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Neural cell adhesion molecule L1 (N-CAM-L1) (NCAM-L1) (CD antigen CD171)

 L1CAM_HUMAN             Reviewed;        1257 AA.
P32004; A0AV65; A4ZYW4; B2RMU7; G3XAF4; Q8TA87;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
30-AUG-2017, entry version 195.
RecName: Full=Neural cell adhesion molecule L1;
Short=N-CAM-L1;
Short=NCAM-L1;
AltName: CD_antigen=CD171;
Flags: Precursor;
Name=L1CAM; Synonyms=CAML1, MIC5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=1932117; DOI=10.1016/0167-4781(91)90108-X;
Kobayashi M., Miura M., Asou H., Uyemura K.;
"Molecular cloning of cell adhesion molecule L1 from human nervous
tissue: a comparison of the primary sequences of L1 molecules of
different origin.";
Biochim. Biophys. Acta 1090:238-240(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=1769655;
Hlavin M.L., Lemmon V.;
"Molecular structure and functional testing of human L1CAM: an
interspecies comparison.";
Genomics 11:416-423(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1627459; DOI=10.1007/BF02919404;
Reid R.A., Hemperly J.J.;
"Variants of human L1 cell adhesion molecule arise through alternate
splicing of RNA.";
J. Mol. Neurosci. 3:127-135(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9286695; DOI=10.1006/geno.1997.4822;
Brenner V., Nyakatura G., Rosenthal A., Platzer M.;
"Genomic organization of two novel genes on human Xq28: compact head
to head arrangement of IDH gamma and TRAP delta is conserved in rat
and mouse.";
Genomics 44:8-14(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=9479034; DOI=10.1016/S0378-1119(97)00614-8;
Coutelle O., Nyakatura G., Taudien S., Elgar G., Brenner S.,
Platzer M., Drescher B., Jouet M., Kenwrick S., Rosenthal A.;
"The neural cell adhesion molecule L1: genomic organisation and
differential splicing is conserved between man and the pufferfish
Fugu.";
Gene 208:7-15(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Son Y.S.;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[10]
PROTEIN SEQUENCE OF 20-36.
PubMed=3136168;
Wolff J.M., Frank R., Mujoo K., Spiro R.C., Reisfeld R.A.,
Rathjen F.G.;
"A human brain glycoprotein related to the mouse cell adhesion
molecule L1.";
J. Biol. Chem. 263:11943-11947(1988).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 332-371.
PubMed=2387585; DOI=10.1016/0888-7543(90)90203-7;
Djabali M., Mattei M.-G., Nguyen C., Roux D., Demengeot J.,
Denizot F., Moos M., Schachner M., Goridis C., Jordan B.R.;
"The gene encoding L1, a neural adhesion molecule of the
immunoglobulin family, is located on the X chromosome in mouse and
man.";
Genomics 7:587-593(1990).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 353-1176, AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 1082-1176.
TISSUE=Fetal brain;
PubMed=1923824; DOI=10.1093/nar/19.19.5395;
Rosenthal A., Mackinnon R.N., Jones D.S.C.;
"PCR walking from microdissection clone M54 identifies three exons
from the human gene for the neural cell adhesion molecule L1 (CAM-
L1).";
Nucleic Acids Res. 19:5395-5401(1991).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1257.
PubMed=1993895; DOI=10.1111/j.1471-4159.1991.tb01994.x;
Harper J.R., Prince J.T., Healy P.A., Stuart J.K., Nauman S.J.,
Stallcup W.B.;
"Isolation and sequence of partial cDNA clones of human L1: homology
of human and rodent L1 in the cytoplasmic region.";
J. Neurochem. 56:797-804(1991).
[14]
PHOSPHORYLATION AT SER-1181.
PubMed=8592152;
Wong E.V., Schaefer A.W., Landreth G., Lemmon V.;
"Casein kinase II phosphorylates the neural cell adhesion molecule
L1.";
J. Neurochem. 66:779-786(1996).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
INVOLVEMENT IN L1 SYNDROME, VARIANTS 26-TYR--GLU-1257 DEL; ASN-37;
MET-38; 66-GLN--GLU-1257 DEL; 109-GLN--GLU-1257 DEL; 133-GLU--GLU-1257
DEL; 138-TRP--GLU-1257 DEL; ILE-172; GLY-184; 187-MET--VAL-198 DEL;
ASP-254; ARG-276; PRO-313; 366-TRP--GLU-1257 DEL; LYS-369;
423-GLN--GLU-1257 DEL; ARG-480; ASN-516; TYR-516; HIS-525; MET-627;
PRO-645; 662-TRP--GLU-1257 DEL; SER-714; ARG-754; 760-ARG--GLU-1257
DEL; 789-GLN--GLU-1257 DEL; 811-TYR--GLU-1257 DEL; 891-TYR--GLU-1257
DEL; 901-ARG--GLU-1257 DEL; 1064-SER--GLU-1257 DEL; ASN-1071 DEL AND
GLN-1080, VARIANTS HSAS/MASA SER-179; ARG-335 AND MET-752, VARIANT
MASA TYR-202, AND VARIANTS HSAS GLN-184 AND PRO-415.
PubMed=19846429; DOI=10.1136/jmg.2009.071688;
Vos Y.J., de Walle H.E., Bos K.K., Stegeman J.A., Ten Berge A.M.,
Bruining M., van Maarle M.C., Elting M.W., den Hollander N.S.,
Hamel B., Fortuna A.M., Sunde L.E., Stolte-Dijkstra I.,
Schrander-Stumpel C.T., Hofstra R.M.;
"Genotype-phenotype correlations in L1 syndrome: a guide for genetic
counselling and mutation analysis.";
J. Med. Genet. 47:169-175(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-1177 (ISOFORM 2), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-1172 (ISOFORM 3), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
INVOLVEMENT IN L1 SYNDROME, VARIANTS CYS-635 AND ILE-768, AND
GLYCOSYLATION.
PubMed=22222883; DOI=10.1007/s10048-011-0307-4;
Marx M., Diestel S., Bozon M., Keglowich L., Drouot N., Bouche E.,
Frebourg T., Minz M., Saugier-Veber P., Castellani V., Schaefer M.K.;
"Pathomechanistic characterization of two exonic L1CAM variants
located in trans in an obligate carrier of X-linked hydrocephalus.";
Neurogenetics 13:49-59(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
VARIANT HSAS TYR-264.
PubMed=8401576; DOI=10.1038/ng0893-331;
Jouet M., Rosenthal A., Macfarlane J., Kenwrick S., Donnai D.;
"A missense mutation confirms the L1 defect in X-linked hydrocephalus
(HSAS).";
Nat. Genet. 4:331-331(1993).
[26]
VARIANT HSAS/MASA LEU-1194.
PubMed=7881431; DOI=10.1093/hmg/3.12.2255;
Fransen E., Schrander-Stumpel C., Vits L., Coucke P., van Camp G.,
Willems P.J.;
"X-linked hydrocephalus and MASA syndrome present in one family are
due to a single missense mutation in exon 28 of the L1CAM gene.";
Hum. Mol. Genet. 3:2255-2256(1994).
[27]
INVOLVEMENT IN MASA, INVOLVEMENT IN HSAS, VARIANTS HSAS GLN-184 AND
ARG-452, AND VARIANT MASA GLN-210.
PubMed=7920659; DOI=10.1038/ng0794-402;
Jouet M., Rosenthal A., Armstrong G., Macfarlane J., Stevenson R.,
Paterson J., Metzenberg A., Ionasescu V., Temple K., Kenwrick S.;
"X-linked spastic paraplegia (SPG1), MASA syndrome and X-linked
hydrocephalus result from mutations in the L1 gene.";
Nat. Genet. 7:402-407(1994).
[28]
VARIANTS MASA GLN-210 AND ASN-598.
PubMed=7920660; DOI=10.1038/ng0794-408;
Vits L., van Camp G., Coucke P., Fransen E., de Boulle K.,
Reyniers E., Korn B., Poustka A., Wilson G., Schrander-Stumpel C.,
Winter R.M., Schwartz C., Willems P.J.;
"MASA syndrome is due to mutations in the neural cell adhesion gene
L1CAM.";
Nat. Genet. 7:408-413(1994).
[29]
VARIANT HSAS/MASA LEU-941, VARIANT MASA LYS-309, AND VARIANTS HSAS
SER-9; SER-121; PHE-768 AND CYS-1070.
PubMed=7762552;
Jouet M., Moncla A., Paterson J., McKeown C., Fryer A., Carpenter N.,
Holmberg E., Wadelius C., Kenwrick S.;
"New domains of neural cell-adhesion molecule L1 implicated in X-
linked hydrocephalus and MASA syndrome.";
Am. J. Hum. Genet. 56:1304-1314(1995).
[30]
VARIANT HSAS/MASA LEU-1194, VARIANTS HSAS GLN-184; TYR-264 AND
ARG-452, AND VARIANTS MASA GLN-210 AND ASN-598.
PubMed=8556302;
Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.;
"CRASH syndrome: clinical spectrum of corpus callosum hypoplasia,
retardation, adducted thumbs, spastic paraparesis and hydrocephalus
due to mutations in one single gene, L1.";
Eur. J. Hum. Genet. 3:273-284(1995).
[31]
ERRATUM.
Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.;
Eur. J. Hum. Genet. 4:126-126(1996).
[32]
INVOLVEMENT IN MASA, INVOLVEMENT IN HSAS, AND VARIANTS HSAS/MASA
SER-179 AND ARG-370.
PubMed=7562969; DOI=10.1136/jmg.32.7.549;
Ruiz J.C., Cuppens H., Legius E., Fryns J.-P., Glover T., Marynen P.,
Cassiman J.-J.;
"Mutations in L1-CAM in two families with X linked complicated spastic
paraplegia, MASA syndrome, and HSAS.";
J. Med. Genet. 32:549-552(1995).
[33]
VARIANT HSAS GLU-655.
PubMed=9118141; DOI=10.1007/BF00261591;
Izumoto S., Yamasaki M., Arita N., Hiraga S., Ohnishi T., Fujitani K.,
Sakoda S., Hayakawa T.;
"A new mutation of the L1CAM gene in an X-linked hydrocephalus
family.";
Childs Nerv. Syst. 12:742-747(1996).
[34]
VARIANTS HSAS CYS-194 AND LEU-240.
PubMed=8929944; DOI=10.1136/jmg.33.2.103;
Gu S.-M., Orth U., Veske A., Enders H., Kluender K., Schloesser M.,
Engel W., Schwinger E., Gal A.;
"Five novel mutations in the L1CAM gene in families with X linked
hydrocephalus.";
J. Med. Genet. 33:103-106(1996).
[35]
VARIANT MASA PRO-482, VARIANTS HSAS SER-526 DEL; PRO-542 AND THR-741,
VARIANT HSAS/MASA MET-752, AND VARIANT ILE-768.
PubMed=9268105;
DOI=10.1002/(SICI)1096-8628(19970822)71:3<336::AID-AJMG15>3.0.CO;2-L;
Gu S.-M., Orth U., Zankl M., Schroeder J., Gal A.;
"Molecular analysis of the L1CAM gene in patients with X-linked
hydrocephalus demonstrates eight novel mutations and suggests non-
allelic heterogeneity of the trait.";
Am. J. Med. Genet. 71:336-340(1997).
[36]
VARIANTS MASA ASP-268 AND ASP-426.
PubMed=9300653; DOI=10.1093/hmg/6.10.1625;
Fransen E., Van Camp G., Vits L., Willems P.J.;
"L1-associated diseases: clinical geneticists divide, molecular
geneticists unite.";
Hum. Mol. Genet. 6:1625-1632(1997).
[37]
VARIANTS HSAS GLN-184; 439-VAL--THR-443 DEL; CYS-784 AND
936-LEU--LEU-948 DEL.
PubMed=9195224;
DOI=10.1002/(SICI)1098-1004(1997)9:6<512::AID-HUMU3>3.0.CO;2-3;
Macfarlane J.R., Du J.-S., Pepys M.E., Ramsden S., Donnai D.,
Charlton R., Garrett C., Tolmie J., Yates J.R.W., Berry C., Goudie D.,
Moncla A., Lunt P., Hodgson S., Jouet M., Kenwrick S.;
"Nine novel L1 CAM mutations in families with X-linked
hydrocephalus.";
Hum. Mutat. 9:512-518(1997).
[38]
VARIANT HSAS/MASA ARG-698, VARIANT MASA ASP-691, AND VARIANT HSAS
PRO-935.
PubMed=9521424;
DOI=10.1002/(SICI)1098-1004(1998)11:3<222::AID-HUMU7>3.0.CO;2-J;
Du Y.-Z., Srivastava A.K., Schwartz C.E.;
"Multiple exon screening using restriction endonuclease fingerprinting
(REF): detection of six novel mutations in the L1 cell adhesion
molecule (L1CAM) gene.";
Hum. Mutat. 11:222-230(1998).
[39]
VARIANT MASA PRO-632.
PubMed=9452110;
Vits L., Chitayat D., van Camp G., Holden J.J.A., Fransen E.,
Willems P.J.;
"Evidence for somatic and germline mosaicism in CRASH syndrome.";
Hum. Mutat. Suppl. 1:S284-S287(1998).
[40]
VARIANTS HSAS/MASA ARG-335 AND CYS-473, AND VARIANTS HSAS THR-219;
CYS-386 AND LEU-1224.
PubMed=9744477;
DOI=10.1002/(SICI)1098-1004(1998)12:4<259::AID-HUMU7>3.0.CO;2-A;
Saugier-Veber P., Martin C., le Meur N., Lyonnet S., Munnich A.,
David A., Henocq A., Heron D., Jonveaux P., Odent S., Manouvrier S.,
Moncla A., Morichon N., Philip N., Satge D., Tosi M., Frebourg T.;
"Identification of novel L1CAM mutations using fluorescence-assisted
mismatch analysis.";
Hum. Mutat. 12:259-266(1998).
[41]
VARIANTS MASA CYS-674 AND ASP-691, AND VARIANT HSAS/MASA ARG-698.
PubMed=9832035; DOI=10.1136/jmg.35.11.901;
Michaelis R.C., Du Y.-Z., Schwartz C.E.;
"The site of a missense mutation in the extracellular Ig or FN domains
of L1CAM influences infant mortality and the severity of X linked
hydrocephalus.";
J. Med. Genet. 35:901-904(1998).
[42]
VARIANTS HSAS TRP-184; CYS-335; ILE-408; ASP-421; TYR-497; THR-691 AND
PRO-751, VARIANTS ASN-30; TRP-739 AND GLU-1239, AND VARIANT HSAS/MASA
ARG-370.
PubMed=10797421;
DOI=10.1002/(SICI)1096-8628(20000501)92:1<40::AID-AJMG7>3.0.CO;2-R;
Finckh U., Schroeder J., Ressler B., Veske A., Gal A.;
"Spectrum and detection rate of L1CAM mutations in isolated and
familial cases with clinically suspected L1-disease.";
Am. J. Med. Genet. 92:40-46(2000).
[43]
VARIANT MASA TYR-202.
PubMed=10805190;
Sztriha L., Frossard P., Hofstra R.M., Verlind E., Nork M.;
"Novel missense mutation in the L1 gene in a child with corpus
callosum agenesis, retardation, adducted thumbs, spastic paraparesis,
and hydrocephalus.";
J. Child Neurol. 15:239-243(2000).
[44]
VARIANT HSAS/MASA MET-752, AND POSSIBLE INVOLVEMENT IN HIRSCHSPRUNG
DISEASE.
PubMed=11857550; DOI=10.1002/ajmg.10185;
Parisi M.A., Kapur R.P., Neilson I., Hofstra R.M.W., Holloway L.W.,
Michaelis R.C., Leppig K.A.;
"Hydrocephalus and intestinal aganglionosis: is L1CAM a modifier gene
in Hirschsprung disease?";
Am. J. Med. Genet. 108:51-56(2002).
[45]
VARIANT HSAS PRO-415.
PubMed=12435569; DOI=10.1016/S0887-8994(02)00440-X;
Sztriha L., Vos Y.J., Verlind E., Johansen J., Berg B.;
"X-linked hydrocephalus: a novel missense mutation in the L1CAM
gene.";
Pediatr. Neurol. 27:293-296(2002).
[46]
CHARACTERIZATION OF VARIANT HSAS TYR-264, SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
PubMed=12514225;
Ruenker A.E., Bartsch U., Nave K.A., Schachner M.;
"The C264Y missense mutation in the extracellular domain of L1 impairs
protein trafficking in vitro and in vivo.";
J. Neurosci. 23:277-286(2003).
[47]
VARIANT ACCPX LEU-240.
PubMed=16650080; DOI=10.1111/j.1399-0004.2006.00607.x;
Basel-Vanagaite L., Straussberg R., Friez M.J., Inbar D.,
Korenreich L., Shohat M., Schwartz C.E.;
"Expanding the phenotypic spectrum of L1CAM-associated disease.";
Clin. Genet. 69:414-419(2006).
[48]
VARIANT MASA ASN-770.
PubMed=16816908; DOI=10.1007/s10072-006-0610-2;
Simonati A., Boaretto F., Vettori A., Dabrilli P., Criscuolo L.,
Rizzuto N., Mostacciuolo M.L.;
"A novel missense mutation in the L1CAM gene in a boy with L1
disease.";
Neurol. Sci. 27:114-117(2006).
[49]
CHARACTERIZATION OF VARIANTS HSAS GLN-184 AND LEU-1036, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=20621658; DOI=10.1016/j.nbd.2010.05.029;
Schaefer M.K., Nam Y.C., Moumen A., Keglowich L., Bouche E.,
Kueffner M., Bock H.H., Rathjen F.G., Raoul C., Frotscher M.;
"L1 syndrome mutations impair neuronal L1 function at different levels
by divergent mechanisms.";
Neurobiol. Dis. 40:222-237(2010).
[50]
INVOLVEMENT OF VARIANT HSAS/MASA ARG-698 IN HYDROCEPHALUS WITH
HIRSCHSPRUNG DISEASE.
PubMed=22344793; DOI=10.1002/ajmg.a.35244;
Fernandez R.M., Nunez-Torres R., Garcia-Diaz L., de Agustin J.C.,
Antinolo G., Borrego S.;
"Association of X-linked hydrocephalus and Hirschsprung disease:
Report of a new patient with a mutation in the L1CAM gene.";
Am. J. Med. Genet. A 158:816-820(2012).
[51]
CHARACTERIZATION OF VARIANTS MASA GLN-210 AND LYS-309,
CHARACTERIZATION OF VARIANTS HSAS THR-219 AND CYS-264,
CHARACTERIZATION OF VARIANT HSAS/MASA LEU-941, AND SUBCELLULAR
LOCATION.
PubMed=22973895; DOI=10.1111/jnc.12015;
Tagliavacca L., Colombo F., Racchetti G., Meldolesi J.;
"L1CAM and its cell-surface mutants: new mechanisms and effects
relevant to the physiology and pathology of neural cells.";
J. Neurochem. 124:397-409(2013).
[52]
CHARACTERIZATION OF VARIANT VAL-120, CHARACTERIZATION OF VARIANTS MASA
GLN-210 AND LYS-309, CHARACTERIZATION OF VARIANTS HSAS GLN-184;
TYR-264 AND CYS-1070, AND MUTAGENESIS OF 1147-LYS--VAL-1153.
PubMed=24155914; DOI=10.1371/journal.pone.0076974;
Kudumala S., Freund J., Hortsch M., Godenschwege T.A.;
"Differential effects of human L1CAM mutations on complementing
guidance and synaptic defects in Drosophila melanogaster.";
PLoS ONE 8:E76974-E76974(2013).
[53]
VARIANT 789-GLN--GLU-1257 DEL, CHARACTERIZATION OF VARIANTS ASN-37;
MET-38 AND ILE-172, CHARACTERIZATION OF VARIANT MASA TYR-202, AND
SUBCELLULAR LOCATION.
PubMed=26891472; DOI=10.1111/cge.12763;
Christaller W.A., Vos Y., Gebre-Medhin S., Hofstra R.M.,
Schaefer M.K.;
"L1 syndrome diagnosis complemented with functional analysis of L1CAM
variants located to the two N-terminal Ig-like domains.";
Clin. Genet. 91:115-120(2017).
-!- FUNCTION: Neural cell adhesion molecule involved in the dynamics
of cell adhesion and in the generation of transmembrane signals at
tyrosine kinase receptors. During brain development, critical in
multiple processes, including neuronal migration, axonal growth
and fasciculation, and synaptogenesis. In the mature brain, plays
a role in the dynamics of neuronal structure and function,
including synaptic plasticity. {ECO:0000269|PubMed:20621658,
ECO:0000305}.
-!- SUBUNIT: Interacts with SHTN1; the interaction occurs in axonal
growth cones. {ECO:0000250|UniProtKB:Q05695}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12514225,
ECO:0000269|PubMed:20621658, ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:26891472}; Single-pass type I membrane protein
{ECO:0000250|UniProtKB:Q05695}. Cell projection, growth cone
{ECO:0000250|UniProtKB:Q05695}. Cell projection, axon
{ECO:0000269|PubMed:20621658}. Cell projection, dendrite.
Note=Colocalized with SHTN1 in close apposition with actin
filaments in filopodia and lamellipodia of axonalne growth cones
of hippocampal neurons (By similarity). In neurons, detected
predominantly in axons and cell body, weak localization to
dendrites (PubMed:20621658). {ECO:0000250|UniProtKB:Q05695,
ECO:0000269|PubMed:20621658}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P32004-1; Sequence=Displayed;
Name=2;
IsoId=P32004-2; Sequence=VSP_002591;
Note=Contains a phosphoserine at position 1177.
{ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692};
Name=3;
IsoId=P32004-3; Sequence=VSP_046317, VSP_002591;
Note=Contains a phosphoserine at position 1172.
{ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692};
-!- DISEASE: Hydrocephalus due to stenosis of the aqueduct of Sylvius
(HSAS) [MIM:307000]: Hydrocephalus is a condition in which
abnormal accumulation of cerebrospinal fluid in the brain causes
increased intracranial pressure inside the skull. This is usually
due to blockage of cerebrospinal fluid outflow in the brain
ventricles or in the subarachnoid space at the base of the brain.
In children is typically characterized by enlargement of the head,
prominence of the forehead, brain atrophy, mental deterioration,
and convulsions. In adults the syndrome includes incontinence,
imbalance, and dementia. HSAS is characterized by mental
retardation and enlarged brain ventricles.
{ECO:0000269|PubMed:10797421, ECO:0000269|PubMed:11857550,
ECO:0000269|PubMed:12435569, ECO:0000269|PubMed:12514225,
ECO:0000269|PubMed:19846429, ECO:0000269|PubMed:20621658,
ECO:0000269|PubMed:22344793, ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:24155914, ECO:0000269|PubMed:7562969,
ECO:0000269|PubMed:7762552, ECO:0000269|PubMed:7881431,
ECO:0000269|PubMed:7920659, ECO:0000269|PubMed:8401576,
ECO:0000269|PubMed:8556302, ECO:0000269|PubMed:8929944,
ECO:0000269|PubMed:9118141, ECO:0000269|PubMed:9195224,
ECO:0000269|PubMed:9268105, ECO:0000269|PubMed:9521424,
ECO:0000269|PubMed:9744477, ECO:0000269|PubMed:9832035}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. L1CAM mutations have also been found in few patients
affected by hydrocephalus with Hirschsprung disease, suggesting a
role of this gene acting either in a direct or indirect way in the
pathogenesis of Hirschsprung disease (PubMed:22344793).
{ECO:0000269|PubMed:22344793}.
-!- DISEASE: Mental retardation, aphasia, shuffling gait, and adducted
thumbs syndrome (MASA) [MIM:303350]: An X-linked recessive
syndrome with a highly variable clinical spectrum. Main clinical
features include spasticity and hyperreflexia of lower limbs,
shuffling gait, mental retardation, aphasia and adducted thumbs.
The features of spasticity have been referred to as complicated
spastic paraplegia type 1 (SPG1). Some patients manifest corpus
callosum hypoplasia and hydrocephalus. Inter- and intrafamilial
variability is very wide, such that patients with hydrocephalus,
MASA, SPG1, and agenesis of corpus callosum can be present within
the same family. {ECO:0000269|PubMed:10797421,
ECO:0000269|PubMed:10805190, ECO:0000269|PubMed:11857550,
ECO:0000269|PubMed:16816908, ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:22344793, ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:24155914, ECO:0000269|PubMed:26891472,
ECO:0000269|PubMed:7562969, ECO:0000269|PubMed:7762552,
ECO:0000269|PubMed:7881431, ECO:0000269|PubMed:7920659,
ECO:0000269|PubMed:7920660, ECO:0000269|PubMed:8556302,
ECO:0000269|PubMed:9268105, ECO:0000269|PubMed:9300653,
ECO:0000269|PubMed:9452110, ECO:0000269|PubMed:9521424,
ECO:0000269|PubMed:9744477, ECO:0000269|PubMed:9832035}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Defects in L1CAM may contribute to Hirschsprung
disease by modifying the effects of Hirschsprung disease-
associated genes to cause intestinal aganglionosis.
{ECO:0000269|PubMed:11857550}.
-!- DISEASE: Agenesis of the corpus callosum, X-linked, partial
(ACCPX) [MIM:304100]: A syndrome characterized by partial corpus
callosum agenesis, hypoplasia of inferior vermis and cerebellum,
mental retardation, seizures and spasticity. Other features
include microcephaly, unusual facies, and Hirschsprung disease in
some patients. {ECO:0000269|PubMed:16650080}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in L1CAM are associated with a wide
phenotypic spectrum which varies from severe hydrocephalus and
prenatal death (HSAS) to a milder phenotype (MASA). These
variations may even occur within the same family. Due to the
overlap of phenotypes between HSAS and MASA, many authors use the
general concept of L1 syndrome which covers both ends of the
spectrum. {ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:22222883, ECO:0000269|PubMed:26891472}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
L1/neurofascin/NgCAM family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/L1CAMID44110chXq28.html";
-!- WEB RESOURCE: Name=L1CAM; Note=L1CAM mutation Web Page;
URL="http://www.l1cammutationdatabase.info/";
-----------------------------------------------------------------------
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EMBL; X59847; CAA42508.1; -; mRNA.
EMBL; M77640; AAC14352.1; -; mRNA.
EMBL; M74387; AAA59476.1; -; mRNA.
EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z29373; CAA82564.1; -; Genomic_DNA.
EMBL; EF506611; ABP88252.1; -; mRNA.
EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471172; EAW72787.1; -; Genomic_DNA.
EMBL; BC025843; AAH25843.1; -; mRNA.
EMBL; BC126229; AAI26230.1; -; mRNA.
EMBL; BC136447; AAI36448.1; -; mRNA.
EMBL; M55271; AAA36353.1; ALT_SEQ; mRNA.
EMBL; X58775; CAA41576.1; -; Genomic_DNA.
EMBL; X58776; CAB37831.1; -; mRNA.
CCDS; CCDS14733.1; -. [P32004-1]
CCDS; CCDS14734.1; -. [P32004-2]
CCDS; CCDS48192.1; -. [P32004-3]
PIR; A41060; A41060.
RefSeq; NP_000416.1; NM_000425.4. [P32004-1]
RefSeq; NP_001137435.1; NM_001143963.2. [P32004-3]
RefSeq; NP_001265045.1; NM_001278116.1. [P32004-1]
RefSeq; NP_076493.1; NM_024003.3. [P32004-2]
UniGene; Hs.522818; -.
DisProt; DP00666; -.
ProteinModelPortal; P32004; -.
SMR; P32004; -.
BioGrid; 110094; 24.
ELM; P32004; -.
IntAct; P32004; 4.
MINT; MINT-1369985; -.
STRING; 9606.ENSP00000359074; -.
iPTMnet; P32004; -.
PhosphoSitePlus; P32004; -.
SwissPalm; P32004; -.
DMDM; 1705571; -.
EPD; P32004; -.
MaxQB; P32004; -.
PaxDb; P32004; -.
PeptideAtlas; P32004; -.
PRIDE; P32004; -.
Ensembl; ENST00000361699; ENSP00000355380; ENSG00000198910. [P32004-2]
Ensembl; ENST00000361981; ENSP00000354712; ENSG00000198910. [P32004-3]
Ensembl; ENST00000370055; ENSP00000359072; ENSG00000198910. [P32004-3]
Ensembl; ENST00000370060; ENSP00000359077; ENSG00000198910. [P32004-1]
GeneID; 3897; -.
KEGG; hsa:3897; -.
UCSC; uc004fjc.5; human. [P32004-1]
CTD; 3897; -.
DisGeNET; 3897; -.
GeneCards; L1CAM; -.
GeneReviews; L1CAM; -.
HGNC; HGNC:6470; L1CAM.
HPA; CAB010896; -.
HPA; HPA005830; -.
MalaCards; L1CAM; -.
MIM; 303350; phenotype.
MIM; 304100; phenotype.
MIM; 307000; phenotype.
MIM; 308840; gene.
neXtProt; NX_P32004; -.
OpenTargets; ENSG00000198910; -.
Orphanet; 2182; Hydrocephalus with stenosis of the aqueduct of Sylvius.
Orphanet; 2466; MASA syndrome.
Orphanet; 1497; X-linked complicated corpus callosum dysgenesis.
Orphanet; 306617; X-linked complicated spastic paraplegia type 1.
PharmGKB; PA30259; -.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000231380; -.
HOVERGEN; HBG000144; -.
InParanoid; P32004; -.
KO; K06550; -.
OMA; CFIKRSK; -.
OrthoDB; EOG091G00LY; -.
PhylomeDB; P32004; -.
TreeFam; TF351098; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-373760; L1CAM interactions.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
Reactome; R-HSA-445144; Signal transduction by L1.
SIGNOR; P32004; -.
ChiTaRS; L1CAM; human.
GeneWiki; L1_(protein); -.
GenomeRNAi; 3897; -.
PMAP-CutDB; P32004; -.
PRO; PR:P32004; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000198910; -.
CleanEx; HS_L1CAM; -.
ExpressionAtlas; P32004; baseline and differential.
Genevisible; P32004; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IDA:CAFA.
GO; GO:0061564; P:axon development; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; TAS:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IDA:UniProtKB.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 11.
InterPro; IPR003961; FN3_dom.
InterPro; IPR007110; Ig-like_dom.
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.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 5.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hereditary spastic paraplegia; Hirschsprung disease;
Immunoglobulin domain; Membrane; Mental retardation;
Neurodegeneration; Neurogenesis; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:3136168}.
CHAIN 20 1257 Neural cell adhesion molecule L1.
/FTId=PRO_0000015022.
TOPO_DOM 20 1120 Extracellular. {ECO:0000255}.
TRANSMEM 1121 1143 Helical. {ECO:0000255}.
TOPO_DOM 1144 1257 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 125 Ig-like C2-type 1.
DOMAIN 139 226 Ig-like C2-type 2.
DOMAIN 240 328 Ig-like C2-type 3.
DOMAIN 333 420 Ig-like C2-type 4.
DOMAIN 425 507 Ig-like C2-type 5.
DOMAIN 518 607 Ig-like C2-type 6.
DOMAIN 615 712 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 717 810 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 814 916 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 920 1015 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1016 1115 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 554 556 Cell attachment site. {ECO:0000255}.
MOD_RES 1163 1163 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1178 1178 Phosphoserine.
{ECO:0000250|UniProtKB:P11627}.
MOD_RES 1181 1181 Phosphoserine; by CaMK2.
{ECO:0000269|PubMed:8592152}.
MOD_RES 1194 1194 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1243 1243 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1244 1244 Phosphoserine.
{ECO:0000250|UniProtKB:P11627}.
MOD_RES 1248 1248 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 490 490 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 588 588 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 671 671 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 726 726 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 777 777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 825 825 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 849 849 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 876 876 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 979 979 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1022 1022 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1030 1030 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1071 1071 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1105 1105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 114 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 158 209 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 264 312 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 354 404 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 448 497 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 539 591 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 26 31 YEGHHV -> L (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_046317.
VAR_SEQ 1177 1180 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:1627459,
ECO:0000303|Ref.6}.
/FTId=VSP_002591.
VARIANT 9 9 W -> S (in HSAS).
{ECO:0000269|PubMed:7762552}.
/FTId=VAR_003921.
VARIANT 26 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078350.
VARIANT 30 30 H -> N. {ECO:0000269|PubMed:10797421}.
/FTId=VAR_030403.
VARIANT 37 37 I -> N (probable disease-associated
mutation found in L1 syndrome; loss of
localization at the cell surface;
retention in the endoplasmic reticulum;
loss of homophilic interactions at the
cell surface).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:26891472}.
/FTId=VAR_078351.
VARIANT 38 38 T -> M (no effect on localization at the
cell surface; dbSNP:rs201151358).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:26891472}.
/FTId=VAR_078352.
VARIANT 66 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078353.
VARIANT 109 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078354.
VARIANT 120 120 L -> V (no effect on axon guidance
activity, nor on synapse formation, when
assayed in a heterologous system;
dbSNP:rs796052697).
{ECO:0000269|PubMed:24155914}.
/FTId=VAR_078355.
VARIANT 121 121 G -> S (in HSAS).
{ECO:0000269|PubMed:7762552}.
/FTId=VAR_003922.
VARIANT 133 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078356.
VARIANT 138 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078357.
VARIANT 172 172 M -> I (probable disease-associated
mutation found in a patient with L1
syndrome; loss of homophilic interactions
at the cell surface; no effect on the
localization at the cell surface).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:26891472}.
/FTId=VAR_078358.
VARIANT 179 179 I -> S (in HSAS and MASA;
dbSNP:rs137852523).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:7562969}.
/FTId=VAR_003923.
VARIANT 184 184 R -> G (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078359.
VARIANT 184 184 R -> Q (in HSAS; severe; reduced axon
arborization; partial loss of
localization at the cell surface;
retention in the endoplasmic reticulum;
in neurons, restricted to cell bodies and
proximal segments of processes; loss of
axon guidance and of proper synapse
formation, when assayed in a heterologous
system; dbSNP:rs137852521).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:20621658,
ECO:0000269|PubMed:24155914,
ECO:0000269|PubMed:7920659,
ECO:0000269|PubMed:8556302,
ECO:0000269|PubMed:9195224}.
/FTId=VAR_003924.
VARIANT 184 184 R -> W (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030404.
VARIANT 187 198 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078360.
VARIANT 194 194 Y -> C (in HSAS).
{ECO:0000269|PubMed:8929944}.
/FTId=VAR_003925.
VARIANT 202 202 D -> Y (in MASA; loss of homophilic
interactions at the cell surface; no
effect on localization at the cell
surface). {ECO:0000269|PubMed:10805190,
ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:26891472}.
/FTId=VAR_030405.
VARIANT 210 210 H -> Q (in MASA; decrease in cell-matrix
adhesion; decreased cell migration; loss
of axon guidance and of proper synapse
formation, when assayed in a heterologous
system; no effect on the localization at
the cell surface; no effect on cell
proliferation, when transfected in
pheochromocytoma PC12 cells; no effect on
neurite outgrowth, when assayed in NGF-
treated pheochromocytoma PC12 cells;
dbSNP:rs28933683).
{ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:24155914,
ECO:0000269|PubMed:7920659,
ECO:0000269|PubMed:7920660,
ECO:0000269|PubMed:8556302}.
/FTId=VAR_003926.
VARIANT 219 219 I -> T (in HSAS; decrease in cell-matrix
adhesion; decreased cell migration; no
effect on the localization at the cell
surface; no effect on cell proliferation,
when transfected in pheochromocytoma PC12
cells; no effect on neurite outgrowth,
when assayed in NGF-treated
pheochromocytoma PC12 cells).
{ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:9744477}.
/FTId=VAR_003927.
VARIANT 240 240 P -> L (in HSAS and ACCPX;
dbSNP:rs137852526).
{ECO:0000269|PubMed:16650080,
ECO:0000269|PubMed:8929944}.
/FTId=VAR_003928.
VARIANT 254 254 A -> D (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078361.
VARIANT 264 264 C -> Y (in HSAS; severe; loss of
localization to the cell surface;
retention in the endoplasmic reticulum;
loss of axon guidance, when assayed in a
heterologous system; dbSNP:rs137852518).
{ECO:0000269|PubMed:12514225,
ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:24155914,
ECO:0000269|PubMed:8401576,
ECO:0000269|PubMed:8556302}.
/FTId=VAR_003929.
VARIANT 268 268 G -> D (in MASA).
{ECO:0000269|PubMed:9300653}.
/FTId=VAR_030406.
VARIANT 276 276 W -> R (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078362.
VARIANT 309 309 E -> K (in MASA; decrease in neurite
outgrowth, when assayed in NGF-treated
pheochromocytoma PC12 cells; decrease in
cell-matrix adhesion; decreased cell
migration; no effect on axon guidance, on
subcellular location to synaptic
terminals, nor on proper synapse
formation, when assayed in a heterologous
system; no effect on the localization at
the cell surface; no effect on cell
proliferation, when transfected in
pheochromocytoma PC12 cells;
dbSNP:rs367665974).
{ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:24155914,
ECO:0000269|PubMed:7762552}.
/FTId=VAR_003930.
VARIANT 313 313 L -> P (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078363.
VARIANT 335 335 W -> C (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030407.
VARIANT 335 335 W -> R (in HSAS and MASA; also in a
patient with hydrocephalus and
Hirschsprung disease).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:9744477}.
/FTId=VAR_003931.
VARIANT 366 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078364.
VARIANT 369 369 N -> K (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078365.
VARIANT 370 370 G -> R (in HSAS and MASA;
dbSNP:rs137852524).
{ECO:0000269|PubMed:10797421,
ECO:0000269|PubMed:7562969}.
/FTId=VAR_003932.
VARIANT 386 386 R -> C (in HSAS).
{ECO:0000269|PubMed:9744477}.
/FTId=VAR_003933.
VARIANT 408 408 N -> I (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030408.
VARIANT 415 415 A -> P (in HSAS).
{ECO:0000269|PubMed:12435569,
ECO:0000269|PubMed:19846429}.
/FTId=VAR_027512.
VARIANT 421 421 V -> D (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030409.
VARIANT 423 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078366.
VARIANT 426 426 A -> D (in MASA).
{ECO:0000269|PubMed:9300653}.
/FTId=VAR_030410.
VARIANT 439 443 Missing (in HSAS).
{ECO:0000269|PubMed:9195224}.
/FTId=VAR_003934.
VARIANT 452 452 G -> R (in HSAS; severe;
dbSNP:rs137852520).
{ECO:0000269|PubMed:7920659,
ECO:0000269|PubMed:8556302}.
/FTId=VAR_003935.
VARIANT 473 473 R -> C (in HSAS and MASA).
{ECO:0000269|PubMed:9744477}.
/FTId=VAR_003936.
VARIANT 480 480 G -> R (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078367.
VARIANT 482 482 L -> P (in MASA).
{ECO:0000269|PubMed:9268105}.
/FTId=VAR_030411.
VARIANT 497 497 C -> Y (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030412.
VARIANT 516 516 D -> N (found in a patient with L1
syndrome; unknown pathological
significance).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078368.
VARIANT 516 516 D -> Y (found in a patient with L1
syndrome; unknown pathological
significance).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078369.
VARIANT 525 525 R -> H (found in a patient with L1
syndrome; unknown pathological
significance; dbSNP:rs782401498).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078370.
VARIANT 526 526 Missing (in HSAS).
{ECO:0000269|PubMed:9268105}.
/FTId=VAR_030413.
VARIANT 542 542 S -> P (in HSAS).
{ECO:0000269|PubMed:9268105}.
/FTId=VAR_030414.
VARIANT 598 598 D -> N (in MASA; dbSNP:rs137852519).
{ECO:0000269|PubMed:7920660,
ECO:0000269|PubMed:8556302}.
/FTId=VAR_003937.
VARIANT 627 627 T -> M (in dbSNP:rs398123360).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078371.
VARIANT 632 632 R -> P (in MASA).
{ECO:0000269|PubMed:9452110}.
/FTId=VAR_003938.
VARIANT 635 635 W -> C (probable disease-associated
mutation found in L1 syndrome; loss of
localization at the cell surface;
retention in the endoplasmic reticulum;
loss of transport into axons; loss of
neurite outgrowth; loss of cell-cell
adhesion). {ECO:0000269|PubMed:22222883}.
/FTId=VAR_078372.
VARIANT 645 645 I -> P (probable disease-associated
mutation found in L1 syndrome; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078373.
VARIANT 655 655 K -> E (in HSAS).
{ECO:0000269|PubMed:9118141}.
/FTId=VAR_030415.
VARIANT 662 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078374.
VARIANT 674 674 S -> C (in MASA; associated with callosal
agenesis). {ECO:0000269|PubMed:9832035}.
/FTId=VAR_027513.
VARIANT 691 691 A -> D (in MASA; associated with callosal
agenesis). {ECO:0000269|PubMed:9521424,
ECO:0000269|PubMed:9832035}.
/FTId=VAR_003939.
VARIANT 691 691 A -> T (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030416.
VARIANT 698 698 G -> R (in HSAS and MASA; associated with
callosal agenesis; also found in a
patient affected by hydrocephalus with
Hirschsprung disease).
{ECO:0000269|PubMed:9521424,
ECO:0000269|PubMed:9832035}.
/FTId=VAR_003940.
VARIANT 714 714 P -> S (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078375.
VARIANT 739 739 R -> W (in dbSNP:rs142424573).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030417.
VARIANT 741 741 M -> T (in HSAS).
{ECO:0000269|PubMed:9268105}.
/FTId=VAR_030418.
VARIANT 751 751 R -> P (in HSAS).
{ECO:0000269|PubMed:10797421}.
/FTId=VAR_030419.
VARIANT 752 752 V -> M (in HSAS and MASA; also found in a
patient with the diagnosis of L1
syndrome; also in a patient with
hydrocephalus and Hirschsprung disease;
dbSNP:rs137852525).
{ECO:0000269|PubMed:11857550,
ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:9268105}.
/FTId=VAR_014421.
VARIANT 754 754 W -> R (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078376.
VARIANT 760 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078377.
VARIANT 768 768 V -> F (in HSAS).
{ECO:0000269|PubMed:7762552}.
/FTId=VAR_003941.
VARIANT 768 768 V -> I (decreased cell-cell adhesion; no
effect on subcellular localization; no
effect on neurite outgrowth;
dbSNP:rs36021462).
{ECO:0000269|PubMed:22222883,
ECO:0000269|PubMed:9268105}.
/FTId=VAR_030420.
VARIANT 770 770 D -> N (in MASA; associated with callosal
agenesis; dbSNP:rs148516831).
{ECO:0000269|PubMed:16816908}.
/FTId=VAR_027514.
VARIANT 784 784 Y -> C (in HSAS; dbSNP:rs797045674).
{ECO:0000269|PubMed:9195224}.
/FTId=VAR_003942.
VARIANT 789 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429,
ECO:0000269|PubMed:26891472}.
/FTId=VAR_078378.
VARIANT 811 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078379.
VARIANT 891 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078380.
VARIANT 901 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078381.
VARIANT 935 935 L -> P (in HSAS).
{ECO:0000269|PubMed:9521424}.
/FTId=VAR_003943.
VARIANT 936 948 Missing (in HSAS).
{ECO:0000269|PubMed:9195224}.
/FTId=VAR_003944.
VARIANT 941 941 P -> L (in HSAS and MASA; decrease in
neurite outgrowth, when assayed in NGF-
treated pheochromocytoma PC12 cells;
decrease in cell-matrix adhesion;
decreased cell migration; no effect on
the localization at the cell surface; no
effect on cell proliferation, when
transfected in pheochromocytoma PC12
cells). {ECO:0000269|PubMed:22973895,
ECO:0000269|PubMed:7762552}.
/FTId=VAR_003945.
VARIANT 958 958 L -> V (in dbSNP:rs35902890).
/FTId=VAR_059413.
VARIANT 1036 1036 W -> L (in HSAS; partial loss of
localization at the cell surface;
retention in the endoplasmic reticulum;
in neurons, partial loss of localization
to axons, but enriched on proximal
dendrites).
{ECO:0000269|PubMed:20621658}.
/FTId=VAR_078382.
VARIANT 1064 1257 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078383.
VARIANT 1070 1070 Y -> C (in HSAS; partial loss of axon
guidance and loss of proper synapse
formation, when assayed in a heterologous
system). {ECO:0000269|PubMed:24155914,
ECO:0000269|PubMed:7762552}.
/FTId=VAR_003946.
VARIANT 1071 1071 Missing (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078384.
VARIANT 1080 1080 L -> Q (probable disease-associated
mutation found in L1 syndrome).
{ECO:0000269|PubMed:19846429}.
/FTId=VAR_078385.
VARIANT 1194 1194 S -> L (in HSAS and MASA;
dbSNP:rs137852522).
{ECO:0000269|PubMed:7881431,
ECO:0000269|PubMed:8556302}.
/FTId=VAR_003947.
VARIANT 1224 1224 S -> L (in HSAS).
{ECO:0000269|PubMed:9744477}.
/FTId=VAR_003948.
VARIANT 1239 1239 G -> E. {ECO:0000269|PubMed:10797421}.
/FTId=VAR_030421.
MUTAGEN 1147 1153 KGGKYSV->AGGAASA: Loss of axon guidance,
when assayed in a heterologous system,
but normal synapse formation.
{ECO:0000269|PubMed:24155914}.
CONFLICT 4 4 A -> V (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 216 216 T -> I (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 250 250 S -> T (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 276 277 WL -> SV (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 288 288 V -> A (in Ref. 6; ABP88252).
{ECO:0000305}.
CONFLICT 357 357 Q -> E (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 515 515 K -> T (in Ref. 6; ABP88252).
{ECO:0000305}.
CONFLICT 626 626 L -> V (in Ref. 1; CAA42508).
{ECO:0000305}.
CONFLICT 660 660 E -> G (in Ref. 6; ABP88252).
{ECO:0000305}.
CONFLICT 936 936 L -> V (in Ref. 12; CAB37831).
{ECO:0000305}.
CONFLICT 1116 1117 GF -> WLC (in Ref. 13; no nucleotide
entry). {ECO:0000305}.
CONFLICT 1164 1164 E -> V (in Ref. 6; ABP88252).
{ECO:0000305}.
SEQUENCE 1257 AA; 140003 MW; 5EDD764DA86C0E63 CRC64;
MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT DDISLKCEAS
GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN NSNFAQRFQG IYRCFASNKL
GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE GESVVLPCNP PPSAEPLRIY WMNSKILHIK
QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP
RLLFPTNSSS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL
KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA RLDCQVQGRP
QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM VTQCEARNRH GLLLANAYIY
VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA FGAPVPSVQW LDEDGTTVLQ DERFFPYANG
TLGIRDLQAN DTGRYFCLAA NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ
ASFDPSLQPS ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV
ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI EFEDKEMAPE
KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP SPVSETVVTP EAAPEKNPVD
VKGEGNETTN MVITWKPLRW MDWNAPQVQY RVQWRPQGTR GPWQEQIVSD PFLVVSNTST
FVPYEIKVQA VNSQGKGPEP QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ
VKGHLRGYNV TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG
RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG YVLSYHPLDE
GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG PGEAIVREGG TMALSGISDF
GNISATAGEN YSVVSWVPKE GQCNFRFHIL FKALGEEKGG ASLSPQYVSY NQSSYTQWDL
QPDTDYEIHL FKERMFRHQM AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL
CFIKRSKGGK YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK
PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI NPAVALE


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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