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P32004

- L1CAM_HUMAN

UniProt

P32004 - L1CAM_HUMAN

Protein

Neural cell adhesion molecule L1

Gene

L1CAM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Cell adhesion molecule with an important role in the development of the nervous system. Involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. Binds to axonin on neurons.

    GO - Molecular functioni

    1. sialic acid binding Source: Ensembl

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. blood coagulation Source: Reactome
    3. cell adhesion Source: ProtInc
    4. cell-cell adhesion mediated by integrin Source: Ensembl
    5. cell death Source: UniProtKB-KW
    6. cell surface receptor signaling pathway Source: Ensembl
    7. chemotaxis Source: BHF-UCL
    8. heterophilic cell-cell adhesion Source: Ensembl
    9. homophilic cell adhesion Source: Ensembl
    10. homotypic cell-cell adhesion Source: Ensembl
    11. leukocyte cell-cell adhesion Source: Ensembl
    12. leukocyte migration Source: Reactome
    13. nervous system development Source: ProtInc
    14. positive regulation of calcium-mediated signaling Source: Ensembl
    15. positive regulation of cell-cell adhesion Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cell adhesion, Differentiation, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_12560. Basigin interactions.
    REACT_22205. L1CAM interactions.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_22272. Signal transduction by L1.
    REACT_22365. Recycling pathway of L1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neural cell adhesion molecule L1
    Short name:
    N-CAM-L1
    Short name:
    NCAM-L1
    Alternative name(s):
    CD_antigen: CD171
    Gene namesi
    Name:L1CAM
    Synonyms:CAML1, MIC5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6470. L1CAM.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome
    4. presynaptic membrane Source: Ensembl
    5. terminal bouton Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.14 Publications
    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).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91W → S in HSAS. 1 Publication
    VAR_003921
    Natural varianti121 – 1211G → S in HSAS. 1 Publication
    VAR_003922
    Natural varianti179 – 1791I → S in HSAS, MASA and SPG1. 1 Publication
    VAR_003923
    Natural varianti184 – 1841R → Q in HSAS; severe. 3 Publications
    VAR_003924
    Natural varianti184 – 1841R → W in HSAS. 1 Publication
    VAR_030404
    Natural varianti194 – 1941Y → C in HSAS. 1 Publication
    VAR_003925
    Natural varianti219 – 2191I → T in HSAS. 1 Publication
    VAR_003927
    Natural varianti240 – 2401P → L in HSAS and ACCPX. 2 Publications
    VAR_003928
    Natural varianti264 – 2641C → Y in HSAS; severe. 2 Publications
    VAR_003929
    Natural varianti335 – 3351W → C in HSAS. 1 Publication
    VAR_030407
    Natural varianti335 – 3351W → R in HSAS and MASA; also in a patient with hydrocephalus and Hirschsprung disease. 1 Publication
    VAR_003931
    Natural varianti370 – 3701G → R in HSAS, MASA and SPG1. 2 Publications
    VAR_003932
    Natural varianti386 – 3861R → C in HSAS. 1 Publication
    VAR_003933
    Natural varianti408 – 4081N → I in HSAS. 1 Publication
    VAR_030408
    Natural varianti415 – 4151A → P in HSAS. 1 Publication
    VAR_027512
    Natural varianti421 – 4211V → D in HSAS. 1 Publication
    VAR_030409
    Natural varianti439 – 4435Missing in HSAS.
    VAR_003934
    Natural varianti452 – 4521G → R in HSAS; severe. 2 Publications
    VAR_003935
    Natural varianti473 – 4731R → C in HSAS and MASA. 1 Publication
    VAR_003936
    Natural varianti497 – 4971C → Y in HSAS. 1 Publication
    VAR_030412
    Natural varianti526 – 5261Missing in HSAS. 1 Publication
    VAR_030413
    Natural varianti542 – 5421S → P in HSAS. 1 Publication
    VAR_030414
    Natural varianti655 – 6551K → E in HSAS. 1 Publication
    VAR_030415
    Natural varianti691 – 6911A → T in HSAS. 1 Publication
    VAR_030416
    Natural varianti698 – 6981G → R in HSAS and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease. 2 Publications
    VAR_003940
    Natural varianti741 – 7411M → T in HSAS. 1 Publication
    VAR_030418
    Natural varianti751 – 7511R → P in HSAS. 1 Publication
    VAR_030419
    Natural varianti768 – 7681V → F in HSAS. 1 Publication
    VAR_003941
    Natural varianti784 – 7841Y → C in HSAS. 1 Publication
    VAR_003942
    Natural varianti935 – 9351L → P in HSAS. 1 Publication
    VAR_003943
    Natural varianti936 – 94813Missing in HSAS.
    VAR_003944Add
    BLAST
    Natural varianti941 – 9411P → L in HSAS and MASA. 1 Publication
    VAR_003945
    Natural varianti1070 – 10701Y → C in HSAS. 1 Publication
    VAR_003946
    Natural varianti1194 – 11941S → L in HSAS and MASA. 2 Publications
    VAR_003947
    Natural varianti1224 – 12241S → L in HSAS. 1 Publication
    VAR_003948
    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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791I → S in HSAS, MASA and SPG1. 1 Publication
    VAR_003923
    Natural varianti202 – 2021D → Y in MASA. 1 Publication
    VAR_030405
    Natural varianti210 – 2101H → Q in MASA. 3 Publications
    Corresponds to variant rs28933683 [ dbSNP | Ensembl ].
    VAR_003926
    Natural varianti268 – 2681G → D in MASA. 1 Publication
    VAR_030406
    Natural varianti309 – 3091E → K in MASA. 1 Publication
    VAR_003930
    Natural varianti335 – 3351W → R in HSAS and MASA; also in a patient with hydrocephalus and Hirschsprung disease. 1 Publication
    VAR_003931
    Natural varianti370 – 3701G → R in HSAS, MASA and SPG1. 2 Publications
    VAR_003932
    Natural varianti426 – 4261A → D in MASA. 1 Publication
    VAR_030410
    Natural varianti473 – 4731R → C in HSAS and MASA. 1 Publication
    VAR_003936
    Natural varianti482 – 4821L → P in MASA. 1 Publication
    VAR_030411
    Natural varianti598 – 5981D → N in MASA. 2 Publications
    VAR_003937
    Natural varianti632 – 6321R → P in MASA. 1 Publication
    VAR_003938
    Natural varianti674 – 6741S → C in MASA; associated with callosal agenesis. 1 Publication
    VAR_027513
    Natural varianti691 – 6911A → D in MASA; associated with callosal agenesis. 2 Publications
    VAR_003939
    Natural varianti698 – 6981G → R in HSAS and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease. 2 Publications
    VAR_003940
    Natural varianti752 – 7521V → M in MASA; also in a patient with hydrocephalus and Hirschsprung disease. 2 Publications
    VAR_014421
    Natural varianti770 – 7701D → N in MASA; associated with callosal agenesis. 1 Publication
    VAR_027514
    Natural varianti941 – 9411P → L in HSAS and MASA. 1 Publication
    VAR_003945
    Natural varianti1194 – 11941S → L in HSAS and MASA. 2 Publications
    VAR_003947
    Spastic paraplegia 1, X-linked (SPG1) [MIM:303350]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791I → S in HSAS, MASA and SPG1. 1 Publication
    VAR_003923
    Natural varianti370 – 3701G → R in HSAS, MASA and SPG1. 2 Publications
    VAR_003932
    Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease-associated genes to cause intestinal aganglionosis.1 Publication
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401P → L in HSAS and ACCPX. 2 Publications
    VAR_003928

    Keywords - Diseasei

    Disease mutation, Hereditary spastic paraplegia, Hirschsprung disease, Mental retardation, Neurodegeneration

    Organism-specific databases

    MIMi303350. phenotype.
    304100. phenotype.
    307000. phenotype.
    Orphaneti388. Hirschsprung disease.
    2182. Hydrocephalus with stenosis of aqueduct of Sylvius.
    2466. MASA syndrome.
    1497. X-linked complicated corpus callosum dysgenesis.
    306617. X-linked complicated spastic paraplegia type 1.
    PharmGKBiPA30259.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 12571238Neural cell adhesion molecule L1PRO_0000015022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi57 ↔ 114PROSITE-ProRule annotation
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi158 ↔ 209PROSITE-ProRule annotation
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi264 ↔ 312PROSITE-ProRule annotation
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi354 ↔ 404PROSITE-ProRule annotation
    Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi448 ↔ 497PROSITE-ProRule annotation
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi539 ↔ 591PROSITE-ProRule annotation
    Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi671 – 6711N-linked (GlcNAc...)2 Publications
    Glycosylationi726 – 7261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi777 – 7771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi825 – 8251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi849 – 8491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi876 – 8761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi979 – 9791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1030 – 10301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1071 – 10711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1105 – 11051N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1163 – 11631Phosphoserine1 Publication
    Modified residuei1181 – 11811Phosphoserine; by CaMK21 Publication
    Modified residuei1194 – 11941Phosphoserine1 Publication
    Modified residuei1248 – 12481Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP32004.
    PaxDbiP32004.
    PRIDEiP32004.

    PTM databases

    PhosphoSiteiP32004.

    Miscellaneous databases

    PMAP-CutDBP32004.

    Expressioni

    Gene expression databases

    ArrayExpressiP32004.
    BgeeiP32004.
    CleanExiHS_L1CAM.
    GenevestigatoriP32004.

    Organism-specific databases

    HPAiCAB010896.
    HPA005830.

    Interactioni

    Protein-protein interaction databases

    BioGridi110094. 15 interactions.
    IntActiP32004. 4 interactions.
    MINTiMINT-1369985.
    STRINGi9606.ENSP00000359074.

    Structurei

    3D structure databases

    DisProtiDP00666.
    ProteinModelPortaliP32004.
    SMRiP32004. Positions 31-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 11201101ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1144 – 1257114CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1121 – 114323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 12591Ig-like C2-type 1Add
    BLAST
    Domaini139 – 22688Ig-like C2-type 2Add
    BLAST
    Domaini240 – 32889Ig-like C2-type 3Add
    BLAST
    Domaini333 – 42088Ig-like C2-type 4Add
    BLAST
    Domaini425 – 50783Ig-like C2-type 5Add
    BLAST
    Domaini518 – 60790Ig-like C2-type 6Add
    BLAST
    Domaini615 – 71298Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini717 – 81094Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini814 – 916103Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini920 – 101596Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1016 – 1115100Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi554 – 5563Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 5 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG293951.
    HOGENOMiHOG000231380.
    HOVERGENiHBG000144.
    KOiK06550.
    PhylomeDBiP32004.
    TreeFamiTF351098.

    Family and domain databases

    Gene3Di2.60.40.10. 11 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR026966. Neurofascin/L1/NrCAM_C.
    [Graphical view]
    PfamiPF13882. Bravo_FIGEY. 1 hit.
    PF00041. fn3. 4 hits.
    PF07679. I-set. 4 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 4 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 5 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    PROSITEiPS50853. FN3. 5 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P32004-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT     50
    DDISLKCEAS GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN 100
    NSNFAQRFQG IYRCFASNKL GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE 150
    GESVVLPCNP PPSAEPLRIY WMNSKILHIK QDERVTMGQN GNLYFANVLT 200
    SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP RLLFPTNSSS 250
    HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL 300
    KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA 350
    RLDCQVQGRP QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM 400
    VTQCEARNRH GLLLANAYIY VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA 450
    FGAPVPSVQW LDEDGTTVLQ DERFFPYANG TLGIRDLQAN DTGRYFCLAA 500
    NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ ASFDPSLQPS 550
    ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV 600
    ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI 650
    EFEDKEMAPE KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP 700
    SPVSETVVTP EAAPEKNPVD VKGEGNETTN MVITWKPLRW MDWNAPQVQY 750
    RVQWRPQGTR GPWQEQIVSD PFLVVSNTST FVPYEIKVQA VNSQGKGPEP 800
    QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ VKGHLRGYNV 850
    TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG 900
    RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG 950
    YVLSYHPLDE GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG 1000
    PGEAIVREGG TMALSGISDF GNISATAGEN YSVVSWVPKE GQCNFRFHIL 1050
    FKALGEEKGG ASLSPQYVSY NQSSYTQWDL QPDTDYEIHL FKERMFRHQM 1100
    AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL CFIKRSKGGK 1150
    YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK 1200
    PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI 1250
    NPAVALE 1257
    Length:1,257
    Mass (Da):140,003
    Last modified:October 1, 1996 - v2
    Checksum:i5EDD764DA86C0E63
    GO
    Isoform 2 (identifier: P32004-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1177-1180: Missing.

    Note: Contains a phosphoserine at position 1177.

    Show »
    Length:1,253
    Mass (Da):139,517
    Checksum:i23AD19B26C8C9971
    GO
    Isoform 3 (identifier: P32004-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-31: YEGHHV → L
         1177-1180: Missing.

    Note: Contains a phosphoserine at position 1172.

    Show »
    Length:1,248
    Mass (Da):138,908
    Checksum:iF5954FD80954368B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41A → V in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti216 – 2161T → I in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti250 – 2501S → T in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti276 – 2772WL → SV in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti288 – 2881V → A in ABP88252. 1 PublicationCurated
    Sequence conflicti357 – 3571Q → E in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti515 – 5151K → T in ABP88252. 1 PublicationCurated
    Sequence conflicti626 – 6261L → V in CAA42508. (PubMed:1932117)Curated
    Sequence conflicti660 – 6601E → G in ABP88252. 1 PublicationCurated
    Sequence conflicti936 – 9361L → V in CAB37831. (PubMed:1923824)Curated
    Sequence conflicti1116 – 11172GF → WLC no nucleotide entry (PubMed:1993895)Curated
    Sequence conflicti1164 – 11641E → V in ABP88252. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91W → S in HSAS. 1 Publication
    VAR_003921
    Natural varianti30 – 301H → N.1 Publication
    VAR_030403
    Natural varianti121 – 1211G → S in HSAS. 1 Publication
    VAR_003922
    Natural varianti179 – 1791I → S in HSAS, MASA and SPG1. 1 Publication
    VAR_003923
    Natural varianti184 – 1841R → Q in HSAS; severe. 3 Publications
    VAR_003924
    Natural varianti184 – 1841R → W in HSAS. 1 Publication
    VAR_030404
    Natural varianti194 – 1941Y → C in HSAS. 1 Publication
    VAR_003925
    Natural varianti202 – 2021D → Y in MASA. 1 Publication
    VAR_030405
    Natural varianti210 – 2101H → Q in MASA. 3 Publications
    Corresponds to variant rs28933683 [ dbSNP | Ensembl ].
    VAR_003926
    Natural varianti219 – 2191I → T in HSAS. 1 Publication
    VAR_003927
    Natural varianti240 – 2401P → L in HSAS and ACCPX. 2 Publications
    VAR_003928
    Natural varianti264 – 2641C → Y in HSAS; severe. 2 Publications
    VAR_003929
    Natural varianti268 – 2681G → D in MASA. 1 Publication
    VAR_030406
    Natural varianti309 – 3091E → K in MASA. 1 Publication
    VAR_003930
    Natural varianti335 – 3351W → C in HSAS. 1 Publication
    VAR_030407
    Natural varianti335 – 3351W → R in HSAS and MASA; also in a patient with hydrocephalus and Hirschsprung disease. 1 Publication
    VAR_003931
    Natural varianti370 – 3701G → R in HSAS, MASA and SPG1. 2 Publications
    VAR_003932
    Natural varianti386 – 3861R → C in HSAS. 1 Publication
    VAR_003933
    Natural varianti408 – 4081N → I in HSAS. 1 Publication
    VAR_030408
    Natural varianti415 – 4151A → P in HSAS. 1 Publication
    VAR_027512
    Natural varianti421 – 4211V → D in HSAS. 1 Publication
    VAR_030409
    Natural varianti426 – 4261A → D in MASA. 1 Publication
    VAR_030410
    Natural varianti439 – 4435Missing in HSAS.
    VAR_003934
    Natural varianti452 – 4521G → R in HSAS; severe. 2 Publications
    VAR_003935
    Natural varianti473 – 4731R → C in HSAS and MASA. 1 Publication
    VAR_003936
    Natural varianti482 – 4821L → P in MASA. 1 Publication
    VAR_030411
    Natural varianti497 – 4971C → Y in HSAS. 1 Publication
    VAR_030412
    Natural varianti526 – 5261Missing in HSAS. 1 Publication
    VAR_030413
    Natural varianti542 – 5421S → P in HSAS. 1 Publication
    VAR_030414
    Natural varianti598 – 5981D → N in MASA. 2 Publications
    VAR_003937
    Natural varianti632 – 6321R → P in MASA. 1 Publication
    VAR_003938
    Natural varianti655 – 6551K → E in HSAS. 1 Publication
    VAR_030415
    Natural varianti674 – 6741S → C in MASA; associated with callosal agenesis. 1 Publication
    VAR_027513
    Natural varianti691 – 6911A → D in MASA; associated with callosal agenesis. 2 Publications
    VAR_003939
    Natural varianti691 – 6911A → T in HSAS. 1 Publication
    VAR_030416
    Natural varianti698 – 6981G → R in HSAS and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease. 2 Publications
    VAR_003940
    Natural varianti739 – 7391R → W.1 Publication
    VAR_030417
    Natural varianti741 – 7411M → T in HSAS. 1 Publication
    VAR_030418
    Natural varianti751 – 7511R → P in HSAS. 1 Publication
    VAR_030419
    Natural varianti752 – 7521V → M in MASA; also in a patient with hydrocephalus and Hirschsprung disease. 2 Publications
    VAR_014421
    Natural varianti768 – 7681V → F in HSAS. 1 Publication
    VAR_003941
    Natural varianti768 – 7681V → I.1 Publication
    Corresponds to variant rs36021462 [ dbSNP | Ensembl ].
    VAR_030420
    Natural varianti770 – 7701D → N in MASA; associated with callosal agenesis. 1 Publication
    VAR_027514
    Natural varianti784 – 7841Y → C in HSAS. 1 Publication
    VAR_003942
    Natural varianti935 – 9351L → P in HSAS. 1 Publication
    VAR_003943
    Natural varianti936 – 94813Missing in HSAS.
    VAR_003944Add
    BLAST
    Natural varianti941 – 9411P → L in HSAS and MASA. 1 Publication
    VAR_003945
    Natural varianti958 – 9581L → V.
    Corresponds to variant rs35902890 [ dbSNP | Ensembl ].
    VAR_059413
    Natural varianti1070 – 10701Y → C in HSAS. 1 Publication
    VAR_003946
    Natural varianti1194 – 11941S → L in HSAS and MASA. 2 Publications
    VAR_003947
    Natural varianti1224 – 12241S → L in HSAS. 1 Publication
    VAR_003948
    Natural varianti1239 – 12391G → E.1 Publication
    VAR_030421

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 316YEGHHV → L in isoform 3. 1 PublicationVSP_046317
    Alternative sequencei1177 – 11804Missing in isoform 2 and isoform 3. 2 PublicationsVSP_002591

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59847 mRNA. Translation: CAA42508.1.
    M77640 mRNA. Translation: AAC14352.1.
    M74387 mRNA. Translation: AAA59476.1.
    U52111 Genomic DNA. No translation available.
    Z29373 Genomic DNA. Translation: CAA82564.1.
    EF506611 mRNA. Translation: ABP88252.1.
    U52112 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72787.1.
    BC025843 mRNA. Translation: AAH25843.1.
    BC126229 mRNA. Translation: AAI26230.1.
    BC136447 mRNA. Translation: AAI36448.1.
    M55271 mRNA. Translation: AAA36353.1. Sequence problems.
    X58775 Genomic DNA. Translation: CAA41576.1.
    X58776 mRNA. Translation: CAB37831.1.
    CCDSiCCDS14733.1. [P32004-1]
    CCDS14734.1. [P32004-2]
    CCDS48192.1. [P32004-3]
    PIRiA41060.
    RefSeqiNP_000416.1. NM_000425.4. [P32004-1]
    NP_001137435.1. NM_001143963.2. [P32004-3]
    NP_001265045.1. NM_001278116.1. [P32004-1]
    NP_076493.1. NM_024003.3. [P32004-2]
    UniGeneiHs.522818.

    Genome annotation databases

    EnsembliENST00000361699; ENSP00000355380; ENSG00000198910. [P32004-2]
    ENST00000361981; ENSP00000354712; ENSG00000198910. [P32004-3]
    ENST00000370055; ENSP00000359072; ENSG00000198910. [P32004-3]
    ENST00000370060; ENSP00000359077; ENSG00000198910. [P32004-1]
    GeneIDi3897.
    KEGGihsa:3897.
    UCSCiuc004fjb.4. human. [P32004-1]
    uc004fjc.4. human. [P32004-2]
    uc010nuo.4. human.

    Polymorphism databases

    DMDMi1705571.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    L1CAM

    L1CAM mutation Web Page

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59847 mRNA. Translation: CAA42508.1 .
    M77640 mRNA. Translation: AAC14352.1 .
    M74387 mRNA. Translation: AAA59476.1 .
    U52111 Genomic DNA. No translation available.
    Z29373 Genomic DNA. Translation: CAA82564.1 .
    EF506611 mRNA. Translation: ABP88252.1 .
    U52112 Genomic DNA. No translation available.
    CH471172 Genomic DNA. Translation: EAW72787.1 .
    BC025843 mRNA. Translation: AAH25843.1 .
    BC126229 mRNA. Translation: AAI26230.1 .
    BC136447 mRNA. Translation: AAI36448.1 .
    M55271 mRNA. Translation: AAA36353.1 . Sequence problems.
    X58775 Genomic DNA. Translation: CAA41576.1 .
    X58776 mRNA. Translation: CAB37831.1 .
    CCDSi CCDS14733.1. [P32004-1 ]
    CCDS14734.1. [P32004-2 ]
    CCDS48192.1. [P32004-3 ]
    PIRi A41060.
    RefSeqi NP_000416.1. NM_000425.4. [P32004-1 ]
    NP_001137435.1. NM_001143963.2. [P32004-3 ]
    NP_001265045.1. NM_001278116.1. [P32004-1 ]
    NP_076493.1. NM_024003.3. [P32004-2 ]
    UniGenei Hs.522818.

    3D structure databases

    DisProti DP00666.
    ProteinModelPortali P32004.
    SMRi P32004. Positions 31-1006.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110094. 15 interactions.
    IntActi P32004. 4 interactions.
    MINTi MINT-1369985.
    STRINGi 9606.ENSP00000359074.

    PTM databases

    PhosphoSitei P32004.

    Polymorphism databases

    DMDMi 1705571.

    Proteomic databases

    MaxQBi P32004.
    PaxDbi P32004.
    PRIDEi P32004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361699 ; ENSP00000355380 ; ENSG00000198910 . [P32004-2 ]
    ENST00000361981 ; ENSP00000354712 ; ENSG00000198910 . [P32004-3 ]
    ENST00000370055 ; ENSP00000359072 ; ENSG00000198910 . [P32004-3 ]
    ENST00000370060 ; ENSP00000359077 ; ENSG00000198910 . [P32004-1 ]
    GeneIDi 3897.
    KEGGi hsa:3897.
    UCSCi uc004fjb.4. human. [P32004-1 ]
    uc004fjc.4. human. [P32004-2 ]
    uc010nuo.4. human.

    Organism-specific databases

    CTDi 3897.
    GeneCardsi GC0XM153126.
    GeneReviewsi L1CAM.
    HGNCi HGNC:6470. L1CAM.
    HPAi CAB010896.
    HPA005830.
    MIMi 303350. phenotype.
    304100. phenotype.
    307000. phenotype.
    308840. gene.
    neXtProti NX_P32004.
    Orphaneti 388. Hirschsprung disease.
    2182. Hydrocephalus with stenosis of aqueduct of Sylvius.
    2466. MASA syndrome.
    1497. X-linked complicated corpus callosum dysgenesis.
    306617. X-linked complicated spastic paraplegia type 1.
    PharmGKBi PA30259.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293951.
    HOGENOMi HOG000231380.
    HOVERGENi HBG000144.
    KOi K06550.
    PhylomeDBi P32004.
    TreeFami TF351098.

    Enzyme and pathway databases

    Reactomei REACT_12560. Basigin interactions.
    REACT_22205. L1CAM interactions.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_22272. Signal transduction by L1.
    REACT_22365. Recycling pathway of L1.

    Miscellaneous databases

    ChiTaRSi L1CAM. human.
    GeneWikii L1_(protein).
    GenomeRNAii 3897.
    NextBioi 15299.
    PMAP-CutDB P32004.
    PROi P32004.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P32004.
    Bgeei P32004.
    CleanExi HS_L1CAM.
    Genevestigatori P32004.

    Family and domain databases

    Gene3Di 2.60.40.10. 11 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR026966. Neurofascin/L1/NrCAM_C.
    [Graphical view ]
    Pfami PF13882. Bravo_FIGEY. 1 hit.
    PF00041. fn3. 4 hits.
    PF07679. I-set. 4 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 4 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    PROSITEi PS50853. FN3. 5 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of cell adhesion molecule L1 from human nervous tissue: a comparison of the primary sequences of L1 molecules of different origin."
      Kobayashi M., Miura M., Asou H., Uyemura K.
      Biochim. Biophys. Acta 1090:238-240(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Molecular structure and functional testing of human L1CAM: an interspecies comparison."
      Hlavin M.L., Lemmon V.
      Genomics 11:416-423(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    3. "Variants of human L1 cell adhesion molecule arise through alternate splicing of RNA."
      Reid R.A., Hemperly J.J.
      J. Mol. Neurosci. 3:127-135(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "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."
      Brenner V., Nyakatura G., Rosenthal A., Platzer M.
      Genomics 44:8-14(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The neural cell adhesion molecule L1: genomic organisation and differential splicing is conserved between man and the pufferfish Fugu."
      Coutelle O., Nyakatura G., Taudien S., Elgar G., Brenner S., Platzer M., Drescher B., Jouet M., Kenwrick S., Rosenthal A.
      Gene 208:7-15(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    6. Son Y.S.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    7. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreas.
    10. "A human brain glycoprotein related to the mouse cell adhesion molecule L1."
      Wolff J.M., Frank R., Mujoo K., Spiro R.C., Reisfeld R.A., Rathjen F.G.
      J. Biol. Chem. 263:11943-11947(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-36.
    11. "The gene encoding L1, a neural adhesion molecule of the immunoglobulin family, is located on the X chromosome in mouse and man."
      Djabali M., Mattei M.-G., Nguyen C., Roux D., Demengeot J., Denizot F., Moos M., Schachner M., Goridis C., Jordan B.R.
      Genomics 7:587-593(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-371.
    12. "PCR walking from microdissection clone M54 identifies three exons from the human gene for the neural cell adhesion molecule L1 (CAM-L1)."
      Rosenthal A., Mackinnon R.N., Jones D.S.C.
      Nucleic Acids Res. 19:5395-5401(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 353-1176, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1082-1176.
      Tissue: Fetal brain.
    13. "Isolation and sequence of partial cDNA clones of human L1: homology of human and rodent L1 in the cytoplasmic region."
      Harper J.R., Prince J.T., Healy P.A., Stuart J.K., Nauman S.J., Stallcup W.B.
      J. Neurochem. 56:797-804(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1257.
    14. "Casein kinase II phosphorylates the neural cell adhesion molecule L1."
      Wong E.V., Schaefer A.W., Landreth G., Lemmon V.
      J. Neurochem. 66:779-786(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1181.
    15. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671.
      Tissue: Plasma.
    16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671.
      Tissue: Liver.
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1172 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "A missense mutation confirms the L1 defect in X-linked hydrocephalus (HSAS)."
      Jouet M., Rosenthal A., Macfarlane J., Kenwrick S., Donnai D.
      Nat. Genet. 4:331-331(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HSAS TYR-264.
    23. "X-linked hydrocephalus and MASA syndrome present in one family are due to a single missense mutation in exon 28 of the L1CAM gene."
      Fransen E., Schrander-Stumpel C., Vits L., Coucke P., van Camp G., Willems P.J.
      Hum. Mol. Genet. 3:2255-2256(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HSAS/MASA LEU-1194.
    24. "X-linked spastic paraplegia (SPG1), MASA syndrome and X-linked hydrocephalus result from mutations in the L1 gene."
      Jouet M., Rosenthal A., Armstrong G., Macfarlane J., Stevenson R., Paterson J., Metzenberg A., Ionasescu V., Temple K., Kenwrick S.
      Nat. Genet. 7:402-407(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS GLN-184 AND ARG-452, VARIANT MASA GLN-210.
    25. Cited for: VARIANTS MASA GLN-210 AND ASN-598.
    26. "New domains of neural cell-adhesion molecule L1 implicated in X-linked hydrocephalus and MASA syndrome."
      Jouet M., Moncla A., Paterson J., McKeown C., Fryer A., Carpenter N., Holmberg E., Wadelius C., Kenwrick S.
      Am. J. Hum. Genet. 56:1304-1314(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS/MASA SER-9; SER-121; LYS-309; PHE-768; LEU-941 AND CYS-1070.
    27. "CRASH syndrome: clinical spectrum of corpus callosum hypoplasia, retardation, adducted thumbs, spastic paraparesis and hydrocephalus due to mutations in one single gene, L1."
      Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.
      Eur. J. Hum. Genet. 3:273-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS/MASA GLN-184; GLN-210; TYR-264; ARG-452; ASN-598 AND LEU-1194.
    28. Erratum
      Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J.
      Eur. J. Hum. Genet. 4:126-126(1996)
    29. "Mutations in L1-CAM in two families with X linked complicated spastic paraplegia, MASA syndrome, and HSAS."
      Ruiz J.C., Cuppens H., Legius E., Fryns J.-P., Glover T., Marynen P., Cassiman J.-J.
      J. Med. Genet. 32:549-552(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS/MASA/SPG1 SER-179 AND ARG-370.
    30. "A new mutation of the L1CAM gene in an X-linked hydrocephalus family."
      Izumoto S., Yamasaki M., Arita N., Hiraga S., Ohnishi T., Fujitani K., Sakoda S., Hayakawa T.
      Childs Nerv. Syst. 12:742-747(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HSAS GLU-655.
    31. "Five novel mutations in the L1CAM gene in families with X linked hydrocephalus."
      Gu S.-M., Orth U., Veske A., Enders H., Kluender K., Schloesser M., Engel W., Schwinger E., Gal A.
      J. Med. Genet. 33:103-106(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS CYS-194 AND LEU-240.
    32. "Molecular analysis of the L1CAM gene in patients with X-linked hydrocephalus demonstrates eight novel mutations and suggests non-allelic heterogeneity of the trait."
      Gu S.-M., Orth U., Zankl M., Schroeder J., Gal A.
      Am. J. Med. Genet. 71:336-340(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MASA PRO-482, VARIANTS HSAS SER-526 DEL; PRO-542; THR-741 AND MET-752, VARIANT ILE-768.
    33. "L1-associated diseases: clinical geneticists divide, molecular geneticists unite."
      Fransen E., Van Camp G., Vits L., Willems P.J.
      Hum. Mol. Genet. 6:1625-1632(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MASA ASP-268 AND ASP-426.
    34. Cited for: VARIANTS HSAS GLN-184; 439-VAL--THR-443 DEL; CYS-784 AND 936-LEU--LEU-948 DEL.
    35. "Multiple exon screening using restriction endonuclease fingerprinting (REF): detection of six novel mutations in the L1 cell adhesion molecule (L1CAM) gene."
      Du Y.-Z., Srivastava A.K., Schwartz C.E.
      Hum. Mutat. 11:222-230(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS/MASA ASP-691; ARG-698 AND PRO-935.
    36. "Evidence for somatic and germline mosaicism in CRASH syndrome."
      Vits L., Chitayat D., van Camp G., Holden J.J.A., Fransen E., Willems P.J.
      Hum. Mutat. Suppl. 1:S284-S287(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MASA PRO-632.
    37. Cited for: VARIANTS HSAS/MASA THR-219; ARG-335; CYS-386; CYS-473 AND LEU-1224.
    38. "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."
      Michaelis R.C., Du Y.-Z., Schwartz C.E.
      J. Med. Genet. 35:901-904(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MASA CYS-674; ASP-691 AND ARG-698.
    39. "Spectrum and detection rate of L1CAM mutations in isolated and familial cases with clinically suspected L1-disease."
      Finckh U., Schroeder J., Ressler B., Veske A., Gal A.
      Am. J. Med. Genet. 92:40-46(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HSAS TRP-184; CYS-335; ARG-370; ILE-408; ASP-421; TYR-497; THR-691 AND PRO-751, VARIANTS ASN-30; TRP-739 AND GLU-1239.
    40. "Novel missense mutation in the L1 gene in a child with corpus callosum agenesis, retardation, adducted thumbs, spastic paraparesis, and hydrocephalus."
      Sztriha L., Frossard P., Hofstra R.M., Verlind E., Nork M.
      J. Child Neurol. 15:239-243(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MASA TYR-202.
    41. "Hydrocephalus and intestinal aganglionosis: is L1CAM a modifier gene in Hirschsprung disease?"
      Parisi M.A., Kapur R.P., Neilson I., Hofstra R.M.W., Holloway L.W., Michaelis R.C., Leppig K.A.
      Am. J. Med. Genet. 108:51-56(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MASA MET-752, POSSIBLE INVOLVEMENT IN HIRSCHSPRUNG DISEASE.
    42. "X-linked hydrocephalus: a novel missense mutation in the L1CAM gene."
      Sztriha L., Vos Y.J., Verlind E., Johansen J., Berg B.
      Pediatr. Neurol. 27:293-296(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HSAS PRO-415.
    43. Cited for: VARIANT ACCPX LEU-240.
    44. "A novel missense mutation in the L1CAM gene in a boy with L1 disease."
      Simonati A., Boaretto F., Vettori A., Dabrilli P., Criscuolo L., Rizzuto N., Mostacciuolo M.L.
      Neurol. Sci. 27:114-117(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MASA ASN-770.
    45. "Association of X-linked hydrocephalus and Hirschsprung disease: Report of a new patient with a mutation in the L1CAM gene."
      Fernandez R.M., Nunez-Torres R., Garcia-Diaz L., de Agustin J.C., Antinolo G., Borrego S.
      Am. J. Med. Genet. A 158:816-820(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT OF VARIANT HSAS ARG-698 IN HYDROCEPHALUS WITH HIRSCHSPRUNG DISEASE.

    Entry informationi

    Entry nameiL1CAM_HUMAN
    AccessioniPrimary (citable) accession number: P32004
    Secondary accession number(s): A0AV65
    , A4ZYW4, B2RMU7, G3XAF4, Q8TA87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 170 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3