Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96EV8 (DTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DTNBP1
Synonyms:BLOC1S8
ORF Names:My031
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Associates with the BLOC-2 complex to facilitate the transport of TYRP1 independent of AP-3 function. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. Plays a role in the regulation of cell surface exposure of DRD2. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation. Appears to promote neuronal transmission and viability through regulating the expression of SNAP25 and SYN1, modulating PI3-kinase-Akt signaling and influencing glutamatergic release. Regulates the expression of SYN1 through binding to its promoter. Modulates prefrontal cortical activity via the dopamine/D2 pathway. Ref.8 Ref.11 Ref.12 Ref.13 Ref.18 Ref.22 Ref.23

Subunit structure

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 (Ref.10). 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. Ref.11 Ref.12 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26

Subcellular location

Isoform 1: Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; Cytoplasmic side. 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. Ref.9 Ref.10 Ref.11 Ref.19 Ref.21 Ref.23 Ref.25

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 butalso 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. Ref.9 Ref.10 Ref.11 Ref.19 Ref.21 Ref.23 Ref.25

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. Ref.9 Ref.10 Ref.11 Ref.19 Ref.21 Ref.23 Ref.25

Tissue specificity

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. Ref.9 Ref.10 Ref.25

Post-translational modification

Acetylated in the N-terminal.

Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1 degradation. Ref.19

Isoforms 1 and 2 highly phosphorylated by PRKDC in vitro. Isoform 3 only weakly phosphorylated by PRKDC in vitro. Ref.21

Involvement in disease

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. Ref.1

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 (Ref.8). Protein levels and expression are reduced in nerve terminals of the hippocampus and there is an increased release of glutamate in schizophrenic patients (Ref.9). 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 ofabout 60% (Ref.15).

Sequence similarities

Belongs to the dysbindin family.

Sequence caution

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

Ontologies

Keywords
   Biological processSensory transduction
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoplasmic vesicle
Endoplasmic reticulum
Endosome
Membrane
Nucleus
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseAlbinism
Hermansky-Pudlak syndrome
Schizophrenia
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

anterograde axon cargo transport

Inferred from sequence or structural similarity. Source: UniProtKB

anterograde synaptic vesicle transport

Inferred from sequence or structural similarity. Source: UniProtKB

blood coagulation

Inferred from electronic annotation. Source: Ensembl

melanosome organization

Non-traceable author statement Ref.26. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

neuron projection development

Inferred from direct assay Ref.10. Source: UniProtKB

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

platelet dense granule organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neurotransmitter secretion

Inferred from sequence or structural similarity. Source: UniProtKB

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

regulation of dopamine receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dopamine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentBLOC-1 complex

Inferred from direct assay PubMed 15102850Ref.26. Source: UniProtKB

axon

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from direct assay Ref.10. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic density

Inferred from direct assay Ref.10. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasm

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle membrane

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: Q96EV8-1)

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.
Note: Major isoform.
Isoform 2 (identifier: Q96EV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     272-351: PESSTCQNEI...TPDGGEDSDS → RVDKLALAEPGQYRCHSPPKVRRENHLPVTYA
Note: May be due to intron retention.
Isoform 3 (identifier: Q96EV8-3)

Also known as: Dysbindin 1-B;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Dysbindin
PRO_0000191001

Regions

Region173 – 331159Dysbindin
Region243 – 25614Nuclear export signal
Coiled coil88 – 18194 Potential

Amino acid modifications

Modified residue311N6-acetyllysine
Modified residue331N6-acetyllysine
Modified residue351N6-acetyllysine
Modified residue3161Phosphoserine Ref.14 Ref.16
Modified residue3211Phosphoserine Ref.14 Ref.16

Natural variations

Alternative sequence1 – 8181Missing in isoform 3.
VSP_046062
Alternative sequence272 – 35180PESST…EDSDS → RVDKLALAEPGQYRCHSPPK VRRENHLPVTYA in isoform 2.
VSP_009023
Natural variant2141G → D.
Corresponds to variant rs16876589 [ dbSNP | Ensembl ].
VAR_053069
Natural variant2721P → S.
Corresponds to variant rs17470454 [ dbSNP | Ensembl ].
VAR_029644

Experimental info

Mutagenesis2151Y → A: Reduced interaction with AP3M1. Ref.20
Mutagenesis243 – 25614LMDIS…LDVFL → AMDASDQEAADVFA: Abolishes cytoplasmic location. Increased expression of SYN1. Ref.23
Sequence conflict2421D → V in CAB66572. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Dysbindin 1-A) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0504C86E12B66C08

