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Q91WZ8

- DTBP1_MOUSE

UniProt

Q91WZ8 - DTBP1_MOUSE

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Protein

Dysbindin

Gene

Dtnbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.16 Publications

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. anterograde axon cargo transport Source: UniProtKB
  3. anterograde synaptic vesicle transport Source: UniProtKB
  4. blood coagulation Source: MGI
  5. muscle organ development Source: MGI
  6. neuron projection development Source: UniProtKB
  7. neuron projection morphogenesis Source: UniProtKB
  8. organelle organization Source: UniProtKB
  9. platelet dense granule organization Source: MGI
  10. positive regulation of gene expression Source: UniProtKB
  11. positive regulation of neurotransmitter secretion Source: UniProtKB
  12. regulation of dopamine receptor signaling pathway Source: UniProtKB
  13. regulation of dopamine secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Sensory transduction

Names & Taxonomyi

Protein namesi
Recommended name:
Dysbindin
Alternative name(s):
Biogenesis of lysosome-related organelles complex 1 subunit 8
Short name:
BLOC-1 subunit 8
Dysbindin-1
Dystrobrevin-binding protein 1
Hermansky-Pudlak syndrome 7 protein homolog
Short name:
HPS7 protein homolog
Gene namesi
Name:Dtnbp1
Synonyms:Bloc1s8, Sdy
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:2137586. Dtnbp1.

Subcellular locationi

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. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Endoplasmic reticulum By similarity. 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.By similarity
Isoform 3 : Cytoplasm. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Melanosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctionsynapsepostsynaptic cell membrane. Endoplasmic reticulum By similarity
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.By similarity

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. BLOC-1 complex Source: UniProtKB
  3. cell junction Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB
  5. dendritic spine Source: UniProtKB
  6. endoplasmic reticulum membrane Source: UniProtKB
  7. endosome Source: UniProtKB-KW
  8. growth cone Source: UniProtKB
  9. neuron projection Source: UniProtKB
  10. nucleus Source: UniProtKB
  11. plasma membrane Source: MGI
  12. postsynaptic density Source: UniProtKB
  13. postsynaptic membrane Source: UniProtKB-KW
  14. sarcolemma Source: UniProtKB
  15. sarcoplasm Source: MGI
  16. synaptic vesicle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

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).8 Publications

Disruption phenotypei

Null mice exhibit cognitive abnormalities including schizophrenia-related behaviors such as impaired working memory under stressful conditions. There is higher acoustic startle reactivity to stimuli. Pyramidal neurons are hypoexcitable on dopamine-2 receptor stimulation. There is reduced expression of Ca2+/calmodulin-dependent protein kinase II (CaMKII) and CaMKKbeta in the medial prefrontal cortex mPFC. There is increased expression levels of cell surface dopamine receptor D2 in cortical neurons. Expression levels of SYN1 are lower in both cortex and in the hippocampal formation (HF).3 Publications

Keywords - Diseasei

Albinism, Hermansky-Pudlak syndrome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352DysbindinPRO_0000191002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ91WZ8.
PaxDbiQ91WZ8.
PRIDEiQ91WZ8.

PTM databases

PhosphoSiteiQ91WZ8.

Expressioni

Tissue specificityi

Detected in brain, in hippocampus and dentate gyrus neurons. Detected at axon bundles and axon terminals, notably in the cerebellum and hippocampus. Detected in neuropil in hippocampus, lateral septum, basal ganglia and substantia nigra. Highly expressed in pyramidal cells of hippocampus CA2 and CA3. Detected at the heart and skeletal muscle sarcolemma (at protein level). Ubiquitously expressed. The highest expression is observed in testis, liver, kidney, brain, heart and lung. Expressed at lower levels in stomach and small intestine.6 Publications

Gene expression databases

BgeeiQ91WZ8.
CleanExiMM_DTNBP1.
ExpressionAtlasiQ91WZ8. baseline and differential.
GenevestigatoriQ91WZ8.

Interactioni

Subunit structurei

Interacts with AP3M1 and TRIM32. Interacts (isoform 1 and isoform 2 only) with the DNA-dependent protein kinase complex DNA-PK; the interaction phosphorylates DTNBP1 in vitro. Interacts directly in this complex with XRCC5 and XRCC6. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus (By similarity). Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. This BLOC-1 complex also associates with the BLOC-2 complex in endosomes. Binds to DTNA and DTNB but may not be a physiological binding partner (PubMed:16448387 and PubMed:16980328). Interacts (via its coiled coil domain) with KXD1. Interacts with AP3B2, BLOC1S5, BLOC1S6, CMYA5, PI4K2, RNF151 and SNAPIN/BLOC1S8. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cmya5Q70KF45EBI-643186,EBI-782290
DtnaQ9D2N43EBI-643186,EBI-296019

Protein-protein interaction databases

BioGridi220491. 3 interactions.
IntActiQ91WZ8. 4 interactions.
MINTiMINT-197141.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 325153DysbindinAdd
BLAST
Regioni243 – 25614Nuclear export signalBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili88 – 17689Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the dysbindin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG81712.
GeneTreeiENSGT00390000010667.
HOGENOMiHOG000272621.
HOVERGENiHBG051416.
InParanoidiQ91WZ8.
OMAiTVPYLPK.
OrthoDBiEOG72VH6B.
PhylomeDBiQ91WZ8.
TreeFamiTF332997.

Family and domain databases

InterProiIPR007531. Dysbindin.
[Graphical view]
PANTHERiPTHR16294. PTHR16294. 1 hit.
PfamiPF04440. Dysbindin. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q91WZ8-1) [UniParc]FASTAAdd to Basket

Also known as: Dysbindin 1-A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKGKPRTAP RLPKYSAGLE
60 70 80 90 100
LLSRYEDAWA ALHRRAKECA DAGELVDSEV VMLSAHWEKK RTSLNELQGQ
110 120 130 140 150
LQQLPALLQD LESLMASLAH LETSFEEVEN HLLHLEDLCG QCELERHKQA
160 170 180 190 200
QAQHLESYKK SKRKELEAFK AELDTEHTQK ALEMEHTQQL KLKERQKFFE
210 220 230 240 250
EAFQQDMEQY LSTGYLQIAE RREPMGSMSS MEVNVDVLEQ MDLMDISDQE
260 270 280 290 300
ALDVFLNSGG EDNIVMSPGV EMESNPNQNE MSLQIPSPSE SASQPPASPS
310 320 330 340 350
ACTDLDTADA PLIQSDEEEV QVDTALVTLH TDRKSTPGVS DDSDQCDSTQ

DI
Length:352
Mass (Da):39,651
Last modified:December 1, 2001 - v1
Checksum:iEE60FB10ECE95361
GO
Isoform 2 (identifier: Q91WZ8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     171-222: Missing.

Show »
Length:300
Mass (Da):33,323
Checksum:iD13F78AB2A09E4C8
GO
Isoform 3 (identifier: Q91WZ8-3) [UniParc]FASTAAdd to Basket

Also known as: Dysbindin 1-C

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Show »
Length:271
Mass (Da):30,582
Checksum:i71C7294BC4488139
GO

Sequence cautioni

The sequence AAH48682.1 differs from that shown. Reason: Frameshift at position 1.
The sequence BAE35265.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511A → T in BAE35265. (PubMed:16141072)Curated
Sequence conflicti280 – 2801E → G in BAE35265. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform 3. 1 PublicationVSP_021939Add
BLAST
Alternative sequencei171 – 22252Missing in isoform 2. 1 PublicationVSP_009024Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ404859 mRNA. Translation: CAC37976.1.
AY265461 mRNA. Translation: AAP91871.1.
AK010924 mRNA. Translation: BAB27270.2.
AK159656 mRNA. Translation: BAE35265.1. Different initiation.
BC018350 mRNA. Translation: AAH18350.1.
BC048682 mRNA. Translation: AAH48682.1. Frameshift.
BC058574 mRNA. Translation: AAH58574.1.
CCDSiCCDS36647.1. [Q91WZ8-1]
RefSeqiNP_080048.2. NM_025772.4. [Q91WZ8-1]
UniGeneiMm.352311.

Genome annotation databases

EnsembliENSMUST00000072329; ENSMUSP00000072170; ENSMUSG00000057531. [Q91WZ8-1]
GeneIDi94245.
KEGGimmu:94245.
UCSCiuc007qgw.1. mouse. [Q91WZ8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ404859 mRNA. Translation: CAC37976.1 .
AY265461 mRNA. Translation: AAP91871.1 .
AK010924 mRNA. Translation: BAB27270.2 .
AK159656 mRNA. Translation: BAE35265.1 . Different initiation.
BC018350 mRNA. Translation: AAH18350.1 .
BC048682 mRNA. Translation: AAH48682.1 . Frameshift.
BC058574 mRNA. Translation: AAH58574.1 .
CCDSi CCDS36647.1. [Q91WZ8-1 ]
RefSeqi NP_080048.2. NM_025772.4. [Q91WZ8-1 ]
UniGenei Mm.352311.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 220491. 3 interactions.
IntActi Q91WZ8. 4 interactions.
MINTi MINT-197141.

PTM databases

PhosphoSitei Q91WZ8.

Proteomic databases

MaxQBi Q91WZ8.
PaxDbi Q91WZ8.
PRIDEi Q91WZ8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072329 ; ENSMUSP00000072170 ; ENSMUSG00000057531 . [Q91WZ8-1 ]
GeneIDi 94245.
KEGGi mmu:94245.
UCSCi uc007qgw.1. mouse. [Q91WZ8-1 ]

Organism-specific databases

CTDi 84062.
MGIi MGI:2137586. Dtnbp1.

Phylogenomic databases

eggNOGi NOG81712.
GeneTreei ENSGT00390000010667.
HOGENOMi HOG000272621.
HOVERGENi HBG051416.
InParanoidi Q91WZ8.
OMAi TVPYLPK.
OrthoDBi EOG72VH6B.
PhylomeDBi Q91WZ8.
TreeFami TF332997.

Miscellaneous databases

ChiTaRSi DTNBP1. mouse.
NextBioi 352255.
PROi Q91WZ8.
SOURCEi Search...

Gene expression databases

Bgeei Q91WZ8.
CleanExi MM_DTNBP1.
ExpressionAtlasi Q91WZ8. baseline and differential.
Genevestigatori Q91WZ8.

