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UniProtKB - P13688 (CEAM1_HUMAN)

Entry version 212 (16 Oct 2019)
Sequence version 2 (01 Jul 1993)
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Protein

Carcinoembryonic antigen-related cell adhesion molecule 1

Gene

CEACAM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Isoform 1: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and functions also as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2 (PubMed:25363763). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Downregulates neutrophil production by acting as a coinhibitory receptor for CSF3R by downregulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Downregulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interfers with the interaction of FLNA with RALA (PubMed:16291724). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity).By similarity4 Publications
Isoform 8: Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Promotes populations of T cells regulating IgA production and secretion associated with control of the commensal microbiota and resistance to enteropathogens (By similarity).By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1566977 Fibronectin matrix formation
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

More...SIGNORi		P13688

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Carcinoembryonic antigen-related cell adhesion molecule 11 Publication
Alternative name(s):
Biliary glycoprotein 11 Publication
Short name:
BGP-1
CD_antigen: CD66a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CEACAM1Imported
Synonyms:BGP1 Publication, BGP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1814 CEACAM1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		109770 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P13688

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini35 – 428ExtracellularSequence analysisAdd BLAST394
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei429 – 452HelicalSequence analysisAdd BLAST24
Topological domaini453 – 526CytoplasmicSequence analysisAdd BLAST74

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi76N → A: Impairs interaction with HAVCR2. 1 Publication1
Mutagenesisi77 – 78RQ → GL: Doesn't affect cell surface expression. Impairs phosphorylation. 1 Publication2
Mutagenesisi81G → A: Impairs interaction with HAVCR2. 1 Publication1
Mutagenesisi457T → D: Decreases the binding to ANXA2. 1 Publication1
Mutagenesisi493Y → F: Impairs phosphorylation; when associated with F-520. 1 Publication1
Mutagenesisi520Y → F: Impairs phosphorylation; when associated with F-493. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		634

Open Targets

More...OpenTargetsi		ENSG00000079385

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26358

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P13688

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00113 Technetium Tc-99m arcitumomab

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CEACAM1

Domain mapping of disease mutations (DMDM)

More...DMDMi		399116

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 34Add BLAST34
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001456235 – 526Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei35Pyrrolidone carboxylic acid1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi104N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi111N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi115N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi152N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi167 ↔ 215PROSITE-ProRule annotation
Glycosylationi182N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi197N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi208N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi224N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi232N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi254N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi259 ↔ 299PROSITE-ProRule annotation
Glycosylationi274N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi288N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi292N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi302N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi309N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi345N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi348 ↔ 396PROSITE-ProRule annotationBy similarity
Glycosylationi351N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi363N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi378N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi405N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Modified residuei493Phosphotyrosine; by SRC, LCK, INSR and EGFR2 Publications1
Modified residuei508PhosphoserineBy similarity1
Modified residuei520Phosphotyrosine; by INSR, SRC and LCK2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Isoform 1: Phosphorylated on serine and tyrosine (By similarity). Isoform 1 is phosphorylated on tyrosine by Src family kinases like SRC and LCK and by receptor like CSF3R, EGFR and INSR upon stimulation (PubMed:15467833, PubMed:18424730, PubMed:7478590). Phosphorylated at Ser-508; mediates activity. Phosphorylated at Tyr-493; regulates activity (By similarity). Phosphorylated at Tyr-493 by EGFR and INSR upon stimulation; this phosphorylation is Ser-508-phosphorylation-dependent; mediates cellular internalization; increases interaction with downstream proteins like SHC1 and FASN (By similarity). Phosphorylated at Tyr-493 and Tyr-520 by LCK; mediates PTPN6 association and is regulated by homophilic ligation of CEACAM1 in the absence of T cell activation (PubMed:18424730). Phosphorylated at Tyr-520; mediates interaction with PTPN11 (By similarity).By similarity3 Publications
Isoform 8: Phosphorylated on serine and threonine.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1179

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P13688

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P13688

MaxQB - The MaxQuant DataBase

More...MaxQBi		P13688

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P13688

PeptideAtlas

More...PeptideAtlasi		P13688

PRoteomics IDEntifications database

More...PRIDEi		P13688

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52961 [P13688-1]
52962 [P13688-10]
52963 [P13688-11]
52964 [P13688-2]
52965 [P13688-3]
52966 [P13688-4]
52967 [P13688-5]
52968 [P13688-6]
52969 [P13688-7]
52970 [P13688-8]
52971 [P13688-9]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P13688-2 [P13688-2]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1070
1072

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P13688

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P13688

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in columnar epithelial cells of the colon (at protein level) (PubMed:10436421). The predominant forms expressed by T cells are those containing a long cytoplasmic domain (PubMed:18424730). Expressed in granulocytes and lymphocytes. Leukocytes only express isoforms 6 and isoform 1 (PubMed:11994468).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced in primary T cells by activation with IL-2.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000079385 Expressed in 158 organ(s), highest expression level in colonic mucosa

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P13688 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P13688 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002146
HPA011041

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Oligomer. Heterodimer. Homodimer (PubMed:26483485). Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin.

Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces homophilic cell adhesion through dissociation of dimer (By similarity). Isoform 1 interacts (via cytoplasmic domain) with PTPN11 (preferentially) and PTPN6; cis-homodimer form is preferred; this interaction is decreased by formation of Isoform 1 /Isoform 8 cis-heterodimers and is dependent on the monomer/dimer equilibrium; this interaction is phosphorylation-dependent (PubMed:23696226).

Isoform 1 interacts with LYN (By similarity). Isoform 1 interacts (via cytoplasmic domain) with SRC (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:7478590). Isoform 1 interacts (via cytoplasmic domain) with LCK; mediates phosphorylation at Tyr-493 and Tyr-520 resulting in PTPN6 association.

Isoform 1 interacts with PTPN6; this interaction is phosphorylation-dependent and causes a profound decrease in TCR stimulation-induced CD247 and ZAP70 phosphorylation.

Isoform 1 interacts with TCR/CD3 complex through TCR beta chain and CD3E; colocalizes at the cell surface and upon stimulation of the TCR/CD3 complex recruits PTPN6 in the TCR/CD3 complex, resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Isoform 1 interacts (via cytoplasmic domain) with SHC1 (via SH2 domain); SHC1 mediates interaction with INSR or EGFR in a Ser-508 phosphorylation-dependent manner (By similarity).

Isoform 1 interacts with EGFR; the interaction is indirect (PubMed:15467833).

Isoform 1 interacts with CSF3R; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Isoform 1 (phosphorylated form) interacts with TLR4 and SYK; recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, leading to a reduction of the inflammasome activity (By similarity).

Isoform 1 interacts with FLNA; inhibits cell migration and cell scattering by interfering with the interaction of FLNA with RALA (PubMed:16291724). Isoform 1 interacts (via cytoplasmic domain) with PXN; the interaction is phosphotyrosyl-dependent (PubMed:11035932).

Isoform 1 interacts with KLRK1; recruits PTPN6 that dephosphorylates VAV1 (PubMed:23696226).

Isoform 1 interacts with CEACAM8 (PubMed:11994468).

Isoform 1 interacts with FASN; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).

Interacts (via Ig-like V-type) with HAVCR2 (via Ig-like V-type); facilitates the maturation and cell surface expression of HAVCR2 thereby regulating T cell tolerance induction (PubMed:25363763). Isoform 8 interacts (via the cytoplasmic domain) with ANXA2; this interaction is regulated by phosphorylation and appears in the AIIt complex (PubMed:14522961).

Interacts (via Lewis X moieties) with CD209 (via C-type lectin domain); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (PubMed:16246332).

By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107103, 12 interactors

Database of interacting proteins

More...DIPi		DIP-42683N

Protein interaction database and analysis system

More...IntActi		P13688, 7 interactors

Molecular INTeraction database

More...MINTi		P13688

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000161559

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P13688

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P13688

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini35 – 142Ig-like V-typeBy similarityAdd BLAST108
Domaini145 – 232Ig-like C2-type 1PROSITE-ProRule annotationAdd BLAST88
Domaini237 – 317Ig-like C2-type 2PROSITE-ProRule annotationAdd BLAST81
Domaini323 – 413Ig-like C2-type 3PROSITE-ProRule annotationAdd BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni39 – 142Required for homophilic bindingBy similarityAdd BLAST104
Regioni450 – 462Interaction with calmodulinBy similarityAdd BLAST13
Regioni452 – 526Interaction with FLNABy similarityAdd BLAST75
Regioni489 – 526Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation levelBy similarityAdd BLAST38
Regioni520 – 523Essential for interaction with PTPN11 and PTPN6By similarity4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Ig-like V-type domain mediates trans-homophilic cell adhesion through homodimerization and this active process is regulated by tyrosine kinase, PTPN11 AND PTPN6. Ig-like C2-type and/or cytoplasmic domains mediate cis-dimer/oligomer.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IFE1 Eukaryota
ENOG410YR1P LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00960000186634

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P13688

KEGG Orthology (KO)

More...KOi		K06499

Identification of Orthologs from Complete Genome Data

More...OMAi		NTSYLWS

Database of Orthologous Groups

More...OrthoDBi		998214at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P13688

TreeFam database of animal gene trees

More...TreeFami		TF336859

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
IPR013151 Immunoglobulin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00047 ig, 1 hit
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48726 SSF48726, 4 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50835 IG_LIKE, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (11+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 11 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 11 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P13688-1) [UniParc]FASTAAdd to basket
Also known as: BGPa, CEACAM1-4L1 Publication, TM1-CEA

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGHLSAPLHR VRVPWQGLLL TASLLTFWNP PTTAQLTTES MPFNVAEGKE 
        60         70         80         90        100
VLLLVHNLPQ QLFGYSWYKG ERVDGNRQIV GYAIGTQQAT PGPANSGRET 
       110        120        130        140        150
IYPNASLLIQ NVTQNDTGFY TLQVIKSDLV NEEATGQFHV YPELPKPSIS 
       160        170        180        190        200
SNNSNPVEDK DAVAFTCEPE TQDTTYLWWI NNQSLPVSPR LQLSNGNRTL 
       210        220        230        240        250
TLLSVTRNDT GPYECEIQNP VSANRSDPVT LNVTYGPDTP TISPSDTYYR 
       260        270        280        290        300
PGANLSLSCY AASNPPAQYS WLINGTFQQS TQELFIPNIT VNNSGSYTCH 
       310        320        330        340        350
ANNSVTGCNR TTVKTIIVTE LSPVVAKPQI KASKTTVTGD KDSVNLTCST 
       360        370        380        390        400
NDTGISIRWF FKNQSLPSSE RMKLSQGNTT LSINPVKRED AGTYWCEVFN 
       410        420        430        440        450
PISKNQSDPI MLNVNYNALP QENGLSPGAI AGIVIGVVAL VALIAVALAC 
       460        470        480        490        500
FLHFGKTGRA SDQRDLTEHK PSVSNHTQDH SNDPPNKMNE VTYSTLNFEA 
       510        520 
QQPTQPTSAS PSLTATEIIY SEVKKQ
Length:526
Mass (Da):57,560
Last modified:July 1, 1993 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCAD1B2328D069AF8
GO
Isoform 2 (identifier: P13688-2) [UniParc]FASTAAdd to basket
Also known as: BGPg, CEACAM1-4C11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     416-417: YN → CK
     418-526: Missing.

Show »
Length:417
Mass (Da):45,950
Checksum:i5D4B9F86184AA4B4
GO
Isoform 3 (identifier: P13688-3) [UniParc]FASTAAdd to basket
Also known as: BGPh, CEACAM1-31 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     320-321: EL → GK
     322-526: Missing.

