Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P32004

- L1CAM_HUMAN

UniProt

P32004 - L1CAM_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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. cell surface Source: UniProtKB
  2. external side of plasma membrane Source: Ensembl
  3. focal adhesion Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: Reactome
  6. presynaptic membrane Source: Ensembl
  7. terminal bouton Source: Ensembl
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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 the 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

BgeeiP32004.
CleanExiHS_L1CAM.
ExpressionAtlasiP32004. baseline and differential.
GenevestigatoriP32004.

Organism-specific databases

HPAiCAB010896.
HPA005830.

Interactioni

Protein-protein interaction databases

BioGridi110094. 20 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.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000231380.
HOVERGENiHBG000144.
InParanoidiP32004.
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) [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

        10         20         30         40         50
MVVALRYVWP LLLCSPCLLI QIPEEYEGHH VMEPPVITEQ SPRRLVVFPT
60 70 80 90 100
DDISLKCEAS GKPEVQFRWT RDGVHFKPKE ELGVTVYQSP HSGSFTITGN
110 120 130 140 150
NSNFAQRFQG IYRCFASNKL GTAMSHEIRL MAEGAPKWPK ETVKPVEVEE
160 170 180 190 200
GESVVLPCNP PPSAEPLRIY WMNSKILHIK QDERVTMGQN GNLYFANVLT
210 220 230 240 250
SDNHSDYICH AHFPGTRTII QKEPIDLRVK ATNSMIDRKP RLLFPTNSSS
260 270 280 290 300
HLVALQGQPL VLECIAEGFP TPTIKWLRPS GPMPADRVTY QNHNKTLQLL
310 320 330 340 350
KVGEEDDGEY RCLAENSLGS ARHAYYVTVE AAPYWLHKPQ SHLYGPGETA
360 370 380 390 400
RLDCQVQGRP QPEVTWRING IPVEELAKDQ KYRIQRGALI LSNVQPSDTM
410 420 430 440 450
VTQCEARNRH GLLLANAYIY VVQLPAKILT ADNQTYMAVQ GSTAYLLCKA
460 470 480 490 500
FGAPVPSVQW LDEDGTTVLQ DERFFPYANG TLGIRDLQAN DTGRYFCLAA
510 520 530 540 550
NDQNNVTIMA NLKVKDATQI TQGPRSTIEK KGSRVTFTCQ ASFDPSLQPS
560 570 580 590 600
ITWRGDGRDL QELGDSDKYF IEDGRLVIHS LDYSDQGNYS CVASTELDVV
610 620 630 640 650
ESRAQLLVVG SPGPVPRLVL SDLHLLTQSQ VRVSWSPAED HNAPIEKYDI
660 670 680 690 700
EFEDKEMAPE KWYSLGKVPG NQTSTTLKLS PYVHYTFRVT AINKYGPGEP
710 720 730 740 750
SPVSETVVTP EAAPEKNPVD VKGEGNETTN MVITWKPLRW MDWNAPQVQY
760 770 780 790 800
RVQWRPQGTR GPWQEQIVSD PFLVVSNTST FVPYEIKVQA VNSQGKGPEP
810 820 830 840 850
QVTIGYSGED YPQAIPELEG IEILNSSAVL VKWRPVDLAQ VKGHLRGYNV
860 870 880 890 900
TYWREGSQRK HSKRHIHKDH VVVPANTTSV ILSGLRPYSS YHLEVQAFNG
910 920 930 940 950
RGSGPASEFT FSTPEGVPGH PEALHLECQS NTSLLLRWQP PLSHNGVLTG
960 970 980 990 1000
YVLSYHPLDE GGKGQLSFNL RDPELRTHNL TDLSPHLRYR FQLQATTKEG
1010 1020 1030 1040 1050
PGEAIVREGG TMALSGISDF GNISATAGEN YSVVSWVPKE GQCNFRFHIL
1060 1070 1080 1090 1100
FKALGEEKGG ASLSPQYVSY NQSSYTQWDL QPDTDYEIHL FKERMFRHQM
1110 1120 1130 1140 1150
AVKTNGTGRV RLPPAGFATE GWFIGFVSAI ILLLLVLLIL CFIKRSKGGK
1160 1170 1180 1190 1200
YSVKDKEDTQ VDSEARPMKD ETFGEYRSLE SDNEEKAFGS SQPSLNGDIK
1210 1220 1230 1240 1250
PLGSDDSLAD YGGSVDVQFN EDGSFIGQYS GKKEKEAAGG NDSSGATSPI

NPAVALE
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. 1 Publication
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. 1 Publication
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. 20 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 the 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.
GeneTreei ENSGT00760000118840.
HOGENOMi HOG000231380.
HOVERGENi HBG000144.
InParanoidi P32004.
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

Bgeei P32004.
CleanExi HS_L1CAM.
ExpressionAtlasi P32004. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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