Q96EV8 (DTBP1_HUMAN) 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
Short name=HPS7 protein

Gene names

Name:	DTNBP1
Synonyms:	BLOC1S8
ORF Names:	My031

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	351 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.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 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. 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 vesicle › secretory vesicle › synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Melanosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction › synapse › postsynaptic 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 expresssion 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. 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 vesicle › secretory vesicle › synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. 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. 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 of about 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 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 initiation Alternative splicing Polymorphism
Disease	Albinism Hermansky-Pudlak syndrome Schizophrenia
Domain	Coiled coil
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara cellular membrane organization Traceable author statement. Source: Reactome melanosome organization Non-traceable author statement Ref.26. Source: UniProtKB neuron projection morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB platelet dense granule organization Inferred from electronic annotation. Source: Compara 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_component	BLOC-1 complex Inferred from direct assay PubMed 15102850Ref.26. Source: UniProtKB axon part Inferred from sequence or structural similarity. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW 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 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: Compara synaptic vesicle membrane Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLOC1S1	P78537	3	EBI-465804,EBI-348630
BLOC1S2	Q6QNY1	6	EBI-465804,EBI-465872
BLOC1S3	Q6QNY0	3	EBI-465804,EBI-465930
BLOC1S5	Q8TDH9	3	EBI-465804,EBI-465861
BLOC1S6	Q9UL45	6	EBI-465804,EBI-465781
SNAPIN	O95295	4	EBI-465804,EBI-296723

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Dysbindin		PRO_0000191001
Regions
	Region	173 – 331	159	Dysbindin
	Region	243 – 256	14	Nuclear export signal
	Coiled coil	88 – 181	94	Potential
Amino acid modifications
	Modified residue	31	1	N6-acetyllysine
	Modified residue	33	1	N6-acetyllysine
	Modified residue	35	1	N6-acetyllysine
	Modified residue	316	1	Phosphoserine Ref.14 Ref.16
	Modified residue	321	1	Phosphoserine Ref.14 Ref.16
Natural variations
	Alternative sequence	1 – 81	81	Missing in isoform 3.		VSP_046062
	Alternative sequence	272 – 351	80	PESST…EDSDS → RVDKLALAEPGQYRCHSPPK VRRENHLPVTYA in isoform 2.		VSP_009023
	Natural variant	214	1	G → D. Corresponds to variant rs16876589 [ dbSNP | Ensembl ].		VAR_053069
	Natural variant	272	1	P → S. Corresponds to variant rs17470454 [ dbSNP | Ensembl ].		VAR_029644
Experimental info
	Mutagenesis	215	1	Y → A: Reduced interaction with AP3M1. Ref.20
	Mutagenesis	243 – 256	14	LMDIS…LDVFL → AMDASDQEAADVFA: Abolishes cytoplasmic location. Increased expression of SYN1. Ref.23
	Sequence conflict	242	1	D → V in CAB66572. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Dysbindin 1-A) [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0504C86E12B66C08	FASTA	351	39,493
	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
	Isoform 2 [UniParc]. Checksum: 7AF6611B9F6D46BD	FASTA	303	34,831
	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 GRVDKLALAE PGQYRCHSPP KVRRENHLPV TYA
	Isoform 3 (Dysbindin 1-B) [UniParc]. Checksum: C945FAB1BB01B410	FASTA	270	30,387
	10 20 30 40 50 60 MLSAHWEKKK TSLVELQEQL QQLPALIADL ESMTANLTHL EASFEEVENN LLHLEDLCGQ 70 80 90 100 110 120 CELERCKHMQ SQQLENYKKN KRKELETFKA ELDAEHAQKV LEMEHTQQMK LKERQKFFEE 130 140 150 160 170 180 AFQQDMEQYL STGYLQIAER REPIGSMSSM EVNVDMLEQM DLMDISDQEA LDVFLNSGGE 190 200 210 220 230 240 ENTVLSPALG PESSTCQNEI TLQVPNPSEL RAKPPSSSST CTDSATRDIS EGGESPVVQS 250 260 270 DEEEVQVDTA LATSHTDREA TPDGGEDSDS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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

GeneReviews

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.
IPI	IPI00328918. IPI00394984.
RefSeq	NP_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.
UniGene	Hs.571148.
3D structure databases
ProteinModelPortal	Q96EV8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96EV8. 31 interactions.
MINT	MINT-1438666.
STRING	9606.ENSP00000341680.
PTM databases
PhosphoSite	Q96EV8.
Polymorphism databases
DMDM	38604971.
Proteomic databases
PaxDb	Q96EV8.
PRIDE	Q96EV8.
Protocols and materials databases
DNASU	84062.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338950; ENSP00000344718; ENSG00000047579. ENST00000344537; ENSP00000341680; ENSG00000047579.
GeneID	84062.
KEGG	hsa:84062.
UCSC	uc003nbl.3. human. uc003nbp.3. human.
Organism-specific databases
CTD	84062.
GeneCards	GC06M015470.
HGNC	HGNC:17328. DTNBP1.
HPA	HPA028053. HPA029615. HPA029616.
MIM	607145. gene. 614076. phenotype.
neXtProt	NX_Q96EV8.
Orphanet	231531. Hermansky-Pudlak syndrome type 7.
PharmGKB	PA27512.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG81712.
HOGENOM	HOG000272621.
HOVERGEN	HBG051416.
OMA	SAHWEKR.
OrthoDB	EOG4FTW21.
PhylomeDB	Q96EV8.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	Q96EV8.
Bgee	Q96EV8.
CleanEx	HS_DTNBP1.
Genevestigator	Q96EV8.
GermOnline	ENSG00000047579. Homo sapiens.
Family and domain databases
InterPro	IPR007531. Dysbindin. [Graphical view]
PANTHER	PTHR16294. PTHR16294. 1 hit.
Pfam	PF04440. Dysbindin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	84062.
NextBio	73219.
SOURCE	Search...

Entry information

Entry name

DTBP1_HUMAN

Accession

Primary (citable) accession number: Q96EV8
Secondary accession number(s): A8K3V3 , Q5THY3, Q5THY4, Q96NV2, Q9H0U2, Q9H3J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	December 1, 2001
Last modified:	May 29, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.