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P13595

- NCAM1_MOUSE

UniProt

P13595 - NCAM1_MOUSE

Protein

Neural cell adhesion molecule 1

Gene

Ncam1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: MGI
    2. homotypic cell-cell adhesion Source: MGI
    3. neuron projection development Source: MGI
    4. positive regulation of calcium-mediated signaling Source: MGI
    5. regulation of exocyst assembly Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neural cell adhesion molecule 1
    Short name:
    N-CAM-1
    Short name:
    NCAM-1
    Alternative name(s):
    CD_antigen: CD56
    Gene namesi
    Name:Ncam1
    Synonyms:Ncam
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:97281. Ncam1.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. axon Source: MGI
    3. cell-cell junction Source: MGI
    4. external side of plasma membrane Source: MGI
    5. growth cone Source: MGI
    6. integral component of membrane Source: UniProtKB-KW
    7. neuronal cell body Source: MGI
    8. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 11151096Neural cell adhesion molecule 1PRO_0000015012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 96
    Disulfide bondi139 ↔ 189
    Glycosylationi222 – 2221N-linked (GlcNAc...); partial1 Publication
    Disulfide bondi235 ↔ 288Curated
    Glycosylationi316 – 3161N-linked (GlcNAc...)1 Publication
    Disulfide bondi330 ↔ 386Curated
    Glycosylationi348 – 3481N-linked (GlcNAc...)1 Publication
    Glycosylationi424 – 4241N-linked (GlcNAc...)1 Publication
    Disulfide bondi427 ↔ 480Curated
    Glycosylationi450 – 4501N-linked (GlcNAc...)3 Publications
    Glycosylationi453 – 4531N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi479 – 4791N-linked (GlcNAc...)1 Publication
    Modified residuei774 – 7741Phosphoserine1 Publication
    Modified residuei946 – 9461Phosphoserine1 Publication
    Modified residuei958 – 9581Phosphoserine1 Publication
    Modified residuei1005 – 10051Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP13595.
    PaxDbiP13595.
    PRIDEiP13595.

    PTM databases

    PhosphoSiteiP13595.

    Expressioni

    Gene expression databases

    GenevestigatoriP13595.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Fgfr2P218032EBI-774943,EBI-6286942

    Protein-protein interaction databases

    BioGridi201699. 3 interactions.
    IntActiP13595. 6 interactions.
    MINTiMINT-1176881.

    Structurei

    Secondary structure

    1
    1115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 3212
    Beta strandi37 – 448
    Beta strandi47 – 493
    Beta strandi51 – 566
    Turni57 – 593
    Beta strandi64 – 7310
    Beta strandi75 – 773
    Beta strandi79 – 857
    Turni88 – 903
    Beta strandi92 – 998
    Beta strandi101 – 1033
    Beta strandi105 – 11511
    Beta strandi119 – 1224
    Beta strandi125 – 1284
    Beta strandi133 – 1375
    Beta strandi140 – 1434
    Beta strandi145 – 15713
    Helixi158 – 1614
    Beta strandi166 – 1683
    Beta strandi174 – 1785
    Beta strandi185 – 1939
    Turni194 – 1974
    Beta strandi198 – 20710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NCMNMR-A20-116[»]
    3NCMNMR-A119-208[»]
    ProteinModelPortaliP13595.
    SMRiP13595. Positions 20-696.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13595.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 711692ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini730 – 1115386CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei712 – 72918HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 11192Ig-like C2-type 1Add
    BLAST
    Domaini116 – 20590Ig-like C2-type 2Add
    BLAST
    Domaini212 – 30291Ig-like C2-type 3Add
    BLAST
    Domaini309 – 40294Ig-like C2-type 4Add
    BLAST
    Domaini407 – 49286Ig-like C2-type 5Add
    BLAST
    Domaini500 – 599100Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini601 – 69696Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 1565Heparin-bindingSequence Analysis
    Regioni161 – 1655Heparin-bindingSequence Analysis

    Sequence similaritiesi

    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG308439.
    HOVERGENiHBG052579.
    InParanoidiP13595.
    KOiK06491.
    PhylomeDBiP13595.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR009138. Neural_cell_adh.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF07679. I-set. 5 hits.
    [Graphical view]
    PRINTSiPR01838. NCAMFAMILY.
    SMARTiSM00060. FN3. 2 hits.
    SM00408. IGc2. 5 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    PROSITEiPS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 5 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13595-1) [UniParc]FASTAAdd to Basket

    Also known as: N-CAM 180

    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

    MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK     50
    DISWFSPNGE KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA 100
    EDGTQSEATV NVKIFQKLMF KNAPTPQEFK EGEDAVIVCD VVSSLPPTII 150
    WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK KTDEGTYRCE GRILARGEIN 200
    FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF PEPTMSWTKD 250
    GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS 300
    IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS 350
    SEEKTLDGHM VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY 400
    LEFQYAPKLQ GPVAVYTWEG NQVNITCEVF AYPSATISWF RDGQLLPSSN 450
    YSNIKIYNTP SASYLEVTPD SENDFGNYNC TAVNRIGQES LEFILVQADT 500
    PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS LGEESWHFKW 550
    YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR 600
    EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI 650
    RLPSGSDHVM LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP 700
    ANGSPTAGLS TGAIVGILIV IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC 750
    GKAGPGAKGK DMEEGKAAFS KDESKEPIVE VRTEEERTPN HDGGKHTEPN 800
    ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA TAQNSPTSET 850
    TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL 900
    SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT 950
    PTPAGAASPL AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA 1000
    TAPASPKSKA ATTNPSQGED LKMDEGNFKT PDIDLAKDVF AALGSPRPAT 1050
    GASGQASELA PSPADSAVPP APAKTEKGPV ETKSEPPESE AKPAPTEVKT 1100
    VPNDATQTKE NESKA 1115
    Length:1,115
    Mass (Da):119,427
    Last modified:July 22, 2008 - v3
    Checksum:i78AF831BABD23918
    GO
    Isoform 2 (identifier: P13595-2) [UniParc]FASTAAdd to Basket

    Also known as: N-CAM 140

    The sequence of this isoform differs from the canonical sequence as follows:
         810-1076: Missing.

    Show »
    Length:848
    Mass (Da):93,540
    Checksum:i4D77D553F474AD8E
    GO
    Isoform 3 (identifier: P13595-3) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: N-CAM 120

    The sequence of this isoform differs from the canonical sequence as follows:
         702-725: NGSPTAGLSTGAIVGILIVIFVLL → TLGGSSTSYTLVSLLFSAVTLLLL
         726-1115: Missing.

    Note: GPI-anchor amidated serine at position Ser-706.

    Show »
    Length:725
    Mass (Da):80,406
    Checksum:i97867C2A61594CC4
    GO
    Isoform 4 (identifier: P13595-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         601-605: EPSAP → KSSLF
         606-1115: Missing.

