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Q9BY67

- CADM1_HUMAN

UniProt

Q9BY67 - CADM1_HUMAN

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Protein

Cell adhesion molecule 1

Gene

CADM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity7 Publications

GO - Molecular functioni

  1. PDZ domain binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. receptor binding Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. apoptotic process Source: UniProtKB-KW
  3. bone development Source: Ensembl
  4. brain development Source: Ensembl
  5. calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: Ensembl
  6. cell-cell junction organization Source: Reactome
  7. cell differentiation Source: UniProtKB-KW
  8. cell junction assembly Source: Reactome
  9. cell recognition Source: UniProtKB
  10. detection of stimulus Source: UniProtKB
  11. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  12. homophilic cell adhesion via plasma membrane adhesion molecules Source: UniProtKB
  13. immune system process Source: UniProtKB-KW
  14. liver development Source: Ensembl
  15. positive regulation of cytokine secretion Source: UniProtKB
  16. positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  17. spermatogenesis Source: UniProtKB-KW
  18. susceptibility to natural killer cell mediated cytotoxicity Source: UniProtKB
  19. synapse assembly Source: Ensembl
  20. unidimensional cell growth Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Cell adhesion, Differentiation, Immunity, Spermatogenesis

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CADM1Imported
Synonyms:IGSF4By similarity, IGSF4A, NECL21 Publication, SYNCAMBy similarity, TSLC11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:5951. CADM1.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. 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.By similarity1 PublicationSequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini45 – 374330ExtracellularSequence AnalysisAdd
BLAST
Transmembranei375 – 39521HelicalSequence AnalysisAdd
BLAST
Topological domaini396 – 44247CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. basolateral plasma membrane Source: UniProtKB
  3. cell-cell junction Source: UniProtKB
  4. dendrite Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. integral component of membrane Source: UniProtKB-KW
  7. plasma membrane Source: UniProtKB
  8. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi406 – 4061Y → A: Nearly abolishes EPB41L3 binding. 1 Publication
Mutagenesisi408 – 4081T → A: Strongly reduced affinity for EPB41L3. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA29764.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444Sequence AnalysisAdd
BLAST
Chaini45 – 442398Cell adhesion molecule 1Sequence AnalysisPRO_0000291968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 124PROSITE-ProRule annotation
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)3 Publications
Glycosylationi113 – 1131N-linked (GlcNAc...)3 Publications
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi166 ↔ 220PROSITE-ProRule annotation
Disulfide bondi267 ↔ 313PROSITE-ProRule annotation
Glycosylationi301 – 3011N-linked (GlcNAc...); atypical1 Publication
Glycosylationi302 – 3021N-linked (GlcNAc...); atypical1 Publication
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Modified residuei434 – 4341PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9BY67.
PaxDbiQ9BY67.
PRIDEiQ9BY67.

PTM databases

PhosphoSiteiQ9BY67.

Expressioni

Gene expression databases

BgeeiQ9BY67.
CleanExiHS_CADM1.
ExpressionAtlasiQ9BY67. baseline and differential.
GenevestigatoriQ9BY67.

Organism-specific databases

HPAiCAB037266.

Interactioni

Subunit structurei

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.By similarity6 Publications

Protein-protein interaction databases

BioGridi117218. 3 interactions.
DIPiDIP-57599N.
IntActiQ9BY67. 4 interactions.
MINTiMINT-1184987.
STRINGi9606.ENSP00000329797.

Structurei

Secondary structure

1
442
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 554Combined sources
Beta strandi60 – 689Combined sources
Beta strandi74 – 774Combined sources
Beta strandi83 – 864Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi106 – 1138Combined sources
Helixi116 – 1183Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi132 – 14110Combined sources
Beta strandi405 – 4073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BINX-ray2.30B400-411[»]
4H5SX-ray1.70B45-144[»]
ProteinModelPortaliQ9BY67.
SMRiQ9BY67. Positions 45-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BY67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 13995Ig-like V-typeSequence AnalysisAdd
BLAST
Domaini144 – 23895Ig-like C2-type 1Sequence AnalysisAdd
BLAST
Domaini243 – 32987Ig-like C2-type 2Sequence AnalysisAdd
BLAST

Domaini

The cytoplasmic domain appears to play a critical role in proapoptosis and tumor suppressor activity in NSCLC.2 Publications

Sequence similaritiesi

Belongs to the nectin family.Curated
Contains 2 Ig-like C2-type (immunoglobulin-like) domains.Sequence Analysis
Contains 1 Ig-like V-type (immunoglobulin-like) domain.Sequence Analysis

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG69486.
GeneTreeiENSGT00770000120518.
HOGENOMiHOG000036057.
HOVERGENiHBG057086.
InParanoidiQ9BY67.
KOiK06781.
OMAiEIYTTIT.
OrthoDBiEOG7PVWPD.
PhylomeDBiQ9BY67.
TreeFamiTF334317.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. 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]
PfamiPF08205. C2-set_2. 1 hit.
PF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9BY67-1) [UniParc]FASTAAdd to Basket

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
MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK
60 70 80 90 100
DVTVIEGEVA TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL
110 120 130 140 150
NFSSSELKVS LTNVSISDEG RYFCQLYTDP PQESYTTITV LVPPRNLMID
160 170 180 190 200
IQKDTAVEGE EIEVNCTAMA SKPATTIRWF KGNTELKGKS EVEEWSDMYT
210 220 230 240 250
VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ YKPQVHIQMT
260 270 280 290 300
YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI
310 320 330 340 350
NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT
360 370 380 390 400
TTTILTIITD SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA
410 420 430 440
RHKGTYFTHE AKGADDAADA DTAIINAEGG QNNSEEKKEY FI
Length:442
Mass (Da):48,509
Last modified:June 26, 2007 - v2
Checksum:iCDEDE1E0C08BDD3A
GO
Isoform 21 Publication (identifier: Q9BY67-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     332-333: DP → GT
     334-442: Missing.

Show »
Length:333
Mass (Da):36,915
Checksum:iD7C1102F46D08492
GO
Isoform 3 (identifier: Q9BY67-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     359-359: T → TDTTATTEPAVHGLTQLPNSAEELDSEDLS

Show »
Length:471
Mass (Da):51,533
Checksum:i322A71AB89E8B21F
GO
Isoform 4 (identifier: Q9BY67-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     359-359: T → TDTTATTEPAVH

Show »
Length:453
Mass (Da):49,633
Checksum:i466DC2D374481CFB
GO
Isoform 5 (identifier: Q9BY67-5) [UniParc]FASTAAdd to Basket

Also known as: E

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

Show »
Length:414
Mass (Da):45,624
Checksum:i4C5AB05F34BA714A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131A → V in CCD32613. (PubMed:22438059)Curated
Sequence conflicti153 – 1531K → R in AAF69029. (PubMed:15893517)Curated
Sequence conflicti333 – 35927PPTTI…LTIIT → TTATTEPAVHGLTQLPNSAE ELDSEDLS in BAC11657. (PubMed:14702039)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti285 – 2851D → E.
Corresponds to variant rs45525440 [ dbSNP | Ensembl ].
VAR_061309

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei332 – 3332DP → GT in isoform 2. 1 PublicationVSP_052461
Alternative sequencei333 – 36028Missing in isoform 5. 2 PublicationsVSP_047405Add
BLAST
Alternative sequencei334 – 442109Missing in isoform 2. 1 PublicationVSP_052462Add
BLAST
Alternative sequencei359 – 3591T → TDTTATTEPAVHGLTQLPNS AEELDSEDLS in isoform 3. 1 PublicationVSP_047406
Alternative sequencei359 – 3591T → TDTTATTEPAVH in isoform 4. 1 PublicationVSP_047407

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
KJ534791 mRNA. Translation: AHW56431.1.
KJ534794 mRNA. Translation: AHW56434.1.
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.
CCDSiCCDS53711.1. [Q9BY67-5]
CCDS73398.1. [Q9BY67-4]
CCDS73399.1. [Q9BY67-3]
CCDS8373.1. [Q9BY67-1]
RefSeqiNP_001091987.1. NM_001098517.1. [Q9BY67-5]
NP_001287972.1. NM_001301043.1. [Q9BY67-3]
NP_001287973.1. NM_001301044.1. [Q9BY67-4]
NP_001287974.1. NM_001301045.1.
NP_055148.3. NM_014333.3. [Q9BY67-1]
UniGeneiHs.370510.

Genome annotation databases

EnsembliENST00000331581; ENSP00000329797; ENSG00000182985. [Q9BY67-3]
ENST00000452722; ENSP00000395359; ENSG00000182985. [Q9BY67-1]
ENST00000537058; ENSP00000439817; ENSG00000182985. [Q9BY67-4]
ENST00000542447; ENSP00000439176; ENSG00000182985. [Q9BY67-5]
GeneIDi23705.
KEGGihsa:23705.
UCSCiuc001pph.5. human.
uc001ppi.4. human. [Q9BY67-1]
uc001ppj.4. human.
uc001ppl.3. human. [Q9BY67-2]

Polymorphism databases

DMDMi150438862.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
KJ534791 mRNA. Translation: AHW56431.1 .
KJ534794 mRNA. Translation: AHW56434.1 .
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.
CCDSi CCDS53711.1. [Q9BY67-5 ]
CCDS73398.1. [Q9BY67-4 ]
CCDS73399.1. [Q9BY67-3 ]
CCDS8373.1. [Q9BY67-1 ]
RefSeqi NP_001091987.1. NM_001098517.1. [Q9BY67-5 ]
NP_001287972.1. NM_001301043.1. [Q9BY67-3 ]
NP_001287973.1. NM_001301044.1. [Q9BY67-4 ]
NP_001287974.1. NM_001301045.1.
NP_055148.3. NM_014333.3. [Q9BY67-1 ]
UniGenei Hs.370510.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BIN X-ray 2.30 B 400-411 [» ]
4H5S X-ray 1.70 B 45-144 [» ]
ProteinModelPortali Q9BY67.
SMRi Q9BY67. Positions 45-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117218. 3 interactions.
DIPi DIP-57599N.
IntActi Q9BY67. 4 interactions.
MINTi MINT-1184987.
STRINGi 9606.ENSP00000329797.

PTM databases

PhosphoSitei Q9BY67.

Polymorphism databases

DMDMi 150438862.

Proteomic databases

MaxQBi Q9BY67.
PaxDbi Q9BY67.
PRIDEi Q9BY67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331581 ; ENSP00000329797 ; ENSG00000182985 . [Q9BY67-3 ]
ENST00000452722 ; ENSP00000395359 ; ENSG00000182985 . [Q9BY67-1 ]
ENST00000537058 ; ENSP00000439817 ; ENSG00000182985 . [Q9BY67-4 ]
ENST00000542447 ; ENSP00000439176 ; ENSG00000182985 . [Q9BY67-5 ]
GeneIDi 23705.
KEGGi hsa:23705.
UCSCi uc001pph.5. human.
uc001ppi.4. human. [Q9BY67-1 ]
uc001ppj.4. human.
uc001ppl.3. human. [Q9BY67-2 ]

Organism-specific databases

CTDi 23705.
GeneCardsi GC11M115044.
HGNCi HGNC:5951. CADM1.
HPAi CAB037266.
MIMi 605686. gene.
neXtProti NX_Q9BY67.
PharmGKBi PA29764.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69486.
GeneTreei ENSGT00770000120518.
HOGENOMi HOG000036057.
HOVERGENi HBG057086.
InParanoidi Q9BY67.
KOi K06781.
OMAi EIYTTIT.
OrthoDBi EOG7PVWPD.
PhylomeDBi Q9BY67.
TreeFami TF334317.

Enzyme and pathway databases

Reactomei REACT_19195. Adherens junctions interactions.
REACT_19268. Nectin/Necl trans heterodimerization.

Miscellaneous databases

ChiTaRSi CADM1. human.
EvolutionaryTracei Q9BY67.
GeneWikii Cell_adhesion_molecule_1.
GenomeRNAii 23705.
NextBioi 35461775.
PROi Q9BY67.
SOURCEi Search...

Gene expression databases

Bgeei Q9BY67.
CleanExi HS_CADM1.
ExpressionAtlasi Q9BY67. baseline and differential.
Genevestigatori Q9BY67.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi 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 ]
Pfami PF08205. C2-set_2. 1 hit.
PF07679. I-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
SMARTi SM00294. 4.1m. 1 hit.
SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Fetal brain.
  4. "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: LungImported.
  5. "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.
    , 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: EmbryoImported.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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: Plasma1 Publication.
  20. "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.
  21. "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.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.

Entry informationi

Entry nameiCADM1_HUMAN
AccessioniPrimary (citable) accession number: Q9BY67
Secondary accession number(s): A4FVB5
, F5H0J4, H0YGA7, H1ZZV9, H1ZZW1, H1ZZW2, Q86WB8, Q8N2F4, X5D2C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: November 26, 2014
This is version 118 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3