UniProtKB - P13688 (CEAM1_HUMAN)
Carcinoembryonic antigen-related cell adhesion molecule 1
CEACAM1
Functioni
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. Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating 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).
Down-regulates 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 PublicationsCell 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 similarityGO - Molecular functioni
- actin binding Source: UniProtKB
- bile acid transmembrane transporter activity Source: UniProtKB
- calmodulin binding Source: UniProtKB
- filamin binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- kinase binding Source: UniProtKB
- protein dimerization activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- protein phosphatase binding Source: UniProtKB
- protein tyrosine kinase binding Source: UniProtKB
GO - Biological processi
- angiogenesis Source: UniProtKB
- bile acid and bile salt transport Source: UniProtKB
- blood vessel development Source: UniProtKB
- cell adhesion Source: UniProtKB
- cell-cell adhesion via plasma-membrane adhesion molecules Source: UniProtKB
- cell migration Source: UniProtKB
- cellular response to insulin stimulus Source: UniProtKB
- common myeloid progenitor cell proliferation Source: UniProtKB
- granulocyte colony-stimulating factor signaling pathway Source: UniProtKB
- homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
- insulin catabolic process Source: UniProtKB
- insulin receptor internalization Source: UniProtKB
- integrin-mediated signaling pathway Source: UniProtKB
- negative regulation of cytotoxic T cell degranulation Source: UniProtKB
- negative regulation of fatty acid biosynthetic process Source: UniProtKB
- negative regulation of granulocyte differentiation Source: UniProtKB
- negative regulation of hepatocyte proliferation Source: UniProtKB
- negative regulation of interleukin-1 production Source: UniProtKB
- negative regulation of lipid biosynthetic process Source: UniProtKB
- negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target Source: UniProtKB
- negative regulation of platelet aggregation Source: UniProtKB
- negative regulation of protein kinase activity Source: UniProtKB
- negative regulation of T cell mediated cytotoxicity Source: UniProtKB
- negative regulation of T cell receptor signaling pathway Source: UniProtKB
- negative regulation of vascular permeability Source: UniProtKB
- positive regulation of vasculogenesis Source: UniProtKB
- regulation of blood vessel remodeling Source: UniProtKB
- regulation of cell growth Source: UniProtKB
- regulation of cell migration Source: UniProtKB
- regulation of endothelial cell differentiation Source: UniProtKB
- regulation of endothelial cell migration Source: UniProtKB
- regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
- regulation of ERK1 and ERK2 cascade Source: UniProtKB
- regulation of homophilic cell adhesion Source: UniProtKB
- regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
- regulation of sprouting angiogenesis Source: UniProtKB
- wound healing, spreading of cells Source: UniProtKB
Enzyme and pathway databases
PathwayCommonsi | P13688 |
Reactomei | R-HSA-1566977, Fibronectin matrix formation R-HSA-202733, Cell surface interactions at the vascular wall R-HSA-6798695, Neutrophil degranulation |
SignaLinki | P13688 |
SIGNORi | P13688 |
Names & Taxonomyi
Protein namesi | Recommended name: Carcinoembryonic antigen-related cell adhesion molecule 11 PublicationAlternative name(s): Biliary glycoprotein 11 Publication Short name: BGP-1 CD_antigen: CD66a |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1814, CEACAM1 |
MIMi | 109770, gene |
neXtProti | NX_P13688 |
VEuPathDBi | HostDB:ENSG00000079385 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type I membrane protein By similarity
- Lateral cell membrane By similarity
- Apical cell membrane By similarity
- Basal cell membrane By similarity
Other locations
- Cell junction 1 Publication
- adherens junction By similarity
Note: Canalicular domain of hepatocyte plasma membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions. Found as dimer in the solution. Predominantly localized to the lateral cell membranes.By similarity
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- Secreted 1 Publication
Plasma membrane
Plasma membrane
Plasma membrane
