NCAM1
entrez
4684
canonical
uniprot
P13591
canonical
ensembl
ENSG00000149294
resolver
ensp
ENSP00000318472
resolver
ensp
ENSP00000384055
resolver
ensp
ENSP00000480132
resolver
ensp
ENSP00000480774
resolver
ensp
ENSP00000481083
resolver
ensp
ENSP00000484943
resolver
enst
ENST00000401611
resolver
enst
ENST00000619839
resolver
genesymbol
NCAM1
resolver
genesymbol_syn
NCAM
resolver
hgnc
HGNC:7656
resolver
uniprot
A0A087WWD4
resolver
uniprot
A8K8T8
resolver
uniprot
H7BYX6
resolver
uniprot
P13592
resolver
uniprot
P13593
resolver
uniprot
Q05C58
resolver
uniprot
Q15829
resolver
uniprot
Q16180
resolver
uniprot
Q16209
resolver
uniprot
Q59FL7
resolver
uniprot
Q86X47
resolver
uniprot
Q96CJ3
resolver
uniprot_entry
A0A087WWD4_HUMAN
resolver
uniprot_entry
H7BYX6_HUMAN
resolver
uniprot_entry
NCAM1_HUMAN
resolver
uniprot_sec
A8K8T8
resolver
uniprot_sec
P13592
resolver
uniprot_sec
P13593
resolver
uniprot_sec
Q05C58
resolver
uniprot_sec
Q15829
resolver
uniprot_sec
Q16180
resolver
uniprot_sec
Q16209
resolver
uniprot_sec
Q59FL7
resolver
uniprot_sec
Q86X47
resolver
uniprot_sec
Q96CJ3
resolver
amino_acid_sequence
MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVQGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTSGLSTGAIVGILIVIFVLLLVVVDITCYFLNKCGLFMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVEAKPECQETETKPAPAEVKTVPNDATQTKENESKA
uniprot
proteins
function
FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.; FUNCTION: (Microbial infection) Acts as a receptor for rabies virus. {ECO:0000269|PubMed:9696812}.; FUNCTION: (Microbial infection) Acts as a receptor for Zika virus. {ECO:0000269|PubMed:32753727}.
uniprot
proteins
mass_dalton
94574
uniprot
proteins
mutagenesis
MUTAGEN 433; /note="N->Q: Loss of polysialic acid addition by ST8SIA4; when associated with Q-459 and Q-488. Loss of polysialic acid addition by ST8SIA2; when associated with Q-459 and Q-488. Significantly decreases polysialic acid addition by ST8SIA2; when associated with Q-488. Decreases polysialic acid addition by ST8SIA2; when associated with Q-459. Decreases polysialic acid addition by ST8SIA4; when associated with Q-459. Does not affect polysialic acid addition by ST8SIA2. Does not affect polysialic acid addition by ST8SIA4."; /evidence="ECO:0000269|PubMed:9774483"; MUTAGEN 459; /note="N->Q: Loss of polysialic acid addition by ST8SIA4; when associated with Q-433 and Q-488. Loss of polysialic acid addition by ST8SIA2; when associated with Q-433 and Q-488. Loss of polysialic acid addition by ST8SIA4; when associated with Q-488. Loss of polysialic acid addition by ST8SIA2; when associated with Q-488. Decreases polysialic acid addition by ST8SIA2. Decreases polysialic acid addition by ST8SIA4."; /evidence="ECO:0000269|PubMed:9774483"; MUTAGEN 488; /note="N->Q: Loss of polysialic acid addition by ST8SIA4; when associated with Q-433 and Q-459. Loss of polysialic acid addition by ST8SIA2; when associated with Q-433 and Q-459. Loss of polysialic acid addition by ST8SIA4; when associated with Q-459. Loss of polysialic acid addition by ST8SIA2; when associated with Q-459. Significantly decreases polysialic acid addition by ST8SIA2."; /evidence="ECO:0000269|PubMed:9774483
uniprot
proteins
post_translational_modification
PTM: Polysialylated at Asn-459 and Asn-488 by ST8SIA2 and ST8SIA4 (PubMed:28810663). Polysialylation modulates cell interactions by conferring both attractive and repulsive properties that are highly regulated by ST8SIA2 and ST8SIA4 (PubMed:28810663). Polysialylation is formed on a-2,3-linked sialic acid of core glycans (PubMed:9774483). {ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9774483}.
uniprot
proteins
pubmed
1339414
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1710251
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28810663
uniprot
proteins
pubmed
2887295
uniprot
proteins
pubmed
3203385
uniprot
proteins
pubmed
3253057
uniprot
proteins
pubmed
32753727
uniprot
proteins
pubmed
8075973
uniprot
proteins
pubmed
9696812
uniprot
proteins
pubmed
9774483
uniprot
proteins
sequence_length
858
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 719..739; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins