P13595 (NCAM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neural cell adhesion molecule 1
Short name=N-CAM-1
Short name=NCAM-1

Alternative name(s):
CD_antigen=CD56

Gene names

Name:	Ncam1
Synonyms:	Ncam

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1115 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	This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Isoform 3: Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Contains 2 fibronectin type-III domains. Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Heparin-binding
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Inferred from direct assay PubMed 7613634. Source: MGI homotypic cell-cell adhesion Inferred from mutant phenotype PubMed 7613634. Source: MGI neuron projection development Inferred from genetic interaction PubMed 21389209. Source: MGI positive regulation of calcium-mediated signaling Inferred from direct assay PubMed 7613634. Source: MGI regulation of exocyst assembly Inferred from mutant phenotype PubMed 21389209. Source: MGI
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW axon Inferred from direct assay PubMed 15065125PubMed 15738425PubMed 15964824. Source: MGI external side of plasma membrane Inferred from direct assay PubMed 17213291PubMed 21708977PubMed 7613634. Source: MGI growth cone Inferred from direct assay PubMed 21389209. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW neuronal cell body Inferred from direct assay PubMed 15065125. Source: MGI
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13595-1)

Also known as: N-CAM 180;

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: P13595-2)

Also known as: N-CAM 140;

The sequence of this isoform differs from the canonical sequence as follows:
     810-1076: Missing.

Isoform 3 (identifier: P13595-3)

Also known as: N-CAM 120;

The sequence of this isoform differs from the canonical sequence as follows:
     702-725: NGSPTAGLSTGAIVGILIVIFVLL → TLGGSSTSYTLVSLLFSAVTLLLL
     726-1115: Missing.

Note: GPI-anchor amidated serine at position Ser-706.

Isoform 4 (identifier: P13595-4)

The sequence of this isoform differs from the canonical sequence as follows:
     601-605: EPSAP → KSSLF
     606-1115: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.5

Chain

20 – 1115

1096

Neural cell adhesion molecule 1

PRO_0000015012

Regions

Topological domain

20 – 711

692

Extracellular Potential

Transmembrane

712 – 729

18

Helical; Potential

Topological domain

730 – 1115

386

Cytoplasmic Potential

Domain

20 – 111

92

Ig-like C2-type 1

Domain

116 – 205

90

Ig-like C2-type 2

Domain

212 – 302

91

Ig-like C2-type 3

Domain

309 – 402

94

Ig-like C2-type 4

Domain

407 – 492

86

Ig-like C2-type 5

Domain

497 – 596

100

Fibronectin type-III 1

Domain

598 – 692

95

Fibronectin type-III 2

Region

152 – 156

5

Heparin-binding Potential

Region

161 – 165

5

Heparin-binding Potential

Amino acid modifications

Modified residue

774

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

887

1

Phosphoserine Ref.11 Ref.14

Modified residue

946

1

Phosphoserine Ref.11 Ref.14

Modified residue

950

1

Phosphothreonine Ref.11 Ref.14

Modified residue

952

1

Phosphothreonine Ref.14

Modified residue

958

1

Phosphoserine Ref.11 Ref.14

Modified residue

1005

1

Phosphoserine Ref.11 Ref.14

Glycosylation

222

1

N-linked (GlcNAc...); partial Ref.10

Glycosylation

316

1

N-linked (GlcNAc...) Ref.10

Glycosylation

348

1

N-linked (GlcNAc...) Ref.10

Glycosylation

424

1

N-linked (GlcNAc...) Ref.10

Glycosylation

450

1

N-linked (GlcNAc...) Ref.10 Ref.15 Ref.16

Glycosylation

453

1

N-linked (GlcNAc...) Ref.15

Glycosylation

479

1

N-linked (GlcNAc...) Ref.10

Disulfide bond

41 ↔ 96

Ref.17 Ref.18

Disulfide bond

139 ↔ 189

Ref.17 Ref.18

Disulfide bond

235 ↔ 288

Probable

Disulfide bond

330 ↔ 386

Probable

Disulfide bond

427 ↔ 480

Probable

Natural variations

Alternative sequence

601 – 605

5

EPSAP → KSSLF in isoform 4.

VSP_034826

Alternative sequence

606 – 1115

510

Missing in isoform 4.

VSP_034827

Alternative sequence

702 – 725

24

NGSPT…IFVLL → TLGGSSTSYTLVSLLFSAVT LLLL in isoform 3.

VSP_034828

Alternative sequence

726 – 1115

390

Missing in isoform 3.

VSP_034829

Alternative sequence

810 – 1076

267

Missing in isoform 2.

VSP_002588

Experimental info

Sequence conflict

20

1

L → M in CAA33148. Ref.4

Sequence conflict

158

1

V → F in AAH11310. Ref.2

Sequence conflict

261 – 268

8

DEKHIFSD → ERSRSSVS in CAA68263. Ref.1

Sequence conflict

273

1

L → V in CAA68263. Ref.1

Sequence conflict

354 – 355

2

KT → QD in CAA68263. Ref.1

Sequence conflict

379

1

T → R in CAA68263. Ref.1

Sequence conflict

379

1

T → R in CAA33148. Ref.4

Sequence conflict

385

1

I → M in CAA68263. Ref.1

Sequence conflict

385

1

I → M in CAA33148. Ref.4

Sequence conflict

399 – 400

2

MY → ID in CAA68263. Ref.1

Sequence conflict

399 – 400

2

MY → ID in CAA33148. Ref.4

Sequence conflict

403

1

F → V in AAH11310. Ref.2

Sequence conflict

403

1

F → V in BAC34554. Ref.3

Sequence conflict

403

1

F → V in BAC38551. Ref.3

Sequence conflict

549

1

K → T in CAA68263. Ref.1

Sequence conflict

572

1

R → T in CAA68263. Ref.1

Sequence conflict

575

1

V → D in CAA68263. Ref.1

Sequence conflict

589 – 594

6

SAATEF → MQPSES in CAA68263. Ref.1

Sequence conflict

600 – 602

3

REP → PEL in CAA68263. Ref.1

Sequence conflict

657

1

D → H in CAA68263. Ref.1

Sequence conflict

733

1

C → W in BAC34554. Ref.3

Sequence conflict

1082

1

T → A in BAC34554. Ref.3

Secondary structure

1

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1115

Helix Strand Turn

Details...

Beta strand

21 – 32

12

Beta strand

37 – 44

8

Beta strand

47 – 49

3

Beta strand

51 – 56

6

Turn

57 – 59

3

Beta strand

64 – 73

10

Beta strand

75 – 77

3

Beta strand

79 – 85

7

Turn

88 – 90

3

Beta strand

92 – 99

8

Beta strand

101 – 103

3

Beta strand

105 – 115

11

Beta strand

119 – 122

4

Beta strand

125 – 128

4

Beta strand

133 – 137

5

Beta strand

140 – 143

4

Beta strand

145 – 157

13

Helix

158 – 161

4

Beta strand

166 – 168

3

Beta strand

174 – 178

5

Beta strand

185 – 193

9

Turn

194 – 197

4

Beta strand

198 – 207

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (N-CAM 180) [UniParc]. Last modified July 22, 2008. Version 3. Checksum: 78AF831BABD23918	FASTA	1,115	119,427
	10 20 30 40 50 60 MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE 70 80 90 100 110 120 KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF 130 140 150 160 170 180 KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK 190 200 210 220 230 240 KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF 250 260 270 280 290 300 PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS 310 320 330 340 350 360 IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM 370 380 390 400 410 420 VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG 430 440 450 460 470 480 NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC 490 500 510 520 530 540 TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS 550 560 570 580 590 600 LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR 610 620 630 640 650 660 EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM 670 680 690 700 710 720 LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV 730 740 750 760 770 780 IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE 790 800 810 820 830 840 VRTEEERTPN HDGGKHTEPN ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA 850 860 870 880 890 900 TAQNSPTSET TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL 910 920 930 940 950 960 SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT PTPAGAASPL 970 980 990 1000 1010 1020 AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA TAPASPKSKA ATTNPSQGED 1030 1040 1050 1060 1070 1080 LKMDEGNFKT PDIDLAKDVF AALGSPRPAT GASGQASELA PSPADSAVPP APAKTEKGPV 1090 1100 1110 ETKSEPPESE AKPAPTEVKT VPNDATQTKE NESKA
	Isoform 2 (N-CAM 140) [UniParc]. Checksum: 4D77D553F474AD8E	FASTA	848	93,540
	10 20 30 40 50 60 MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE 70 80 90 100 110 120 KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF 130 140 150 160 170 180 KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK 190 200 210 220 230 240 KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF 250 260 270 280 290 300 PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS 310 320 330 340 350 360 IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM 370 380 390 400 410 420 VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG 430 440 450 460 470 480 NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC 490 500 510 520 530 540 TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS 550 560 570 580 590 600 LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR 610 620 630 640 650 660 EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM 670 680 690 700 710 720 LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV 730 740 750 760 770 780 IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE 790 800 810 820 830 840 VRTEEERTPN HDGGKHTEPN ETTPLTEPEK GPVETKSEPP ESEAKPAPTE VKTVPNDATQ TKENESKA
	Isoform 3 (N-CAM 120) [UniParc] [UniParc]. Checksum: 97867C2A61594CC4	FASTA	725	80,406
	10 20 30 40 50 60 MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE 70 80 90 100 110 120 KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF 130 140 150 160 170 180 KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK 190 200 210 220 230 240 KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF 250 260 270 280 290 300 PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS 310 320 330 340 350 360 IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM 370 380 390 400 410 420 VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG 430 440 450 460 470 480 NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC 490 500 510 520 530 540 TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS 550 560 570 580 590 600 LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR 610 620 630 640 650 660 EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM 670 680 690 700 710 720 LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ATLGGSSTSY TLVSLLFSAV TLLLL
	Isoform 4 [UniParc]. Checksum: D497D834C34EAEC0	FASTA	605	67,353
	10 20 30 40 50 60 MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE 70 80 90 100 110 120 KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF 130 140 150 160 170 180 KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK 190 200 210 220 230 240 KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF 250 260 270 280 290 300 PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS 310 320 330 340 350 360 IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM 370 380 390 400 410 420 VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG 430 440 450 460 470 480 NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC 490 500 510 520 530 540 TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS 550 560 570 580 590 600 LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR KSSLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a Mr 79,000 polypeptide without a membrane-spanning region." Barthels D., Santoni M.-J., Wille W., Ruppert C., Chaix J.-C., Hirsch M.-R., Fontecilla-Camps J.-C., Goridis C. EMBO J. 6:907-914(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Strain: C57BL/6. Tissue: Brain.
[2]	"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 4). Strain: FVB/N. Tissue: Mammary tumor.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1106 (ISOFORM 2). Strain: C57BL/6J. Tissue: Cerebellum and Spinal ganglion.
[4]	"Differential exon usage involving an unusual splicing mechanism generates at least eight types of NCAM cDNA in mouse brain." Santoni M.J., Barthels D., Vopper G., Boned A., Goridis C., Wille W. EMBO J. 8:385-392(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-700 AND 702-1115 (ISOFORMS 1 AND 2). Strain: C57BL/6. Tissue: Brain.
[5]	"Structural and immunological characterization of the amino-terminal domain of mammalian neural cell adhesion molecules." Rougon G., Marshak D.R. J. Biol. Chem. 261:3396-3401(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-36.
[6]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 38-48; 122-152; 166-177; 555-572; 584-595; 607-619; 652-662 AND 685-691, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[7]	"Analysis of cDNA clones that code for the transmembrane forms of the mouse neural cell adhesion molecule (NCAM) and are generated by alternative RNA splicing." Santoni M.-J., Barthels D., Barbas J.A., Hirsch M.-R., Steinmetz M., Goridis C., Wille W. Nucleic Acids Res. 15:8621-8641(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 529-1115 (ISOFORM 2). Strain: C57BL/6.
[8]	"Differential splicing and alternative polyadenylation generates distinct NCAM transcripts and proteins in the mouse." Barbas J.A., Chaix J.-C., Steinmetz M., Goridis C. EMBO J. 7:625-632(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 642-1115.
[9]	"NCAM-180, the large isoform of the neural cell adhesion molecule of the mouse, is encoded by an alternatively spliced transcript." Barthels D., Vopper G., Wille W. Nucleic Acids Res. 16:4217-4225(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 804-1081 (ISOFORM 1). Strain: C57BL/6J. Tissue: Brain.
[10]	"Identification of N-glycosylation sites of the murine neural cell adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass spectrometry." Albach C., Damoc E., Denzinger T., Schachner M., Przybylski M., Schmitz B. Anal. Bioanal. Chem. 378:1129-1135(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-222; ASN-316; ASN-348; ASN-424; ASN-450 AND ASN-479, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887; SER-946; THR-950; SER-958 AND SER-1005, MASS SPECTROMETRY. Tissue: Embryonic brain.
[12]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, MASS SPECTROMETRY. Tissue: Forebrain.
[13]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, MASS SPECTROMETRY. Tissue: Brain.
[14]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-887; SER-946; THR-950; THR-952; SER-958 AND SER-1005, MASS SPECTROMETRY. Tissue: Brain cortex.
[15]	"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation." Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B. Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-453, MASS SPECTROMETRY. Tissue: Myoblast.
[16]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450, MASS SPECTROMETRY.
[17]	"The three-dimensional structure of the first domain of neural cell adhesion molecule." Thomsen N.K., Soroka V., Jensen P.H., Berezin V., Kiselyov V.V., Bock E., Poulsen F.M. Nat. Struct. Biol. 3:581-585(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 20-116, DISULFIDE BONDS.
[18]	"Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion." Jensen P.H., Soroka V., Thomsen N.K., Ralets I., Berezin V., Bock E., Poulsen F.M. Nat. Struct. Biol. 6:486-493(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 119-208, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00051 mRNA. Translation: CAA68263.1.
BC011310 mRNA. Translation: AAH11310.1.
AK051197 mRNA. Translation: BAC34554.2.
AK082621 mRNA. Translation: BAC38551.2.
X15049 mRNA. Translation: CAA33148.1.
X15051 mRNA. Translation: CAA33150.1.
X15052 mRNA. Translation: CAA33151.1.
X06328 mRNA. Translation: CAA29641.1.
X07195 Genomic DNA. Translation: CAA30173.1.
X07197 Genomic DNA. Translation: CAA30175.1.
X07198 Genomic DNA. Translation: CAB40820.1.
X07200 Genomic DNA. Translation: CAA30177.1.
X07244 mRNA. Translation: CAA30230.1.

IPI

IPI00122971.
IPI00230665.
IPI00830721.
IPI01008428.

PIR

IJMSNL. A29673.

RefSeq

NP_001074914.1. NM_001081445.1.
NP_001106675.1. NM_001113204.1.
NP_035005.2. NM_010875.3.

UniGene

Mm.439182.
Mm.4974.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NCM	NMR	-	A	20-116	[»]
3NCM	NMR	-	A	119-208	[»]

ProteinModelPortal

P13595.

SMR

P13595. Positions 20-696.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13595. 3 interactions.

MINT

MINT-1176881.

PTM databases

PhosphoSite

P13595.

Proteomic databases

PaxDb

P13595.

PRIDE

P13595.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

17967.

KEGG

mmu:17967.

UCSC

uc009pje.2. mouse.
uc009pjf.1. mouse.
uc009pjh.1. mouse.

Organism-specific databases

CTD

4684.

MGI

MGI:97281. Ncam1.

Phylogenomic databases

eggNOG

NOG308439.

HOVERGEN

HBG052579.

InParanoid

P13595.

KO

K06491.

OrthoDB

EOG40VVP1.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.

Gene expression databases

Genevestigator

P13595.

GermOnline

ENSMUSG00000039542. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 7 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR009138. Neural_cell_adh.
[Graphical view]

Pfam

PF00041. fn3. 2 hits.
PF07679. I-set. 5 hits.
[Graphical view]

PRINTS

PR01838. NCAMFAMILY.

SMART

SM00060. FN3. 2 hits.
SM00408. IGc2. 5 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

PROSITE

PS50853. FN3. 2 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NCAM1. mouse.

EvolutionaryTrace

P13595.

NextBio

292903.

SOURCE

Search...

Entry information

Entry name

NCAM1_MOUSE

Accession

Primary (citable) accession number: P13595
Secondary accession number(s): P13594 , Q61949, Q61950, Q6LBU8, Q8BQ96, Q8C4B2, Q921P2, Q9R2A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 22, 2008
Last modified:	April 3, 2013
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program