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Q9BY67 (CADM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell adhesion molecule 1
Alternative name(s):
Immunoglobulin superfamily member 4
Short name=IgSF4
Nectin-like protein 2
Short name=NECL-2
Spermatogenic immunoglobulin superfamily
Short name=SgIgSF
Synaptic cell adhesion molecule
Short name=SynCAM
Tumor suppressor in lung cancer 1
Short name=TSLC-1
Gene names
Name:CADM1
Synonyms:IGSF4, IGSF4A, NECL2, SYNCAM, TSLC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca2+-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. Acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly By similarity. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa. Ref.2 Ref.7 Ref.8 Ref.9 Ref.12 Ref.15 Ref.17 UniProtKB Q8R5M8

Subunit structure

Homodimer. Interacts with FARP1 By similarity. Interacts with CRTAM. Interacts (via C-terminus) with EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP3 and the PDZ domain of MPP6. Ref.8 Ref.9 Ref.13 Ref.15 Ref.16 Ref.22

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell junctionsynapse By similarity. Note: Associates with perinuclear and plasma membranes in vivo. Localized to the basolateral plasma membrane of epithelial cells in gall bladder. Ref.2 Ref.7 UniProtKB Q8R5M8

Domain

The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC. Ref.10 Ref.14

Post-translational modification

Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and synapse induction By similarity.

Sequence similarities

Belongs to the nectin family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Sequence caution

The sequence AAI25103.1 differs from that shown. Reason: Frameshift at position 1.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
Differentiation
Immunity
Spermatogenesis
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction organization

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

bone development

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

calcium-independent cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell junction assembly

Traceable author statement. Source: Reactome

cell recognition

Inferred from direct assay Ref.15. Source: UniProtKB

cell-cell junction organization

Traceable author statement. Source: Reactome

detection of stimulus

Inferred from direct assay Ref.15. Source: UniProtKB

heterophilic cell-cell adhesion

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

homophilic cell adhesion

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of natural killer cell mediated cytotoxicity

Inferred from direct assay Ref.15. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

susceptibility to natural killer cell mediated cytotoxicity

Inferred from direct assay Ref.15. Source: UniProtKB

synapse assembly

Inferred from electronic annotation. Source: Ensembl

unidimensional cell growth

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

cell-cell junction

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.15. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionPDZ domain binding

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

protein C-terminus binding

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity PubMed 12826663. Source: UniProtKB

receptor binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9BY67-1)

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.
Isoform 2 Ref.2 (identifier: Q9BY67-2)

The sequence of this isoform differs from the canonical sequence as follows:
     332-333: DP → GT
     334-442: Missing.
Isoform 3 (identifier: Q9BY67-3)

The sequence of this isoform differs from the canonical sequence as follows:
     359-359: T → TDTTATTEPAVHGLTQLPNSAEELDSEDLS
Isoform 4 (identifier: Q9BY67-4)

The sequence of this isoform differs from the canonical sequence as follows:
     359-359: T → TDTTATTEPAVH
Isoform 5 (identifier: Q9BY67-5)

The sequence of this isoform differs from the canonical sequence as follows:
     333-360: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444 Potential
Chain45 – 442398Cell adhesion molecule 1
PRO_0000291968

Regions

Topological domain45 – 374330Extracellular Potential
Transmembrane375 – 39521Helical; Potential
Topological domain396 – 44247Cytoplasmic Potential
Domain45 – 13995Ig-like V-type
Domain144 – 23895Ig-like C2-type 1
Domain243 – 32987Ig-like C2-type 2

Amino acid modifications

Modified residue4341Phosphoserine By similarity
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Ref.18 Ref.19 Ref.20
Glycosylation1131N-linked (GlcNAc...) Ref.18 Ref.19 Ref.20
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...); atypical Ref.20
Glycosylation3021N-linked (GlcNAc...); atypical Ref.20
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 124 By similarity
Disulfide bond166 ↔ 220 By similarity
Disulfide bond267 ↔ 313 By similarity

Natural variations

Alternative sequence332 – 3332DP → GT in isoform 2. Ref.2
VSP_052461
Alternative sequence333 – 36028Missing in isoform 5.
VSP_047405
Alternative sequence334 – 442109Missing in isoform 2. Ref.2
VSP_052462
Alternative sequence3591T → TDTTATTEPAVHGLTQLPNS AEELDSEDLS in isoform 3.
VSP_047406
Alternative sequence3591T → TDTTATTEPAVH in isoform 4.
VSP_047407
Natural variant2851D → E.
Corresponds to variant rs45525440 [ dbSNP | Ensembl ].
VAR_061309