    Show »
    Length:605
    Mass (Da):67,353
    Checksum:iD497D834C34EAEC0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201L → M in CAA33148. (PubMed:2721486)Curated
    Sequence conflicti158 – 1581V → F in AAH11310. (PubMed:15489334)Curated
    Sequence conflicti261 – 2688DEKHIFSD → ERSRSSVS in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti273 – 2731L → V in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti354 – 3552KT → QD in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti379 – 3791T → R in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti379 – 3791T → R in CAA33148. (PubMed:2721486)Curated
    Sequence conflicti385 – 3851I → M in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti385 – 3851I → M in CAA33148. (PubMed:2721486)Curated
    Sequence conflicti399 – 4002MY → ID in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti399 – 4002MY → ID in CAA33148. (PubMed:2721486)Curated
    Sequence conflicti403 – 4031F → V in AAH11310. (PubMed:15489334)Curated
    Sequence conflicti403 – 4031F → V in BAC34554. (PubMed:16141072)Curated
    Sequence conflicti403 – 4031F → V in BAC38551. (PubMed:16141072)Curated
    Sequence conflicti549 – 5491K → T in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti572 – 5721R → T in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti575 – 5751V → D in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti589 – 5946SAATEF → MQPSES in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti600 – 6023REP → PEL in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti657 – 6571D → H in CAA68263. (PubMed:3595563)Curated
    Sequence conflicti733 – 7331C → W in BAC34554. (PubMed:16141072)Curated
    Sequence conflicti1082 – 10821T → A in BAC34554. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei601 – 6055EPSAP → KSSLF in isoform 4. 1 PublicationVSP_034826
    Alternative sequencei606 – 1115510Missing in isoform 4. 1 PublicationVSP_034827Add
    BLAST
    Alternative sequencei702 – 72524NGSPT…IFVLL → TLGGSSTSYTLVSLLFSAVT LLLL in isoform 3. 1 PublicationVSP_034828Add
    BLAST
    Alternative sequencei726 – 1115390Missing in isoform 3. 1 PublicationVSP_034829Add
    BLAST
    Alternative sequencei810 – 1076267Missing in isoform 2. 3 PublicationsVSP_002588Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00051 mRNA. Translation: CAA68263.1.
    BC011310 mRNA. Translation: AAH11310.1.
    AK051197 mRNA. Translation: BAC34554.2.
    AK082621 mRNA. Translation: BAC38551.2.
    X15049 mRNA. Translation: CAA33148.1.
    X15051 mRNA. Translation: CAA33150.1.
    X15052 mRNA. Translation: CAA33151.1.
    X06328 mRNA. Translation: CAA29641.1.
    X07195 Genomic DNA. Translation: CAA30173.1.
    X07197 Genomic DNA. Translation: CAA30175.1.
    X07198 Genomic DNA. Translation: CAB40820.1.
    X07200 Genomic DNA. Translation: CAA30177.1.
    X07244 mRNA. Translation: CAA30230.1.
    CCDSiCCDS40617.1. [P13595-2]
    CCDS40618.1. [P13595-3]
    PIRiA29673. IJMSNL.
    RefSeqiNP_001074914.1. NM_001081445.1.
    NP_001106675.1. NM_001113204.1.
    NP_035005.2. NM_010875.3.
    UniGeneiMm.439182.
    Mm.4974.

    Genome annotation databases

    GeneIDi17967.
    KEGGimmu:17967.
    UCSCiuc009pje.2. mouse. [P13595-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00051 mRNA. Translation: CAA68263.1 .
    BC011310 mRNA. Translation: AAH11310.1 .
    AK051197 mRNA. Translation: BAC34554.2 .
    AK082621 mRNA. Translation: BAC38551.2 .
    X15049 mRNA. Translation: CAA33148.1 .
    X15051 mRNA. Translation: CAA33150.1 .
    X15052 mRNA. Translation: CAA33151.1 .
    X06328 mRNA. Translation: CAA29641.1 .
    X07195 Genomic DNA. Translation: CAA30173.1 .
    X07197 Genomic DNA. Translation: CAA30175.1 .
    X07198 Genomic DNA. Translation: CAB40820.1 .
    X07200 Genomic DNA. Translation: CAA30177.1 .
    X07244 mRNA. Translation: CAA30230.1 .
    CCDSi CCDS40617.1. [P13595-2 ]
    CCDS40618.1. [P13595-3 ]
    PIRi A29673. IJMSNL.
    RefSeqi NP_001074914.1. NM_001081445.1.
    NP_001106675.1. NM_001113204.1.
    NP_035005.2. NM_010875.3.
    UniGenei Mm.439182.
    Mm.4974.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NCM NMR - A 20-116 [» ]
    3NCM NMR - A 119-208 [» ]
    ProteinModelPortali P13595.
    SMRi P13595. Positions 20-696.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201699. 3 interactions.
    IntActi P13595. 6 interactions.
    MINTi MINT-1176881.

    PTM databases

    PhosphoSitei P13595.

    Proteomic databases

    MaxQBi P13595.
    PaxDbi P13595.
    PRIDEi P13595.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 17967.
    KEGGi mmu:17967.
    UCSCi uc009pje.2. mouse. [P13595-1 ]

    Organism-specific databases

    CTDi 4684.
    MGIi MGI:97281. Ncam1.

    Phylogenomic databases

    eggNOGi NOG308439.
    HOVERGENi HBG052579.
    InParanoidi P13595.
    KOi K06491.
    PhylomeDBi P13595.

    Miscellaneous databases

    ChiTaRSi NCAM1. mouse.
    EvolutionaryTracei P13595.
    NextBioi 292903.
    PROi P13595.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P13595.

    Family and domain databases

    Gene3Di 2.60.40.10. 7 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR009138. Neural_cell_adh.
    [Graphical view ]
    Pfami PF00041. fn3. 2 hits.
    PF07679. I-set. 5 hits.
    [Graphical view ]
    PRINTSi PR01838. NCAMFAMILY.
    SMARTi SM00060. FN3. 2 hits.
    SM00408. IGc2. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    PROSITEi PS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a Mr 79,000 polypeptide without a membrane-spanning region."
      Barthels D., Santoni M.-J., Wille W., Ruppert C., Chaix J.-C., Hirsch M.-R., Fontecilla-Camps J.-C., Goridis C.
      EMBO J. 6:907-914(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Strain: C57BL/6.
      Tissue: Brain.
    2. "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 4).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1106 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Spinal ganglion.
    4. "Differential exon usage involving an unusual splicing mechanism generates at least eight types of NCAM cDNA in mouse brain."
      Santoni M.J., Barthels D., Vopper G., Boned A., Goridis C., Wille W.
      EMBO J. 8:385-392(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-700 AND 702-1115 (ISOFORMS 1 AND 2).
      Strain: C57BL/6.
      Tissue: Brain.
    5. "Structural and immunological characterization of the amino-terminal domain of mammalian neural cell adhesion molecules."
      Rougon G., Marshak D.R.
      J. Biol. Chem. 261:3396-3401(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-36.
    6. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 38-48; 122-152; 166-177; 555-572; 584-595; 607-619; 652-662 AND 685-691, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    7. "Analysis of cDNA clones that code for the transmembrane forms of the mouse neural cell adhesion molecule (NCAM) and are generated by alternative RNA splicing."
      Santoni M.-J., Barthels D., Barbas J.A., Hirsch M.-R., Steinmetz M., Goridis C., Wille W.
      Nucleic Acids Res. 15:8621-8641(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 529-1115 (ISOFORM 2).
      Strain: C57BL/6.
    8. "Differential splicing and alternative polyadenylation generates distinct NCAM transcripts and proteins in the mouse."
      Barbas J.A., Chaix J.-C., Steinmetz M., Goridis C.
      EMBO J. 7:625-632(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 642-1115.
    9. "NCAM-180, the large isoform of the neural cell adhesion molecule of the mouse, is encoded by an alternatively spliced transcript."
      Barthels D., Vopper G., Wille W.
      Nucleic Acids Res. 16:4217-4225(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 804-1081 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Brain.
    10. "Identification of N-glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry."
      Albach C., Damoc E., Denzinger T., Schachner M., Przybylski M., Schmitz B.
      Anal. Bioanal. Chem. 378:1129-1135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-222; ASN-316; ASN-348; ASN-424; ASN-450 AND ASN-479, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946; SER-958 AND SER-1005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    12. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    13. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-453.
      Tissue: Myoblast.
    14. "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-450.
    15. "The three-dimensional structure of the first domain of neural cell adhesion molecule."
      Thomsen N.K., Soroka V., Jensen P.H., Berezin V., Kiselyov V.V., Bock E., Poulsen F.M.
      Nat. Struct. Biol. 3:581-585(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 20-116, DISULFIDE BONDS.
    16. "Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion."
      Jensen P.H., Soroka V., Thomsen N.K., Ralets I., Berezin V., Bock E., Poulsen F.M.
      Nat. Struct. Biol. 6:486-493(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 119-208, DISULFIDE BONDS.

    Entry informationi

    Entry nameiNCAM1_MOUSE
    AccessioniPrimary (citable) accession number: P13595
    Secondary accession number(s): P13594
    , Q61949, Q61950, Q6LBU8, Q8BQ96, Q8C4B2, Q921P2, Q9R2A7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3