Dennd1a
entrez
227801
canonical
uniprot
Q8K382
canonical
ensembl
ENSMUSG00000035392
resolver
ensp
ENSMUSP00000099848
resolver
ensp
ENSMUSP00000195437
resolver
ensp
ENSMUSP00000331065
resolver
enst
ENSMUST00000102787
resolver
genesymbol
Dennd1a
resolver
uniprot
A0MCI0
resolver
uniprot
A2ALU2
resolver
uniprot_entry
DEN1A_MOUSE
resolver
uniprot_sec
A0MCI0
resolver
uniprot_sec
A2ALU2
resolver
activity_regulation
ACTIVITY REGULATION: The guanine nucleotide exchange factor (GEF) activity is autoinhibited. Autoinhibition may be the result of intramolecular interaction between the DENN domain and the C-terminus, which is disrupted upon phosphorylation. Activation is regulated by Akt activation. {ECO:0000250|UniProtKB:Q8TEH3}.
uniprot
proteins
amino_acid_sequence
MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQESQWNELLETLHRLPIPDPGVSVHLSVHSYFTVPDSRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFSEEAFVSHYRSGAMKQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDITENGCVSSAEDPLPKTMPSPQAETQDPRLREDRRPITVHFGQVRPPRPHVVRRPKSNITVEGRRTSVSSPEQPQPYRTLKESDSAEGDETESPEQLVREPWGPTPAPPDRAASIDLLEDVFSSLDVEAPLQPLGQAKSLEDLRAPKDLREQPGSFDYQRLDLCRSERGLSMAAALKLAHPYTKLWSLGQDDMAIPSKPSITSPEKPSALLGTSPALPLRPQNQEGILSPSIKEETPIPTPGSITIPRPQGRKTPELGIVPPPPTARPAKLQAAGGPLGDFSSEPLQMDRERQAALSPALLSGLLPRAVPQGPTELLQPPSPAPGAAGTGSDALLALLDPLNTAWSGSTIPSHPATPSAATPFIPQLSFPPTVTPTPFVQTPLNPFVPSVPVVPPSMPLSSTPARPFGTPPASLGPAYAPSILLSSSGFYAPHRSQPNLSALSMPNLFGQIPMGAHTSPLQPLGPPAVAPSRIRTLPLARSSARAAEAKQGLALRPGESPLLPPRPPQSLQPTPQPSVPTQARDPFEDLLRKTKQDVSPSPAPALAPASTSVEQLRRQWETFE
uniprot
proteins
function
FUNCTION: Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes (PubMed:17182770, PubMed:20159556). Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P (PubMed:20159556). {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}.
uniprot
proteins
mass_dalton
111538
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and/or threonine in an Akt-dependent manner. Phosphorylation probably regulates the guanine nucleotide exchange factor (GEF) activity, possibly by disrupting an intramolecular interaction between the DENN domain and the C-terminus of the protein, thereby relieving the autoinhibition. {ECO:0000250|UniProtKB:Q8TEH3}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17182770
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20159556
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
sequence_length
1016
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}; Peripheral membrane protein {ECO:0000269|PubMed:17182770, ECO:0000269|PubMed:20159556}. Presynaptic cell membrane {ECO:0000269|PubMed:17182770}. Note=Associates to membranes via lipid-binding activity. {ECO:0000269|PubMed:20159556}.
uniprot
proteins