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Neural cell adhesion molecule L1-like protein (Cell adhesion molecule with homology to L1CAM) (Chl1-like protein) (Close homolog of L1) [Cleaved into: Processed neural cell adhesion molecule L1-like protein]

 NCHL1_MOUSE             Reviewed;        1209 AA.
P70232; A2RRK1; Q8BS24; Q8C6W0; Q8C823; Q8VBY7;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
13-FEB-2019, entry version 151.
RecName: Full=Neural cell adhesion molecule L1-like protein;
AltName: Full=Cell adhesion molecule with homology to L1CAM;
AltName: Full=Chl1-like protein;
AltName: Full=Close homolog of L1;
Contains:
RecName: Full=Processed neural cell adhesion molecule L1-like protein;
Flags: Precursor;
Name=Chl1; Synonyms=Call;
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 1), TISSUE SPECIFICITY,
GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
PubMed=8921253; DOI=10.1111/j.1460-9568.1996.tb01306.x;
Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H.,
Montag D., Schachner M.;
"Structural features of a close homologue of L1 (CHL1) in the mouse: a
new member of the L1 family of neural recognition molecules.";
Eur. J. Neurosci. 8:1613-1629(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Vein;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=129/Sv;
PubMed=12391163; DOI=10.1128/MCB.22.22.7967-7981.2002;
Montag-Sallaz M., Schachner M., Montag D.;
"Misguided axonal projections, neural cell adhesion molecule 180 mRNA
upregulation, and altered behavior in mice deficient for the close
homolog of L1.";
Mol. Cell. Biol. 22:7967-7981(2002).
[7]
FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, AND TISSUE
SPECIFICITY.
PubMed=10103075; DOI=10.1046/j.1460-9568.1999.00496.x;
Hillenbrand R., Molthagen M., Montag D., Schachner M.;
"The close homologue of the neural adhesion molecule L1 (CHL1):
patterns of expression and promotion of neurite outgrowth by
heterophilic interactions.";
Eur. J. Neurosci. 11:813-826(1999).
[8]
FUNCTION.
PubMed=10022583;
DOI=10.1002/(SICI)1097-4695(19990215)38:3<428::AID-NEU10>3.0.CO;2-6;
Chen S., Mantei N., Dong L., Schachner M.;
"Prevention of neuronal cell death by neural adhesion molecules L1 and
CHL1.";
J. Neurobiol. 38:428-439(1999).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14659567; DOI=10.1016/S0166-4328(03)00114-1;
Pratte M., Rougon G., Schachner M., Jamon M.;
"Mice deficient for the close homologue of the neural adhesion cell L1
(CHL1) display alterations in emotional reactivity and motor
coordination.";
Behav. Brain Res. 147:31-39(2003).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12812975; DOI=10.1093/hmg/ddg165;
Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J.,
Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K.,
D'Hooge R., De Deyn P.P., Froyen G.;
"CALL interrupted in a patient with non-specific mental retardation:
gene dosage-dependent alteration of murine brain development and
behavior.";
Hum. Mol. Genet. 12:1463-1474(2003).
[11]
FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND
ITGB1/ITGA2 HETERODIMER, MOTIFS, AND MUTAGENESIS OF 555-ASP--ALA-558
AND TYR-1186.
PubMed=12721290; DOI=10.1074/jbc.M303084200;
Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M.,
Maness P.F.;
"Close homolog of L1 is an enhancer of integrin-mediated cell
migration.";
J. Biol. Chem. 278:25024-25031(2003).
[12]
FUNCTION, AND CLEAVAGE BY ADAM8.
PubMed=14761956; DOI=10.1074/jbc.M400560200;
Naus S., Richter M., Wildeboer D., Moss M., Schachner M.,
Bartsch J.W.;
"Ectodomain shedding of the neural recognition molecule CHL1 by the
metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and
suppresses neuronal cell death.";
J. Biol. Chem. 279:16083-16090(2004).
[13]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15504324; DOI=10.1016/j.neuron.2004.10.016;
Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J.,
Maness P.F.;
"Close homolog of L1 modulates area-specific neuronal positioning and
dendrite orientation in the cerebral cortex.";
Neuron 44:423-437(2004).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16623841; DOI=10.1111/j.1460-9568.2006.04710.x;
Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I.,
Irintchev A., Dityatev A., Schachner M.;
"Enhanced perisomatic inhibition and impaired long-term potentiation
in the CA1 region of juvenile CHL1-deficient mice.";
Eur. J. Neurosci. 23:1839-1852(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148; SER-1161 AND
SER-1181, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
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).
-!- FUNCTION: Extracellular matrix and cell adhesion protein that
plays a role in nervous system development and in synaptic
plasticity. Both soluble and membranous forms promote neurite
outgrowth of cerebellar and hippocampal neurons and suppress
neuronal cell death. Plays a role in neuronal positioning of
pyramidal neurons as well as in regulation of both the number of
interneurons and the efficacy of GABAergic synapses. May play a
role in regulating cell migration in nerve regeneration and
cortical development. Potentiates integrin-dependent cell
migration towards extracellular matrix proteins. Recruits ANK3 to
the plasma membrane. {ECO:0000269|PubMed:10022583,
ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:12391163,
ECO:0000269|PubMed:12721290, ECO:0000269|PubMed:12812975,
ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:14761956,
ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:16623841}.
-!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
-!- INTERACTION:
Q9JMB8:Cntn6; NbExp=5; IntAct=EBI-7703109, EBI-7703151;
P18052:Ptpra; NbExp=4; IntAct=EBI-7703109, EBI-6597520;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=Soluble forms produced by cleavage/shedding also
exist.
-!- SUBCELLULAR LOCATION: Processed neural cell adhesion molecule L1-
like protein: Secreted, extracellular space, extracellular matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70232-1; Sequence=Displayed;
Name=2;
IsoId=P70232-2; Sequence=VSP_020083, VSP_020084, VSP_020085;
-!- TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and
in the spinal cord. Detected in the retina and the optic nerve.
Expressed in neurons and glial cells in the central nervous system
and by Schwann cells in the peripheral nervous system.
{ECO:0000269|PubMed:10103075, ECO:0000269|PubMed:15504324,
ECO:0000269|PubMed:8921253}.
-!- DEVELOPMENTAL STAGE: Not detectable in the forebrain at 11 dpc,
weakly detectable at 13 dpc with highest detection at 18 dpc to
postnatal day 7. Down-regulated at postnatal day 15 and further
reduced in four-week-old animals. {ECO:0000269|PubMed:10103075,
ECO:0000269|PubMed:15504324, ECO:0000269|PubMed:8921253}.
-!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment
region.
-!- DOMAIN: The DGEA motif seems to be a recognition site for
integrin.
-!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
inhibited by metalloprotease inhibitors. In brain extracts, these
two soluble forms are also present and are dramatically reduced in
mice lacking ADAM8.
-!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a
sulfated carbohydrate structure type HNK-1 (SO4-3-
GlcUABeta1,3GalBeta1,4GlcNAc). {ECO:0000269|PubMed:8921253}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:8921253}.
-!- DISRUPTION PHENOTYPE: Mice exhibit misguided axonal projections
and aberrant axonal connectivity. They show alterations of
hippocampal fiber organization and olfactory axon projections.
Their exploratory behavior in novel environments is altered
suggesting deficits in information processing and in attention.
They also display signs of decreased stress and are more sociable
and less aggressive. Heterozygous mice exhibit half levels of CHL1
expression in the hippocampus compared to their wild-type
littermates, reflecting a gene dosage effect.
{ECO:0000269|PubMed:12391163, ECO:0000269|PubMed:12812975,
ECO:0000269|PubMed:14659567, ECO:0000269|PubMed:16623841}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
L1/neurofascin/NgCAM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC30699.1; Type=Frameshift; Positions=616, 624, 631, 632, 642, 645; Evidence={ECO:0000305};
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EMBL; X94310; CAA63972.1; -; mRNA.
EMBL; AK040765; BAC30699.1; ALT_FRAME; mRNA.
EMBL; AK048639; BAC33405.1; -; mRNA.
EMBL; AK053039; BAC35247.2; -; mRNA.
EMBL; AC153595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC153598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC161824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466523; EDK99388.1; -; Genomic_DNA.
EMBL; BC131670; AAI31671.1; -; mRNA.
EMBL; BC131671; AAI31672.1; -; mRNA.
EMBL; AJ319655; CAC88131.1; -; Genomic_DNA.
EMBL; AJ319656; CAC88131.1; JOINED; Genomic_DNA.
EMBL; AJ319657; CAC88131.1; JOINED; Genomic_DNA.
CCDS; CCDS39582.1; -. [P70232-1]
PIR; T42718; T42718.
RefSeq; NP_031723.2; NM_007697.2. [P70232-1]
RefSeq; XP_006505535.1; XM_006505472.3. [P70232-1]
RefSeq; XP_017176864.1; XM_017321375.1. [P70232-1]
RefSeq; XP_017176865.1; XM_017321376.1. [P70232-1]
UniGene; Mm.251288; -.
ProteinModelPortal; P70232; -.
SMR; P70232; -.
BioGrid; 198702; 1.
IntAct; P70232; 3.
MINT; P70232; -.
STRING; 10090.ENSMUSP00000063933; -.
iPTMnet; P70232; -.
PhosphoSitePlus; P70232; -.
jPOST; P70232; -.
MaxQB; P70232; -.
PaxDb; P70232; -.
PeptideAtlas; P70232; -.
PRIDE; P70232; -.
Ensembl; ENSMUST00000066905; ENSMUSP00000063933; ENSMUSG00000030077. [P70232-1]
Ensembl; ENSMUST00000203830; ENSMUSP00000144758; ENSMUSG00000030077. [P70232-1]
Ensembl; ENSMUST00000203912; ENSMUSP00000145026; ENSMUSG00000030077. [P70232-2]
GeneID; 12661; -.
KEGG; mmu:12661; -.
UCSC; uc009dcj.1; mouse. [P70232-1]
UCSC; uc009dck.1; mouse. [P70232-2]
CTD; 10752; -.
MGI; MGI:1098266; Chl1.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00940000160080; -.
HOGENOM; HOG000231380; -.
HOVERGEN; HBG000144; -.
InParanoid; P70232; -.
KO; K06758; -.
OMA; DMQATES; -.
TreeFam; TF351098; -.
PRO; PR:P70232; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030077; Expressed in 204 organ(s), highest expression level in Ammon's horn.
ExpressionAtlas; P70232; baseline and differential.
Genevisible; P70232; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030017; C:sarcomere; IBA:GO_Central.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0050890; P:cognition; IMP:MGI.
GO; GO:0035640; P:exploration behavior; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IDA:MGI.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 10.
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; IPR026966; Neurofascin/L1/NrCAM_C.
Pfam; PF13882; Bravo_FIGEY; 1.
Pfam; PF00041; fn3; 4.
Pfam; PF07679; I-set; 2.
Pfam; PF13895; Ig_2; 1.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
Extracellular matrix; Glycoprotein; Immunoglobulin domain; Membrane;
Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1209 Neural cell adhesion molecule L1-like
protein.
/FTId=PRO_0000247897.
CHAIN 26 ? Processed neural cell adhesion molecule
L1-like protein. {ECO:0000255}.
/FTId=PRO_0000314778.
TOPO_DOM 26 1083 Extracellular. {ECO:0000255}.
TRANSMEM 1084 1104 Helical. {ECO:0000255}.
TOPO_DOM 1105 1209 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 124 Ig-like C2-type 1.
DOMAIN 128 223 Ig-like C2-type 2.
DOMAIN 235 328 Ig-like C2-type 3.
DOMAIN 331 417 Ig-like C2-type 4.
DOMAIN 423 510 Ig-like C2-type 5.
DOMAIN 515 607 Ig-like C2-type 6.
DOMAIN 614 709 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 714 807 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 812 914 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 918 1015 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 555 558 DGEA.
MOTIF 1182 1186 FIG[AQ]Y.
SITE 753 754 Cleavage; by ADAM8.
SITE 1040 1041 Cleavage; by ADAM8.
MOD_RES 1148 1148 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1161 1161 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1181 1181 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 562 562 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 822 822 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1027 1027 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 153 204 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 262 310 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 352 401 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 445 494 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 536 591 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 227 227 S -> LKHASDSSSSTEICSQA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020083.
VAR_SEQ 1016 1070 SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDN
DSIFQDVIETRGRE -> K (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020084.
VAR_SEQ 1138 1209 SDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNE
DGSFIGAYTGAKEKGSVESNGSSTATFPLRA -> RKMVLK
QKLLSWSSSRGRTFYSCTKNTLFDGSSVDMKTLQPLRYFSS
NKHT (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020085.
MUTAGEN 555 558 DGEA->AGEV: Inhibition of migration
potentiation.
{ECO:0000269|PubMed:12721290}.
MUTAGEN 1186 1186 Y->A: Inhibition of migration
potentiation.
{ECO:0000269|PubMed:12721290}.
CONFLICT 50 50 D -> G (in Ref. 2; BAC35247).
{ECO:0000305}.
CONFLICT 77 77 D -> E (in Ref. 6; CAC88131).
{ECO:0000305}.
CONFLICT 425 425 I -> V (in Ref. 2; BAC35247).
{ECO:0000305}.
CONFLICT 602 602 E -> K (in Ref. 1; CAA63972).
{ECO:0000305}.
CONFLICT 612 612 P -> G (in Ref. 1; CAA63972).
{ECO:0000305}.
SEQUENCE 1209 AA; 135074 MW; 2C689475920AB84C CRC64;
MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK
GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS
EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI
SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP
TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID
VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE
IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC
DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST
SEKTQVTVLG VPDPPGNLHL SERQNRSVRL SWEAGDDHNS KISEYIVEFE GNREEPGKWE
ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV
QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP
YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG
LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA
GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR
KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST
QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS
DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS
STATFPLRA


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Pathways :
WP1069: Integrin-mediated cell adhesion
WP1185: Integrin-mediated cell adhesion
WP1386: Integrin-mediated cell adhesion
WP185: Integrin-mediated cell adhesion
WP2328: Allograft rejection
WP6: Integrin-mediated cell adhesion
WP74: Integrin-mediated cell adhesion
WP832: Integrin-mediated cell adhesion
WP951: Integrin-mediated cell adhesion
WP1011: T Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1043: Calcium Regulation in the Cardiac Cell
WP1049: G Protein Signaling Pathways
WP1078: G1 to S cell cycle control
WP1083: Cell cycle
WP1130: T Cell Receptor Signaling Pathway
WP1144: B Cell Receptor Signaling Pathway
WP1159: Calcium Regulation in the Cardiac Cell
WP1165: G Protein Signaling Pathways
WP1195: G1 to S cell cycle control
WP1200: Cell cycle
WP1345: T Cell Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP1365: Calcium Regulation in the Cardiac Cell
WP1371: G Protein Signaling Pathways

Related Genes :
[L1CAM CAML1 MIC5] Neural cell adhesion molecule L1 (N-CAM-L1) (NCAM-L1) (CD antigen CD171)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[Uchl1] Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1)
[UCHL1] Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1)
[Adgrl1 Cirl Cirl1 Cl1 Lphn1] Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1)
[Nrcam Kiaa0343] Neuronal cell adhesion molecule (Nr-CAM) (Neuronal surface protein Bravo) (mBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related)
[Adgrl1 Kiaa0821 Lec2 Lphn1] Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1) (Lectomedin-2)
[ADGRL1 KIAA0821 LEC2 LPHN1] Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1) (Lectomedin-2)
[ADGRL1 LPHN1] Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1)
[PKD2L1 PKD2L PKDL TRPP3] Polycystic kidney disease 2-like 1 protein (Polycystin-2 homolog) (Polycystin-2L1) (Polycystin-L) (Polycystin-L1)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[tesA apeA pldC b0494 JW0483] Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[Zfp36l1 Brf1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[ZFP36L1 BERG36 BRF1 ERF1 RNF162B TIS11B] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-response factor 1) (ERF-1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Metallo-beta-lactamase L1 type 3 (EC 3.5.2.6) (B3 metallo-beta-lactamase) (Beta-lactamase type III) (Metallo-beta-lactamase L1 type III) (Penicillinase)
[NFE2L1 HBZ17 NRF1 TCF11] Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) (Protein NRF1, p120 form) (Transcription factor 11) (TCF-11) [Cleaved into: Transcription factor NRF1 (Protein NRF1, p110 form)]
[PKD1L1 UNQ5785/PRO19563] Polycystic kidney disease protein 1-like 1 (PC1-like 1 protein) (Polycystin-1L1)
[Nfe2l1 Nrf1] Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1]
[YME1L1 FTSH1 YME1L UNQ1868/PRO4304] ATP-dependent zinc metalloprotease YME1L1 (EC 3.4.24.-) (ATP-dependent metalloprotease FtsH1) (Meg-4) (Presenilin-associated metalloprotease) (PAMP) (YME1-like protein 1)
[CCL3L1 D17S1718 G0S19-2 SCYA3L1; CCL3L3] C-C motif chemokine 3-like 1 (G0/G1 switch regulatory protein 19-2) (LD78-beta(1-70)) (PAT 464.2) (Small-inducible cytokine A3-like 1) (Tonsillar lymphocyte LD78 beta protein) [Cleaved into: LD78-beta(3-70); LD78-beta(5-70)]
[rplA b3984 JW3947] 50S ribosomal protein L1 (Large ribosomal subunit protein uL1)
[Cadm3 Igsf4b Necl1 Syncam3 Tsll1] Cell adhesion molecule 3 (Immunoglobulin superfamily member 4B) (IgSF4B) (Nectin-like protein 1) (NECL-1) (Synaptic cell adhesion molecule 3) (TSLC1-like protein 1)

Bibliography :