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P32004 (L1CAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural cell adhesion molecule L1

Short name=N-CAM-L1
Short name=NCAM-L1
Alternative name(s):
CD_antigen=CD171
Gene names
Name:L1CAM
Synonyms:CAML1, MIC5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Involvement in 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.
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 (Ref.45). Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.37 Ref.39 Ref.41 Ref.42 Ref.45

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.32 Ref.33 Ref.36 Ref.38 Ref.40 Ref.41 Ref.44 Ref.45

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. Ref.41 Ref.45

Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease-associated genes to cause intestinal aganglionosis. Ref.41 Ref.45

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41 Ref.43 Ref.45

Sequence similarities

Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family.

Contains 5 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
Neurogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary spastic paraplegia
Hirschsprung disease
Mental retardation
Neurodegeneration
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Non-traceable author statement Ref.24. Source: ProtInc

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

chemotaxis

Traceable author statement PubMed 19909241. Source: BHF-UCL

heterophilic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

homophilic cell adhesion

Inferred from electronic annotation. Source: Ensembl

homotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

leukocyte cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

nervous system development

Traceable author statement Ref.2. Source: ProtInc

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionsialic acid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32004-1)

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.
Isoform 2 (identifier: P32004-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1177-1180: Missing.
Note: Contains a phosphoserine at position 1177.
Isoform 3 (identifier: P32004-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.10
Chain20 – 12571238Neural cell adhesion molecule L1
PRO_0000015022

Regions

Topological domain20 – 11201101Extracellular Potential
Transmembrane1121 – 114323Helical; Potential
Topological domain1144 – 1257114Cytoplasmic Potential
Domain35 – 12591Ig-like C2-type 1
Domain139 – 22688Ig-like C2-type 2
Domain240 – 32889Ig-like C2-type 3
Domain333 – 42088Ig-like C2-type 4
Domain425 – 50783Ig-like C2-type 5
Domain518 – 60790Ig-like C2-type 6
Domain615 – 71298Fibronectin type-III 1
Domain717 – 81094Fibronectin type-III 2
Domain814 – 916103Fibronectin type-III 3
Domain920 – 101596Fibronectin type-III 4
Domain1016 – 1115100Fibronectin type-III 5
Motif554 – 5563Cell attachment site Potential

Amino acid modifications

Modified residue11631Phosphoserine Ref.16
Modified residue11811Phosphoserine; by CaMK2 Ref.14
Modified residue11941Phosphoserine Ref.19
Modified residue12481Phosphoserine Ref.17
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation6711N-linked (GlcNAc...) Ref.15 Ref.18
Glycosylation7261N-linked (GlcNAc...) Potential
Glycosylation7771N-linked (GlcNAc...) Potential
Glycosylation8251N-linked (GlcNAc...) Potential
Glycosylation8491N-linked (GlcNAc...) Potential
Glycosylation8761N-linked (GlcNAc...) Potential
Glycosylation9791N-linked (GlcNAc...) Potential
Glycosylation10221N-linked (GlcNAc...) Potential
Glycosylation10301N-linked (GlcNAc...) Potential
Glycosylation10711N-linked (GlcNAc...) Potential
Glycosylation11051N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 114 By similarity
Disulfide bond158 ↔ 209 By similarity
Disulfide bond264 ↔ 312 By similarity
Disulfide bond354 ↔ 404 By similarity
Disulfide bond448 ↔ 497 By similarity
Disulfide bond539 ↔ 591 By similarity

Natural variations

Alternative sequence26 – 316YEGHHV → L in isoform 3.
VSP_046317
Alternative sequence1177 – 11804Missing in isoform 2 and isoform 3.
VSP_002591
Natural variant91W → S in HSAS. Ref.26
VAR_003921
Natural variant301H → N. Ref.39
VAR_030403
Natural variant1211G → S in HSAS. Ref.26
VAR_003922
Natural variant1791I → S in HSAS, MASA and SPG1. Ref.29
VAR_003923
Natural variant1841R → Q in HSAS; severe. Ref.24 Ref.27 Ref.34
VAR_003924
Natural variant1841R → W in HSAS. Ref.39
VAR_030404
Natural variant1941Y → C in HSAS. Ref.31
VAR_003925
Natural variant2021D → Y in MASA. Ref.40
VAR_030405
Natural variant2101H → Q in MASA. Ref.24 Ref.25 Ref.27
Corresponds to variant rs28933683 [ dbSNP | Ensembl ].
VAR_003926
Natural variant2191I → T in HSAS. Ref.37
VAR_003927
Natural variant2401P → L in HSAS and ACCPX. Ref.31 Ref.43
VAR_003928
Natural variant2641C → Y in HSAS; severe. Ref.22 Ref.27
VAR_003929
Natural variant2681G → D in MASA. Ref.33
VAR_030406
Natural variant3091E → K in MASA. Ref.26
VAR_003930
Natural variant3351W → C in HSAS. Ref.39
VAR_030407
Natural variant3351W → R in HSAS and MASA; also in a patient with hydrocephalus and Hirschsprung disease. Ref.37
VAR_003931
Natural variant3701G → R in HSAS, MASA and SPG1. Ref.29 Ref.39
VAR_003932
Natural variant3861R → C in HSAS. Ref.37
VAR_003933
Natural variant4081N → I in HSAS. Ref.39
VAR_030408
Natural variant4151A → P in HSAS. Ref.42
VAR_027512
Natural variant4211V → D in HSAS. Ref.39
VAR_030409
Natural variant4261A → D in MASA. Ref.33
VAR_030410
Natural variant439 – 4435Missing in HSAS.
VAR_003934
Natural variant4521G → R in HSAS; severe. Ref.24 Ref.27
VAR_003935
Natural variant4731R → C in HSAS and MASA. Ref.37
VAR_003936
Natural variant4821L → P in MASA. Ref.32
VAR_030411
Natural variant4971C → Y in HSAS. Ref.39
VAR_030412
Natural variant5261Missing in HSAS. Ref.32
VAR_030413
Natural variant5421S → P in HSAS. Ref.32
VAR_030414
Natural variant5981D → N in MASA. Ref.25 Ref.27
VAR_003937
Natural variant6321R → P in MASA. Ref.36
VAR_003938
Natural variant6551K → E in HSAS. Ref.30
VAR_030415
Natural variant6741S → C in MASA; associated with callosal agenesis. Ref.38
VAR_027513
Natural variant6911A → D in MASA; associated with callosal agenesis. Ref.35 Ref.38
VAR_003939
Natural variant6911A → T in HSAS. Ref.39
VAR_030416
Natural variant6981G → R in HSAS and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease. Ref.35 Ref.38 Ref.45
VAR_003940
Natural variant7391R → W. Ref.39
VAR_030417
Natural variant7411M → T in HSAS. Ref.32
VAR_030418
Natural variant7511R → P in HSAS. Ref.39
VAR_030419
Natural variant7521V → M in MASA; also in a patient with hydrocephalus and Hirschsprung disease. Ref.32 Ref.41
VAR_014421
Natural variant7681V → F in HSAS. Ref.26
VAR_003941
Natural variant7681V → I. Ref.32
Corresponds to variant rs36021462 [ dbSNP | Ensembl ].
VAR_030420
Natural variant7701D → N in MASA; associated with callosal agenesis. Ref.44
VAR_027514
Natural variant7841Y → C in HSAS. Ref.34
VAR_003942
Natural variant9351L → P in HSAS. Ref.35
VAR_003943
Natural variant936 – 94813Missing in HSAS.
VAR_003944
Natural variant9411P → L in HSAS and MASA. Ref.26
VAR_003945
Natural variant9581L → V.
Corresponds to variant rs35902890 [ dbSNP | Ensembl ].
VAR_059413
Natural variant10701Y → C in HSAS. Ref.26
VAR_003946
Natural variant11941S → L in HSAS and MASA. Ref.23 Ref.27
VAR_003947
Natural variant12241S → L in HSAS. Ref.37
VAR_003948
Natural variant12391G → E. Ref.39
VAR_030421

Experimental info

Sequence conflict41A → V in CAA42508. Ref.1
Sequence conflict2161T → I in CAA42508. Ref.1
Sequence conflict2501S → T in CAA42508. Ref.1
Sequence conflict276 – 2772WL → SV in CAA42508. Ref.1
Sequence conflict2881V → A in ABP88252. Ref.6
Sequence conflict3571Q → E in CAA42508. Ref.1
Sequence conflict5151K → T in ABP88252. Ref.6
Sequence conflict6261L → V in CAA42508. Ref.1
Sequence conflict6601E → G in ABP88252. Ref.6
Sequence conflict9361L → V in CAB37831. Ref.12
Sequence conflict1116 – 11172GF → WLC no nucleotide entry Ref.13
Sequence conflict11641E → V in ABP88252. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 5EDD764DA86C0E63

FASTA1,257140,003
        10         20         30         40         50         60 
MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT DDISLKCEAS 

        70         80         90        100        110        120 
GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN NSNFAQRFQG IYRCFASNKL 

       130        140        150        160        170        180 
GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE GESVVLPCNP PPSAEPLRIY WMNSKILHIK 

       190        200        210        220        230        240 
QDERVTMGQN GNLYFANVLT SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP 

       250        260        270        280        290        300 
RLLFPTNSSS HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL 

       310        320        330        340        350        360 
KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA RLDCQVQGRP 

       370        380        390        400        410        420 
QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM VTQCEARNRH GLLLANAYIY 

       430        440        450        460        470        480 
VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA FGAPVPSVQW LDEDGTTVLQ DERFFPYANG 

       490        500        510        520        530        540 
TLGIRDLQAN DTGRYFCLAA NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ 

       550        560        570        580        590        600 
ASFDPSLQPS ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV 

       610        620        630        640        650        660 
ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI EFEDKEMAPE 

