DENND1A
entrez
57706
canonical
uniprot
Q8TEH3
canonical
ensembl
ENSG00000119522
resolver
ensp
ENSP00000362720
resolver
ensp
ENSP00000362722
resolver
ensp
ENSP00000362727
resolver
ensp
ENSP00000377763
resolver
ensp
ENSP00000536284
resolver
ensp
ENSP00000536285
resolver
ensp
ENSP00000673012
resolver
ensp
ENSP00000673014
resolver
enst
ENST00000394215
resolver
genesymbol
DENND1A
resolver
genesymbol
KIAA1608
resolver
genesymbol_syn
FAM31A
resolver
genesymbol_syn
KIAA1608
resolver
hgnc
HGNC:29324
resolver
uniprot
A0A0A0MS48
resolver
uniprot
A8MZA3
resolver
uniprot
B1AM80
resolver
uniprot
B7Z3C8
resolver
uniprot
B7Z669
resolver
uniprot
D3PFD3
resolver
uniprot
Q05C88
resolver
uniprot
Q5VWF0
resolver
uniprot
Q6PJZ5
resolver
uniprot
Q8IVD6
resolver
uniprot
Q9H796
resolver
uniprot
Q9HCG4
resolver
uniprot_entry
A0A0A0MS48_HUMAN
resolver
uniprot_entry
DEN1A_HUMAN
resolver
uniprot_entry
Q9HCG4_HUMAN
resolver
uniprot_sec
A8MZA3
resolver
uniprot_sec
B1AM80
resolver
uniprot_sec
B7Z3C8
resolver
uniprot_sec
B7Z669
resolver
uniprot_sec
D3PFD3
resolver
uniprot_sec
Q05C88
resolver
uniprot_sec
Q5VWF0
resolver
uniprot_sec
Q6PJZ5
resolver
uniprot_sec
Q8IVD6
resolver
uniprot_sec
Q9H796
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:0000269|PubMed:26055712}.
uniprot
proteins
amino_acid_sequence
MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQVRPPRPHVVKRPKSNIAVEGRRTSVPSPEQPQPYRTLRESDSAEGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALKLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPRPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATPFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMPMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPALAPAPDSVEQLRKQWETFE
uniprot
proteins
disease_involvement
DISEASE: Note=Genetic variants in DENND1A may play a role in susceptibility to polycystic ovary syndrome (PCOS), the most common endocrine disease among premenopausal women. PCOS is a complex disorder characterized by infertility, hirsutism, obesity, various menstrual disturbances, and enlarged ovaries studded with atretic follicles. {ECO:0000269|PubMed:22180642, ECO:0000269|PubMed:23208300, ECO:0000269|PubMed:24086769, ECO:0000269|PubMed:25626177}.
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:20154091, PubMed:20937701). Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P (By similarity). {ECO:0000250|UniProtKB:Q8K382, ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}.
uniprot
proteins
mass_dalton
110577
uniprot
proteins
mutagenesis
MUTAGEN 536..538; /note="SDS->EDE: Phosphomimetic mutant; abolishes the intramolecular interaction between the DENN domain and the C-terminus of the protein."; /evidence="ECO:0000269|PubMed:26055712
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:0000269|PubMed:26055712}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20154091
uniprot
proteins
pubmed
20937701
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22180642
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23208300
uniprot
proteins
pubmed
24086769
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25626177
uniprot
proteins
pubmed
26055712
uniprot
proteins
sequence_length
1009
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:20154091, ECO:0000269|PubMed:20937701}; Peripheral membrane protein {ECO:0000269|PubMed:20937701}. Presynaptic cell membrane {ECO:0000269|PubMed:20937701}. Note=Associates to membranes via lipid-binding activity. {ECO:0000250|UniProtKB:Q8K382}.
uniprot
proteins