Plasma membrane
- Cell membrane 1 Publication; Single-pass type I membrane protein By similarity
- Lateral cell membrane By similarity
- Apical cell membrane By similarity
- Basal cell membrane By similarity
Other locations
- secretory vesicle membrane 1 Publication
- Cell junction 1 Publication
- adherens junction By similarity
Note: Predominantly localized to the lateral cell membranes. Found as a mixture of monomer, dimer and oligomer in the plasma membrane. Occurs predominantly as cis-dimers and/or small cis-oligomers in the cell junction regions (By similarity). Co-localizes with ANXA2 in secretory vesicles and with S100A10/p11 at the plasma membrane (PubMed:14522961).By similarity1 Publication
Plasma membrane
- microvillus membrane By similarity; Single-pass type I membrane protein Curated
- Apical cell membrane 1 Publication; Single-pass type I membrane protein Curated
Note: Localized to the apical glycocalyx surface (PubMed:10436421). Colocalizes with CEACAM20 at the apical brush border of intestinal cells.By similarity1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- basal plasma membrane Source: UniProtKB
- integral component of plasma membrane Source: UniProtKB
- lateral plasma membrane Source: UniProtKB
- microvillus membrane Source: UniProtKB-SubCell
- plasma membrane Source: UniProtKB
Other locations
- adherens junction Source: UniProtKB
- cell junction Source: UniProtKB
- cell surface Source: UniProtKB
- cell-cell junction Source: UniProtKB
- integral component of membrane Source: MGI
- membrane Source: ProtInc
- specific granule membrane Source: Reactome
- tertiary granule membrane Source: Reactome
- transport vesicle membrane Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 35 – 428 | ExtracellularSequence analysisAdd BLAST | 394 | |
Transmembranei | 429 – 452 | HelicalSequence analysisAdd BLAST | 24 | |
Topological domaini | 453 – 526 | CytoplasmicSequence analysisAdd BLAST | 74 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Membrane, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 76 | N → A: Impairs interaction with HAVCR2. 1 Publication | 1 | |
Mutagenesisi | 77 – 78 | RQ → GL: Doesn't affect cell surface expression. Impairs phosphorylation. 1 Publication | 2 | |
Mutagenesisi | 81 | G → A: Impairs interaction with HAVCR2. 1 Publication | 1 | |
Mutagenesisi | 457 | T → D: Decreases the binding to ANXA2. 1 Publication | 1 | |
Mutagenesisi | 493 | Y → F: Impairs phosphorylation; when associated with F-520. 1 Publication | 1 | |
Mutagenesisi | 520 | Y → F: Impairs phosphorylation; when associated with F-493. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 634 |
OpenTargetsi | ENSG00000079385 |
PharmGKBi | PA26358 |
Miscellaneous databases
Pharosi | P13688, Tbio |
Chemistry databases
DrugBanki | DB00113, Technetium Tc-99m arcitumomab |
Genetic variation databases
BioMutai | CEACAM1 |
DMDMi | 399116 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 34 | Add BLAST | 34 | |
ChainiPRO_0000014562 | 35 – 526 | Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST | 492 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 35 | Pyrrolidone carboxylic acid1 Publication | 1 | |
Glycosylationi | 104 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 111 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 115 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 152 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Disulfide bondi | 167 ↔ 215 | PROSITE-ProRule annotation | ||
Glycosylationi | 182 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 197 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 208 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 224 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 232 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 254 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 259 ↔ 299 | PROSITE-ProRule annotation | ||
Glycosylationi | 274 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 288 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 292 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 302 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 309 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 345 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 348 ↔ 396 | PROSITE-ProRule annotationBy similarity | ||
Glycosylationi | 351 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 363 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 378 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Glycosylationi | 405 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication | 1 | |
Modified residuei | 493 | Phosphotyrosine; by SRC, LCK, INSR and EGFR2 Publications | 1 | |
Modified residuei | 508 | PhosphoserineBy similarity | 1 | |
Modified residuei | 520 | Phosphotyrosine; by INSR, SRC and LCK2 Publications | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acidProteomic databases
CPTACi | CPTAC-1179 |
EPDi | P13688 |
jPOSTi | P13688 |
MassIVEi | P13688 |
MaxQBi | P13688 |
PaxDbi | P13688 |
PeptideAtlasi | P13688 |
PRIDEi | P13688 |
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] |
TopDownProteomicsi | P13688-2 [P13688-2] |
PTM databases
GlyConnecti | 1070, 14 N-Linked glycans (5 sites) |
GlyGeni | P13688, 24 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site) |
iPTMneti | P13688 |
PhosphoSitePlusi | P13688 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000079385, Expressed in colonic mucosa and 176 other tissues |
ExpressionAtlasi | P13688, baseline and differential |
Genevisiblei | P13688, HS |
Organism-specific databases
HPAi | ENSG00000079385, Tissue enhanced (intestine) |
Interactioni
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 PublicationsBinary interactionsi
P13688
GO - Molecular functioni
- actin binding Source: UniProtKB
- calmodulin binding Source: UniProtKB
- filamin binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- kinase binding Source: UniProtKB
- protein dimerization activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- protein phosphatase binding Source: UniProtKB
- protein tyrosine kinase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 107103, 12 interactors |
DIPi | DIP-42683N |
IntActi | P13688, 11 interactors |
MINTi | P13688 |
STRINGi | 9606.ENSP00000161559 |
Miscellaneous databases
RNActi | P13688, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P13688 |
SMRi | P13688 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P13688 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 35 – 142 | Ig-like V-typeBy similarityAdd BLAST | 108 | |
Domaini | 145 – 232 | Ig-like C2-type 1PROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 237 – 317 | Ig-like C2-type 2PROSITE-ProRule annotationAdd BLAST | 81 | |
Domaini | 323 – 413 | Ig-like C2-type 3PROSITE-ProRule annotationAdd BLAST | 91 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 39 – 142 | Required for homophilic bindingBy similarityAdd BLAST | 104 | |
Regioni | 450 – 462 | Interaction with calmodulinBy similarityAdd BLAST | 13 | |
Regioni | 452 – 526 | Interaction with FLNABy similarityAdd BLAST | 75 | |
Regioni | 461 – 513 | DisorderedSequence analysisAdd BLAST | 53 | |
Regioni | 489 – 526 | Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation levelBy similarityAdd BLAST | 38 | |
Regioni | 520 – 523 | Essential for interaction with PTPN11 and PTPN6By similarity | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 461 – 476 | Basic and acidic residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 477 – 513 | Polar residuesSequence analysisAdd BLAST | 37 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG502RXPD, Eukaryota |
GeneTreei | ENSGT00960000186634 |
HOGENOMi | CLU_024555_2_0_1 |
InParanoidi | P13688 |
OMAi | WENSENY |
OrthoDBi | 998214at2759 |
PhylomeDBi | P13688 |
TreeFami | TF336859 |
Family and domain databases
Gene3Di | 2.60.40.10, 4 hits |
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 |
Pfami | View protein in Pfam PF00047, ig, 1 hit PF13895, Ig_2, 1 hit PF07686, V-set, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 4 hits SM00408, IGc2, 3 hits |
SUPFAMi | SSF48726, SSF48726, 4 hits |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 3 hits |
s (11+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 11 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 11 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
The sequence of this isoform differs from the canonical sequence as follows:
459-464: RASDQR → SSGPLQ
465-526: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
460-468: ASDQRDLTE → TTPMTHLTR
469-526: Missing.
The sequence of this isoform differs from the canonical sequence as follows:
320-416: ELSPVVAKPQ...SDPIMLNVNY → D
459-464: RASDQR → SSGPLQ
465-526: Missing.
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A7I2V3A7 | A0A7I2V3A7_HUMAN | Carcinoembryonic antigen-related ce... | CEACAM1 | 54 | Annotation score: | ||
M0R109 | M0R109_HUMAN | Carcinoembryonic antigen-related ce... | CEACAM1 | 99 | Annotation score: | ||
M0R2K4 | M0R2K4_HUMAN | Carcinoembryonic antigen-related ce... | CEACAM1 | 94 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Sequence conflicti | 142 | P → H in AAA57142 (PubMed:8423792).Curated | 1 | ||
Sequence conflicti | 246 | D → Y in BAA02063 (Ref. 5) Curated | 1 | ||
Isoform 5 (identifier: P13688-5) | |||||
Sequence conflicti | 323 | N → L in AAA57143 (PubMed:8423792).Curated | 1 | ||
Sequence conflicti | 329 | R → G in BAA02063 (Ref. 5) Curated | 1 | ||
Sequence conflicti | 337 | Q → E in AAA57143 (PubMed:8423792).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_049844 | 35 | Q → K1 PublicationCorresponds to variant dbSNP:rs8111171Ensembl. | 1 | |
Natural variantiVAR_049845 | 83 | A → V1 PublicationCorresponds to variant dbSNP:rs8110904Ensembl. | 1 | |
Natural variantiVAR_049846 | 123 | Q → H1 PublicationCorresponds to variant dbSNP:rs8111468Ensembl. | 1 | |
Natural variantiVAR_049847 | 376 | Q → R1 PublicationCorresponds to variant dbSNP:rs41355544Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_012222 | 143 – 416 | Missing in isoform 7. 1 PublicationAdd BLAST | 274 | |
Alternative sequenceiVSP_010938 | 320 – 416 | ELSPV…LNVNY → D in isoform 6 and isoform 11. 2 PublicationsAdd BLAST | 97 | |
Alternative sequenceiVSP_002478 | 320 – 321 | EL → GK in isoform 3. 1 Publication | 2 | |
Alternative sequenceiVSP_009227 | 321 – 416 | LSPVV…LNVNY → RQNLTMLPRLDSNSWAQAIL PSVSQSAEITD in isoform 5. 2 PublicationsAdd BLAST | 96 | |
Alternative sequenceiVSP_040571 | 321 – 416 | LSPVV…LNVNY → MAFHHVAKAGLKLLSSSNPP ASTSQSAKITD in isoform 9. 1 PublicationAdd BLAST | 96 | |
Alternative sequenceiVSP_002480 | 321 – 351 | LSPVV…TCSTN → SPVLGEDEAVPGQHHPQHKP CQEGGCWDVLV in isoform 4. 1 PublicationAdd BLAST | 31 | |
Alternative sequenceiVSP_002479 | 322 – 526 | Missing in isoform 3. 1 PublicationAdd BLAST | 205 | |
Alternative sequenceiVSP_002481 | 352 – 526 | Missing in isoform 4. 1 PublicationAdd BLAST | 175 | |
Alternative sequenceiVSP_002482 | 416 – 417 | YN → CK in isoform 2. 1 Publication | 2 | |
Alternative sequenceiVSP_002483 | 418 – 526 | Missing in isoform 2. 1 PublicationAdd BLAST | 109 | |
Alternative sequenceiVSP_040572 | 459 – 464 | RASDQR → SSGPLQ in isoform 8, isoform 9 and isoform 11. 4 Publications | 6 | |
Alternative sequenceiVSP_040573 | 460 – 468 | ASDQRDLTE → TTPMTHLTR in isoform 10. 1 Publication | 9 | |
Alternative sequenceiVSP_040574 | 465 – 526 | Missing in isoform 8, isoform 9 and isoform 11. 4 PublicationsAdd BLAST | 62 | |
Alternative sequenceiVSP_040575 | 469 – 526 | Missing in isoform 10. 1 PublicationAdd BLAST | 58 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000161559.11; ENSP00000161559.6; ENSG00000079385.23 ENST00000352591.9; ENSP00000244291.6; ENSG00000079385.23 [P13688-6] ENST00000358394.7; ENSP00000351165.2; ENSG00000079385.23 [P13688-5] ENST00000403444.7; ENSP00000384709.3; ENSG00000079385.23 [P13688-8] ENST00000403461.5; ENSP00000384083.1; ENSG00000079385.23 [P13688-11] ENST00000599389.1; ENSP00000471918.1; ENSG00000079385.23 [P13688-9] |
GeneIDi | 634 |
KEGGi | hsa:634 |
MANE-Selecti | ENST00000161559.11; ENSP00000161559.6; NM_001712.5; NP_001703.2 |
UCSCi | uc002otv.3, human [P13688-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
SeattleSNPs |
Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2GK2 | X-ray | 2.20 | A/B | 34-141 | [»] | |
4QXW | X-ray | 2.04 | A/B | 35-141 | [»] | |
4WHD | X-ray | 2.50 | A/B | 34-141 | [»] | |
5DZL | X-ray | 3.40 | A/B/C/D | 35-141 | [»] | |
6AW2 | X-ray | 2.68 | A | 34-141 | [»] | |
6GBG | X-ray | 2.80 | D | 35-142 | [»] | |
6GBH | X-ray | 2.59 | B/D | 35-142 | [»] | |
6V3P | X-ray | 3.25 | A/B | 34-141 | [»] | |
6XNO | X-ray | 1.90 | A/B | 35-141 | [»] | |
6XNT | X-ray | 3.10 | A/B | 35-141 | [»] | |
6XNW | X-ray | 1.90 | A/B/C/D | 35-141 | [»] | |
6XO1 | X-ray | 1.76 | A/B | 35-141 | [»] | |
AlphaFoldDBi | P13688 | |||||
SMRi | P13688 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107103, 12 interactors |
DIPi | DIP-42683N |
IntActi | P13688, 11 interactors |
MINTi | P13688 |
STRINGi | 9606.ENSP00000161559 |
Chemistry databases
DrugBanki | DB00113, Technetium Tc-99m arcitumomab |
PTM databases
GlyConnecti | 1070, 14 N-Linked glycans (5 sites) |
GlyGeni | P13688, 24 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site) |
iPTMneti | P13688 |
PhosphoSitePlusi | P13688 |
Genetic variation databases
BioMutai | CEACAM1 |
DMDMi | 399116 |
Proteomic databases
CPTACi | CPTAC-1179 |
EPDi | P13688 |
jPOSTi | P13688 |
MassIVEi | P13688 |
MaxQBi | P13688 |
PaxDbi | P13688 |
PeptideAtlasi | P13688 |
PRIDEi | P13688 |
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] |
TopDownProteomicsi | P13688-2 [P13688-2] |
Protocols and materials databases
Antibodypediai | 3684, 997 antibodies from 44 providers |
DNASUi | 634 |
Genome annotation databases
Organism-specific databases
CTDi | 634 |
DisGeNETi | 634 |
GeneCardsi | CEACAM1 |
HGNCi | HGNC:1814, CEACAM1 |
HPAi | ENSG00000079385, Tissue enhanced (intestine) |
MIMi | 109770, gene |
neXtProti | NX_P13688 |
OpenTargetsi | ENSG00000079385 |
PharmGKBi | PA26358 |
VEuPathDBi | HostDB:ENSG00000079385 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502RXPD, Eukaryota |
GeneTreei | ENSGT00960000186634 |
HOGENOMi | CLU_024555_2_0_1 |
InParanoidi | P13688 |
OMAi | WENSENY |
OrthoDBi | 998214at2759 |
PhylomeDBi | P13688 |
TreeFami | TF336859 |
Enzyme and pathway databases
PathwayCommonsi | P13688 |
Reactomei | R-HSA-1566977, Fibronectin matrix formation R-HSA-202733, Cell surface interactions at the vascular wall R-HSA-6798695, Neutrophil degranulation |
SignaLinki | P13688 |
SIGNORi | P13688 |
Miscellaneous databases
BioGRID-ORCSi | 634, 17 hits in 1081 CRISPR screens |
EvolutionaryTracei | P13688 |
GeneWikii | CEACAM1 |
GenomeRNAii | 634 |
Pharosi | P13688, Tbio |
PROi | PR:P13688 |
RNActi | P13688, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000079385, Expressed in colonic mucosa and 176 other tissues |
ExpressionAtlasi | P13688, baseline and differential |
Genevisiblei | P13688, HS |
Family and domain databases
Gene3Di | 2.60.40.10, 4 hits |
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 |
Pfami | View protein in Pfam PF00047, ig, 1 hit PF13895, Ig_2, 1 hit PF07686, V-set, 1 hit |
SMARTi | View protein in SMART SM00409, IG, 4 hits SM00408, IGc2, 3 hits |
SUPFAMi | SSF48726, SSF48726, 4 hits |
PROSITEi | View protein in PROSITE PS50835, IG_LIKE, 3 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | CEAM1_HUMAN | |
Accessioni | P13688Primary (citable) accession number: P13688 Secondary accession number(s): A6NE38 Q9UQV9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | July 1, 1993 | |
Last modified: | May 25, 2022 | |
This is version 225 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries - Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families