FASTA35139,493
        10         20         30         40         50         60 
MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKSKPRTVP FLPKYSAGLE LLSRYEDTWA 

        70         80         90        100        110        120 
ALHRRAKDCA SAGELVDSEV VMLSAHWEKK KTSLVELQEQ LQQLPALIAD LESMTANLTH 

       130        140        150        160        170        180 
LEASFEEVEN NLLHLEDLCG QCELERCKHM QSQQLENYKK NKRKELETFK AELDAEHAQK 

       190        200        210        220        230        240 
VLEMEHTQQM KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPIGSMSS MEVNVDMLEQ 

       250        260        270        280        290        300 
MDLMDISDQE ALDVFLNSGG EENTVLSPAL GPESSTCQNE ITLQVPNPSE LRAKPPSSSS 

       310        320        330        340        350 
TCTDSATRDI SEGGESPVVQ SDEEEVQVDT ALATSHTDRE ATPDGGEDSD S 

« Hide

Isoform 2 [UniParc].

Checksum: 7AF6611B9F6D46BD
Show »

FASTA30334,831
Isoform 3 (Dysbindin 1-B) [UniParc].

Checksum: C945FAB1BB01B410
Show »

FASTA27030,387

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Evidence of novel neuronal functions of dysbindin, a susceptibility gene for schizophrenia."
Numakawa T., Yagasaki Y., Ishimoto T., Okada T., Suzuki T., Iwata N., Ozaki N., Taguchi T., Tatsumi M., Kamijima K., Straub R.E., Weinberger D.R., Kunugi H., Hashimoto R.
Hum. Mol. Genet. 13:2699-2708(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Dysbindin engages in c-Jun N-terminal kinase activity and cytoskeletal organization."
Kubota K., Kumamoto N., Matsuzaki S., Hashimoto R., Hattori T., Okuda H., Takamura H., Takeda M., Katayama T., Tohyama M.
Biochem. Biophys. Res. Commun. 379:191-195(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"TRIM32 is an E3 ubiquitin ligase for dysbindin."
Locke M., Tinsley C.L., Benson M.A., Blake D.J.
Hum. Mol. Genet. 18:2344-2358(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001258596.1. NM_001271667.1.
NP_001258597.1. NM_001271668.1.
NP_001258598.1. NM_001271669.1.
NP_115498.2. NM_032122.4.
NP_898861.1. NM_183040.2.
UniGeneHs.571148.

3D structure databases

ProteinModelPortalQ96EV8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123857. 39 interactions.
IntActQ96EV8. 32 interactions.
MINTMINT-1438666.
STRING9606.ENSP00000341680.

PTM databases

PhosphoSiteQ96EV8.

Polymorphism databases

DMDM38604971.

Proteomic databases

PaxDbQ96EV8.
PRIDEQ96EV8.

Protocols and materials databases

DNASU84062.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338950; ENSP00000344718; ENSG00000047579. [Q96EV8-2]
ENST00000344537; ENSP00000341680; ENSG00000047579. [Q96EV8-1]
GeneID84062.
KEGGhsa:84062.
UCSCuc003nbl.3. human. [Q96EV8-1]
uc003nbp.3. human. [Q96EV8-2]

Organism-specific databases

CTD84062.
GeneCardsGC06M015470.
HGNCHGNC:17328. DTNBP1.
HPAHPA028053.
HPA029615.
HPA029616.
MIM607145. gene.
614076. phenotype.
neXtProtNX_Q96EV8.
Orphanet231531. Hermansky-Pudlak syndrome type 7.
PharmGKBPA27512.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81712.
HOGENOMHOG000272621.
HOVERGENHBG051416.
OMATVPYLPK.
OrthoDBEOG72VH6B.
PhylomeDBQ96EV8.
TreeFamTF332997.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ96EV8.
BgeeQ96EV8.
CleanExHS_DTNBP1.
GenevestigatorQ96EV8.

Family and domain databases

InterProIPR007531. Dysbindin.
[Graphical view]
PANTHERPTHR16294. PTHR16294. 1 hit.
PfamPF04440. Dysbindin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDysbindin.
GenomeRNAi84062.
NextBio73219.
PROQ96EV8.
SOURCESearch...

Entry information

Entry nameDTBP1_HUMAN
AccessionPrimary (citable) accession number: Q96EV8
Secondary accession number(s): A8K3V3 expand/collapse secondary AC list , Q5THY3, Q5THY4, Q96NV2, Q9H0U2, Q9H3J5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM