCCCCCCCCCCCCC		50.43UniProtKB CARBOHYD
529N-linked_GlycosylationTCEPEAQNTTYLWWV
EECCCCCCCEEEEEE		41.24UniProtKB CARBOHYD
553N-linked_GlycosylationRLQLSNGNRTLTLFN
CEEECCCCCEEEEEE		37.70UniProtKB CARBOHYD
555PhosphorylationQLSNGNRTLTLFNVT
EECCCCCEEEEEEEC		28.26-
557PhosphorylationSNGNRTLTLFNVTRN
CCCCCEEEEEEECCC		28.79-
560N-linked_GlycosylationNRTLTLFNVTRNDAR
CCEEEEEEECCCCCE		37.0516740002
580N-linked_GlycosylationIQNSVSANRSDPVTL
EECCCCCCCCCCEEE		36.16UniProtKB CARBOHYD
612N-linked_GlycosylationYLSGANLNLSCHSAS
HCCCCCCEEEEECCC		29.70UniProtKB CARBOHYD
650N-linked_GlycosylationAKITPNNNGTYACFV
EEECCCCCCCEEEEE		51.31UniProtKB CARBOHYD
665N-linked_GlycosylationSNLATGRNNSIVKSI
EECCCCCCCCEEEEE		48.20UniProtKB CARBOHYD
680PhosphorylationTVSASGTSPGLSAGA
EEECCCCCCCCCHHH		22.09-
685GPI-anchorGTSPGLSAGATVGIM
CCCCCCCHHHCHHHH		19.382317824
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 CEAM5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEAM5_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 CEAM5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EWS_HUMANEWSR1physical
16189514
HNRPM_RATHnrnpmphysical
11406629
Drug and Disease Associations
Kegg Disease
H00014 Non-small cell lung cancer
H00018 Gastric cancer
H00022 Bladder cancer
H00026 Endometrial Cancer
H00031 Breast cancer
H00046 Cholangiocarcinoma
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 CEAM5_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-246, 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-560, AND MASSSPECTROMETRY.

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