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Q91WZ8 (DTBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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 homolog
Short name=HPS7 protein homolog
Gene names
Name:Dtnbp1
Synonyms:Bloc1s8, Sdy
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length352 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.2 Ref.6 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28

Subunit structure

Interacts with AP3M1 and TRIM32. Interacts (isoform 1 and isoform 2 only) with the DNA-dependent protein kinase complex DNA-PK; the interaction phosphorylates DTNBP1 in vitro. Interacts directly in this complex with XRCC5 and XRCC6. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus By similarity. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. This BLOC-1 complex also associates with the BLOC-2 complex in endosomes. Binds to DTNA and DTNB but may not be a physiological binding partner (Ref.8 and Ref.9). Interacts (via its coiled coil domain) with KXD1. Interacts with AP3B2, BLOC1S5, BLOC1S6, CMYA5, PI4K2, RNF151 and SNAPIN/BLOC1S8. Interacts with XPO1; the interaction exports DTNBP1 out of the nucleus. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.22 Ref.23 Ref.25 Ref.27 Ref.29

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 By similarity. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. Associated with the AP-3 complex at presynaptic terminals. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.22

Isoform 3: Cytoplasm. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. 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 By similarity. The BLOC-1 complex associates with the BLOC-2 complex in early endosome-associated tubules. vesicle membranes and microtubules. Associated with the AP-3 complex at presynaptic terminals. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.22

Tissue specificity

Detected in brain, in hippocampus and dentate gyrus neurons. Detected at axon bundles and axon terminals, notably in the cerebellum and hippocampus. Detected in neuropil in hippocampus, lateral septum, basal ganglia and substantia nigra. Highly expressed in pyramidal cells of hippocampus CA2 and CA3. Detected at the heart and skeletal muscle sarcolemma (at protein level). Ubiquitously expressed. The highest expression is observed in testis, liver, kidney, brain, heart and lung. Expressed at lower levels in stomach and small intestine. Ref.1 Ref.2 Ref.9 Ref.11 Ref.22 Ref.23

Post-translational modification

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

Involvement in disease

Defects in Dtnbp1 are the cause of the sandy (sdy) mutant phenotype, a model for human Hermansky-Pudlak syndrome (HPS). Sdy mice lack dysbindin expression; they have a characteristic sandy coat color and have much fewer melanosomes in the retinal pigment epithelium and choroid. They are fully viable, but present behavioral abnormalities. They have prolonged bleeding times due to platelet storage pool deficiency, and lysosomal storage defects. The number of electron-opaque platelet dense granules is severely reduced, and the platelet serotonin content is strongly reduced. Secretion of lysosomal enzymes from kidney and from thrombin-stimulated platelets is depressed 2- and 3-fold, and ceroid pigment is present in kidney. Sandy mice also display impaired long-term memory retention and working memory and schizophrenia-like behavioral abnormalities. Vesicle morphology and kinetics of transmitter release are affected in both neuroendocrine cells and hippocampal synapses, characterized by larger vesicle size, slower quantal release, fewer release events and reduced readily releasable pool (RRP). Expression levels of SYN1 are lower in both the cortex and the hippocampal formation (HF). Ref.2 Ref.5 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.21

Disruption phenotype

Null mice exhibit cognitive abnormalities including schizophrenia-related behaviors such as impaired working memory under stressful conditions. There is higher acoustic startle reactivity to stimuli. Pyramidal neurons are hypoexcitable on dopamine-2 receptor stimulation. There is reduced expression of Ca2+/calmodulin-dependent protein kinase II (CaMKII) and CaMKKbeta in the medial prefrontal cortex mPFC. There is increased expression levels of cell surface dopamine receptor D2 in cortical neurons. Expression levels of SYN1 are lower in both cortex and in the hippocampal formation (HF). Ref.6 Ref.18 Ref.28

Sequence similarities

Belongs to the dysbindin family.

Sequence caution

The sequence AAH48682.1 differs from that shown. Reason: Frameshift at position 1.

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

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 splicing
   DiseaseAlbinism
Hermansky-Pudlak syndrome
   DomainCoiled coil
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay Ref.9. Source: UniProtKB

anterograde axon cargo transport

Inferred from mutant phenotype Ref.27. Source: UniProtKB

anterograde synaptic vesicle transport

Inferred from mutant phenotype Ref.27. Source: UniProtKB

blood coagulation

Inferred from mutant phenotype Ref.5. Source: MGI

muscle organ development

Traceable author statement Ref.1. Source: MGI

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection morphogenesis

Inferred from direct assay Ref.9. Source: UniProtKB

organelle organization

Inferred from direct assay Ref.2. Source: UniProtKB

platelet dense granule organization

Inferred from mutant phenotype Ref.5. Source: MGI

positive regulation of gene expression

Inferred from direct assay Ref.21. Source: UniProtKB

positive regulation of neurotransmitter secretion

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of dopamine receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dopamine secretion

Inferred from mutant phenotype Ref.26. Source: UniProtKB

   Cellular_componentBLOC-1 complex

Inferred from direct assay PubMed 17182842Ref.22. Source: UniProtKB

axon

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

dendritic spine

Inferred from direct assay Ref.9. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.9. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from direct assay Ref.9. Source: UniProtKB

melanosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.1. Source: MGI

postsynaptic density

Inferred from direct assay Ref.9. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay Ref.1. Source: UniProtKB

sarcoplasm

Inferred from direct assay Ref.7. Source: MGI

synaptic vesicle membrane

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.1Ref.2Ref.9Ref.21Ref.27Ref.29. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cmya5Q70KF45EBI-643186,EBI-782290
DtnaQ9D2N43EBI-643186,EBI-296019

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91WZ8-1)

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.
Isoform 2 (identifier: Q91WZ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     171-222: Missing.
Isoform 3 (identifier: Q91WZ8-3)

Also known as: Dysbindin 1-C;

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 – 352352Dysbindin
PRO_0000191002

Regions

Region173 – 325153Dysbindin
Region243 – 25614Nuclear export signal By similarity
Coiled coil88 – 17689 Potential

Amino acid modifications

Modified residue3151Phosphoserine By similarity

Natural variations

Alternative sequence1 – 8181Missing in isoform 3.
VSP_021939
Alternative sequence171 – 22252Missing in isoform 2.
VSP_009024

Experimental info

Sequence conflict2511A → T in BAE35265. Ref.3
Sequence conflict2801E → G in BAE35265. Ref.3

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: EE60FB10ECE95361

FASTA35239,651
        10         20         30         40         50         60 
MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKGKPRTAP RLPKYSAGLE LLSRYEDAWA 

        70         80         90        100        110        120 
ALHRRAKECA DAGELVDSEV VMLSAHWEKK RTSLNELQGQ LQQLPALLQD LESLMASLAH 

       130        140        150        160        170        180 
LETSFEEVEN HLLHLEDLCG QCELERHKQA QAQHLESYKK SKRKELEAFK AELDTEHTQK 

       190        200        210        220        230        240 
ALEMEHTQQL KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPMGSMSS MEVNVDVLEQ 

       250        260        270        280        290        300 
MDLMDISDQE ALDVFLNSGG EDNIVMSPGV EMESNPNQNE MSLQIPSPSE SASQPPASPS 

       310        320        330        340        350 
ACTDLDTADA PLIQSDEEEV QVDTALVTLH TDRKSTPGVS DDSDQCDSTQ DI 

« Hide

Isoform 2 [UniParc].

Checksum: D13F78AB2A09E4C8
Show »

FASTA30033,323
Isoform 3 (Dysbindin 1-C) [UniParc].

