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Q96EV8

- DTBP1_HUMAN

UniProt

Q96EV8 - DTBP1_HUMAN

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Protein
Dysbindin
Gene
DTNBP1, BLOC1S8, My031
Organism
Homo sapiens (Human)
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.7 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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. 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. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules.7 Publications
Isoform 2 : Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junctionsynapsepostsynaptic cell membrane. Endoplasmic reticulum By similarity. Nucleus
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.7 Publications
Isoform 3 : Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; 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. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals.7 Publications

GO - Cellular componenti

  1. BLOC-1 complex Source: UniProtKB
  2. axon 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
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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 (1 Publication). Protein levels and expression are reduced in nerve terminals of the hippocampus and there is an increased release of glutamate in schizophrenic patients (1 Publication). 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% (1 Publication).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151Y → A: Reduced interaction with AP3M1. 1 Publication
Mutagenesisi243 – 25614LMDIS…LDVFL → AMDASDQEAADVFA: Abolishes cytoplasmic location. Increased expression of SYN1. 1 Publication
Add
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 – 351351Dysbindin
PRO_0000191001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161Phosphoserine2 Publications
Modified residuei321 – 3211Phosphoserine2 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.1 Publication

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.3 Publications

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 (1 Publication). 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.7 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 331159Dysbindin
Add
BLAST
Regioni243 – 25614Nuclear export signal
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili88 – 18194 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the dysbindin family.

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.

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.
VSP_046062Add
BLAST
Alternative sequencei272 – 35180PESST…EDSDS → RVDKLALAEPGQYRCHSPPK VRRENHLPVTYA in isoform 2.
VSP_009023Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421D → V in CAB66572. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

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