CEAM8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CEAM8_HUMAN
• UniProt AC: P31997
• Protein Name: Carcinoembryonic antigen-related cell adhesion molecule 8
• Gene Name: CEACAM8
• Organism: Homo sapiens (Human).
• Sequence Length: 349
• Subcellular Localization: Cell membrane ; Lipid-anchor, GPI-anchor . Cell surface .
• Protein Description: Cell surface glycoprotein that plays a role in cell adhesion in a calcium-independent manner. [PubMed: 8776764]
• Protein Sequence: MGPISAPSCRWRIPWQGLLLTASLFTFWNPPTTAQLTIEAVPSNAAEGKEVLLLVHNLPQDPRGYNWYKGETVDANRRIIGYVISNQQITPGPAYSNRETIYPNASLLMRNVTRNDTGSYTLQVIKLNLMSEEVTGQFSVHPETPKPSISSNNSNPVEDKDAVAFTCEPETQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLLSVTRNDVGPYECEIQNPASANFSDPVTLNVLYGPDAPTISPSDTYYHAGVNLNLSCHAASNPPSQYSWSVNGTFQQYTQKLFIPNITTKNSGSYACHTTNSATGRNRTTVRMITVSDALVQGSSPGLSARATVSIMIGVLARVALI

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
100	Phosphorylation	PAYSNRETIYPNASL CCCCCCCCCCCCCEE	23.67	25072903
102	Phosphorylation	YSNRETIYPNASLLM CCCCCCCCCCCEEEE	9.61	25072903
104	N-linked_Glycosylation	NRETIYPNASLLMRN CCCCCCCCCEEEECC	25.78	UniProtKB CARBOHYD
106	Phosphorylation	ETIYPNASLLMRNVT CCCCCCCEEEECCCC	28.77	25072903
111	N-linked_Glycosylation	NASLLMRNVTRNDTG CCEEEECCCCCCCCC	26.08	UniProtKB CARBOHYD
115	N-linked_Glycosylation	LMRNVTRNDTGSYTL EECCCCCCCCCCEEE	41.66	UniProtKB CARBOHYD
120	Phosphorylation	TRNDTGSYTLQVIKL CCCCCCCEEEEEEEE	16.89	-
126	Methylation	SYTLQVIKLNLMSEE CEEEEEEEEECCCCE	32.25	-
152	N-linked_Glycosylation	PKPSISSNNSNPVED CCCCCCCCCCCCCCC	49.51	UniProtKB CARBOHYD
173	N-linked_Glycosylation	TCEPETQNTTYLWWV EECCCCCCEEEEEEE	41.63	UniProtKB CARBOHYD
197	N-linked_Glycosylation	RLQLSNGNRTLTLLS CEEECCCCEEEEEEE	37.70	UniProtKB CARBOHYD
224	N-linked_Glycosylation	IQNPASANFSDPVTL ECCCCCCCCCCCEEE	34.16	UniProtKB CARBOHYD
256	N-linked_Glycosylation	YHAGVNLNLSCHAAS EECCEEEEEEEECCC	25.38	UniProtKB CARBOHYD
274	N-linked_Glycosylation	SQYSWSVNGTFQQYT HHCEEEECCCHHHHE	37.97	UniProtKB CARBOHYD
288	N-linked_Glycosylation	TQKLFIPNITTKNSG EEEEECCCCCCCCCC	39.15	17623646
288	N-linked_Glycosylation	TQKLFIPNITTKNSG EEEEECCCCCCCCCC	39.15	16740002
296	Phosphorylation	ITTKNSGSYACHTTN CCCCCCCCEEEEECC	14.91	-
309	N-linked_Glycosylation	TNSATGRNRTTVRMI CCCCCCCCCCEEEEE	47.17	UniProtKB CARBOHYD
320	GPI-anchor	VRMITVSDALVQGSS EEEEEEHHHHHCCCC	39.32	2208113

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CEAM8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CEAM8_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CEAM8_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CEAM8_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-288, AND MASSSPECTROMETRY.
PubMed: 16740002