Show »
Length:321
Mass (Da):35,302
Checksum:i81DE2F4E62AD42A7
GO
Isoform 4 (identifier: P13688-4) [UniParc]FASTAAdd to basket
Also known as: BGPi, CEACAM1-3C21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     321-351: LSPVVAKPQIKASKTTVTGDKDSVNLTCSTN → SPVLGEDEAVPGQHHPQHKPCQEGGCWDVLV
     352-526: Missing.

Show »
Length:351
Mass (Da):38,578
Checksum:i33CEF445429E8DD4
GO
Isoform 5 (identifier: P13688-5) [UniParc]FASTAAdd to basket
Also known as: BGPy, CEACAM1-3AL1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     321-416: LSPVVAKPQI...SDPIMLNVNY → RQNLTMLPRLDSNSWAQAILPSVSQSAEITD

Show »
Length:461
Mass (Da):50,349
Checksum:iE7810D2559DF7A8F
GO
Isoform 6 (identifier: P13688-6) [UniParc]FASTAAdd to basket
Also known as: BGPb, CEACAM1-3L1 Publication, TM2-CEA

The sequence of this isoform differs from the canonical sequence as follows:
     320-416: ELSPVVAKPQ...SDPIMLNVNY → D

Show »
Length:430
Mass (Da):46,910
Checksum:i195DE9F171D1414F
GO
Isoform 7 (identifier: P13688-7) [UniParc]FASTAAdd to basket
Also known as: BGPx, CEACAM1-1L1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     143-416: Missing.

Show »
Length:252
Mass (Da):27,431
Checksum:i6C85A702292B6367
GO
Isoform 8 (identifier: P13688-8) [UniParc]FASTAAdd to basket
Also known as: BGPc, CEACAM1-4S1 Publication, TM3-CEA

The sequence of this isoform differs from the canonical sequence as follows:
     459-464: RASDQR → SSGPLQ
     465-526: Missing.

Note: Pseudophosphorylated double mutant Thr-457->Asp and Ser-459->Asp. The single mutant Ser-459->Asp mutant highly binds with ANXA2.1 Publication
Show »
Length:464
Mass (Da):50,521
Checksum:i598E4D71BF05EDA9
GO
Isoform 9 (identifier: P13688-9) [UniParc]FASTAAdd to basket
Also known as: BGPz, CEACAM1-3AS

The sequence of this isoform differs from the canonical sequence as follows:
     321-416: LSPVVAKPQI...SDPIMLNVNY → MAFHHVAKAGLKLLSSSNPPASTSQSAKITD
     459-464: RASDQR → SSGPLQ
     465-526: Missing.

Show »
Length:399
Mass (Da):43,062
Checksum:i0BC49C50F3525841
GO
Isoform 10 (identifier: P13688-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     460-468: ASDQRDLTE → TTPMTHLTR
     469-526: Missing.

Note: No experimental confirmation available.
Show »
Length:468
Mass (Da):51,147
Checksum:i215C1A33EEFFFD68
GO
Isoform 11 (identifier: P13688-11) [UniParc]FASTAAdd to basket
Also known as: BGPd, CEACAM1-3S

The sequence of this isoform differs from the canonical sequence as follows:
     320-416: ELSPVVAKPQ...SDPIMLNVNY → D
     459-464: RASDQR → SSGPLQ
     465-526: Missing.

Show »
Length:368
Mass (Da):39,871
Checksum:i23D7E54B4DC54318
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R109M0R109_HUMAN
Carcinoembryonic antigen-related ce...
CEACAM1
99Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0R2K4M0R2K4_HUMAN
Carcinoembryonic antigen-related ce...
CEACAM1
94Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA57141 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti142P → H in AAA57142 (PubMed:8423792).Curated1
Sequence conflicti246D → Y in BAA02063 (Ref. 5) Curated1
Isoform 5 (identifier: P13688-5)
Sequence conflicti323N → L in AAA57143 (PubMed:8423792).Curated1
Sequence conflicti329R → G in BAA02063 (Ref. 5) Curated1
Sequence conflicti337Q → E in AAA57143 (PubMed:8423792).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04984435Q → K1 PublicationCorresponds to variant dbSNP:rs8111171Ensembl.1
Natural variantiVAR_04984583A → V1 PublicationCorresponds to variant dbSNP:rs8110904Ensembl.1
Natural variantiVAR_049846123Q → H1 PublicationCorresponds to variant dbSNP:rs8111468Ensembl.1
Natural variantiVAR_049847376Q → R1 PublicationCorresponds to variant dbSNP:rs41355544Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012222143 – 416Missing in isoform 7. 1 PublicationAdd BLAST274
Alternative sequenceiVSP_010938320 – 416ELSPV…LNVNY → D in isoform 6 and isoform 11. 2 PublicationsAdd BLAST97
Alternative sequenceiVSP_002478320 – 321EL → GK in isoform 3. 1 Publication2
Alternative sequenceiVSP_009227321 – 416LSPVV…LNVNY → RQNLTMLPRLDSNSWAQAIL PSVSQSAEITD in isoform 5. 2 PublicationsAdd BLAST96
Alternative sequenceiVSP_040571321 – 416LSPVV…LNVNY → MAFHHVAKAGLKLLSSSNPP ASTSQSAKITD in isoform 9. 1 PublicationAdd BLAST96
Alternative sequenceiVSP_002480321 – 351LSPVV…TCSTN → SPVLGEDEAVPGQHHPQHKP CQEGGCWDVLV in isoform 4. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_002479322 – 526Missing in isoform 3. 1 PublicationAdd BLAST205
Alternative sequenceiVSP_002481352 – 526Missing in isoform 4. 1 PublicationAdd BLAST175
Alternative sequenceiVSP_002482416 – 417YN → CK in isoform 2. 1 Publication2
Alternative sequenceiVSP_002483418 – 526Missing in isoform 2. 1 PublicationAdd BLAST109
Alternative sequenceiVSP_040572459 – 464RASDQR → SSGPLQ in isoform 8, isoform 9 and isoform 11. 4 Publications6
Alternative sequenceiVSP_040573460 – 468ASDQRDLTE → TTPMTHLTR in isoform 10. 1 Publication9
Alternative sequenceiVSP_040574465 – 526Missing in isoform 8, isoform 9 and isoform 11. 4 PublicationsAdd BLAST62
Alternative sequenceiVSP_040575469 – 526Missing in isoform 10. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J03858 mRNA Translation: AAA51826.1
X14831 mRNA Translation: CAA32940.1
X16354 mRNA Translation: CAA34404.1
X16356 mRNA Translation: CAA34405.1
D90311 mRNA Translation: BAA14341.1
D90312 mRNA Translation: BAA14342.1
D90313 mRNA Translation: BAA14343.1
M69176 mRNA Translation: AAA51825.1
M72238 mRNA Translation: AAA58393.1
M72238 mRNA Translation: AAA58394.1
M76741 Genomic DNA Translation: AAA57141.1 Sequence problems.
M76742 mRNA Translation: AAA57142.1
M76743 mRNA Translation: AAA57143.1
M76744 mRNA Translation: AAA57144.1
S71326 mRNA Translation: AAB31183.1
D12502 mRNA Translation: BAA02063.1
AY766113 mRNA Translation: AAV34600.1
DQ989182 Genomic DNA Translation: ABI75349.1
AC004785 Genomic DNA Translation: AAC18433.1
AC004785 Genomic DNA Translation: AAC18434.1
AC004785 Genomic DNA Translation: AAC18435.1
AC004785 Genomic DNA Translation: AAC18436.1
AC004785 Genomic DNA Translation: AAC18437.1
AC004785 Genomic DNA Translation: AAC18438.1
AC004785 Genomic DNA Translation: AAC18439.1
CH471126 Genomic DNA Translation: EAW57137.1
CH471126 Genomic DNA Translation: EAW57140.1
CH471126 Genomic DNA Translation: EAW57141.1
CH471126 Genomic DNA Translation: EAW57143.1
BC014473 mRNA Translation: AAH14473.1
X67277 Genomic DNA Translation: CAA47694.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12609.1 [P13688-1]
CCDS46089.1 [P13688-8]
CCDS54272.1 [P13688-11]
CCDS54273.1 [P13688-6]
CCDS54274.1 [P13688-5]

Protein sequence database of the Protein Information Resource

More...PIRi		A32164
B48078
JH0394
JH0395
JH0396

NCBI Reference Sequences

More...RefSeqi		NP_001020083.1, NM_001024912.2 [P13688-8]
NP_001171742.1, NM_001184813.1 [P13688-6]
NP_001171744.1, NM_001184815.1 [P13688-5]
NP_001171745.1, NM_001184816.1 [P13688-11]
NP_001192273.1, NM_001205344.1 [P13688-10]
NP_001703.2, NM_001712.4 [P13688-1]
XP_011525508.1, XM_011527206.1 [P13688-4]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000161559; ENSP00000161559; ENSG00000079385 [P13688-1]
ENST00000352591; ENSP00000244291; ENSG00000079385 [P13688-6]
ENST00000358394; ENSP00000351165; ENSG00000079385 [P13688-5]
ENST00000403444; ENSP00000384709; ENSG00000079385 [P13688-8]
ENST00000403461; ENSP00000384083; ENSG00000079385 [P13688-11]
ENST00000599389; ENSP00000471918; ENSG00000079385 [P13688-9]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		634

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:634

UCSC genome browser

More...UCSCi		uc002otv.3 human [P13688-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03858 mRNA Translation: AAA51826.1
X14831 mRNA Translation: CAA32940.1
X16354 mRNA Translation: CAA34404.1
X16356 mRNA Translation: CAA34405.1
D90311 mRNA Translation: BAA14341.1
D90312 mRNA Translation: BAA14342.1
D90313 mRNA Translation: BAA14343.1
M69176 mRNA Translation: AAA51825.1
M72238 mRNA Translation: AAA58393.1
M72238 mRNA Translation: AAA58394.1
M76741 Genomic DNA Translation: AAA57141.1 Sequence problems.
M76742 mRNA Translation: AAA57142.1
M76743 mRNA Translation: AAA57143.1
M76744 mRNA Translation: AAA57144.1
S71326 mRNA Translation: AAB31183.1
D12502 mRNA Translation: BAA02063.1
AY766113 mRNA Translation: AAV34600.1
DQ989182 Genomic DNA Translation: ABI75349.1
AC004785 Genomic DNA Translation: AAC18433.1
AC004785 Genomic DNA Translation: AAC18434.1
AC004785 Genomic DNA Translation: AAC18435.1
AC004785 Genomic DNA Translation: AAC18436.1
AC004785 Genomic DNA Translation: AAC18437.1
AC004785 Genomic DNA Translation: AAC18438.1
AC004785 Genomic DNA Translation: AAC18439.1
CH471126 Genomic DNA Translation: EAW57137.1
CH471126 Genomic DNA Translation: EAW57140.1
CH471126 Genomic DNA Translation: EAW57141.1
CH471126 Genomic DNA Translation: EAW57143.1
BC014473 mRNA Translation: AAH14473.1
X67277 Genomic DNA Translation: CAA47694.1
CCDSiCCDS12609.1 [P13688-1]
CCDS46089.1 [P13688-8]
CCDS54272.1 [P13688-11]
CCDS54273.1 [P13688-6]
CCDS54274.1 [P13688-5]
PIRiA32164
B48078
JH0394
JH0395
JH0396
RefSeqiNP_001020083.1, NM_001024912.2 [P13688-8]
NP_001171742.1, NM_001184813.1 [P13688-6]
NP_001171744.1, NM_001184815.1 [P13688-5]
NP_001171745.1, NM_001184816.1 [P13688-11]
NP_001192273.1, NM_001205344.1 [P13688-10]
NP_001703.2, NM_001712.4 [P13688-1]
XP_011525508.1, XM_011527206.1 [P13688-4]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GK2X-ray2.20A/B34-141[»]
4QXWX-ray2.04A/B35-141[»]
4WHDX-ray2.50A/B34-141[»]
5DZLX-ray3.40A/B/C/D35-141[»]
6AW2X-ray2.68A34-141[»]
6GBGX-ray2.80D35-142[»]
6GBHX-ray2.59B/D35-142[»]
SMRiP13688
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107103, 12 interactors
DIPiDIP-42683N
IntActiP13688, 7 interactors
MINTiP13688
STRINGi9606.ENSP00000161559

Chemistry databases

DrugBankiDB00113 Technetium Tc-99m arcitumomab

PTM databases

GlyConnecti1070
1072
iPTMnetiP13688
PhosphoSitePlusiP13688

Polymorphism and mutation databases

BioMutaiCEACAM1
DMDMi399116

Proteomic databases

CPTACiCPTAC-1179
jPOSTiP13688
MassIVEiP13688
MaxQBiP13688
PaxDbiP13688
PeptideAtlasiP13688
PRIDEiP13688
ProteomicsDBi52961 [P13688-1]
52962 [P13688-10]
52963 [P13688-11]
52964 [P13688-2]
52965 [P13688-3]
52966 [P13688-4]
52967 [P13688-5]
52968 [P13688-6]
52969 [P13688-7]
52970 [P13688-8]
52971 [P13688-9]
TopDownProteomicsiP13688-2 [P13688-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		634

Genome annotation databases

EnsembliENST00000161559; ENSP00000161559; ENSG00000079385 [P13688-1]
ENST00000352591; ENSP00000244291; ENSG00000079385 [P13688-6]
ENST00000358394; ENSP00000351165; ENSG00000079385 [P13688-5]
ENST00000403444; ENSP00000384709; ENSG00000079385 [P13688-8]
ENST00000403461; ENSP00000384083; ENSG00000079385 [P13688-11]
ENST00000599389; ENSP00000471918; ENSG00000079385 [P13688-9]
GeneIDi634
KEGGihsa:634
UCSCiuc002otv.3 human [P13688-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		634
DisGeNETi634

GeneCards: human genes, protein and diseases

More...GeneCardsi		CEACAM1
HGNCiHGNC:1814 CEACAM1
HPAiCAB002146
HPA011041
MIMi109770 gene
neXtProtiNX_P13688
OpenTargetsiENSG00000079385
PharmGKBiPA26358

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IFE1 Eukaryota
ENOG410YR1P LUCA
GeneTreeiENSGT00960000186634
InParanoidiP13688
KOiK06499
OMAiNTSYLWS
OrthoDBi998214at2759
PhylomeDBiP13688
TreeFamiTF336859

Enzyme and pathway databases

ReactomeiR-HSA-1566977 Fibronectin matrix formation
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-6798695 Neutrophil degranulation
SIGNORiP13688

Miscellaneous databases

EvolutionaryTraceiP13688

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CEACAM1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		634
PharosiP13688

Protein Ontology

More...PROi		PR:P13688

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000079385 Expressed in 158 organ(s), highest expression level in colonic mucosa
ExpressionAtlasiP13688 baseline and differential
GenevisibleiP13688 HS

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013106 Ig_V-set
IPR013151 Immunoglobulin
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF13895 Ig_2, 1 hit
PF07686 V-set, 1 hit
SMARTiView protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 3 hits
SUPFAMiSSF48726 SSF48726, 4 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCEAM1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13688
Secondary accession number(s): A6NE38
, A8MY49, O60430, Q069I7, Q13854, Q13857, Q13858, Q13859, Q13860, Q15600, Q15601, Q16170, Q5UB49, Q7KYP5, Q96CA7, Q9UQV9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 1, 1993
Last modified: October 16, 2019
This is version 212 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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