Experimental info

Mutagenesis4061Y → A: Nearly abolishes EPB41L3 binding. Ref.22
Mutagenesis4081T → A: Strongly reduced affinity for EPB41L3. Ref.22
Sequence conflict131A → V in CCD32613. Ref.2
Sequence conflict1531K → R in AAF69029. Ref.1
Sequence conflict333 – 35927PPTTI…LTIIT → TTATTEPAVHGLTQLPNSAE ELDSEDLS in BAC11657. Ref.4

Secondary structure

....................... 442
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: CDEDE1E0C08BDD3A

FASTA44248,509
        10         20         30         40         50         60 
MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA 

        70         80         90        100        110        120 
TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG 

       130        140        150        160        170        180 
RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF 

       190        200        210        220        230        240 
KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ 

       250        260        270        280        290        300 
YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI 

       310        320        330        340        350        360 
NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT TTTILTIITD 

       370        380        390        400        410        420 
SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA RHKGTYFTHE AKGADDAADA 

       430        440 
DTAIINAEGG QNNSEEKKEY FI 

« Hide

Isoform 2 [UniParc].

Checksum: D7C1102F46D08492
Show »

FASTA33336,915
Isoform 3 [UniParc].

Checksum: 322A71AB89E8B21F
Show »

FASTA47151,533
Isoform 4 [UniParc].

Checksum: 466DC2D374481CFB
Show »

FASTA45349,633
Isoform 5 [UniParc].

Checksum: 4C5AB05F34BA714A
Show »

FASTA41445,624

References

« Hide 'large scale' references
[1]"Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane."
Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B., Fan M., Peng X., Qiang B., Yuan J.
Biochim. Biophys. Acta 1669:142-154(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"CADM1 isoforms differentially regulate human mast cell survival and homotypic adhesion."
Moiseeva E.P., Leyland M.L., Bradding P.
Cell. Mol. Life Sci. 69:2751-2764(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
Tissue: Mast cell.
[3]"Cloning of a secretory isoform of SgIGSF/TSLC-1."
Ito A., Koma Y., Nagano T.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Lung.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryo.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[7]"TSLC1 is a tumor-suppressor gene in human non-small-cell lung cancer."
Kuramochi M., Fukuhara H., Nobukuni T., Kanbe T., Maruyama T., Ghosh H.P., Pletcher M., Isomura M., Onizuka M., Kitamura T., Sekiya T., Reeves R.H., Murakami Y.
Nat. Genet. 27:427-430(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer."
Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., Shibuya M., Murakami Y.
Cancer Res. 62:5129-5133(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPB41L3.
[9]"The tumor suppressor protein TSLC1 is involved in cell-cell adhesion."
Masuda M., Yageta M., Fukuhara H., Kuramochi M., Maruyama T., Nomoto A., Murakami Y.
J. Biol. Chem. 277:31014-31019(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION.
[10]"The cytoplasmic domain is critical to the tumor suppressor activity of TSLC1 in non-small cell lung cancer."
Mao X., Seidlitz E., Ghosh K., Murakami Y., Ghosh H.P.
Cancer Res. 63:7979-7985(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[11]"Promoter methylation of the TSLC1 gene in advanced lung tumors and various cancer cell lines."
Fukami T., Fukuhara H., Kuramochi M., Maruyama T., Isogai K., Sakamoto M., Takamoto S., Murakami Y.
Int. J. Cancer 107:53-59(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[12]"Expression of the TSLC1 adhesion molecule in pulmonary epithelium and its down-regulation in pulmonary adenocarcinoma other than bronchioloalveolar carcinoma."
Ito A., Okada M., Uchino K., Wakayama T., Koma Y., Iseki S., Tsubota N., Okita Y., Kitamura Y.
Lab. Invest. 83:1175-1183(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue of Drosophila tumor suppressor Dlg."
Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M., Maruyama T., Kitamura T., Murakami Y.
Oncogene 22:6160-6165(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP3.
[14]"Re-expression of TSLC1 in a non-small-cell lung cancer cell line induces apoptosis and inhibits tumor growth."
Mao X., Seidlitz E., Truant R., Hitt M., Ghosh H.P.
Oncogene 23:5632-5642(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[15]"The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM."
Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.
Blood 106:779-786(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CRTAM.
[16]"Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and is a ligand for class-I-restricted T-cell-associated molecule."
Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.
J. Biol. Chem. 280:21955-21964(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTAM.
[17]"The spermatogenic Ig superfamily/synaptic cell adhesion molecule mast-cell adhesion molecule promotes interaction with nerves."
Furuno T., Ito A., Koma Y., Watabe K., Yokozaki H., Bienenstock J., Nakanishi M., Kitamura Y.
J. Immunol. 174:6934-6942(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113.
Tissue: Plasma.
[19]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113.
Tissue: Liver.
[20]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-113; ASN-301 AND ASN-302.
Tissue: Leukemic T-cell.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)."
Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C., Obrink B., Hallberg B.M.
J. Biol. Chem. 286:4511-4516(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 400-411 IN COMPLEX WITH EPB41L3, MUTAGENESIS OF TYR-406 AND THR-408, INTERACTION WITH EPB41L3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132811 mRNA. Translation: AAF69029.1.
HE586496 mRNA. Translation: CCD32610.1.
HE586497 mRNA. Translation: CCD32611.1.
HE586498 mRNA. Translation: CCD32612.1.
HE586499 mRNA. Translation: CCD32613.1.
AB094146 mRNA. Translation: BAC66178.1.
AK075502 mRNA. Translation: BAC11657.1.
AP000462 Genomic DNA. No translation available.
AP000465 Genomic DNA. No translation available.
AP003174 Genomic DNA. No translation available.
AP003179 Genomic DNA. No translation available.
AP005020 Genomic DNA. No translation available.
BC125102 mRNA. Translation: AAI25103.1. Frameshift.
RefSeqNP_001091987.1. NM_001098517.1.
NP_055148.3. NM_014333.3.
XP_005271548.1. XM_005271491.2.
XP_005271549.1. XM_005271492.2.
XP_005271550.1. XM_005271493.2.
UniGeneHs.370510.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BINX-ray2.30B400-411[»]
4H5SX-ray1.70B45-144[»]
ProteinModelPortalQ9BY67.
SMRQ9BY67. Positions 45-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117218. 3 interactions.
DIPDIP-57599N.
IntActQ9BY67. 4 interactions.
MINTMINT-1184987.
STRING9606.ENSP00000329797.

PTM databases

PhosphoSiteQ9BY67.

Polymorphism databases

DMDM150438862.

Proteomic databases

PaxDbQ9BY67.
PRIDEQ9BY67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331581; ENSP00000329797; ENSG00000182985. [Q9BY67-3]
ENST00000452722; ENSP00000395359; ENSG00000182985. [Q9BY67-1]
ENST00000537058; ENSP00000439817; ENSG00000182985. [Q9BY67-4]
ENST00000542447; ENSP00000439176; ENSG00000182985. [Q9BY67-5]
GeneID23705.
KEGGhsa:23705.
UCSCuc001ppi.4. human. [Q9BY67-1]
uc001ppl.3. human. [Q9BY67-2]

Organism-specific databases

CTD23705.
GeneCardsGC11M115044.
HGNCHGNC:5951. CADM1.
HPACAB037266.
MIM605686. gene.
neXtProtNX_Q9BY67.
PharmGKBPA29764.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69486.
HOGENOMHOG000036057.
HOVERGENHBG057086.
KOK06781.
OMAEIYTTIT.
OrthoDBEOG7PVWPD.
PhylomeDBQ9BY67.
TreeFamTF334317.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ9BY67.
BgeeQ9BY67.
CleanExHS_CADM1.
GenevestigatorQ9BY67.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028807. Cadm.
IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR003585. Neurexin-like.
[Graphical view]
PANTHERPTHR23277:SF15. PTHR23277:SF15. 1 hit.
PfamPF08205. C2-set_2. 1 hit.
PF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCADM1. human.
EvolutionaryTraceQ9BY67.
GeneWikiCell_adhesion_molecule_1.
GenomeRNAi23705.
NextBio35461775.
PROQ9BY67.
SOURCESearch...

Entry information

Entry nameCADM1_HUMAN
AccessionPrimary (citable) accession number: Q9BY67
Secondary accession number(s): A4FVB5 expand/collapse secondary AC list , F5H0J4, H0YGA7, H1ZZV9, H1ZZW1, H1ZZW2, Q86WB8, Q8N2F4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM