CEACAM1
entrez
634
canonical
uniprot
P13688
canonical
ensembl
ENSG00000079385
resolver
ensp
ENSP00000161559
resolver
ensp
ENSP00000244291
resolver
ensp
ENSP00000351165
resolver
ensp
ENSP00000384083
resolver
ensp
ENSP00000384709
resolver
ensp
ENSP00000649176
resolver
ensp
ENSP00000649177
resolver
genesymbol
CEACAM1
resolver
genesymbol_syn
BGP
resolver
genesymbol_syn
BGP1
resolver
hgnc
HGNC:1814
resolver
uniprot
A6NE38
resolver
uniprot
A8MY49
resolver
uniprot
O60430
resolver
uniprot
Q069I7
resolver
uniprot
Q13854
resolver
uniprot
Q13857
resolver
uniprot
Q13858
resolver
uniprot
Q13859
resolver
uniprot
Q13860
resolver
uniprot
Q15600
resolver
uniprot
Q15601
resolver
uniprot
Q16170
resolver
uniprot
Q3KRG8
resolver
uniprot
Q5UB49
resolver
uniprot
Q7KYP5
resolver
uniprot
Q96CA7
resolver
uniprot
Q9UQV9
resolver
uniprot_entry
CEAM1_HUMAN
resolver
uniprot_entry
Q3KRG8_HUMAN
resolver
uniprot_sec
A6NE38
resolver
uniprot_sec
A8MY49
resolver
uniprot_sec
O60430
resolver
uniprot_sec
Q069I7
resolver
uniprot_sec
Q13854
resolver
uniprot_sec
Q13857
resolver
uniprot_sec
Q13858
resolver
uniprot_sec
Q13859
resolver
uniprot_sec
Q13860
resolver
uniprot_sec
Q15600
resolver
uniprot_sec
Q15601
resolver
uniprot_sec
Q16170
resolver
uniprot_sec
Q5UB49
resolver
uniprot_sec
Q7KYP5
resolver
uniprot_sec
Q96CA7
resolver
uniprot_sec
Q9UQV9
resolver
amino_acid_sequence
MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTATEIIYSEVKKQ
uniprot
proteins
function
FUNCTION: [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 also functions 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; interferes 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). {ECO:0000250|UniProtKB:P16573, ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:16291724, ECO:0000269|PubMed:18424730, ECO:0000269|PubMed:23696226, ECO:0000269|PubMed:25363763}.; FUNCTION: [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). {ECO:0000250|UniProtKB:P16573, ECO:0000250|UniProtKB:P31809}.
uniprot
proteins
mass_dalton
57560
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="N->A: Impairs interaction with HAVCR2."; /evidence="ECO:0000269|PubMed:25363763"; MUTAGEN 77..78; /note="RQ->GL: Doesn't affect cell surface expression. Impairs phosphorylation."; /evidence="ECO:0000269|PubMed:18424730"; MUTAGEN 81; /note="G->A: Impairs interaction with HAVCR2."; /evidence="ECO:0000269|PubMed:25363763"; MUTAGEN 457; /note="T->D: Decreases the binding to ANXA2."; /evidence="ECO:0000269|PubMed:14522961"; MUTAGEN 493; /note="Y->F: Impairs phosphorylation; when associated with F-520."; /evidence="ECO:0000269|PubMed:18424730"; MUTAGEN 520; /note="Y->F: Impairs phosphorylation; when associated with F-493."; /evidence="ECO:0000269|PubMed:18424730
uniprot
proteins
post_translational_modification
PTM: [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). {ECO:0000250|UniProtKB:P16573, ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:15467833, ECO:0000269|PubMed:18424730, ECO:0000269|PubMed:7478590}.; PTM: [Isoform 8]: Phosphorylated on serine and threonine. {ECO:0000269|PubMed:14522961}.
uniprot
proteins
protein_family
CEA family
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
10436421
uniprot
proteins
pubmed
11035932
uniprot
proteins
pubmed
11501563
uniprot
proteins
pubmed
11994468
uniprot
proteins
pubmed
14522961
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15467833
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16246332
uniprot
proteins
pubmed
16291724
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16929097
uniprot
proteins
pubmed
18424730
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
2025273
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23696226
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2457922
uniprot
proteins
pubmed
25363763
uniprot
proteins
pubmed
2537311
uniprot
proteins
pubmed
26483485
uniprot
proteins
pubmed
7478590
uniprot
proteins
pubmed
7628460
uniprot
proteins
pubmed
8018919
uniprot
proteins
pubmed
8055923
uniprot
proteins
pubmed
8423792
uniprot
proteins
sequence_length
526
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:P16573}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000269|PubMed:16291724}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. 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. {ECO:0000250|UniProtKB:P16573}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:2025273}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:2025273}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:2025273}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane {ECO:0000269|PubMed:14522961}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16573}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:14522961}. Lateral cell membrane {ECO:0000250|UniProtKB:P16573}. Apical cell membrane {ECO:0000250|UniProtKB:P16573}. Basal cell membrane {ECO:0000250|UniProtKB:P16573}. Cell junction {ECO:0000269|PubMed:8018919}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P16573}. 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). {ECO:0000250|UniProtKB:P16573, ECO:0000269|PubMed:14522961}.; SUBCELLULAR LOCATION: Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P31809}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:10436421}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized to the apical glycocalyx surface (PubMed:10436421). Colocalizes with CEACAM20 at the apical brush border of intestinal cells. {ECO:0000250|UniProtKB:P31809, ECO:0000269|PubMed:10436421}.
uniprot
proteins
transmembrane_region
TRANSMEM 429..452; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins