APLP1
entrez
333
canonical
uniprot
P51693
canonical
ensembl
ENSG00000105290
resolver
ensp
ENSP00000221891
resolver
ensp
ENSP00000498366
resolver
ensp
ENSP00000568080
resolver
ensp
ENSP00000630107
resolver
genesymbol
APLP1
resolver
hgnc
HGNC:597
resolver
uniprot
O00113
resolver
uniprot
Q96A92
resolver
uniprot_entry
APLP1_HUMAN
resolver
uniprot_sec
O00113
resolver
uniprot_sec
Q96A92
resolver
amino_acid_sequence
MGPASPAARGLSRRPGQPPLPLLLPLLLLLLRAQPAIGSLAGGSPGAAEAPGSAQVAGLCGRLTLHRDLRTGRWEPDPQRSRRCLRDPQRVLEYCRQMYPELQIARVEQATQAIPMERWCGGSRSGSCAHPHHQVVPFRCLPGEFVSEALLVPEGCRFLHQERMDQCESSTRRHQEAQEACSSQGLILHGSGMLLPCGSDRFRGVEYVCCPPPGTPDPSGTAVGDPSTRSWPPGSRVEGAEDEEEEESFPQPVDDYFVEPPQAEEEEETVPPPSSHTLAVVGKVTPTPRPTDGVDIYFGMPGEISEHEGFLRAKMDLEERRMRQINEVMREWAMADNQSKNLPKADRQALNEHFQSILQTLEEQVSGERQRLVETHATRVIALINDQRRAALEGFLAALQADPPQAERVLLALRRYLRAEQKEQRHTLRHYQHVAAVDPEKAQQMRFQVHTHLQVIEERVNQSLGLLDQNPHLAQELRPQIQELLHSEHLGPSELEAPAPGGSSEDKGGLQPPDSKDDTPMTLPKGSTEQDAASPEKEKMNPLEQYERKVNASVPRGFPFHSSEIQRDELAPAGTGVSREAVSGLLIMGAGGGSLIVLSMLLLRRKKPYGAISHGVVEVDPMLTLEEQQLRELQRHGYENPTYRFLEERP
uniprot
proteins
function
FUNCTION: May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. {ECO:0000250}.; FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis. {ECO:0000250}.
uniprot
proteins
mass_dalton
72176
uniprot
proteins
mutagenesis
MUTAGEN 426; /note="H->A: Reduced affinity for heparin. Reduces homodimerization."; /evidence="ECO:0000269|PubMed:21574595"; MUTAGEN 429; /note="R->A: Strongly reduced affinity for heparin. Strongly reduced homodimerization."; /evidence="ECO:0000269|PubMed:21574595"; MUTAGEN 433; /note="H->A: Reduced affinity for heparin. Reduces homodimerization."; /evidence="ECO:0000269|PubMed:21574595
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by caspases during neuronal apoptosis. Cleaved, in vitro, at Asp-620 by caspase-3 (By similarity). {ECO:0000250}.; PTM: N- and O-glycosylated. O-glycosylation with core 1 or possibly core 8 glycans. Glycosylation on Ser-227 is the preferred site to Thr-228. {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360}.
uniprot
proteins
protein_family
APP family
uniprot
proteins
pubmed
12135352
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
21574595
uniprot
proteins
pubmed
23234360
uniprot
proteins
pubmed
7494461
uniprot
proteins
pubmed
7929392
uniprot
proteins
pubmed
9428684
uniprot
proteins
pubmed
9521588
uniprot
proteins
pubmed
9890987
uniprot
proteins
sequence_length
650
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [C30]: Cytoplasm. Note=C-terminally processed in the Golgi complex.
uniprot
proteins
transmembrane_region
TRANSMEM 581..603; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins