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Q12860

- CNTN1_HUMAN

UniProt

Q12860 - CNTN1_HUMAN

Protein

Contactin-1

Gene

CNTN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth By similarity.By similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: Ensembl

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell adhesion Source: ProtInc
    3. cerebellum development Source: Ensembl
    4. Notch signaling pathway Source: Reactome
    5. positive regulation of gene expression Source: Ensembl
    6. positive regulation of neuron projection development Source: Ensembl
    7. positive regulation of sodium ion transport Source: Ensembl

    Keywords - Biological processi

    Cell adhesion, Notch signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_22205. L1CAM interactions.
    REACT_22312. Neurofascin interactions.
    SignaLinkiQ12860.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Contactin-1
    Alternative name(s):
    Glycoprotein gp135
    Neural cell surface protein F3
    Gene namesi
    Name:CNTN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:2171. CNTN1.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: ProtInc
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Compton-North congenital myopathy (CNCM) [MIM:612540]: Familial lethal form of congenital onset muscle weakness, inherited in an autosomal-recessive fashion and characterized by a secondary loss of beta2-syntrophin and alpha-dystrobrevin from the muscle sarcolemma, central nervous system involvement, and fetal akinesia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi612540. phenotype.
    Orphaneti210163. Congenital lethal myopathy, Compton-North type.
    PharmGKBiPA26685.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – ?993973Contactin-1PRO_0000014685Add
    BLAST
    Propeptidei?994 – 101825Removed in mature formPRO_0000014686Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi65 ↔ 114PROSITE-ProRule annotation
    Disulfide bondi158 ↔ 211PROSITE-ProRule annotation
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi263 ↔ 310PROSITE-ProRule annotation
    Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi352 ↔ 391PROSITE-ProRule annotation
    Disulfide bondi436 ↔ 484PROSITE-ProRule annotation
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi494 – 4941N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi526 ↔ 583PROSITE-ProRule annotation
    Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi933 – 9331N-linked (GlcNAc...)Sequence Analysis
    Lipidationi993 – 9931GPI-anchor amidated serineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ12860.
    PaxDbiQ12860.
    PRIDEiQ12860.

    PTM databases

    PhosphoSiteiQ12860.

    Expressioni

    Tissue specificityi

    Strongly expressed in brain and in neuroblastoma and retinoblastoma cell lines. Lower levels of expression in lung, pancreas, kidney and skeletal muscle.2 Publications

    Gene expression databases

    ArrayExpressiQ12860.
    BgeeiQ12860.
    CleanExiHS_CNTN1.
    GenevestigatoriQ12860.

    Organism-specific databases

    HPAiCAB025200.
    HPA041060.

    Interactioni

    Subunit structurei

    Monomer. Interacts with CNTNAP1 in cis form. Interacts with NOTCH1 and TNR By similarity. Binds to the carbonic-anhydrase like domain of PTPRZ1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi107672. 10 interactions.
    DIPiDIP-59714N.
    IntActiQ12860. 4 interactions.
    MINTiMINT-2806030.
    STRINGi9606.ENSP00000325660.

    Structurei

    Secondary structure

    1
    1018
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi146 – 1494
    Beta strandi154 – 1563
    Beta strandi162 – 1665
    Beta strandi169 – 1768
    Beta strandi184 – 1896
    Turni191 – 1933
    Beta strandi196 – 2005
    Helixi203 – 2053
    Beta strandi207 – 2159
    Helixi216 – 2183
    Beta strandi220 – 2234
    Beta strandi227 – 2326
    Beta strandi240 – 2478
    Beta strandi251 – 2544
    Beta strandi259 – 26911
    Beta strandi272 – 2776
    Beta strandi287 – 2893
    Turni290 – 2934
    Beta strandi294 – 2974
    Helixi302 – 3043
    Beta strandi306 – 3149
    Beta strandi317 – 32812
    Beta strandi816 – 8216
    Beta strandi824 – 8285
    Beta strandi839 – 84911
    Helixi851 – 8533
    Beta strandi855 – 8606
    Beta strandi864 – 8685
    Beta strandi876 – 8849
    Beta strandi886 – 8883
    Beta strandi896 – 8994

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EE2NMR-A798-903[»]
    3S97X-ray2.30C/D133-329[»]
    ProteinModelPortaliQ12860.
    SMRiQ12860. Positions 37-1001.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12860.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 13191Ig-like C2-type 1Add
    BLAST
    Domaini137 – 22387Ig-like C2-type 2Add
    BLAST
    Domaini241 – 32686Ig-like C2-type 3Add
    BLAST
    Domaini331 – 40777Ig-like C2-type 4Add
    BLAST
    Domaini413 – 50088Ig-like C2-type 5Add
    BLAST
    Domaini504 – 60198Ig-like C2-type 6Add
    BLAST
    Domaini606 – 70499Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini709 – 80698Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini811 – 90696Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 100094Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi602 – 6098Gly/Pro-rich

    Sequence similaritiesi

    Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG293951.
    HOVERGENiHBG051047.
    InParanoidiQ12860.
    KOiK06759.
    OMAiFTWYRRY.
    OrthoDBiEOG7J17Z5.
    PhylomeDBiQ12860.
    TreeFamiTF351103.

    Family and domain databases

    Gene3Di2.60.40.10. 10 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view]
    PfamiPF00041. fn3. 3 hits.
    PF07679. I-set. 3 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 4 hits.
    SM00409. IG. 2 hits.
    SM00408. IGc2. 4 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    PROSITEiPS50853. FN3. 4 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12860-1) [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

    MKMWLLVSHL VIISITTCLA EFTWYRRYGH GVSEEDKGFG PIFEEQPINT     50
    IYPEESLEGK VSLNCRARAS PFPVYKWRMN NGDVDLTSDR YSMVGGNLVI 100
    NNPDKQKDAG IYYCLASNNY GMVRSTEATL SFGYLDPFPP EERPEVRVKE 150
    GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF ITMDKRRFVS QTNGNLYIAN 200
    VEASDKGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY PADIVVQFKD 250
    VYALMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI 300
    QLEDEGIYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW 350
    PCVATGKPIP TIRWLKNGYA YHKGELRLYD VTFENAGMYQ CIAENTYGAI 400
    YANAELKILA LAPTFEMNPM KKKILAAKGG RVIIECKPKA APKPKFSWSK 450
    GTEWLVNSSR ILIWEDGSLE INNITRNDGG IYTCFAENNR GKANSTGTLV 500
    ITDPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW SFNGYVIDFN 550
    KENIHYQRNF MLDSNGELLI RNAQLKHAGR YTCTAQTIVD NSSASADLVV 600
    RGPPGPPGGL RIEDIRATSV ALTWSRGSDN HSPISKYTIQ TKTILSDDWK 650
    DAKTDPPIIE GNMEAARAVD LIPWMEYEFR VVATNTLGRG EPSIPSNRIK 700
    TDGAAPNVAP SDVGGGGGRN RELTITWAPL SREYHYGNNF GYIVAFKPFD 750
    GEEWKKVTVT NPDTGRYVHK DETMSPSTAF QVKVKAFNNK GDGPYSLVAV 800
    INSAQDAPSE APTEVGVKVL SSSEISVHWE HVLEKIVESY QIRYWAAHDK 850
    EEAANRVQVT SQEYSARLEN LLPDTQYFIE VGACNSAGCG PPSDMIEAFT 900
    KKAPPSQPPR IISSVRSGSR YIITWDHVVA LSNESTVTGY KVLYRPDGQH 950
    DGKLYSTHKH SIEVPIPRDG EYVVEVRAHS DGGDGVVSQV KISGAPTLSP 1000
    SLLGLLLPAF GILVYLEF 1018
    Length:1,018
    Mass (Da):113,320
    Last modified:November 1, 1996 - v1
    Checksum:i4B8FDC5BFD434ED5
    GO
    Isoform 2 (identifier: Q12860-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         21-31: Missing.

    Show »
    Length:1,007
    Mass (Da):111,867
    Checksum:i0078E9F82F498EE0
    GO
    Isoform 3 (identifier: Q12860-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         603-627: PPGPPGGLRIEDIRATSVALTWSRG → KNRKGGEKNMVDSFLPVCASLPPTW
         628-1018: Missing.

    Show »
    Length:627
    Mass (Da):70,604
    Checksum:i86825008EAAA085A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti682 – 6821V → I AA sequence (PubMed:2026173)Curated
    Sequence conflicti687 – 6871L → P AA sequence (PubMed:2026173)Curated
    Sequence conflicti689 – 6891R → I AA sequence (PubMed:2026173)Curated
    Sequence conflicti692 – 6921P → F AA sequence (PubMed:2026173)Curated
    Isoform 3 (identifier: Q12860-3)
    Sequence conflicti610 – 6101K → I in BAF82233. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti794 – 7941P → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035506
    Natural varianti798 – 7981V → L.
    Corresponds to variant rs1056020 [ dbSNP | Ensembl ].
    VAR_011722
    Natural varianti824 – 8241E → G.
    Corresponds to variant rs11553341 [ dbSNP | Ensembl ].
    VAR_049866

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei21 – 3111Missing in isoform 2. 1 PublicationVSP_002500Add
    BLAST
    Alternative sequencei603 – 62725PPGPP…TWSRG → KNRKGGEKNMVDSFLPVCAS LPPTW in isoform 3. 2 PublicationsVSP_011959Add
    BLAST
    Alternative sequencei628 – 1018391Missing in isoform 3. 2 PublicationsVSP_011960Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21488 mRNA. Translation: CAA79696.1.
    U07819 mRNA. Translation: AAA67920.1.
    U07820 mRNA. Translation: AAA67921.1.
    AK289544 mRNA. Translation: BAF82233.1.
    AK289698 mRNA. Translation: BAF82387.1.
    BC036569 mRNA. Translation: AAH36569.1.
    CCDSiCCDS58225.1. [Q12860-3]
    CCDS8737.1. [Q12860-1]
    CCDS8738.1. [Q12860-2]
    PIRiA54744.
    S15394.
    RefSeqiNP_001242992.1. NM_001256063.1. [Q12860-3]
    NP_001242993.1. NM_001256064.1. [Q12860-3]
    NP_001834.2. NM_001843.3. [Q12860-1]
    NP_778203.1. NM_175038.2. [Q12860-2]
    XP_005268708.1. XM_005268651.1. [Q12860-1]
    XP_006719304.1. XM_006719241.1. [Q12860-1]
    UniGeneiHs.143434.
    Hs.739161.
    Hs.741112.

    Genome annotation databases

    EnsembliENST00000347616; ENSP00000325660; ENSG00000018236. [Q12860-1]
    ENST00000348761; ENSP00000261160; ENSG00000018236. [Q12860-2]
    ENST00000547702; ENSP00000448004; ENSG00000018236. [Q12860-3]
    ENST00000547849; ENSP00000448653; ENSG00000018236. [Q12860-3]
    ENST00000551295; ENSP00000447006; ENSG00000018236. [Q12860-1]
    GeneIDi1272.
    KEGGihsa:1272.
    UCSCiuc001rmm.2. human. [Q12860-1]
    uc001rmo.4. human. [Q12860-3]
    uc031qgz.1. human. [Q12860-2]

    Polymorphism databases

    DMDMi2497301.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21488 mRNA. Translation: CAA79696.1 .
    U07819 mRNA. Translation: AAA67920.1 .
    U07820 mRNA. Translation: AAA67921.1 .
    AK289544 mRNA. Translation: BAF82233.1 .
    AK289698 mRNA. Translation: BAF82387.1 .
    BC036569 mRNA. Translation: AAH36569.1 .
    CCDSi CCDS58225.1. [Q12860-3 ]
    CCDS8737.1. [Q12860-1 ]
    CCDS8738.1. [Q12860-2 ]
    PIRi A54744.
    S15394.
    RefSeqi NP_001242992.1. NM_001256063.1. [Q12860-3 ]
    NP_001242993.1. NM_001256064.1. [Q12860-3 ]
    NP_001834.2. NM_001843.3. [Q12860-1 ]
    NP_778203.1. NM_175038.2. [Q12860-2 ]
    XP_005268708.1. XM_005268651.1. [Q12860-1 ]
    XP_006719304.1. XM_006719241.1. [Q12860-1 ]
    UniGenei Hs.143434.
    Hs.739161.
    Hs.741112.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EE2 NMR - A 798-903 [» ]
    3S97 X-ray 2.30 C/D 133-329 [» ]
    ProteinModelPortali Q12860.
    SMRi Q12860. Positions 37-1001.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107672. 10 interactions.
    DIPi DIP-59714N.
    IntActi Q12860. 4 interactions.
    MINTi MINT-2806030.
    STRINGi 9606.ENSP00000325660.

    PTM databases

    PhosphoSitei Q12860.

    Polymorphism databases

    DMDMi 2497301.

    Proteomic databases

    MaxQBi Q12860.
    PaxDbi Q12860.
    PRIDEi Q12860.

    Protocols and materials databases

    DNASUi 1272.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347616 ; ENSP00000325660 ; ENSG00000018236 . [Q12860-1 ]
    ENST00000348761 ; ENSP00000261160 ; ENSG00000018236 . [Q12860-2 ]
    ENST00000547702 ; ENSP00000448004 ; ENSG00000018236 . [Q12860-3 ]
    ENST00000547849 ; ENSP00000448653 ; ENSG00000018236 . [Q12860-3 ]
    ENST00000551295 ; ENSP00000447006 ; ENSG00000018236 . [Q12860-1 ]
    GeneIDi 1272.
    KEGGi hsa:1272.
    UCSCi uc001rmm.2. human. [Q12860-1 ]
    uc001rmo.4. human. [Q12860-3 ]
    uc031qgz.1. human. [Q12860-2 ]

    Organism-specific databases

    CTDi 1272.
    GeneCardsi GC12P041086.
    HGNCi HGNC:2171. CNTN1.
    HPAi CAB025200.
    HPA041060.
    MIMi 600016. gene.
    612540. phenotype.
    neXtProti NX_Q12860.
    Orphaneti 210163. Congenital lethal myopathy, Compton-North type.
    PharmGKBi PA26685.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293951.
    HOVERGENi HBG051047.
    InParanoidi Q12860.
    KOi K06759.
    OMAi FTWYRRY.
    OrthoDBi EOG7J17Z5.
    PhylomeDBi Q12860.
    TreeFami TF351103.

    Enzyme and pathway databases

    Reactomei REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_22205. L1CAM interactions.
    REACT_22312. Neurofascin interactions.
    SignaLinki Q12860.

    Miscellaneous databases

    EvolutionaryTracei Q12860.
    GeneWikii CNTN1.
    GenomeRNAii 1272.
    NextBioi 5153.
    PROi Q12860.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12860.
    Bgeei Q12860.
    CleanExi HS_CNTN1.
    Genevestigatori Q12860.

    Family and domain databases

    Gene3Di 2.60.40.10. 10 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view ]
    Pfami PF00041. fn3. 3 hits.
    PF07679. I-set. 3 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 4 hits.
    SM00409. IG. 2 hits.
    SM00408. IGc2. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 4 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of the human cell adhesion molecule contactin."
      Reid R.A., Bronson D.D., Young K.M., Hemperly J.J.
      Brain Res. Mol. Brain Res. 21:1-8(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Neuroblastoma.
    2. "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12."
      Berglund E.O., Ranscht B.
      Genomics 21:571-582(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    3. "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 3).
      Tissue: Amygdala and Cerebellum.
    4. "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 3).
      Tissue: Brain.
    5. "Isolation and characterization of a membrane glycoprotein from human brain with sequence similarities to cell adhesion proteins from chicken and mouse."
      Berglund E., Stigbrand T., Carlsson S.R.
      Eur. J. Biochem. 197:549-554(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-40 AND 679-693 (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Brain cortex.
    6. "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-494.
      Tissue: Plasma.
    7. Cited for: GLYCOSYLATION AT ASN-494.
    8. "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
      Bouyain S., Watkins D.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRZ1.
    9. "Solution structures of the FN3 domain of human contactin 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 791-903.
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-794.
    11. "Mutations in contactin-1, a neural adhesion and neuromuscular junction protein, cause a familial form of lethal congenital myopathy."
      Compton A.G., Albrecht D.E., Seto J.T., Cooper S.T., Ilkovski B., Jones K.J., Challis D., Mowat D., Ranscht B., Bahlo M., Froehner S.C., North K.N.
      Am. J. Hum. Genet. 83:714-724(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CNCM.

    Entry informationi

    Entry nameiCNTN1_HUMAN
    AccessioniPrimary (citable) accession number: Q12860
    Secondary accession number(s): A8K0H9
    , A8K0Y3, Q12861, Q14030, Q7M4P0, Q8N466
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 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 chromosome 12
      Human chromosome 12: 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