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Q91WZ8

- DTBP1_MOUSE

UniProt

Q91WZ8 - DTBP1_MOUSE

Protein

Dysbindin

Gene

Dtnbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: UniProtKB

    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

    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 membrane Source: UniProtKB-SubCell
    8. growth cone Source: UniProtKB
    9. melanosome membrane Source: UniProtKB-SubCell
    10. neuron projection Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. plasma membrane Source: MGI
    13. postsynaptic density Source: UniProtKB
    14. postsynaptic membrane Source: UniProtKB-SubCell
    15. sarcolemma Source: UniProtKB
    16. sarcoplasm Source: MGI
    17. synaptic vesicle membrane Source: UniProtKB

    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

    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.
    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

    MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKGKPRTAP RLPKYSAGLE    50
    LLSRYEDAWA ALHRRAKECA DAGELVDSEV VMLSAHWEKK RTSLNELQGQ 100
    LQQLPALLQD LESLMASLAH LETSFEEVEN HLLHLEDLCG QCELERHKQA 150
    QAQHLESYKK SKRKELEAFK AELDTEHTQK ALEMEHTQQL KLKERQKFFE 200
    EAFQQDMEQY LSTGYLQIAE RREPMGSMSS MEVNVDVLEQ MDLMDISDQE 250
    ALDVFLNSGG EDNIVMSPGV EMESNPNQNE MSLQIPSPSE SASQPPASPS 300
    ACTDLDTADA PLIQSDEEEV QVDTALVTLH TDRKSTPGVS DDSDQCDSTQ 350
    DI 352
    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

    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.
    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

    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 1, 2014
    This is version 104 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