Checksum: 71C7294BC4488139
Show »

FASTA27130,582

References

« Hide 'large scale' references
[1]"Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain."
Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.
J. Biol. Chem. 276:24232-24241(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH DTNA AND DTNB, SUBCELLULAR LOCATION.
Strain: C57BL/6J.
Tissue: Brain and Liver.
[2]"Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)."
Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P., Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A., Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W., Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.
Nat. Genet. 35:84-89(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH DTNB; BLOC1S5 AND BLOC1S6, DISEASE.
Strain: DBA/2J.
Tissue: Kidney.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Limb, Liver and Mammary tumor.
[5]"Sandy: a new mouse model for platelet storage pool deficiency."
Swank R.T., Sweet H.O., Davisson M.T., Reddington M., Novak E.K.
Genet. Res. 58:51-62(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[6]"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: DISRUPTION PHENOTYPE, FUNCTION.
[7]"Myospryn is a novel binding partner for dysbindin in muscle."
Benson M.A., Tinsley C.L., Blake D.J.
J. Biol. Chem. 279:10450-10458(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CMYA5.
[8]"Reinvestigation of the dysbindin subunit of BLOC-1 (biogenesis of lysosome-related organelles complex-1) as a dystrobrevin-binding protein."
Nazarian R., Starcevic M., Spencer M.J., Dell'Angelica E.C.
Biochem. J. 395:587-598(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[9]"Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin."
Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A., Kamins J., Hahn C.G., Blake D.J., Arnold S.E.
Hum. Mol. Genet. 15:3041-3054(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SNAPIN.
[10]"BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein trafficking on endosomes."
Di Pietro S.M., Falcon-Perez J.M., Tenza D., Setty S.R., Marks M.S., Raposo G., Dell'Angelica E.C.
Mol. Biol. Cell 17:4027-4038(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[11]"BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes."
Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M., Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E., Faundez V.
Mol. Biol. Cell 17:4014-4026(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"RNF151, a testis-specific RING finger protein, interacts with dysbindin."
Nian H., Fan C., Liao S., Shi Y., Zhang K., Liu Y., Han C.
Arch. Biochem. Biophys. 465:157-163(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF151, SUBCELLULAR LOCATION.
[13]"Behavioral abnormalities and dopamine reductions in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia."
Hattori S., Murotani T., Matsuzaki S., Ishizuka T., Kumamoto N., Takeda M., Tohyama M., Yamatodani A., Kunugi H., Hashimoto R.
Biochem. Biophys. Res. Commun. 373:298-302(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISEASE.
[14]"DTNBP1, a schizophrenia susceptibility gene, affects kinetics of transmitter release."
Chen X.W., Feng Y.Q., Hao C.J., Guo X.L., He X., Zhou Z.Y., Guo N., Huang H.P., Xiong W., Zheng H., Zuo P.L., Zhang C.X., Li W., Zhou Z.
J. Cell Biol. 181:791-801(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, FUNCTION.
[15]"Impaired long-term memory retention and working memory in sdy mutant mice with a deletion in Dtnbp1, a susceptibility gene for schizophrenia."
Takao K., Toyama K., Nakanishi K., Hattori S., Takamura H., Takeda M., Miyakawa T., Hashimoto R.
Mol. Brain 1:11-11(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[16]"Dysbindin-1 and its protein family with special attention to the potential role of dysbindin-1 in neuronal functions and the pathophysiology of schizophrenia."
Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C., Arnold S.E.
(In) Javitt D.C., Kantrowitz J. (eds.); Handbook of neurochemistry and molecular neurobiology (3rd ed.), pp.27:107-241, Springer Science, New York (2009)
Cited for: REVIEW.
[17]"Behavioral characterization of dysbindin-1 deficient sandy mice."
Bhardwaj S.K., Baharnoori M., Sharif-Askari B., Kamath A., Williams S., Srivastava L.K.
Behav. Brain Res. 197:435-441(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, FUNCTION.
[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: DISRUPTION PHENOTYPE, FUNCTION.
[19]"Neurobehavioral abnormalities in the dysbindin-1 mutant, sandy, on a C57BL/6J genetic background."
Cox M.M., Tucker A.M., Tang J., Talbot K., Richer D.C., Yeh L., Arnold S.E.
Genes Brain Behav. 8:390-397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[20]"The sandy (sdy) mouse: a dysbindin-1 mutant relevant to schizophrenia research."
Talbot K.
Prog. Brain Res. 179:87-94(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON DISEASE.
[21]"Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression."
Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.
J. Biol. Chem. 285:38630-38640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, FUNCTION.
[22]"The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R., Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C., Dell'Angelica E.C.
Mol. Psychiatry 15:204-215(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[23]"Direct interaction of dysbindin with the AP-3 complex via its mu subunit."
Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K.
Neurochem. Int. 54:431-438(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH THE AP-C COMPLEX, FUNCTION.
[24]"Dysfunction of dopamine release in the prefrontal cortex of dysbindin deficient sandy mice: an in vivo microdialysis study."
Nagai T., Kitahara Y., Shiraki A., Hikita T., Taya S., Kaibuchi K., Yamada K.
Neurosci. Lett. 470:134-138(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Dysbindin-1, a schizophrenia-related protein, functionally interacts with the DNA-dependent protein kinase complex in an isoform-dependent manner."
Oyama S., Yamakawa H., Sasagawa N., Hosoi Y., Futai E., Ishiura S.
PLoS ONE 4:E4199-E4199(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP3B2.
[26]"Role of dysbindin in dopamine receptor trafficking and cortical GABA function."
Ji Y., Yang F., Papaleo F., Wang H.X., Gao W.J., Weinberger D.R., Lu B.
Proc. Natl. Acad. Sci. U.S.A. 106:19593-19598(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE AP-3 COMPLEX, INTERACTION WITH PI4K2A.
[28]"Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-like behaviors via dopamine/D2 pathways."
Papaleo F., Yang F., Garcia S., Chen J., Lu B., Crawley J.N., Weinberger D.R.
Mol. Psychiatry 17:85-98(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[29]"The BLOS1-Interacting Protein KXD1 is Involved in the Biogenesis of Lysosome-Related Organelles."
Yang Q., He X., Yang L., Zhou Z., Cullinane A.R., Wei A., Zhang Z., Hao Z., Zhang A., He M., Feng Y., Gao X., Gahl W.A., Huizing M., Li W.
Traffic 13:1160-1169(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KXD1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ404859 mRNA. Translation: CAC37976.1.
AY265461 mRNA. Translation: AAP91871.1.
AK010924 mRNA. Translation: BAB27270.2.
AK159656 mRNA. Translation: BAE35265.1. Different initiation.
BC018350 mRNA. Translation: AAH18350.1.
BC048682 mRNA. Translation: AAH48682.1. Frameshift.
BC058574 mRNA. Translation: AAH58574.1.
CCDSCCDS36647.1. [Q91WZ8-1]
RefSeqNP_080048.2. NM_025772.4. [Q91WZ8-1]
UniGeneMm.352311.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220491. 3 interactions.
IntActQ91WZ8. 4 interactions.
MINTMINT-197141.

PTM databases

PhosphoSiteQ91WZ8.

Proteomic databases

PaxDbQ91WZ8.
PRIDEQ91WZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072329; ENSMUSP00000072170; ENSMUSG00000057531. [Q91WZ8-1]
GeneID94245.
KEGGmmu:94245.
UCSCuc007qgw.1. mouse. [Q91WZ8-1]

Organism-specific databases

CTD84062.
MGIMGI:2137586. Dtnbp1.

Phylogenomic databases

eggNOGNOG81712.
GeneTreeENSGT00390000010667.
HOGENOMHOG000272621.
HOVERGENHBG051416.
InParanoidQ91WZ8.
OMATVPYLPK.
OrthoDBEOG72VH6B.
PhylomeDBQ91WZ8.
TreeFamTF332997.

Gene expression databases

BgeeQ91WZ8.
CleanExMM_DTNBP1.
GenevestigatorQ91WZ8.

Family and domain databases

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

Other

ChiTaRSDTNBP1. mouse.
NextBio352255.
PROQ91WZ8.
SOURCESearch...

Entry information

Entry nameDTBP1_MOUSE
AccessionPrimary (citable) accession number: Q91WZ8
Secondary accession number(s): Q3TWK1 expand/collapse secondary AC list , Q6WXQ1, Q80ZN4, Q9CY43
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot