Dtnbp1
entrez
94245
canonical
uniprot
Q91WZ8
canonical
ensembl
ENSMUSG00000057531
resolver
ensp
ENSMUSP00000072170
resolver
genesymbol
Dtnbp1
resolver
genesymbol_syn
Bloc1s8
resolver
genesymbol_syn
Sdy
resolver
uniprot
Q3TWK1
resolver
uniprot
Q6WXQ1
resolver
uniprot
Q80ZN4
resolver
uniprot
Q9CY43
resolver
uniprot_entry
DTBP1_MOUSE
resolver
uniprot_sec
Q3TWK1
resolver
uniprot_sec
Q6WXQ1
resolver
uniprot_sec
Q80ZN4
resolver
uniprot_sec
Q9CY43
resolver
amino_acid_sequence
MLETLRERLLSVQQDFTSGLKTLSDKSREAKVKGKPRTAPRLPKYSAGLELLSRYEDAWAALHRRAKECADAGELVDSEVVMLSAHWEKKRTSLNELQGQLQQLPALLQDLESLMASLAHLETSFEEVENHLLHLEDLCGQCELERHKQAQAQHLESYKKSKRKELEAFKAELDTEHTQKALEMEHTQQLKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPMGSMSSMEVNVDVLEQMDLMDISDQEALDVFLNSGGEDNIVMSPGVEMESNPNQNEMSLQIPSPSESASQPPASPSACTDLDTADAPLIQSDEEEVQVDTALVTLHTDRKSTPGVSDDSDQCDSTQDI
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Dtnbp1 are the cause of the sandy (sdy) mutant phenotype, a model for human Hermansky-Pudlak syndrome (HPS). Sdy mice lack dysbindin expression; they have a characteristic sandy coat color and have much fewer melanosomes in the retinal pigment epithelium and choroid. They are fully viable, but present behavioral abnormalities. They have prolonged bleeding times due to platelet storage pool deficiency, and lysosomal storage defects. The number of electron-opaque platelet dense granules is severely reduced, and the platelet serotonin content is strongly reduced. Secretion of lysosomal enzymes from kidney and from thrombin-stimulated platelets is depressed 2- and 3-fold, and ceroid pigment is present in kidney. Sandy mice also display impaired long-term memory retention and working memory and schizophrenia-like behavioral abnormalities. Vesicle morphology and kinetics of transmitter release are affected in both neuroendocrine cells and hippocampal synapses, characterized by larger vesicle size, slower quantal release, fewer release events and reduced readily releasable pool (RRP). Expression levels of SYN1 are lower in both the cortex and the hippocampal formation (HF). {ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:18504299, ECO:0000269|PubMed:18555792, ECO:0000269|PubMed:18945333, ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19220483, ECO:0000269|PubMed:1936982, ECO:0000269|PubMed:20921223}.
uniprot
proteins
function
FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Associates with the BLOC-2 complex to facilitate the transport of TYRP1 independent of AP-3 function. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. Plays a role in the regulation of cell surface exposure of DRD2. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation. Appears to promote neuronal transmission and viability through regulating the expression of SNAP25 and SYN1, modulating PI3-kinase-Akt signaling and influencing glutamatergic release. Regulates the expression of SYN1 through binding to its promoter. Modulates prefrontal cortical activity via the dopamine/D2 pathway. {ECO:0000269|PubMed:12923531, ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:16448387, ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:18504299, ECO:0000269|PubMed:18555792, ECO:0000269|PubMed:18984010, ECO:0000269|PubMed:19094965, ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:19546860, ECO:0000269|PubMed:19887632, ECO:0000269|PubMed:20045719, ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:20956979, ECO:0000269|PubMed:21998198}.
uniprot
proteins
mass_dalton
39651
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation. {ECO:0000250}.
uniprot
proteins
protein_family
Dysbindin family
uniprot
proteins
pubmed
11316798
uniprot
proteins
pubmed
12923531
uniprot
proteins
pubmed
14688250
uniprot
proteins
pubmed
15345706
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16448387
uniprot
proteins
pubmed
16760431
uniprot
proteins
pubmed
16837549
uniprot
proteins
pubmed
16980328
uniprot
proteins
pubmed
17577571
uniprot
proteins
pubmed
18504299
uniprot
proteins
pubmed
18555792
uniprot
proteins
pubmed
18945333
uniprot
proteins
pubmed
18984010
uniprot
proteins
pubmed
19094965
uniprot
proteins
pubmed
19142223
uniprot
proteins
pubmed
19220483
uniprot
proteins
pubmed
1936982
uniprot
proteins
pubmed
19428785
uniprot
proteins
pubmed
19546860
uniprot
proteins
pubmed
19887632
uniprot
proteins
pubmed
20045719
uniprot
proteins
pubmed
20302821
uniprot
proteins
pubmed
20921223
uniprot
proteins
pubmed
20956979
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21998198
uniprot
proteins
pubmed
22554196
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; Cytoplasmic side. Postsynaptic density. Endoplasmic reticulum {ECO:0000250}. Nucleus. Note=Mainly cytoplasmic but shuttles between the cytoplasm and nucleus. Exported out of the nucleus via its NES in a XPO1-dependent manner. Nuclear localization is required for regulation of the expression of genes such as SYN1. Detected in neuron cell bodies, axons and dendrites. Mainly located to the postsynaptic density. Detected at tubulovesicular elements in the vicinity of the Golgi apparatus and of melanosomes. Occasionally detected at the membrane of pigmented melanosomes in cultured melanoma cells (By similarity). The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Postsynaptic cell membrane. Endoplasmic reticulum {ECO:0000250}. Note=Exclusivley cytoplasmic. Predominantly found in the postsynaptic density (PSD). Little association with synaptic vesicles (By similarity). The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Vesicle membranes and microtubules. Associated with the AP-3 complex at presynaptic terminals. {ECO:0000250}.
uniprot
proteins