Q91WZ8 (DTBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dysbindin

Alternative name(s):
Biogenesis of lysosome-related organelles complex 1 subunit 8
Short name=BLOC-1 subunit 8
Dysbindin-1
Dystrobrevin-binding protein 1
Hermansky-Pudlak syndrome 7 protein homolog
Short name=HPS7 protein homolog

Gene names

Name:	Dtnbp1
Synonyms:	Bloc1s8, Sdy

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence 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 junction › synapse › postsynaptic cell membrane › postsynaptic 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 expresssion 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 vesicle › secretory vesicle › synaptic 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 junction › synapse › postsynaptic 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 process	Sensory transduction
Cellular component	Cell junction Cell membrane Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Endosome Membrane Nucleus Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Disease	Albinism Hermansky-Pudlak syndrome
Domain	Coiled coil
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 morphogenesis Inferred from direct assay Ref.9. 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_component	BLOC-1 complex Inferred from direct assay PubMed 17182842Ref.22. Source: UniProtKB axon part Inferred from direct assay Ref.9. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW 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 nucleus Inferred from direct assay Ref.1. Source: UniProtKB 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cmya5	Q70KF4	5	EBI-643186,EBI-782290
Dtna	Q9D2N4	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	Dysbindin		PRO_0000191002
Regions
	Region	173 – 325	153	Dysbindin
	Region	243 – 256	14	Nuclear export signal By similarity
	Coiled coil	88 – 176	89	Potential
Amino acid modifications
	Modified residue	31	1	N6-acetyllysine By similarity
	Modified residue	33	1	N6-acetyllysine By similarity
	Modified residue	315	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 81	81	Missing in isoform 3.		VSP_021939
	Alternative sequence	171 – 222	52	Missing in isoform 2.		VSP_009024
Experimental info
	Sequence conflict	251	1	A → T in BAE35265. Ref.3
	Sequence conflict	280	1	E → G in BAE35265. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Dysbindin 1-A) [UniParc]. Last modified December 1, 2001. Version 1. Checksum: EE60FB10ECE95361	FASTA	352	39,651
	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
	Isoform 2 [UniParc]. Checksum: D13F78AB2A09E4C8	FASTA	300	33,323
	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 EPMGSMSSME 190 200 210 220 230 240 VNVDVLEQMD LMDISDQEAL DVFLNSGGED NIVMSPGVEM ESNPNQNEMS LQIPSPSESA 250 260 270 280 290 300 SQPPASPSAC TDLDTADAPL IQSDEEEVQV DTALVTLHTD RKSTPGVSDD SDQCDSTQDI
	Isoform 3 (Dysbindin 1-C) [UniParc]. Checksum: 71C7294BC4488139	FASTA	271	30,582
	10 20 30 40 50 60 MLSAHWEKKR TSLNELQGQL QQLPALLQDL ESLMASLAHL ETSFEEVENH LLHLEDLCGQ 70 80 90 100 110 120 CELERHKQAQ AQHLESYKKS KRKELEAFKA ELDTEHTQKA LEMEHTQQLK LKERQKFFEE 130 140 150 160 170 180 AFQQDMEQYL STGYLQIAER REPMGSMSSM EVNVDVLEQM DLMDISDQEA LDVFLNSGGE 190 200 210 220 230 240 DNIVMSPGVE MESNPNQNEM SLQIPSPSES ASQPPASPSA CTDLDTADAP LIQSDEEEVQ 250 260 270 VDTALVTLHT DRKSTPGVSD DSDQCDSTQD I

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00128563. IPI00395220. IPI00816938.
RefSeq	NP_080048.2. NM_025772.4.
UniGene	Mm.352311.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91WZ8. 4 interactions.
MINT	MINT-197141.
PTM databases
PhosphoSite	Q91WZ8.
Proteomic databases
PaxDb	Q91WZ8.
PRIDE	Q91WZ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000072329; ENSMUSP00000072170; ENSMUSG00000057531.
GeneID	94245.
KEGG	mmu:94245.
UCSC	uc007qgw.1. mouse. uc007qgx.1. mouse.
Organism-specific databases
CTD	84062.
MGI	MGI:2137586. Dtnbp1.
Phylogenomic databases
eggNOG	NOG81712.
GeneTree	ENSGT00390000010667.
HOGENOM	HOG000272621.
HOVERGEN	HBG051416.
InParanoid	Q91WZ8.
OMA	SAHWEKR.
OrthoDB	EOG4FTW21.
Gene expression databases
Bgee	Q91WZ8.
CleanEx	MM_DTNBP1.
Genevestigator	Q91WZ8.
GermOnline	ENSMUSG00000057531. Mus musculus.
Family and domain databases
InterPro	IPR007531. Dysbindin. [Graphical view]
PANTHER	PTHR16294. PTHR16294. 1 hit.
Pfam	PF04440. Dysbindin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DTNBP1. mouse.
NextBio	352255.
SOURCE	Search...

Entry information

Entry name

DTBP1_MOUSE

Accession

Primary (citable) accession number: Q91WZ8
Secondary accession number(s): Q3TWK1 , Q6WXQ1, Q80ZN4, Q9CY43

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program