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DTBP1_HUMAN
ID   DTBP1_HUMAN             Reviewed;         351 AA.
AC   Q96EV8; A8K3V3; Q5THY3; Q5THY4; Q96NV2; Q9H0U2; Q9H3J5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Dysbindin;
DE   AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 8;
DE            Short=BLOC-1 subunit 8;
DE   AltName: Full=Dysbindin-1;
DE   AltName: Full=Dystrobrevin-binding protein 1;
DE   AltName: Full=Hermansky-Pudlak syndrome 7 protein;
DE            Short=HPS7 protein;
GN   Name=DTNBP1; Synonyms=BLOC1S8; ORFNames=My031;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN HPS7.
RC   TISSUE=Placenta;
RX   PubMed=12923531; DOI=10.1038/ng1229;
RA   Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P.,
RA   Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A.,
RA   Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W.,
RA   Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.;
RT   "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a
RT   member of the biogenesis of lysosome-related organelles complex 1 (BLOC-
RT   1).";
RL   Nat. Genet. 35:84-89(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Jiang Y., Straub R.E., Sullivan P.F., Chen X., O'Neill F.A., Walsh D.,
RA   Kendler K.S., Riley B.P.;
RT   "Localization and identification of a human DTNBP1 gene from a putative
RT   schizophrenia susceptibility locus on 6p22.3 by in silico cloning.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lung, and Neuroblastoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-351 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Mao Y.M., Xie Y., Ying K.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   ASSOCIATION WITH SCHIZOPHRENIA, AND FUNCTION.
RX   PubMed=15345706; DOI=10.1093/hmg/ddh280;
RA   Numakawa T., Yagasaki Y., Ishimoto T., Okada T., Suzuki T., Iwata N.,
RA   Ozaki N., Taguchi T., Tatsumi M., Kamijima K., Straub R.E.,
RA   Weinberger D.R., Kunugi H., Hashimoto R.;
RT   "Evidence of novel neuronal functions of dysbindin, a susceptibility gene
RT   for schizophrenia.";
RL   Hum. Mol. Genet. 13:2699-2708(2004).
RN   [9]
RP   ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15124027; DOI=10.1172/jci200420425;
RA   Talbot K., Eidem W.L., Tinsley C.L., Benson M.A., Thompson E.W.,
RA   Smith R.J., Hahn C.G., Siegel S.J., Trojanowski J.Q., Gur R.E., Blake D.J.,
RA   Arnold S.E.;
RT   "Dysbindin-1 is reduced in intrinsic, glutamatergic terminals of the
RT   hippocampal formation in schizophrenia.";
RL   J. Clin. Invest. 113:1353-1363(2004).
RN   [10]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16980328; DOI=10.1093/hmg/ddl246;
RA   Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A., Kamins J.,
RA   Hahn C.G., Blake D.J., Arnold S.E.;
RT   "Dysbindin-1 is a synaptic and microtubular protein that binds brain
RT   snapin.";
RL   Hum. Mol. Genet. 15:3041-3054(2006).
RN   [11]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=16837549; DOI=10.1091/mbc.e06-05-0379;
RA   Di Pietro S.M., Falcon-Perez J.M., Tenza D., Setty S.R., Marks M.S.,
RA   Raposo G., Dell'Angelica E.C.;
RT   "BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein
RT   trafficking on endosomes.";
RL   Mol. Biol. Cell 17:4027-4038(2006).
RN   [12]
RP   IDENTIFICATION IN THE BLOC-1 COMPLEX, AND FUNCTION.
RX   PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA   Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA   Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA   Dell'Angelica E.C., Raposo G., Marks M.S.;
RT   "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT   endosomes toward lysosome-related organelles.";
RL   Mol. Biol. Cell 18:768-780(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=17989303; DOI=10.1523/jneurosci.1689-07.2007;
RA   Iizuka Y., Sei Y., Weinberger D.R., Straub R.E.;
RT   "Evidence that the BLOC-1 protein dysbindin modulates dopamine D2 receptor
RT   internalization and signaling but not D1 internalization.";
RL   J. Neurosci. 27:12390-12395(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [15]
RP   ASSOCIATION WITH SCHIZOPHRENIA.
RX   PubMed=19617633; DOI=10.1093/hmg/ddp329;
RA   Tang J., LeGros R.P., Louneva N., Yeh L., Cohen J.W., Hahn C.G.,
RA   Blake D.J., Arnold S.E., Talbot K.;
RT   "Dysbindin-1 in dorsolateral prefrontal cortex of schizophrenia cases is
RT   reduced in an isoform-specific manner unrelated to dysbindin-1 mRNA
RT   expression.";
RL   Hum. Mol. Genet. 18:3851-3863(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [17]
RP   REVIEW.
RA   Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C.,
RA   Arnold S.E.;
RT   "Dysbindin-1 and its protein family with special attention to the potential
RT   role of dysbindin-1 in neuronal functions and the pathophysiology of
RT   schizophrenia.";
RL   (In) Javitt D.C., Kantrowitz J. (eds.);
RL   Handbook of neurochemistry and molecular neurobiology (3rd ed.),
RL   pp.27:107-241, Springer Science, New York (2009).
RN   [18]
RP   FUNCTION.
RX   PubMed=19094965; DOI=10.1016/j.bbrc.2008.12.017;
RA   Kubota K., Kumamoto N., Matsuzaki S., Hashimoto R., Hattori T., Okuda H.,
RA   Takamura H., Takeda M., Katayama T., Tohyama M.;
RT   "Dysbindin engages in c-Jun N-terminal kinase activity and cytoskeletal
RT   organization.";
RL   Biochem. Biophys. Res. Commun. 379:191-195(2009).
RN   [19]
RP   INTERACTION WITH TRIM32, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX   PubMed=19349376; DOI=10.1093/hmg/ddp167;
RA   Locke M., Tinsley C.L., Benson M.A., Blake D.J.;
RT   "TRIM32 is an E3 ubiquitin ligase for dysbindin.";
RL   Hum. Mol. Genet. 18:2344-2358(2009).
RN   [20]
RP   INTERACTION WITH AP3M1, AND MUTAGENESIS OF TYR-215.
RX   PubMed=19428785; DOI=10.1016/j.neuint.2009.01.014;
RA   Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K.;
RT   "Direct interaction of dysbindin with the AP-3 complex via its mu
RT   subunit.";
RL   Neurochem. Int. 54:431-438(2009).
RN   [21]
RP   SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3),
RP   INTERACTION WITH AP3B2; XRCC5 AND XRCC6 IN THE DNA-DEPENDENT PROTEIN KINASE
RP   COMPLEX DNA-PK, AND PHOSPHORYLATION.
RX   PubMed=19142223; DOI=10.1371/journal.pone.0004199;
RA   Oyama S., Yamakawa H., Sasagawa N., Hosoi Y., Futai E., Ishiura S.;
RT   "Dysbindin-1, a schizophrenia-related protein, functionally interacts with
RT   the DNA-dependent protein kinase complex in an isoform-dependent manner.";
RL   PLoS ONE 4:E4199-E4199(2009).
RN   [22]
RP   ASSOCIATION WITH SCHIZOPHRENIA, AND FUNCTION.
RX   PubMed=20180862; DOI=10.1111/j.1601-183x.2010.00574.x;
RA   Fallgatter A.J., Ehlis A.C., Herrmann M.J., Hohoff C., Reif A.,
RA   Freitag C.M., Deckert J.;
RT   "DTNBP1 (dysbindin) gene variants modulate prefrontal brain function in
RT   schizophrenic patients--support for the glutamate hypothesis of
RT   schizophrenias.";
RL   Genes Brain Behav. 9:489-497(2010).
RN   [23]
RP   SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH XPO1, AND MUTAGENESIS OF
RP   243-LEU--LEU-256.
RX   PubMed=20921223; DOI=10.1074/jbc.m110.107912;
RA   Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.;
RT   "Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related
RT   protein, regulates synapsin I expression.";
RL   J. Biol. Chem. 285:38630-38640(2010).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [25]
RP   ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1; 2 AND 3),
RP   AND SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
RX   PubMed=21390302; DOI=10.1371/journal.pone.0016886;
RA   Talbot K., Louneva N., Cohen J.W., Kazi H., Blake D.J., Arnold S.E.;
RT   "Synaptic dysbindin-1 reductions in schizophrenia occur in an isoform-
RT   specific manner indicating their subsynaptic location.";
RL   PLoS ONE 6:E16886-E16886(2011).
RN   [26]
RP   IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP   COMPLEX.
RX   PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA   Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA   Bonifacino J.S., Hurley J.H.;
RT   "Assembly and architecture of biogenesis of lysosome-related organelles
RT   complex-1 (BLOC-1).";
RL   J. Biol. Chem. 287:5882-5890(2012).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC       for normal biogenesis of lysosome-related organelles (LRO), such as
CC       platelet dense granules and melanosomes. In concert with the AP-3
CC       complex, the BLOC-1 complex is required to target membrane protein
CC       cargos into vesicles assembled at cell bodies for delivery into
CC       neurites and nerve terminals. The BLOC-1 complex, in association with
CC       SNARE proteins, is also proposed to be involved in neurite extension.
CC       Associates with the BLOC-2 complex to facilitate the transport of TYRP1
CC       independent of AP-3 function. Plays a role in synaptic vesicle
CC       trafficking and in neurotransmitter release. Plays a role in the
CC       regulation of cell surface exposure of DRD2. May play a role in actin
CC       cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8
CC       phosphorylation. Appears to promote neuronal transmission and viability
CC       through regulating the expression of SNAP25 and SYN1, modulating PI3-
CC       kinase-Akt signaling and influencing glutamatergic release. Regulates
CC       the expression of SYN1 through binding to its promoter. Modulates
CC       prefrontal cortical activity via the dopamine/D2 pathway.
CC       {ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:16837549,
CC       ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:17989303,
CC       ECO:0000269|PubMed:19094965, ECO:0000269|PubMed:20180862,
CC       ECO:0000269|PubMed:20921223}.
CC   -!- SUBUNIT: Interacts (via its coiled coil domain) with KXD1. Interacts
CC       with CMYA5, PI4K2 and RNF151 (By similarity). Component of the
CC       biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed
CC       of at least BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC       DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts directly in the complex
CC       with BLOC1S5, BLOC1S6 and SNAPIN/BLOC1S8. The BLOC-1 complex associates
CC       with the AP-3 protein complex and membrane protein cargos. This BLOC-1
CC       complex also associates with the BLOC-2 complex in endosomes. Binds to
CC       DTNA and DTNB but may not be a physiological binding partner
CC       (PubMed:16980328). Interacts (isoform 1 and isoform 2 only) with the
CC       DNA-dependent protein kinase complex DNA-PK; the interaction
CC       phosphorylates DTNBP1 in vitro. Interacts directly in this complex with
CC       XRCC5 and XRCC6. Interacts with AP3M1, AP3B2 and TRIM32. Interacts with
CC       XPO1; the interaction exports DTNBP1 out of the nucleus. {ECO:0000250,
CC       ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:16980328,
CC       ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:19142223,
CC       ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:19428785,
CC       ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:22203680}.
CC   -!- INTERACTION:
CC       Q96EV8; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-465804, EBI-465861;
CC       Q96EV8; Q9UL45: BLOC1S6; NbExp=9; IntAct=EBI-465804, EBI-465781;
CC       Q96EV8; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-465804, EBI-2837444;
CC       Q96EV8; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-465804, EBI-10247802;
CC       Q96EV8; Q494R4: CCDC153; NbExp=3; IntAct=EBI-465804, EBI-10241443;
CC       Q96EV8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-465804, EBI-10175300;
CC       Q96EV8; O60941: DTNB; NbExp=3; IntAct=EBI-465804, EBI-740402;
CC       Q96EV8; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-465804, EBI-10285373;
CC       Q96EV8; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-465804, EBI-2514791;
CC       Q96EV8; Q8IY31: IFT20; NbExp=3; IntAct=EBI-465804, EBI-744203;
CC       Q96EV8; Q7Z3B3: KANSL1; NbExp=3; IntAct=EBI-465804, EBI-740244;
CC       Q96EV8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-465804, EBI-2125614;
CC       Q96EV8; O95678: KRT75; NbExp=3; IntAct=EBI-465804, EBI-2949715;
CC       Q96EV8; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-465804, EBI-10172876;
CC       Q96EV8; O43482: OIP5; NbExp=3; IntAct=EBI-465804, EBI-536879;
CC       Q96EV8; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-465804, EBI-10181968;
CC       Q96EV8; O00560: SDCBP; NbExp=3; IntAct=EBI-465804, EBI-727004;
CC       Q96EV8; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-465804, EBI-10313866;
CC       Q96EV8; O95295: SNAPIN; NbExp=7; IntAct=EBI-465804, EBI-296723;
CC       Q96EV8; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-465804, EBI-10172867;
CC       Q96EV8; P14373: TRIM27; NbExp=3; IntAct=EBI-465804, EBI-719493;
CC       Q96EV8; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-465804, EBI-6116822;
CC       Q96EV8; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-465804, EBI-712969;
CC       Q96EV8-1; P13010: XRCC5; NbExp=2; IntAct=EBI-16749108, EBI-357997;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC       {ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Endosome membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Melanosome membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Postsynaptic density
CC       {ECO:0000269|PubMed:21390302}. Endoplasmic reticulum {ECO:0000250}.
CC       Nucleus {ECO:0000269|PubMed:21390302}. Note=Mainly cytoplasmic but
CC       shuttles between the cytoplasm and nucleus. Exported out of the nucleus
CC       via its NES in a XPO1-dependent manner. Nuclear localization is
CC       required for regulation of the expression of genes such as SYN1.
CC       Detected in neuron cell bodies, axons and dendrites. Mainly located to
CC       the postsynaptic density. Detected at tubulovesicular elements in the
CC       vicinity of the Golgi apparatus and of melanosomes. Occasionally
CC       detected at the membrane of pigmented melanosomes in cultured melanoma
CC       cells. The BLOC-1 complex associates with the BLOC-2 complex in early
CC       endosome-associated tubules.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000269|PubMed:21390302}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Endosome membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Melanosome membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Postsynaptic cell membrane
CC       {ECO:0000269|PubMed:21390302}. Endoplasmic reticulum {ECO:0000250}.
CC       Nucleus {ECO:0000269|PubMed:21390302}. Note=Shuttles between the
CC       cytoplasm and nucleus. Exported out of the nucleus via its NES in a
CC       XPO1-dependent manner. Nuclear localization is required for regulation
CC       of the expression of genes such as SYN1. Mainly expressed in the
CC       dendritic spine. Predominantly a synaptic vesicle isoform but also
CC       highly expressed in the nucleus. The BLOC-1 complex associates with the
CC       BLOC-2 complex in early endosome-associated tubules. Associated with
CC       the AP-3 complex at presynaptic terminals.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC       {ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane {ECO:0000269|PubMed:21390302}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Endosome membrane
CC       {ECO:0000269|PubMed:21390302}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21390302}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21390302}. Melanosome membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Postsynaptic cell membrane
CC       {ECO:0000269|PubMed:21390302}. Endoplasmic reticulum {ECO:0000250}.
CC       Note=Exclusivley cytoplasmic. Predominantly found in the postsynaptic
CC       density (PSD). Little association with synaptic vesicles. The BLOC-1
CC       complex associates with the BLOC-2 complex in early endosome-associated
CC       tubules. Associated with the AP-3 complex at presynaptic terminals.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC       Name=1; Synonyms=Dysbindin 1-A;
CC         IsoId=Q96EV8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96EV8-2; Sequence=VSP_009023;
CC       Name=3; Synonyms=Dysbindin 1-B;
CC         IsoId=Q96EV8-3; Sequence=VSP_046062;
CC   -!- TISSUE SPECIFICITY: Detected in brain, in neurons and in neuropil.
CC       Isoform 1 is expressed in the cerebral cortex, and hippocampal frontal
CC       (HF). Specific expression in the posterior half of the superior
CC       temporal gyrus (pSTG). Higher expression of isoform 2 and 3 in the HF
CC       than in the pSTG while isoform 1 shows no difference in expression in
CC       these areas. In the HF, detected in dentate gyrus (DG) and in pyramidal
CC       cells of hippocampus CA2 and CA3 (at protein level). Expressed in all
CC       principal neuronal populations of the HF, namely pyramidal neurons in
CC       the subiculum and CA1-3, granule cells in the dense cell layer of the
CC       DG (DGg), and polymorph cells in the hilus of the DG (DGh). Maximal
CC       levels in CA2, CA3, and DGh. Isoform 2 not expressed in the cerebral
CC       cortex. {ECO:0000269|PubMed:16980328}.
CC   -!- PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1
CC       degradation. {ECO:0000269|PubMed:19349376}.
CC   -!- PTM: Isoforms 1 and 2 highly phosphorylated by PRKDC in vitro. Isoform
CC       3 only weakly phosphorylated by PRKDC in vitro.
CC       {ECO:0000269|PubMed:19142223}.
CC   -!- DISEASE: Hermansky-Pudlak syndrome 7 (HPS7) [MIM:614076]: A form of
CC       Hermansky-Pudlak syndrome, a genetically heterogeneous autosomal
CC       recessive disorder characterized by oculocutaneous albinism, bleeding
CC       due to platelet storage pool deficiency, and lysosomal storage defects.
CC       This syndrome results from defects of diverse cytoplasmic organelles
CC       including melanosomes, platelet dense granules and lysosomes. Ceroid
CC       storage in the lungs is associated with pulmonary fibrosis, a common
CC       cause of premature death in individuals with HPS.
CC       {ECO:0000269|PubMed:12923531}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Note=Defects in DTNBP1 are associated with susceptibility to
CC       schizophrenia, a mental disorder characterized by a breakdown of
CC       thought processes and by poor emotional responsiveness. Genetic
CC       mutations lead to alterations in the glutamatergic transmission in the
CC       brain and modified Akt signaling (PubMed:15345706). Protein levels and
CC       expression are reduced in nerve terminals of the hippocampus and there
CC       is an increased release of glutamate in schizophrenic patients
CC       (PubMed:15124027). Levels of isoform 1 are reduced in the pSTG, but not
CC       in HF, by about 48% in 92% of schizophrenic patients. In the HF, there
CC       is an average of 33% reduction in synaptic expression of isoform 2 in
CC       67% of cases, and of isoform 3, an average reduction of 35% in 80% of
CC       cases. In the dorsolateral prefrontal cortex (DLPFC), significant
CC       reductions in levels of isoform 3 are observed about 71% of
CC       schizophrenic patients showed an average reduction of this isoform of
CC       about 60% (PubMed:19617633). {ECO:0000269|PubMed:15124027,
CC       ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:19617633}.
CC   -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG43145.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY265460; AAP91870.1; -; mRNA.
DR   EMBL; AF394226; AAL46636.1; -; mRNA.
DR   EMBL; AL136637; CAB66572.1; -; mRNA.
DR   EMBL; AK054593; BAB70770.1; -; mRNA.
DR   EMBL; AK290718; BAF83407.1; -; mRNA.
DR   EMBL; AL021978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL022343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011912; AAH11912.1; -; mRNA.
DR   EMBL; AF061734; AAG43145.1; ALT_INIT; mRNA.
DR   CCDS; CCDS4534.1; -. [Q96EV8-1]
DR   CCDS; CCDS4535.1; -. [Q96EV8-2]
DR   RefSeq; NP_001258596.1; NM_001271667.1. [Q96EV8-3]
DR   RefSeq; NP_001258597.1; NM_001271668.1.
DR   RefSeq; NP_001258598.1; NM_001271669.1.
DR   RefSeq; NP_115498.2; NM_032122.4. [Q96EV8-1]
DR   RefSeq; NP_898861.1; NM_183040.2. [Q96EV8-2]
DR   AlphaFoldDB; Q96EV8; -.
DR   SMR; Q96EV8; -.
DR   BioGRID; 123857; 162.
DR   ComplexPortal; CPX-1910; BLOC-1 complex.
DR   CORUM; Q96EV8; -.
DR   IntAct; Q96EV8; 124.
DR   MINT; Q96EV8; -.
DR   STRING; 9606.ENSP00000341680; -.
DR   iPTMnet; Q96EV8; -.
DR   PhosphoSitePlus; Q96EV8; -.
DR   BioMuta; DTNBP1; -.
DR   DMDM; 38604971; -.
DR   EPD; Q96EV8; -.
DR   jPOST; Q96EV8; -.
DR   MassIVE; Q96EV8; -.
DR   MaxQB; Q96EV8; -.
DR   PaxDb; Q96EV8; -.
DR   PeptideAtlas; Q96EV8; -.
DR   PRIDE; Q96EV8; -.
DR   ProteomicsDB; 76455; -. [Q96EV8-1]
DR   ProteomicsDB; 76456; -. [Q96EV8-2]
DR   Antibodypedia; 25035; 449 antibodies from 35 providers.
DR   DNASU; 84062; -.
DR   Ensembl; ENST00000338950.9; ENSP00000344718.5; ENSG00000047579.20. [Q96EV8-2]
DR   Ensembl; ENST00000344537.10; ENSP00000341680.6; ENSG00000047579.20. [Q96EV8-1]
DR   GeneID; 84062; -.
DR   KEGG; hsa:84062; -.
DR   MANE-Select; ENST00000344537.10; ENSP00000341680.6; NM_032122.5; NP_115498.2.
DR   UCSC; uc003nbm.4; human. [Q96EV8-1]
DR   CTD; 84062; -.
DR   DisGeNET; 84062; -.
DR   GeneCards; DTNBP1; -.
DR   GeneReviews; DTNBP1; -.
DR   HGNC; HGNC:17328; DTNBP1.
DR   HPA; ENSG00000047579; Tissue enhanced (retina).
DR   MalaCards; DTNBP1; -.
DR   MIM; 607145; gene.
DR   MIM; 614076; phenotype.
DR   neXtProt; NX_Q96EV8; -.
DR   OpenTargets; ENSG00000047579; -.
DR   Orphanet; 231531; Hermansky-Pudlak syndrome due to BLOC-1 deficiency.
DR   PharmGKB; PA27512; -.
DR   VEuPathDB; HostDB:ENSG00000047579; -.
DR   eggNOG; ENOG502QRS9; Eukaryota.
DR   GeneTree; ENSGT00940000156479; -.
DR   InParanoid; Q96EV8; -.
DR   OMA; SRYEESW; -.
DR   PhylomeDB; Q96EV8; -.
DR   TreeFam; TF332997; -.
DR   PathwayCommons; Q96EV8; -.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   SignaLink; Q96EV8; -.
DR   SIGNOR; Q96EV8; -.
DR   BioGRID-ORCS; 84062; 11 hits in 1077 CRISPR screens.
DR   ChiTaRS; DTNBP1; human.
DR   GeneWiki; Dysbindin; -.
DR   GenomeRNAi; 84062; -.
DR   Pharos; Q96EV8; Tbio.
DR   PRO; PR:Q96EV8; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96EV8; protein.
DR   Bgee; ENSG00000047579; Expressed in tendon of biceps brachii and 178 other tissues.
DR   ExpressionAtlas; Q96EV8; baseline and differential.
DR   Genevisible; Q96EV8; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR   GO; GO:0030496; C:midbody; IDA:HPA.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR   GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR   GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR   GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR   GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060155; P:platelet dense granule organization; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0061646; P:positive regulation of glutamate neurotransmitter secretion in response to membrane depolarization; IEA:Ensembl.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
DR   GO; GO:0043506; P:regulation of JUN kinase activity; IEA:Ensembl.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   InterPro; IPR007531; Dysbindin.
DR   PANTHER; PTHR16294; PTHR16294; 1.
DR   Pfam; PF04440; Dysbindin; 1.
PE   1: Evidence at protein level;
KW   Albinism; Alternative initiation; Alternative splicing; Cell membrane;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW   Endosome; Hermansky-Pudlak syndrome; Membrane; Nucleus; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Schizophrenia;
KW   Sensory transduction; Synapse; Ubl conjugation.
FT   CHAIN           1..351
FT                   /note="Dysbindin"
FT                   /id="PRO_0000191001"
FT   REGION          173..331
FT                   /note="Dysbindin"
FT   REGION          286..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          88..181
FT                   /evidence="ECO:0000255"
FT   MOTIF           243..256
FT                   /note="Nuclear export signal"
FT   COMPBIAS        286..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WZ8"
FT   VAR_SEQ         1..81
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046062"
FT   VAR_SEQ         272..351
FT                   /note="PESSTCQNEITLQVPNPSELRAKPPSSSSTCTDSATRDISEGGESPVVQSDE
FT                   EEVQVDTALATSHTDREATPDGGEDSDS -> RVDKLALAEPGQYRCHSPPKVRRENHL
FT                   PVTYA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009023"
FT   VARIANT         214
FT                   /note="G -> D (in dbSNP:rs16876589)"
FT                   /id="VAR_053069"
FT   VARIANT         272
FT                   /note="P -> S (in dbSNP:rs17470454)"
FT                   /id="VAR_029644"
FT   MUTAGEN         215
FT                   /note="Y->A: Reduced interaction with AP3M1."
FT                   /evidence="ECO:0000269|PubMed:19428785"
FT   MUTAGEN         243..256
FT                   /note="LMDISDQEALDVFL->AMDASDQEAADVFA: Abolishes
FT                   cytoplasmic location. Increased expression of SYN1."
FT                   /evidence="ECO:0000269|PubMed:20921223"
FT   CONFLICT        242
FT                   /note="D -> V (in Ref. 3; CAB66572)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  39493 MW;  0504C86E12B66C08 CRC64;
     MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKSKPRTVP FLPKYSAGLE LLSRYEDTWA
     ALHRRAKDCA SAGELVDSEV VMLSAHWEKK KTSLVELQEQ LQQLPALIAD LESMTANLTH
     LEASFEEVEN NLLHLEDLCG QCELERCKHM QSQQLENYKK NKRKELETFK AELDAEHAQK
     VLEMEHTQQM KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPIGSMSS MEVNVDMLEQ
     MDLMDISDQE ALDVFLNSGG EENTVLSPAL GPESSTCQNE ITLQVPNPSE LRAKPPSSSS
     TCTDSATRDI SEGGESPVVQ SDEEEVQVDT ALATSHTDRE ATPDGGEDSD S
 
 
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