P32004 (L1CAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Defects in L1CAM are the cause of 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. Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31 Ref.33 Ref.35 Ref.36 Defects in L1CAM are the cause of mental retardation-aphasia-shuffling gait-adducted thumbs syndrome (MASA) [MIM:303350]; also known as corpus callosum hypoplasia, psychomotor retardation, adducted thumbs, spastic paraparesis, and hydrocephalus or CRASH syndrome. MASA is 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. Ref.18 Ref.19 Ref.26 Ref.27 Ref.30 Ref.32 Ref.34 Ref.35 Ref.38 Defects in L1CAM are the cause of spastic paraplegia X-linked type 1 (SPG1) [MIM:303350]. Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Ref.35 Note=Defects in L1CAM may contribute to Hirschsprung disease by modifying the effects of Hirschsprung disease-associated genes to cause intestinal aganglionosis. Ref.35 Defects in L1CAM are a cause of partial agenesis of the corpus callosum (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. Ref.35 Ref.37
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 process	Cell adhesion Differentiation Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary spastic paraplegia Hirschsprung disease Mental retardation Neurodegeneration
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell death Inferred from electronic annotation. Source: UniProtKB-KW leukocyte migration Traceable author statement. Source: Reactome
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.8
	Chain	20 – 1257	1238	Neural cell adhesion molecule L1		PRO_0000015022
Regions
	Topological domain	20 – 1120	1101	Extracellular Potential
	Transmembrane	1121 – 1143	23	Helical; Potential
	Topological domain	1144 – 1257	114	Cytoplasmic Potential
	Domain	35 – 125	91	Ig-like C2-type 1
	Domain	139 – 226	88	Ig-like C2-type 2
	Domain	240 – 328	89	Ig-like C2-type 3
	Domain	333 – 420	88	Ig-like C2-type 4
	Domain	425 – 507	83	Ig-like C2-type 5
	Domain	518 – 607	90	Ig-like C2-type 6
	Domain	612 – 707	96	Fibronectin type-III 1
	Domain	714 – 807	94	Fibronectin type-III 2
	Domain	812 – 913	102	Fibronectin type-III 3
	Domain	914 – 1011	98	Fibronectin type-III 4
	Domain	1016 – 1108	93	Fibronectin type-III 5
	Motif	554 – 556	3	Cell attachment site Potential
Amino acid modifications
	Modified residue	1163	1	Phosphoserine Ref.13
	Modified residue	1181	1	Phosphoserine By similarity
	Modified residue	1190	1	Phosphoserine Ref.13
	Modified residue	1191	1	Phosphoserine Ref.13
	Modified residue	1194	1	Phosphoserine Ref.13
	Modified residue	1247	1	Phosphothreonine By similarity
	Modified residue	1248	1	Phosphoserine Ref.14
	Glycosylation	100	1	N-linked (GlcNAc...) Potential
	Glycosylation	203	1	N-linked (GlcNAc...) Potential
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	294	1	N-linked (GlcNAc...) Potential
	Glycosylation	433	1	N-linked (GlcNAc...) Potential
	Glycosylation	479	1	N-linked (GlcNAc...) Potential
	Glycosylation	490	1	N-linked (GlcNAc...) Potential
	Glycosylation	505	1	N-linked (GlcNAc...) Potential
	Glycosylation	588	1	N-linked (GlcNAc...) Potential
	Glycosylation	671	1	N-linked (GlcNAc...) Ref.12 Ref.15
	Glycosylation	726	1	N-linked (GlcNAc...) Potential
	Glycosylation	777	1	N-linked (GlcNAc...) Potential
	Glycosylation	825	1	N-linked (GlcNAc...) Potential
	Glycosylation	849	1	N-linked (GlcNAc...) Potential
	Glycosylation	876	1	N-linked (GlcNAc...) Potential
	Glycosylation	979	1	N-linked (GlcNAc...) Potential
	Glycosylation	1022	1	N-linked (GlcNAc...) Potential
	Glycosylation	1030	1	N-linked (GlcNAc...) Potential
	Glycosylation	1071	1	N-linked (GlcNAc...) Potential
	Glycosylation	1105	1	N-linked (GlcNAc...) Potential
	Disulfide bond	57 ↔ 114		By similarity
	Disulfide bond	158 ↔ 209		By similarity
	Disulfide bond	264 ↔ 312		By similarity
	Disulfide bond	354 ↔ 404		By similarity
	Disulfide bond	448 ↔ 497		By similarity
	Disulfide bond	539 ↔ 591		By similarity
Natural variations
	Alternative sequence	1177 – 1180	4	Missing in isoform 2.		VSP_002591
	Natural variant	9	1	W → S in HSAS. Ref.20		VAR_003921
	Natural variant	30	1	H → N. Ref.33		VAR_030403
	Natural variant	121	1	G → S in HSAS. Ref.20		VAR_003922
	Natural variant	179	1	I → S in HSAS, MASA and SPG1. Ref.23		VAR_003923
	Natural variant	184	1	R → Q in HSAS; severe. Ref.18 Ref.21 Ref.28		VAR_003924
	Natural variant	184	1	R → W in HSAS. Ref.33		VAR_030404
	Natural variant	194	1	Y → C in HSAS. Ref.25		VAR_003925
	Natural variant	202	1	D → Y in MASA. Ref.34		VAR_030405
	Natural variant	210	1	H → Q in MASA. Ref.18 Ref.19 Ref.21 Corresponds to variant rs28933683 [ dbSNP | Ensembl ].		VAR_003926
	Natural variant	219	1	I → T in HSAS. Ref.31		VAR_003927
	Natural variant	240	1	P → L in HSAS and ACCPX. Ref.25 Ref.37		VAR_003928
	Natural variant	264	1	C → Y in HSAS; severe. Ref.16 Ref.21		VAR_003929
	Natural variant	268	1	G → D in MASA. Ref.27		VAR_030406
	Natural variant	309	1	E → K in MASA. Ref.20		VAR_003930
	Natural variant	335	1	W → C in HSAS. Ref.33		VAR_030407
	Natural variant	335	1	W → R in HSAS and MASA; also in a patient with hydrocephalus and Hirschsprung disease. Ref.31		VAR_003931
	Natural variant	370	1	G → R in HSAS, MASA and SPG1. Ref.23 Ref.33		VAR_003932
	Natural variant	386	1	R → C in HSAS. Ref.31		VAR_003933
	Natural variant	408	1	N → I in HSAS. Ref.33		VAR_030408
	Natural variant	415	1	A → P in HSAS. Ref.36		VAR_027512
	Natural variant	421	1	V → D in HSAS. Ref.33		VAR_030409
	Natural variant	426	1	A → D in MASA. Ref.27		VAR_030410
	Natural variant	439 – 443	5	Missing in HSAS.		VAR_003934
	Natural variant	452	1	G → R in HSAS; severe. Ref.18 Ref.21		VAR_003935
	Natural variant	473	1	R → C in HSAS and MASA. Ref.31		VAR_003936
	Natural variant	482	1	L → P in MASA. Ref.26		VAR_030411
	Natural variant	497	1	C → Y in HSAS. Ref.33		VAR_030412
	Natural variant	526	1	Missing in HSAS.		VAR_030413
	Natural variant	542	1	S → P in HSAS. Ref.26		VAR_030414
	Natural variant	598	1	D → N in MASA. Ref.19 Ref.21		VAR_003937
	Natural variant	632	1	R → P in MASA. Ref.30		VAR_003938
	Natural variant	655	1	K → E in HSAS. Ref.24		VAR_030415
	Natural variant	674	1	S → C in MASA; associated with callosal agenesis. Ref.32		VAR_027513
	Natural variant	691	1	A → D in MASA; associated with callosal agenesis. Ref.29 Ref.32		VAR_003939
	Natural variant	691	1	A → T in HSAS. Ref.33		VAR_030416
	Natural variant	698	1	G → R in HSAS and MASA; associated with callosal agenesis. Ref.29 Ref.32		VAR_003940
	Natural variant	739	1	R → W. Ref.33		VAR_030417
	Natural variant	741	1	M → T in HSAS. Ref.26		VAR_030418
	Natural variant	751	1	R → P in HSAS. Ref.33		VAR_030419
	Natural variant	752	1	V → M in MASA; also in a patient with hydrocephalus and Hirschsprung disease. Ref.26 Ref.35		VAR_014421
	Natural variant	768	1	V → F in HSAS. Ref.20		VAR_003941
	Natural variant	768	1	V → I. Ref.26 Corresponds to variant rs36021462 [ dbSNP | Ensembl ].		VAR_030420
	Natural variant	770	1	D → N in MASA; associated with callosal agenesis. Ref.38		VAR_027514
	Natural variant	784	1	Y → C in HSAS. Ref.28		VAR_003942
	Natural variant	935	1	L → P in HSAS. Ref.29		VAR_003943
	Natural variant	936 – 948	13	Missing in HSAS.		VAR_003944
	Natural variant	941	1	P → L in HSAS and MASA. Ref.20		VAR_003945
	Natural variant	958	1	L → V. Corresponds to variant rs35902890 [ dbSNP | Ensembl ].		VAR_059413
	Natural variant	1070	1	Y → C in HSAS. Ref.20		VAR_003946
	Natural variant	1194	1	S → L in HSAS and MASA. Ref.17 Ref.21		VAR_003947
	Natural variant	1224	1	S → L in HSAS. Ref.31		VAR_003948
	Natural variant	1239	1	G → E. Ref.33		VAR_030421
Experimental info
	Sequence conflict	4	1	A → V in CAA42508. Ref.1
	Sequence conflict	216	1	T → I in CAA42508. Ref.1
	Sequence conflict	250	1	S → T in CAA42508. Ref.1
	Sequence conflict	276 – 277	2	WL → SV in CAA42508. Ref.1
	Sequence conflict	357	1	Q → E in CAA42508. Ref.1
	Sequence conflict	626	1	L → V in CAA42508. Ref.1
	Sequence conflict	936	1	L → V in CAB37831. Ref.10
	Sequence conflict	1116 – 1117	2	GF → WLC Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 5EDD764DA86C0E63	FASTA	1,257	140,003
	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
	Isoform 2 [UniParc]. Checksum: 23AD19B26C8C9971	FASTA	1,253	139,517
	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 ETFGEYSDNE EKAFGSSQPS LNGDIKPLGS 1210 1220 1230 1240 1250 DDSLADYGGS VDVQFNEDGS FIGQYSGKKE KEAAGGNDSS GATSPINPAV ALE

References

	« Hide 'large scale' referencesShow '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: 1932117] [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: 1769655] [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: 1627459] [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: 9286695] [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: 9479034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[6]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Pancreas.
[8]	"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: 3136168] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-36.
[9]	"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: 2387585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-371.
[10]	"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: 1923824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 353-1176, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1082-1176. Tissue: Fetal brain.
[11]	"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: 1993895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1030-1257.
[12]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671, MASS SPECTROMETRY. Tissue: Plasma.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163; SER-1190; SER-1191 AND SER-1194, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-671, MASS SPECTROMETRY. Tissue: Liver.
[16]	"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: 8401576] [Abstract] Cited for: VARIANT HSAS TYR-264.
[17]	"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: 7881431] [Abstract] Cited for: VARIANT HSAS/MASA LEU-1194.
[18]	"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: 7920659] [Abstract] Cited for: VARIANTS HSAS GLN-184 AND ARG-452, VARIANT MASA GLN-210.
[19]	"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: 7920660] [Abstract] Cited for: VARIANTS MASA GLN-210 AND ASN-598.
[20]	"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: 7762552] [Abstract] Cited for: VARIANTS HSAS/MASA SER-9; SER-121; LYS-309; PHE-768; LEU-941 AND CYS-1070.
[21]	"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: 8556302] [Abstract] Cited for: VARIANTS HSAS/MASA GLN-184; GLN-210; TYR-264; ARG-452; ASN-598 AND LEU-1194.
[22]	Erratum Fransen E., Lemmon V., van Camp G., Vits L., Coucke P., Willems P.J. Eur. J. Hum. Genet. 4:126-126(1996)
[23]	"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: 7562969] [Abstract] Cited for: VARIANTS HSAS/MASA/SPG1 SER-179 AND ARG-370.
[24]	"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: 9118141] [Abstract] Cited for: VARIANT HSAS GLU-655.
[25]	"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: 8929944] [Abstract] Cited for: VARIANTS HSAS CYS-194 AND LEU-240.
[26]	"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: 9268105] [Abstract] Cited for: VARIANT MASA PRO-482, VARIANTS HSAS SER-526 DEL; PRO-542; THR-741 AND MET-752, VARIANT ILE-768.
[27]	"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: 9300653] [Abstract] Cited for: VARIANTS MASA ASP-268 AND ASP-426.
[28]	"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: 9195224] [Abstract] Cited for: VARIANTS HSAS GLN-184; 439-VAL--THR-443 DEL; CYS-784 AND 936-LEU--LEU-948 DEL.
[29]	"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: 9521424] [Abstract] Cited for: VARIANTS HSAS/MASA ASP-691; ARG-698 AND PRO-935.
[30]	"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: 9452110] [Abstract] Cited for: VARIANT MASA PRO-632.
[31]	"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: 9744477] [Abstract] Cited for: VARIANTS HSAS/MASA THR-219; ARG-335; CYS-386; CYS-473 AND LEU-1224.
[32]	"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: 9832035] [Abstract] Cited for: VARIANTS MASA CYS-674; ASP-691 AND ARG-698.
[33]	"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: 10797421] [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.
[34]	"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: 10805190] [Abstract] Cited for: VARIANT MASA TYR-202.
[35]	"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: 11857550] [Abstract] Cited for: VARIANT MASA MET-752, POSSIBLE INVOLVEMENT IN HIRSCHSPRUNG DISEASE.
[36]	"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: 12435569] [Abstract] Cited for: VARIANT HSAS PRO-415.
[37]	"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: 16650080] [Abstract] Cited for: VARIANT ACCPX LEU-240.
[38]	"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: 16816908] [Abstract] Cited for: VARIANT MASA ASN-770.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

L1CAM

L1CAM mutation Web Page

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59847 mRNA. Translation: CAA42508.1. M77640 mRNA. Translation: AAC14352.1. M74387 mRNA. Translation: AAA59476.1. Z29373 Genomic DNA. Translation: CAA82564.1. U52111 Genomic DNA. No translation available. U52112 Genomic DNA. No translation available. 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.
IPI	IPI00334532. IPI00871467.
PIR	A41060.
RefSeq	NP_000416.1. NM_000425.3. NP_001137435.1. NM_001143963.1. NP_076493.1. NM_024003.2.
UniGene	Hs.522818.
3D structure databases
ProteinModelPortal	P32004.
SMR	P32004. Positions 31-1005.
ModBase	Search...
Protein-protein interaction databases
IntAct	P32004. 2 interactions.
MINT	MINT-1369985.
STRING	P32004.
PTM databases
PhosphoSite	P32004.
Polymorphism databases
DMDM	1705571.
Proteomic databases
PRIDE	P32004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370057; ENSP00000359074; ENSG00000198910. ENST00000370060; ENSP00000359077; ENSG00000198910.
GeneID	3897.
KEGG	hsa:3897.
UCSC	uc004fjb.1. human. uc004fjc.1. human.
Organism-specific databases
CTD	3897.
GeneCards	GC0XM153126.
H-InvDB	HIX0056110.
HGNC	HGNC:6470. L1CAM.
HPA	CAB010896. HPA005830.
MIM	303350. phenotype. 304100. phenotype. 307000. phenotype. 308840. gene.
neXtProt	NX_P32004.
Orphanet	388. Hirschsprung disease. 2182. Hydrocephalus with stenosis of aqueduct of Sylvius. 2466. MASA syndrome. 1497. X-linked complicated corpus callosum dysgenesis.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18379.
HOGENOM	HBG445523.
HOVERGEN	HBG000144.
OMA	YRVQWRP.
OrthoDB	EOG4NGGKS.
PhylomeDB	P32004.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P32004.
Bgee	P32004.
CleanEx	HS_L1CAM.
Genevestigator	P32004.
GermOnline	ENSG00000198910. Homo sapiens.
Family and domain databases
InterPro	IPR003961. Fibronectin_type3. IPR007110. Ig-like. IPR013783. Ig-like_fold. IPR013098. Ig_I-set. IPR003599. Ig_sub. IPR003598. Ig_sub2. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 11 hits.
KO	K06550.
Pfam	PF00041. fn3. 4 hits. PF07679. I-set. 5 hits. [Graphical view]
SMART	SM00060. FN3. 4 hits. SM00409. IG. 1 hit. SM00408. IGc2. 5 hits. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 4 hits.
PROSITE	PS50853. FN3. 5 hits. PS50835. IG_LIKE. 6 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	15299.
PMAP-CutDB	P32004.
SOURCE	Search...

Entry information

Entry name

L1CAM_HUMAN

Accession

Primary (citable) accession number: P32004
Secondary accession number(s): A0AV65, B2RMU7, Q8TA87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.