Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96EV8

- DTBP1_HUMAN

UniProt

Q96EV8 - DTBP1_HUMAN

Protein

Dysbindin

Gene

DTNBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.7 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: Ensembl
    5. melanosome organization Source: UniProtKB
    6. membrane organization Source: Reactome
    7. neuron projection development Source: UniProtKB
    8. neuron projection morphogenesis Source: UniProtKB
    9. platelet dense granule organization Source: Ensembl
    10. positive regulation of gene expression Source: UniProtKB
    11. positive regulation of neurotransmitter secretion Source: UniProtKB
    12. post-Golgi vesicle-mediated transport Source: Reactome
    13. regulation of dopamine receptor signaling pathway Source: UniProtKB
    14. regulation of dopamine secretion Source: UniProtKB

    Keywords - Biological processi

    Sensory transduction

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

    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
    Short name:
    HPS7 protein
    Gene namesi
    Name:DTNBP1
    Synonyms:BLOC1S8
    ORF Names:My031
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17328. DTNBP1.

    Subcellular locationi

    Isoform 1 : Cytoplasm 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Melanosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density 1 Publication. Endoplasmic reticulum By similarity. Nucleus 1 Publication
    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. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules.
    Isoform 2 : Cytoplasm 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Melanosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctionsynapsepostsynaptic cell membrane 1 Publication. Endoplasmic reticulum By similarity. Nucleus 1 Publication
    Note: 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. Mainly expressed in the dendritic spine. Predominantly a synaptic vesicle isoform but also highly expressed in the nucleus. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals.
    Isoform 3 : Cytoplasm 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Melanosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctionsynapsepostsynaptic cell membrane 1 Publication. Endoplasmic reticulum By similarity
    Note: Exclusivley cytoplasmic. Predominantly found in the postsynaptic density (PSD). Little association with synaptic vesicles. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals.

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. BLOC-1 complex Source: UniProtKB
    3. cell junction Source: UniProtKB-KW
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: Reactome
    6. dendritic spine Source: UniProtKB
    7. endoplasmic reticulum membrane Source: UniProtKB
    8. endosome membrane Source: UniProtKB-SubCell
    9. growth cone Source: UniProtKB
    10. melanosome membrane Source: UniProtKB-SubCell
    11. neuron projection Source: UniProtKB
    12. nucleus Source: UniProtKB
    13. postsynaptic density Source: UniProtKB
    14. postsynaptic membrane Source: UniProtKB-SubCell
    15. sarcolemma Source: UniProtKB
    16. sarcoplasm Source: Ensembl
    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

    Hermansky-Pudlak syndrome 7 (HPS7) [MIM:614076]: A form of Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal recessive disorder characterized by oculocutaneous albinism, bleeding due to platelet storage pool deficiency, and lysosomal storage defects. This syndrome results from defects of diverse cytoplasmic organelles including melanosomes, platelet dense granules and lysosomes. Ceroid storage in the lungs is associated with pulmonary fibrosis, a common cause of premature death in individuals with HPS.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Defects in DTNBP1 are associated with susceptibility to schizophrenia, a mental disorder characterized by a breakdown of thought processes and by poor emotional responsiveness. Genetic mutations lead to alterations in the glutamatergic transmisssion in the brain and modified Akt signaling (PubMed:15345706). Protein levels and expression are reduced in nerve terminals of the hippocampus and there is an increased release of glutamate in schizophrenic patients (PubMed:15124027). Levels of isoform 1 are reduced in the pSTG, but not in HF, by about 48% in 92% of schizophrenic patients. In the HF, there is an average of 33% reduction in synaptic expression of isoform 2 in 67% of cases, and of isoform 3, an average reduction of 35% in 80% of cases. In the dorsolateral prefrontal cortex (DLPFC), significant reductions in levels of isoform 3 are observed about 71% of schizophrenic patients showed an average reduction of this isoform of about 60% (PubMed:19617633).3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151Y → A: Reduced interaction with AP3M1. 2 Publications
    Mutagenesisi243 – 25614LMDIS…LDVFL → AMDASDQEAADVFA: Abolishes cytoplasmic location. Increased expression of SYN1. 1 PublicationAdd
    BLAST

    Keywords - Diseasei

    Albinism, Hermansky-Pudlak syndrome, Schizophrenia

    Organism-specific databases

    MIMi614076. phenotype.
    Orphaneti231531. Hermansky-Pudlak syndrome type 7.
    PharmGKBiPA27512.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351DysbindinPRO_0000191001Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei316 – 3161Phosphoserine3 Publications
    Modified residuei321 – 3211Phosphoserine3 Publications

    Post-translational modificationi

    Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation.1 Publication
    Isoforms 1 and 2 highly phosphorylated by PRKDC in vitro. Isoform 3 only weakly phosphorylated by PRKDC in vitro.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96EV8.
    PaxDbiQ96EV8.
    PRIDEiQ96EV8.

    PTM databases

    PhosphoSiteiQ96EV8.

    Expressioni

    Tissue specificityi

    Detected in brain, in neurons and in neuropil. Isoform 1 is expressed in the cerebral cortex, and hippocampal frontal (HF). Specific expression in the posterior half of the superior temporal gyrus (pSTG). Higher expression of isoform 2 and 3 in the HF than in the pSTG while isoform 1 shows no difference in expression in these areas. In the HF, detected in dentate gyrus (DG) and in pyramidal cells of hippocampus CA2 and CA3 (at protein level). Expressed in all principal neuronal populations of the HF, namely pyramidal neurons in the subiculum and CA1-3, granule cells in the dense cell layer of the DG (DGg), and polymorph cells in the hilus of the DG (DGh). Maximal levels in CA2, CA3, and DGh. Isoform 2 not expressed in the cerebral cortex.1 Publication

    Gene expression databases

    ArrayExpressiQ96EV8.
    BgeeiQ96EV8.
    CleanExiHS_DTNBP1.
    GenevestigatoriQ96EV8.

    Organism-specific databases

    HPAiHPA028053.
    HPA029615.
    HPA029616.

    Interactioni

    Subunit structurei

    Interacts (via its coiled coil domain) with KXD1. Interacts with CMYA5, PI4K2 and RNF151 By similarity. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of at least BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly in the complex with BLOC1S5, BLOC1S6 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:16980328). 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 AP3M1, AP3B2 and TRIM32. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLOC1S1P785373EBI-465804,EBI-348630
    BLOC1S2Q6QNY16EBI-465804,EBI-465872
    BLOC1S3Q6QNY03EBI-465804,EBI-465930
    BLOC1S5Q8TDH93EBI-465804,EBI-465861
    BLOC1S6Q9UL456EBI-465804,EBI-465781
    SNAPINO952954EBI-465804,EBI-296723

    Protein-protein interaction databases

    BioGridi123857. 39 interactions.
    IntActiQ96EV8. 32 interactions.
    MINTiMINT-1438666.
    STRINGi9606.ENSP00000341680.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96EV8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 331159DysbindinAdd
    BLAST
    Regioni243 – 25614Nuclear export signalAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili88 – 18194Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the dysbindin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG81712.
    HOGENOMiHOG000272621.
    HOVERGENiHBG051416.
    OMAiTVPYLPK.
    OrthoDBiEOG72VH6B.
    PhylomeDBiQ96EV8.
    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 and alternative initiation. Align

    Isoform 1 (identifier: Q96EV8-1) [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 KVKSKPRTVP FLPKYSAGLE    50
    LLSRYEDTWA ALHRRAKDCA SAGELVDSEV VMLSAHWEKK KTSLVELQEQ 100
    LQQLPALIAD LESMTANLTH LEASFEEVEN NLLHLEDLCG QCELERCKHM 150
    QSQQLENYKK NKRKELETFK AELDAEHAQK VLEMEHTQQM KLKERQKFFE 200
    EAFQQDMEQY LSTGYLQIAE RREPIGSMSS MEVNVDMLEQ MDLMDISDQE 250
    ALDVFLNSGG EENTVLSPAL GPESSTCQNE ITLQVPNPSE LRAKPPSSSS 300
    TCTDSATRDI SEGGESPVVQ SDEEEVQVDT ALATSHTDRE ATPDGGEDSD 350
    S 351

    Note: Major isoform.

    Length:351
    Mass (Da):39,493
    Last modified:December 1, 2001 - v1
    Checksum:i0504C86E12B66C08
    GO
    Isoform 2 (identifier: Q96EV8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         272-351: PESSTCQNEI...TPDGGEDSDS → RVDKLALAEPGQYRCHSPPKVRRENHLPVTYA

    Note: May be due to intron retention.

    Show »
    Length:303
    Mass (Da):34,831
    Checksum:i7AF6611B9F6D46BD
    GO
    Isoform 3 (identifier: Q96EV8-3) [UniParc]FASTAAdd to Basket

    Also known as: Dysbindin 1-B

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

    Show »
    Length:270
    Mass (Da):30,387
    Checksum:iC945FAB1BB01B410
    GO

    Sequence cautioni

    The sequence AAG43145.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti242 – 2421D → V in CAB66572. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141G → D.
    Corresponds to variant rs16876589 [ dbSNP | Ensembl ].
    VAR_053069
    Natural varianti272 – 2721P → S.
    Corresponds to variant rs17470454 [ dbSNP | Ensembl ].
    VAR_029644

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform 3. CuratedVSP_046062Add
    BLAST
    Alternative sequencei272 – 35180PESST…EDSDS → RVDKLALAEPGQYRCHSPPK VRRENHLPVTYA in isoform 2. 2 PublicationsVSP_009023Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY265460 mRNA. Translation: AAP91870.1.
    AF394226 mRNA. Translation: AAL46636.1.
    AL136637 mRNA. Translation: CAB66572.1.
    AK054593 mRNA. Translation: BAB70770.1.
    AK290718 mRNA. Translation: BAF83407.1.
    AL022343, AL021978 Genomic DNA. Translation: CAI21976.1.
    AL022343, AL021978 Genomic DNA. Translation: CAI21977.1.
    AL021978, AL022343 Genomic DNA. Translation: CAI42339.1.
    AL021978, AL022343 Genomic DNA. Translation: CAI42340.1.
    BC011912 mRNA. Translation: AAH11912.1.
    AF061734 mRNA. Translation: AAG43145.1. Different initiation.
    CCDSiCCDS4534.1. [Q96EV8-1]
    CCDS4535.1. [Q96EV8-2]
    RefSeqiNP_001258596.1. NM_001271667.1. [Q96EV8-3]
    NP_001258597.1. NM_001271668.1.
    NP_001258598.1. NM_001271669.1.
    NP_115498.2. NM_032122.4. [Q96EV8-1]
    NP_898861.1. NM_183040.2. [Q96EV8-2]
    UniGeneiHs.571148.

    Genome annotation databases

    EnsembliENST00000338950; ENSP00000344718; ENSG00000047579. [Q96EV8-2]
    ENST00000344537; ENSP00000341680; ENSG00000047579. [Q96EV8-1]
    GeneIDi84062.
    KEGGihsa:84062.
    UCSCiuc003nbl.3. human. [Q96EV8-1]
    uc003nbp.3. human. [Q96EV8-2]

    Polymorphism databases

    DMDMi38604971.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY265460 mRNA. Translation: AAP91870.1 .
    AF394226 mRNA. Translation: AAL46636.1 .
    AL136637 mRNA. Translation: CAB66572.1 .
    AK054593 mRNA. Translation: BAB70770.1 .
    AK290718 mRNA. Translation: BAF83407.1 .
    AL022343 , AL021978 Genomic DNA. Translation: CAI21976.1 .
    AL022343 , AL021978 Genomic DNA. Translation: CAI21977.1 .
    AL021978 , AL022343 Genomic DNA. Translation: CAI42339.1 .
    AL021978 , AL022343 Genomic DNA. Translation: CAI42340.1 .
    BC011912 mRNA. Translation: AAH11912.1 .
    AF061734 mRNA. Translation: AAG43145.1 . Different initiation.
    CCDSi CCDS4534.1. [Q96EV8-1 ]
    CCDS4535.1. [Q96EV8-2 ]
    RefSeqi NP_001258596.1. NM_001271667.1. [Q96EV8-3 ]
    NP_001258597.1. NM_001271668.1.
    NP_001258598.1. NM_001271669.1.
    NP_115498.2. NM_032122.4. [Q96EV8-1 ]
    NP_898861.1. NM_183040.2. [Q96EV8-2 ]
    UniGenei Hs.571148.

    3D structure databases

    ProteinModelPortali Q96EV8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123857. 39 interactions.
    IntActi Q96EV8. 32 interactions.
    MINTi MINT-1438666.
    STRINGi 9606.ENSP00000341680.

    PTM databases

    PhosphoSitei Q96EV8.

    Polymorphism databases

    DMDMi 38604971.

    Proteomic databases

    MaxQBi Q96EV8.
    PaxDbi Q96EV8.
    PRIDEi Q96EV8.

    Protocols and materials databases

    DNASUi 84062.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338950 ; ENSP00000344718 ; ENSG00000047579 . [Q96EV8-2 ]
    ENST00000344537 ; ENSP00000341680 ; ENSG00000047579 . [Q96EV8-1 ]
    GeneIDi 84062.
    KEGGi hsa:84062.
    UCSCi uc003nbl.3. human. [Q96EV8-1 ]
    uc003nbp.3. human. [Q96EV8-2 ]

    Organism-specific databases

    CTDi 84062.
    GeneCardsi GC06M015470.
    GeneReviewsi DTNBP1.
    HGNCi HGNC:17328. DTNBP1.
    HPAi HPA028053.
    HPA029615.
    HPA029616.
    MIMi 607145. gene.
    614076. phenotype.
    neXtProti NX_Q96EV8.
    Orphaneti 231531. Hermansky-Pudlak syndrome type 7.
    PharmGKBi PA27512.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81712.
    HOGENOMi HOG000272621.
    HOVERGENi HBG051416.
    OMAi TVPYLPK.
    OrthoDBi EOG72VH6B.
    PhylomeDBi Q96EV8.
    TreeFami TF332997.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    GeneWikii Dysbindin.
    GenomeRNAii 84062.
    NextBioi 73219.
    PROi Q96EV8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96EV8.
    Bgeei Q96EV8.
    CleanExi HS_DTNBP1.
    Genevestigatori Q96EV8.

    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. "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 1), INVOLVEMENT IN HPS7.
      Tissue: Placenta.
    2. "Localization and identification of a human DTNBP1 gene from a putative schizophrenia susceptibility locus on 6p22.3 by in silico cloning."
      Jiang Y., Straub R.E., Sullivan P.F., Chen X., O'Neill F.A., Walsh D., Kendler K.S., Riley B.P.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Lung and Neuroblastoma.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Muscle.
    7. Mao Y.M., Xie Y., Ying K.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-351 (ISOFORM 1).
      Tissue: Fetal brain.
    8. Cited for: ASSOCIATION WITH SCHIZOPHRENIA, FUNCTION.
    9. "Dysbindin-1 is reduced in intrinsic, glutamatergic terminals of the hippocampal formation in schizophrenia."
      Talbot K., Eidem W.L., Tinsley C.L., Benson M.A., Thompson E.W., Smith R.J., Hahn C.G., Siegel S.J., Trojanowski J.Q., Gur R.E., Blake D.J., Arnold S.E.
      J. Clin. Invest. 113:1353-1363(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION.
    10. "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.
    11. "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.
    12. "BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles."
      Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C., Dell'Angelica E.C., Raposo G., Marks M.S.
      Mol. Biol. Cell 18:768-780(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, FUNCTION.
    13. "Evidence that the BLOC-1 protein dysbindin modulates dopamine D2 receptor internalization and signaling but not D1 internalization."
      Iizuka Y., Sei Y., Weinberger D.R., Straub R.E.
      J. Neurosci. 27:12390-12395(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Dysbindin-1 in dorsolateral prefrontal cortex of schizophrenia cases is reduced in an isoform-specific manner unrelated to dysbindin-1 mRNA expression."
      Tang J., LeGros R.P., Louneva N., Yeh L., Cohen J.W., Hahn C.G., Blake D.J., Arnold S.E., Talbot K.
      Hum. Mol. Genet. 18:3851-3863(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH SCHIZOPHRENIA.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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.
    18. Cited for: FUNCTION.
    19. Cited for: INTERACTION WITH TRIM32, SUBCELLULAR LOCATION, UBIQUITINATION.
    20. "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: INTERACTION WITH AP3M1, MUTAGENESIS OF TYR-215.
    21. "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: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), INTERACTION WITH AP3B2; XRCC5 AND XRCC6 IN THE DNA-DEPENDENT PROTEIN KINASE COMPLEX DNA-PK, PHOSPHORYLATION.
    22. "DTNBP1 (dysbindin) gene variants modulate prefrontal brain function in schizophrenic patients--support for the glutamate hypothesis of schizophrenias."
      Fallgatter A.J., Ehlis A.C., Herrmann M.J., Hohoff C., Reif A., Freitag C.M., Deckert J.
      Genes Brain Behav. 9:489-497(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH SCHIZOPHRENIA, FUNCTION.
    23. "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: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH XPO1, MUTAGENESIS OF 243-LEU--LEU-256.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Synaptic dysbindin-1 reductions in schizophrenia occur in an isoform-specific manner indicating their subsynaptic location."
      Talbot K., Louneva N., Cohen J.W., Kazi H., Blake D.J., Arnold S.E.
      PLoS ONE 6:E16886-E16886(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
    26. "Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1)."
      Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C., Bonifacino J.S., Hurley J.H.
      J. Biol. Chem. 287:5882-5890(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, COMPOSITION OF THE BLOC-1 COMPLEX.

    Entry informationi

    Entry nameiDTBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q96EV8
    Secondary accession number(s): A8K3V3
    , Q5THY3, Q5THY4, Q96NV2, Q9H0U2, Q9H3J5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3