Family and domain databases

InterProi IPR007531. Dysbindin.
[Graphical view ]
PANTHERi PTHR16294. PTHR16294. 1 hit.
Pfami PF04440. Dysbindin. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain."
    Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.
    J. Biol. Chem. 276:24232-24241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH DTNA AND DTNB, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Brain and Liver.
  2. "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)."
    Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P., Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A., Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W., Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.
    Nat. Genet. 35:84-89(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH DTNB; BLOC1S5 AND BLOC1S6, DISEASE.
    Strain: DBA/2J.
    Tissue: Kidney.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N-3.
    Tissue: Limb, Liver and Mammary tumor.
  5. "Sandy: a new mouse model for platelet storage pool deficiency."
    Swank R.T., Sweet H.O., Davisson M.T., Reddington M., Novak E.K.
    Genet. Res. 58:51-62(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  6. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Myospryn is a novel binding partner for dysbindin in muscle."
    Benson M.A., Tinsley C.L., Blake D.J.
    J. Biol. Chem. 279:10450-10458(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMYA5.
  8. "Reinvestigation of the dysbindin subunit of BLOC-1 (biogenesis of lysosome-related organelles complex-1) as a dystrobrevin-binding protein."
    Nazarian R., Starcevic M., Spencer M.J., Dell'Angelica E.C.
    Biochem. J. 395:587-598(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  9. "Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin."
    Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A., Kamins J., Hahn C.G., Blake D.J., Arnold S.E.
    Hum. Mol. Genet. 15:3041-3054(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SNAPIN.
  10. "BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein trafficking on endosomes."
    Di Pietro S.M., Falcon-Perez J.M., Tenza D., Setty S.R., Marks M.S., Raposo G., Dell'Angelica E.C.
    Mol. Biol. Cell 17:4027-4038(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "RNF151, a testis-specific RING finger protein, interacts with dysbindin."
    Nian H., Fan C., Liao S., Shi Y., Zhang K., Liu Y., Han C.
    Arch. Biochem. Biophys. 465:157-163(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF151, SUBCELLULAR LOCATION.
  13. "Behavioral abnormalities and dopamine reductions in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia."
    Hattori S., Murotani T., Matsuzaki S., Ishizuka T., Kumamoto N., Takeda M., Tohyama M., Yamatodani A., Kunugi H., Hashimoto R.
    Biochem. Biophys. Res. Commun. 373:298-302(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISEASE.
  14. "DTNBP1, a schizophrenia susceptibility gene, affects kinetics of transmitter release."
    Chen X.W., Feng Y.Q., Hao C.J., Guo X.L., He X., Zhou Z.Y., Guo N., Huang H.P., Xiong W., Zheng H., Zuo P.L., Zhang C.X., Li W., Zhou Z.
    J. Cell Biol. 181:791-801(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  15. "Impaired long-term memory retention and working memory in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia."
    Takao K., Toyama K., Nakanishi K., Hattori S., Takamura H., Takeda M., Miyakawa T., Hashimoto R.
    Mol. Brain 1:11-11(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  16. "Dysbindin-1 and its protein family with special attention to the potential role of dysbindin-1 in neuronal functions and the pathophysiology of schizophrenia."
    Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C., Arnold S.E.
    (In) Javitt D.C., Kantrowitz J. (eds.); Handbook of neurochemistry and molecular neurobiology (3rd ed.), pp.27:107-241, Springer Science, New York (2009)
    Cited for: REVIEW.
  17. Cited for: DISEASE, FUNCTION.
  18. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  19. "Neurobehavioral abnormalities in the dysbindin-1 mutant, sandy, on a C57BL/6J genetic background."
    Cox M.M., Tucker A.M., Tang J., Talbot K., Richer D.C., Yeh L., Arnold S.E.
    Genes Brain Behav. 8:390-397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  20. "The sandy (sdy) mouse: a dysbindin-1 mutant relevant to schizophrenia research."
    Talbot K.
    Prog. Brain Res. 179:87-94(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON DISEASE.
  21. "Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression."
    Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.
    J. Biol. Chem. 285:38630-38640(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, FUNCTION.
  22. "The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
    Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R., Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C., Dell'Angelica E.C.
    Mol. Psychiatry 15:204-215(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  23. "Direct interaction of dysbindin with the AP-3 complex via its mu subunit."
    Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K.
    Neurochem. Int. 54:431-438(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH THE AP-C COMPLEX, FUNCTION.
  24. "Dysfunction of dopamine release in the prefrontal cortex of dysbindin deficient sandy mice: an in vivo microdialysis study."
    Nagai T., Kitahara Y., Shiraki A., Hikita T., Taya S., Kaibuchi K., Yamada K.
    Neurosci. Lett. 470:134-138(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Dysbindin-1, a schizophrenia-related protein, functionally interacts with the DNA-dependent protein kinase complex in an isoform-dependent manner."
    Oyama S., Yamakawa H., Sasagawa N., Hosoi Y., Futai E., Ishiura S.
    PLoS ONE 4:E4199-E4199(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP3B2.
  26. "Role of dysbindin in dopamine receptor trafficking and cortical GABA function."
    Ji Y., Yang F., Papaleo F., Wang H.X., Gao W.J., Weinberger D.R., Lu B.
    Proc. Natl. Acad. Sci. U.S.A. 106:19593-19598(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
    Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
    Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, INTERACTION WITH PI4K2A.
  28. "Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-like behaviors via dopamine/D2 pathways."
    Papaleo F., Yang F., Garcia S., Chen J., Lu B., Crawley J.N., Weinberger D.R.
    Mol. Psychiatry 17:85-98(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  29. "The BLOS1-Interacting Protein KXD1 is Involved in the Biogenesis of Lysosome-Related Organelles."
    Yang Q., He X., Yang L., Zhou Z., Cullinane A.R., Wei A., Zhang Z., Hao Z., Zhang A., He M., Feng Y., Gao X., Gahl W.A., Huizing M., Li W.
    Traffic 13:1160-1169(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KXD1.

Entry informationi

Entry nameiDTBP1_MOUSE
AccessioniPrimary (citable) accession number: Q91WZ8
Secondary accession number(s): Q3TWK1
, Q6WXQ1, Q80ZN4, Q9CY43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3