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Neural cell adhesion molecule 1 (N-CAM-1) (NCAM-1) (CD antigen CD56)

 NCAM1_MOUSE             Reviewed;        1115 AA.
P13595; P13594; Q61949; Q61950; Q6LBU8; Q8BQ96; Q8C4B2; Q921P2;
Q9R2A7;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 3.
10-OCT-2018, entry version 187.
RecName: Full=Neural cell adhesion molecule 1;
Short=N-CAM-1;
Short=NCAM-1;
AltName: CD_antigen=CD56;
Flags: Precursor;
Name=Ncam1; Synonyms=Ncam;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=3595563;
Barthels D., Santoni M.-J., Wille W., Ruppert C., Chaix J.-C.,
Hirsch M.-R., Fontecilla-Camps J.-C., Goridis C.;
"Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a
Mr 79,000 polypeptide without a membrane-spanning region.";
EMBO J. 6:907-914(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1106 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-700 AND 702-1115 (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=2721486;
Santoni M.J., Barthels D., Vopper G., Boned A., Goridis C., Wille W.;
"Differential exon usage involving an unusual splicing mechanism
generates at least eight types of NCAM cDNA in mouse brain.";
EMBO J. 8:385-392(1989).
[5]
PROTEIN SEQUENCE OF 20-36.
PubMed=3512556;
Rougon G., Marshak D.R.;
"Structural and immunological characterization of the amino-terminal
domain of mammalian neural cell adhesion molecules.";
J. Biol. Chem. 261:3396-3401(1986).
[6]
PROTEIN SEQUENCE OF 38-48; 122-152; 166-177; 555-572; 584-595;
607-619; 652-662 AND 685-691, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 529-1115 (ISOFORM 2).
STRAIN=C57BL/6J;
PubMed=3684567; DOI=10.1093/nar/15.21.8621;
Santoni M.-J., Barthels D., Barbas J.A., Hirsch M.-R., Steinmetz M.,
Goridis C., Wille W.;
"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.";
Nucleic Acids Res. 15:8621-8641(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 642-1115.
PubMed=3396534;
Barbas J.A., Chaix J.-C., Steinmetz M., Goridis C.;
"Differential splicing and alternative polyadenylation generates
distinct NCAM transcripts and proteins in the mouse.";
EMBO J. 7:625-632(1988).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 804-1081 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=2454455; DOI=10.1093/nar/16.10.4217;
Barthels D., Vopper G., Wille W.;
"NCAM-180, the large isoform of the neural cell adhesion molecule of
the mouse, is encoded by an alternatively spliced transcript.";
Nucleic Acids Res. 16:4217-4225(1988).
[10]
GLYCOSYLATION AT ASN-222; ASN-316; ASN-348; ASN-424; ASN-450 AND
ASN-479, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain;
PubMed=14658030; DOI=10.1007/s00216-003-2383-2;
Albach C., Damoc E., Denzinger T., Schachner M., Przybylski M.,
Schmitz B.;
"Identification of N-glycosylation sites of the murine neural cell
adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass
spectrometry.";
Anal. Bioanal. Chem. 378:1129-1135(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-946; SER-958 AND
SER-1005, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770; SER-774; SER-887;
SER-890; SER-926; THR-929; SER-946; SER-958; THR-1001; SER-1005 AND
THR-1030, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
STRUCTURE BY NMR OF 20-116, AND DISULFIDE BONDS.
PubMed=8673600; DOI=10.1038/nsb0796-581;
Thomsen N.K., Soroka V., Jensen P.H., Berezin V., Kiselyov V.V.,
Bock E., Poulsen F.M.;
"The three-dimensional structure of the first domain of neural cell
adhesion molecule.";
Nat. Struct. Biol. 3:581-585(1996).
[17]
STRUCTURE BY NMR OF 119-208, AND DISULFIDE BONDS.
PubMed=10331878; DOI=10.1038/8292;
Jensen P.H., Soroka V., Thomsen N.K., Ralets I., Berezin V., Bock E.,
Poulsen F.M.;
"Structure and interactions of NCAM modules 1 and 2, basic elements in
neural cell adhesion.";
Nat. Struct. Biol. 6:486-493(1999).
-!- FUNCTION: This protein is a cell adhesion molecule involved in
neuron-neuron adhesion, neurite fasciculation, outgrowth of
neurites, etc.
-!- INTERACTION:
P21803:Fgfr2; NbExp=2; IntAct=EBI-774943, EBI-6286942;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Lipid-anchor, GPI-
anchor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=N-CAM 180;
IsoId=P13595-1; Sequence=Displayed;
Name=2; Synonyms=N-CAM 140;
IsoId=P13595-2; Sequence=VSP_002588;
Name=3; Synonyms=N-CAM 120;
IsoId=P13595-3, P13594-1;
Sequence=VSP_034828, VSP_034829;
Note=Contains a GPI-anchor amidated serine at position 706.
{ECO:0000255};
Name=4;
IsoId=P13595-4; Sequence=VSP_034826, VSP_034827;
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EMBL; Y00051; CAA68263.1; -; mRNA.
EMBL; BC011310; AAH11310.1; -; mRNA.
EMBL; AK051197; BAC34554.2; -; mRNA.
EMBL; AK082621; BAC38551.2; -; mRNA.
EMBL; X15049; CAA33148.1; -; mRNA.
EMBL; X15051; CAA33150.1; -; mRNA.
EMBL; X15052; CAA33151.1; -; mRNA.
EMBL; X06328; CAA29641.1; -; mRNA.
EMBL; X07195; CAA30173.1; -; Genomic_DNA.
EMBL; X07197; CAA30175.1; -; Genomic_DNA.
EMBL; X07198; CAB40820.1; -; Genomic_DNA.
EMBL; X07200; CAA30177.1; -; Genomic_DNA.
EMBL; X07244; CAA30230.1; -; mRNA.
CCDS; CCDS40617.1; -. [P13595-2]
CCDS; CCDS40618.1; -. [P13595-3]
PIR; A29673; IJMSNL.
RefSeq; NP_001074914.1; NM_001081445.1.
RefSeq; NP_001106675.1; NM_001113204.1.
RefSeq; NP_001297994.1; NM_001311065.1.
RefSeq; NP_035005.2; NM_010875.3.
UniGene; Mm.439182; -.
UniGene; Mm.4974; -.
PDB; 2NCM; NMR; -; A=20-116.
PDB; 3NCM; NMR; -; A=119-208.
PDBsum; 2NCM; -.
PDBsum; 3NCM; -.
ProteinModelPortal; P13595; -.
SMR; P13595; -.
BioGrid; 201699; 7.
CORUM; P13595; -.
IntAct; P13595; 9.
MINT; P13595; -.
STRING; 10090.ENSMUSP00000130668; -.
iPTMnet; P13595; -.
PhosphoSitePlus; P13595; -.
SwissPalm; P13595; -.
MaxQB; P13595; -.
PaxDb; P13595; -.
PeptideAtlas; P13595; -.
PRIDE; P13595; -.
GeneID; 17967; -.
KEGG; mmu:17967; -.
UCSC; uc009pje.2; mouse. [P13595-1]
CTD; 4684; -.
MGI; MGI:97281; Ncam1.
eggNOG; ENOG410IQJI; Eukaryota.
eggNOG; ENOG410XTGB; LUCA.
HOVERGEN; HBG052579; -.
InParanoid; P13595; -.
KO; K06491; -.
PhylomeDB; P13595; -.
ChiTaRS; Ncam1; mouse.
EvolutionaryTrace; P13595; -.
PRO; PR:P13595; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030275; F:LRR domain binding; ISO:MGI.
GO; GO:0019902; F:phosphatase binding; ISO:MGI.
GO; GO:0007568; P:aging; ISO:MGI.
GO; GO:0007413; P:axonal fasciculation; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0071679; P:commissural neuron axon guidance; IGI:ARUK-UCL.
GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
GO; GO:0007611; P:learning or memory; ISO:MGI.
GO; GO:0033555; P:multicellular organismal response to stress; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0048666; P:neuron development; ISO:MGI.
GO; GO:0031175; P:neuron projection development; IGI:MGI.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:MGI.
GO; GO:0001928; P:regulation of exocyst assembly; IMP:MGI.
GO; GO:2001260; P:regulation of semaphorin-plexin signaling pathway; IGI:ARUK-UCL.
GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
GO; GO:0042220; P:response to cocaine; ISO:MGI.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0010288; P:response to lead ion; ISO:MGI.
GO; GO:0021794; P:thalamus development; ISO:MGI.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR033019; Ncam1.
InterPro; IPR009138; Neural_cell_adh.
PANTHER; PTHR44059:SF2; PTHR44059:SF2; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07679; I-set; 3.
PRINTS; PR01838; NCAMFAMILY.
SMART; SM00060; FN3; 2.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SMART; SM00406; IGv; 2.
SUPFAM; SSF48726; SSF48726; 5.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; GPI-anchor; Heparin-binding; Immunoglobulin domain;
Lipoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:3512556}.
CHAIN 20 1115 Neural cell adhesion molecule 1.
/FTId=PRO_0000015012.
TOPO_DOM 20 711 Extracellular. {ECO:0000255}.
TRANSMEM 712 729 Helical. {ECO:0000255}.
TOPO_DOM 730 1115 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 111 Ig-like C2-type 1.
DOMAIN 116 205 Ig-like C2-type 2.
DOMAIN 212 302 Ig-like C2-type 3.
DOMAIN 309 402 Ig-like C2-type 4.
DOMAIN 407 492 Ig-like C2-type 5.
DOMAIN 500 599 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 601 696 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 152 156 Heparin-binding. {ECO:0000255}.
REGION 161 165 Heparin-binding. {ECO:0000255}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 926 926 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 929 929 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 946 946 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 958 958 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 1001 1001 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1005 1005 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 1030 1030 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:14658030}.
CARBOHYD 316 316 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14658030}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14658030}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14658030}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14658030,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14658030}.
DISULFID 41 96 {ECO:0000244|PDB:2NCM,
ECO:0000269|PubMed:8673600}.
DISULFID 139 189 {ECO:0000244|PDB:3NCM,
ECO:0000269|PubMed:10331878}.
DISULFID 235 288 {ECO:0000305}.
DISULFID 330 386 {ECO:0000305}.
DISULFID 427 480 {ECO:0000305}.
VAR_SEQ 601 605 EPSAP -> KSSLF (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034826.
VAR_SEQ 606 1115 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_034827.
VAR_SEQ 702 725 NGSPTAGLSTGAIVGILIVIFVLL -> TLGGSSTSYTLVS
LLFSAVTLLLL (in isoform 3).
{ECO:0000303|PubMed:3595563}.
/FTId=VSP_034828.
VAR_SEQ 726 1115 Missing (in isoform 3).
{ECO:0000303|PubMed:3595563}.
/FTId=VSP_034829.
VAR_SEQ 810 1076 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2721486,
ECO:0000303|PubMed:3684567}.
/FTId=VSP_002588.
CONFLICT 20 20 L -> M (in Ref. 4; CAA33148).
{ECO:0000305}.
CONFLICT 158 158 V -> F (in Ref. 2; AAH11310).
{ECO:0000305}.
CONFLICT 261 268 DEKHIFSD -> ERSRSSVS (in Ref. 1;
CAA68263). {ECO:0000305}.
CONFLICT 273 273 L -> V (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 354 355 KT -> QD (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 379 379 T -> R (in Ref. 1; CAA68263 and 4;
CAA33148). {ECO:0000305}.
CONFLICT 385 385 I -> M (in Ref. 1; CAA68263 and 4;
CAA33148). {ECO:0000305}.
CONFLICT 399 400 MY -> ID (in Ref. 1; CAA68263 and 4;
CAA33148). {ECO:0000305}.
CONFLICT 403 403 F -> V (in Ref. 2; AAH11310 and 3;
BAC34554/BAC38551). {ECO:0000305}.
CONFLICT 549 549 K -> T (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 572 572 R -> T (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 575 575 V -> D (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 589 594 SAATEF -> MQPSES (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 600 602 REP -> PEL (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 657 657 D -> H (in Ref. 1; CAA68263).
{ECO:0000305}.
CONFLICT 733 733 C -> W (in Ref. 3; BAC34554).
{ECO:0000305}.
CONFLICT 1082 1082 T -> A (in Ref. 3; BAC34554).
{ECO:0000305}.
STRAND 21 32 {ECO:0000244|PDB:2NCM}.
STRAND 37 44 {ECO:0000244|PDB:2NCM}.
STRAND 47 49 {ECO:0000244|PDB:2NCM}.
STRAND 51 56 {ECO:0000244|PDB:2NCM}.
TURN 57 59 {ECO:0000244|PDB:2NCM}.
STRAND 64 73 {ECO:0000244|PDB:2NCM}.
STRAND 75 77 {ECO:0000244|PDB:2NCM}.
STRAND 79 85 {ECO:0000244|PDB:2NCM}.
TURN 88 90 {ECO:0000244|PDB:2NCM}.
STRAND 92 99 {ECO:0000244|PDB:2NCM}.
STRAND 101 103 {ECO:0000244|PDB:2NCM}.
STRAND 105 115 {ECO:0000244|PDB:2NCM}.
STRAND 119 122 {ECO:0000244|PDB:3NCM}.
STRAND 125 128 {ECO:0000244|PDB:3NCM}.
STRAND 133 137 {ECO:0000244|PDB:3NCM}.
STRAND 140 143 {ECO:0000244|PDB:3NCM}.
STRAND 145 157 {ECO:0000244|PDB:3NCM}.
HELIX 158 161 {ECO:0000244|PDB:3NCM}.
STRAND 166 168 {ECO:0000244|PDB:3NCM}.
STRAND 174 178 {ECO:0000244|PDB:3NCM}.
STRAND 185 193 {ECO:0000244|PDB:3NCM}.
TURN 194 197 {ECO:0000244|PDB:3NCM}.
STRAND 198 207 {ECO:0000244|PDB:3NCM}.
SEQUENCE 1115 AA; 119427 MW; 78AF831BABD23918 CRC64;
MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF
KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF
PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS
IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM
VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG
NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC
TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS
LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR
EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM
LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV
IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE
VRTEEERTPN HDGGKHTEPN ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA
TAQNSPTSET TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL
SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT PTPAGAASPL
AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA TAPASPKSKA ATTNPSQGED
LKMDEGNFKT PDIDLAKDVF AALGSPRPAT GASGQASELA PSPADSAVPP APAKTEKGPV
ETKSEPPESE AKPAPTEVKT VPNDATQTKE NESKA


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