       670        680        690        700        710        720 
KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP SPVSETVVTP EAAPEKNPVD 

       730        740        750        760        770        780 
VKGEGNETTN MVITWKPLRW MDWNAPQVQY RVQWRPQGTR GPWQEQIVSD PFLVVSNTST 

       790        800        810        820        830        840 
FVPYEIKVQA VNSQGKGPEP QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ 

       850        860        870        880        890        900 
VKGHLRGYNV TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG 

       910        920        930        940        950        960 
RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG YVLSYHPLDE 

       970        980        990       1000       1010       1020 
GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG PGEAIVREGG TMALSGISDF 

      1030       1040       1050       1060       1070       1080 
GNISATAGEN YSVVSWVPKE GQCNFRFHIL FKALGEEKGG ASLSPQYVSY NQSSYTQWDL 

      1090       1100       1110       1120       1130       1140 
QPDTDYEIHL FKERMFRHQM AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL 

      1150       1160       1170       1180       1190       1200 
CFIKRSKGGK YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK 

      1210       1220       1230       1240       1250 
PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI NPAVALE 

« Hide

Isoform 2 [UniParc].

Checksum: 23AD19B26C8C9971
Show »

FASTA1,253139,517
Isoform 3 [UniParc].

Checksum: F5954FD80954368B
Show »

FASTA1,248138,908

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"MASA syndrome is due to mutations in the neural cell adhesion gene L1CAM."
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.
Nat. Genet. 7:408-413(1994) [PubMed] [Europe PMC] [Abstract]
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]"Nine novel L1 CAM mutations in families with X-linked hydrocephalus."
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.
Hum. Mutat. 9:512-518(1997) [PubMed] [Europe PMC] [Abstract]
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]"Identification of novel L1CAM mutations using fluorescence-assisted mismatch analysis."
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.
Hum. Mutat. 12:259-266(1998) [PubMed] [Europe PMC] [Abstract]
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]"Expanding the phenotypic spectrum of L1CAM-associated disease."
Basel-Vanagaite L., Straussberg R., Friez M.J., Inbar D., Korenreich L., Shohat M., Schwartz C.E.
Clin. Genet. 69:414-419(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14733.1. [P32004-1]
CCDS14734.1. [P32004-2]
CCDS48192.1. [P32004-3]
PIRA41060.
RefSeqNP_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]
UniGeneHs.522818.

3D structure databases

DisProtDP00666.
ProteinModelPortalP32004.
SMRP32004. Positions 31-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110094. 15 interactions.
IntActP32004. 4 interactions.
MINTMINT-1369985.
STRING9606.ENSP00000359074.

PTM databases

PhosphoSiteP32004.

Polymorphism databases

DMDM1705571.

Proteomic databases

MaxQBP32004.
PaxDbP32004.
PRIDEP32004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361699; ENSP00000355380; ENSG00000198910. [P32004-2]
ENST00000361981; ENSP00000354712; ENSG00000198910. [P32004-3]
ENST00000370055; ENSP00000359072; ENSG00000198910. [P32004-3]
ENST00000370057; ENSP00000359074; ENSG00000198910. [P32004-1]
ENST00000370060; ENSP00000359077; ENSG00000198910. [P32004-1]
ENST00000593479; ENSP00000470850; ENSG00000267951. [P32004-1]
ENST00000594481; ENSP00000469550; ENSG00000267951. [P32004-3]
ENST00000595648; ENSP00000468824; ENSG00000267951. [P32004-3]
ENST00000598793; ENSP00000472482; ENSG00000267951. [P32004-2]
ENST00000599241; ENSP00000472713; ENSG00000267951. [P32004-1]
GeneID3897.
KEGGhsa:3897.
UCSCuc004fjb.4. human. [P32004-1]
uc004fjc.4. human. [P32004-2]
uc010nuo.4. human.

Organism-specific databases

CTD3897.
GeneCardsGC0XM153126.
GeneReviewsL1CAM.
HGNCHGNC:6470. L1CAM.
HPACAB010896.
HPA005830.
MIM303350. phenotype.
304100. phenotype.
307000. phenotype.
308840. gene.
neXtProtNX_P32004.
Orphanet388. 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.
PharmGKBPA30259.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293951.
HOGENOMHOG000231380.
HOVERGENHBG000144.
KOK06550.
PhylomeDBP32004.
TreeFamTF351098.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP32004.
BgeeP32004.
CleanExHS_L1CAM.
GenevestigatorP32004.

Family and domain databases

Gene3D2.60.40.10. 11 hits.
InterProIPR003961. 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]
PfamPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 4 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 5 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSL1CAM. human.
GeneWikiL1_(protein).
GenomeRNAi3897.
NextBio15299.
PMAP-CutDBP32004.
PROP32004.
SOURCESearch...

Entry information

Entry nameL1CAM_HUMAN
AccessionPrimary (citable) accession number: P32004
Secondary accession number(s): A0AV65 expand/collapse secondary AC list , A4ZYW4, B2RMU7, G3XAF4, Q8TA87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries