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O15394 (NCAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

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

Names and origin

Protein namesRecommended name:
Neural cell adhesion molecule 2

Short name=N-CAM-2
Short name=NCAM-2
Gene names
Name:NCAM2
Synonyms:NCAM21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed most strongly in adult and fetal brain.

Sequence similarities

Contains 2 fibronectin type-III domains.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 837818Neural cell adhesion molecule 2
PRO_0000015018

Regions

Topological domain20 – 697678Extracellular Potential
Transmembrane698 – 71821Helical; Potential
Topological domain719 – 837119Cytoplasmic Potential
Domain21 – 10888Ig-like C2-type 1
Domain113 – 20290Ig-like C2-type 2
Domain208 – 29790Ig-like C2-type 3
Domain302 – 39695Ig-like C2-type 4
Domain401 – 49191Ig-like C2-type 5
Domain498 – 59194Fibronectin type-III 1
Domain593 – 68896Fibronectin type-III 2

Amino acid modifications

Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Ref.4
Glycosylation4741N-linked (GlcNAc...) Potential
Glycosylation5621N-linked (GlcNAc...) Ref.4
Disulfide bond42 ↔ 93 Probable
Disulfide bond136 ↔ 186 Probable
Disulfide bond232 ↔ 281 Probable
Disulfide bond322 ↔ 380 Probable
Disulfide bond422 ↔ 475 Probable

Natural variations

Natural variant3471D → N.
Corresponds to variant rs35654962 [ dbSNP | Ensembl ].
VAR_047897
Natural variant3501L → P. Ref.1
Corresponds to variant rs232518 [ dbSNP | Ensembl ].
VAR_047898

Experimental info

Sequence conflict491E → R in AAB80803. Ref.1
Sequence conflict721E → G in AAB80803. Ref.1
Sequence conflict1631F → L in AAB80803. Ref.1
Sequence conflict3741D → G in AAB80803. Ref.1
Sequence conflict662 – 6676YEVQIT → MKFRLP in AAB80803. Ref.1

Secondary structure

........................................................................................................................................ 837
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15394 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 878EC1110562B3F3

FASTA83793,046
        10         20         30         40         50         60 
MSLLLSFYLL GLLVSSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK 

        70         80         90        100        110        120 
IISTQRVVVQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV 

       130        140        150        160        170        180 
VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTISD NRFAMLANNN LQILNINKSD 

       190        200        210        220        230        240 
EGIYRCEGRV EARGEIDFRD IIVIVNVPPA ISMPQKSFNA TAERGEEMTF SCRASGSPEP 

       250        260        270        280        290        300 
AISWFRNGKL IEENEKYILK GSNTELTVRN IINSDGGPYV CRATNKAGED EKQAFLQVFV 

       310        320        330        340        350        360 
QPHIIQLKNE TTYENGQVTL VCDAEGEPIP EITWKRAVDG FTFTEGDKSL DGRIEVKGQH 

       370        380        390        400        410        420 
GSSSLHIKDV KLSDSGRYDC EAASRIGGHQ KSMYLDIEYA PKFISNQTIY YSWEGNPINI 

       430        440        450        460        470        480 
SCDVKSNPPA SIHWRRDKLV LPAKNTTNLK TYSTGRKMIL EIAPTSDNDF GRYNCTATNH 

       490        500        510        520        530        540 
IGTRFQEYIL ALADVPSSPY GVKIIELSQT TAKVSFNKPD SHGGVPIHHY QVDVKEVASE 

       550        560        570        580        590        600 
IWKIVRSHGV QTMVVLNNLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH 

       610        620        630        640        650        660 
GQPSSGKSFK LSITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM 

       670        680        690        700        710        720 
GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAVIGLGVA ALLLILVVTD 

       730        740        750        760        770        780 
VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERVT 

       790        800        810        820        830 
NHEDGSPVNE PNETTPLTEP EKLPLKEEDG KEALNPETIE IKVSNDIIQS KEDDSKA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel human neural cell adhesion molecule gene (NCAM2) that maps to chromosome region 21q21 and is potentially involved in Down syndrome."
Paoloni-Giacobino A., Chen H., Antonarakis S.E.
Genomics 43:43-51(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-350.
Tissue: Brain.
[2]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Brain.
[4]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-445 AND ASN-562.
[5]"Solution structure of the fibronectin type-III domain of human neural cell adhesion molecule 2."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 486-591.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U75330 mRNA. Translation: AAB80803.1.
AP001138 Genomic DNA. No translation available.
BC052946 mRNA. Translation: AAH52946.1.
CCDSCCDS42910.1.
RefSeqNP_004531.2. NM_004540.3.
UniGeneHs.473450.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DOCNMR-A486-591[»]
2JLLX-ray2.30A301-689[»]
2KBGNMR-A592-693[»]
2V5TX-ray2.00A115-301[»]
2VAJX-ray2.70A21-113[»]
2WIMX-ray3.00A/B19-301[»]
2XY1X-ray1.90A209-398[»]
2XY2X-ray1.77A19-207[»]
2XYCX-ray2.65A301-591[»]
ProteinModelPortalO15394.
SMRO15394. Positions 19-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110765. 1 interaction.
DIPDIP-56211N.
IntActO15394. 2 interactions.
STRING9606.ENSP00000383392.

PTM databases

PhosphoSiteO15394.

Proteomic databases

MaxQBO15394.
PaxDbO15394.
PRIDEO15394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000400546; ENSP00000383392; ENSG00000154654.
GeneID4685.
KEGGhsa:4685.
UCSCuc002yld.2. human.

Organism-specific databases

CTD4685.
GeneCardsGC21P022370.
H-InvDBHIX0027799.
HGNCHGNC:7657. NCAM2.
HPAHPA030900.
MIM602040. gene.
neXtProtNX_O15394.
PharmGKBPA31460.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308439.
HOGENOMHOG000074124.
HOVERGENHBG052579.
InParanoidO15394.
KOK06491.
OMAEPTISWY.
OrthoDBEOG75MVVH.
PhylomeDBO15394.
TreeFamTF326195.

Gene expression databases

ArrayExpressO15394.
BgeeO15394.
CleanExHS_NCAM2.
GenevestigatorO15394.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR009138. Neural_cell_adh.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF07679. I-set. 5 hits.
[Graphical view]
PRINTSPR01838. NCAMFAMILY.
SMARTSM00060. FN3. 2 hits.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCAM2. human.
EvolutionaryTraceO15394.
GenomeRNAi4685.
NextBio18068.
PROO15394.
SOURCESearch...

Entry information

Entry nameNCAM2_HUMAN
AccessionPrimary (citable) accession number: O15394
Secondary accession number(s): A8MQ06, Q7Z7F2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM