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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-Experimental evidence at protein leveli

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

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • bile acid transmembrane transporter activity Source: UniProtKB
  • filamin 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

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079385-MONOMER.
ReactomeiR-HSA-1566977. Fibronectin matrix formation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-6798695. Neutrophil degranulation.
SIGNORiP13688.

Names & Taxonomyi

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
Gene namesi
Name:CEACAM1Imported
Synonyms:BGP1 Publication, BGP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1814. CEACAM1.

Subcellular locationi

Isoform 1 :
  • 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
  • Cell junction 1 Publication
  • Cell junctionadherens 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
Isoform 2 :
Isoform 3 :
Isoform 4 :
Isoform 8 :
  • Cell membrane 1 Publication; Single-pass type I membrane protein By similarity
  • Cytoplasmic vesiclesecretory vesicle membrane 1 Publication
  • Lateral cell membrane By similarity
  • Apical cell membrane By similarity
  • Basal cell membrane By similarity
  • Cell junction 1 Publication
  • Cell junctionadherens 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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 428ExtracellularSequence analysisAdd BLAST394
Transmembranei429 – 452HelicalSequence analysisAdd BLAST24
Topological domaini453 – 526CytoplasmicSequence analysisAdd BLAST74

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • basal plasma membrane Source: UniProtKB
  • cell-cell junction Source: UniProtKB
  • cell junction Source: UniProtKB
  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • lateral plasma membrane Source: UniProtKB
  • membrane Source: ProtInc
  • plasma membrane Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi634.
OpenTargetsiENSG00000079385.
PharmGKBiPA26358.

Chemistry databases

DrugBankiDB00113. Arcitumomab.

Polymorphism and mutation databases

BioMutaiCEACAM1.
DMDMi399116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Add BLAST34
ChainiPRO_000001456235 – 526Carcinoembryonic antigen-related cell adhesion molecule 1Add BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35Pyrrolidone carboxylic acid1 Publication1
Glycosylationi104N-linked (GlcNAc...)1 Publication1
Glycosylationi111N-linked (GlcNAc...)1 Publication1
Glycosylationi115N-linked (GlcNAc...)1
Glycosylationi152N-linked (GlcNAc...)1 Publication1
Disulfide bondi167 ↔ 215Curated
Glycosylationi182N-linked (GlcNAc...)Sequence analysis1
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Glycosylationi208N-linked (GlcNAc...)1 Publication1
Glycosylationi224N-linked (GlcNAc...)1 Publication1
Glycosylationi232N-linked (GlcNAc...)Sequence analysis1
Glycosylationi254N-linked (GlcNAc...)1
Disulfide bondi259 ↔ 299Curated
Glycosylationi274N-linked (GlcNAc...)Sequence analysis1
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1
Glycosylationi292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi302N-linked (GlcNAc...)Sequence analysis1
Glycosylationi309N-linked (GlcNAc...)Sequence analysis1
Glycosylationi345N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi348 ↔ 396PROSITE-ProRule annotationBy similarity
Glycosylationi351N-linked (GlcNAc...)Sequence analysis1
Glycosylationi363N-linked (GlcNAc...)1 Publication1
Glycosylationi378N-linked (GlcNAc...)1 Publication1
Glycosylationi405N-linked (GlcNAc...)1 Publication1
Modified residuei493Phosphotyrosine; by SRC; LCK; INSR and EGFRBy similarity2 Publications1
Modified residuei508PhosphoserineBy similarity1
Modified residuei520Phosphotyrosine; by INSR; SRC and LCKBy similarity2 Publications1

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

MaxQBiP13688.
PaxDbiP13688.
PeptideAtlasiP13688.
PRIDEiP13688.
TopDownProteomicsiP13688-2. [P13688-2]

PTM databases

iPTMnetiP13688.
PhosphoSitePlusiP13688.

Expressioni

Tissue specificityi

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).2 Publications

Inductioni

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

Gene expression databases

BgeeiENSG00000079385.
CleanExiHS_CEACAM1.
ExpressionAtlasiP13688. baseline and differential.
GenevisibleiP13688. HS.

Organism-specific databases

HPAiCAB002146.
HPA011041.

Interactioni

Subunit structurei

Monomer. Oligomer. Heterodimer. Homodimer. 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 recuits 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 similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CARTPTQ165683EBI-4314481,EBI-4314526
CEACAM6P401992EBI-4314481,EBI-4314501
uspa1Q8GH8712EBI-4314481,EBI-7936357From a different organism.

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • filamin 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

BioGridi107103. 12 interactors.
DIPiDIP-42683N.
IntActiP13688. 6 interactors.
MINTiMINT-5002435.
STRINGi9606.ENSP00000161559.

Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 46Combined sources10
Beta strandi51 – 56Combined sources6
Beta strandi60 – 73Combined sources14
Helixi75 – 77Combined sources3
Beta strandi78 – 83Combined sources6
Turni84 – 87Combined sources4
Beta strandi88 – 91Combined sources4
Beta strandi99 – 101Combined sources3
Beta strandi107 – 109Combined sources3
Helixi114 – 116Combined sources3
Beta strandi118 – 126Combined sources9
Beta strandi132 – 141Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP13688.
SMRiP13688.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13688.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 142Ig-like V-typeAdd BLAST108
Domaini145 – 232Ig-like C2-type 1Add BLAST88
Domaini237 – 317Ig-like C2-type 2Add BLAST81
Domaini323 – 413Ig-like C2-type 3Add BLAST91

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. CEA family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOVERGENiHBG007922.
InParanoidiP13688.
KOiK06499.
OMAiNDPPNKM.
OrthoDBiEOG091G0AMM.
PhylomeDBiP13688.
TreeFamiTF336859.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (11)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 11 isoformsi produced by alternative splicing. AlignAdd to basket

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 'canonical' 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
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

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Natural variantiVAR_04984435Q → K.1 PublicationCorresponds to variant rs8111171dbSNPEnsembl.1
Natural variantiVAR_04984583A → V.1 PublicationCorresponds to variant rs8110904dbSNPEnsembl.1
Natural variantiVAR_049846123Q → H.1 PublicationCorresponds to variant rs8111468dbSNPEnsembl.1
Natural variantiVAR_049847376Q → R.1 PublicationCorresponds to variant rs41355544dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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]
UniGeneiHs.512682.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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]
UniGeneiHs.512682.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP13688.
SMRiP13688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107103. 12 interactors.
DIPiDIP-42683N.
IntActiP13688. 6 interactors.
MINTiMINT-5002435.
STRINGi9606.ENSP00000161559.

Chemistry databases

DrugBankiDB00113. Arcitumomab.

PTM databases

iPTMnetiP13688.
PhosphoSitePlusiP13688.

Polymorphism and mutation databases

BioMutaiCEACAM1.
DMDMi399116.

Proteomic databases

MaxQBiP13688.
PaxDbiP13688.
PeptideAtlasiP13688.
PRIDEiP13688.
TopDownProteomicsiP13688-2. [P13688-2]

Protocols and materials databases

DNASUi634.
Structural Biology KnowledgebaseSearch...

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

CTDi634.
DisGeNETi634.
GeneCardsiCEACAM1.
H-InvDBHIX0017795.
HGNCiHGNC:1814. CEACAM1.
HPAiCAB002146.
HPA011041.
MIMi109770. gene.
neXtProtiNX_P13688.
OpenTargetsiENSG00000079385.
PharmGKBiPA26358.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFE1. Eukaryota.
ENOG410YR1P. LUCA.
GeneTreeiENSGT00760000119187.
HOVERGENiHBG007922.
InParanoidiP13688.
KOiK06499.
OMAiNDPPNKM.
OrthoDBiEOG091G0AMM.
PhylomeDBiP13688.
TreeFamiTF336859.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079385-MONOMER.
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.
GeneWikiiCEACAM1.
GenomeRNAii634.
PROiP13688.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079385.
CleanExiHS_CEACAM1.
ExpressionAtlasiP13688. baseline and differential.
GenevisibleiP13688. HS.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF13895. Ig_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCEAM1_HUMAN
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
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 185 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.