| UniProt ID | DTBP1_HUMAN | |
|---|---|---|
| UniProt AC | Q96EV8 | |
| Protein Name | Dysbindin | |
| Gene Name | DTNBP1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 351 | |
| Subcellular Localization |
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 junctio |
|
| Protein Description | 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.. | |
| Protein Sequence | MLETLRERLLSVQQDFTSGLKTLSDKSREAKVKSKPRTVPFLPKYSAGLELLSRYEDTWAALHRRAKDCASAGELVDSEVVMLSAHWEKKKTSLVELQEQLQQLPALIADLESMTANLTHLEASFEEVENNLLHLEDLCGQCELERCKHMQSQQLENYKKNKRKELETFKAELDAEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDISDQEALDVFLNSGGEENTVLSPALGPESSTCQNEITLQVPNPSELRAKPPSSSSTCTDSATRDISEGGESPVVQSDEEEVQVDTALATSHTDREATPDGGEDSDS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Phosphorylation | TLRERLLSVQQDFTS HHHHHHHHHHHHHHH | 23.59 | 25159151 | |
| 21 | Ubiquitination | QDFTSGLKTLSDKSR HHHHHHHHHCCHHHC | 51.44 | - | |
| 31 | Acetylation | SDKSREAKVKSKPRT CHHHCCHHHCCCCCC | 45.50 | 19608861 | |
| 33 | Acetylation | KSREAKVKSKPRTVP HHCCHHHCCCCCCCC | 52.64 | 19608861 | |
| 35 | Acetylation | REAKVKSKPRTVPFL CCHHHCCCCCCCCCC | 32.57 | 19608861 | |
| 53 | Phosphorylation | SAGLELLSRYEDTWA HHHHHHHHHHHHHHH | 45.50 | 24719451 | |
| 113 | Phosphorylation | ALIADLESMTANLTH HHHHHHHHHHHCCHH | 28.82 | - | |
| 115 | Phosphorylation | IADLESMTANLTHLE HHHHHHHHHCCHHHH | 22.98 | - | |
| 119 | Phosphorylation | ESMTANLTHLEASFE HHHHHCCHHHHHHHH | 24.99 | - | |
| 124 | Phosphorylation | NLTHLEASFEEVENN CCHHHHHHHHHHHHH | 24.66 | - | |
| 159 | Ubiquitination | SQQLENYKKNKRKEL HHHHHHHHHHHHHHH | 62.54 | - | |
| 170 | Ubiquitination | RKELETFKAELDAEH HHHHHHHHHHHHHHH | 48.66 | - | |
| 191 | Ubiquitination | MEHTQQMKLKERQKF CHHHHHHHHHHHHHH | 52.66 | - | |
| 297 | Phosphorylation | ELRAKPPSSSSTCTD HHCCCCCCCCCCCCC | 51.91 | 28450419 | |
| 298 | Phosphorylation | LRAKPPSSSSTCTDS HCCCCCCCCCCCCCC | 33.80 | 28450419 | |
| 299 | Phosphorylation | RAKPPSSSSTCTDSA CCCCCCCCCCCCCCC | 33.72 | 28450419 | |
| 300 | Phosphorylation | AKPPSSSSTCTDSAT CCCCCCCCCCCCCCC | 29.46 | 26657352 | |
| 301 | Phosphorylation | KPPSSSSTCTDSATR CCCCCCCCCCCCCCC | 22.75 | 28450419 | |
| 303 | Phosphorylation | PSSSSTCTDSATRDI CCCCCCCCCCCCCCC | 32.83 | 26552605 | |
| 305 | Phosphorylation | SSSTCTDSATRDISE CCCCCCCCCCCCCCC | 17.24 | 28985074 | |
| 307 | Phosphorylation | STCTDSATRDISEGG CCCCCCCCCCCCCCC | 32.59 | 26552605 | |
| 311 | Phosphorylation | DSATRDISEGGESPV CCCCCCCCCCCCCCC | 34.18 | 30266825 | |
| 316 | Phosphorylation | DISEGGESPVVQSDE CCCCCCCCCCCCCCC | 26.69 | 30266825 | |
| 321 | Phosphorylation | GESPVVQSDEEEVQV CCCCCCCCCCCEEEC | 35.07 | 30266825 | |
| 330 | Phosphorylation | EEEVQVDTALATSHT CCEEECCHHHHCCCC | 25.39 | 30266825 | |
| 334 | Phosphorylation | QVDTALATSHTDREA ECCHHHHCCCCCCCC | 23.14 | 22167270 | |
| 335 | Phosphorylation | VDTALATSHTDREAT CCHHHHCCCCCCCCC | 20.84 | 22167270 | |
| 337 | Phosphorylation | TALATSHTDREATPD HHHHCCCCCCCCCCC | 36.20 | 22167270 | |
| 349 | Phosphorylation | TPDGGEDSDS----- CCCCCCCCCC----- | 35.14 | 30278072 | |
| 351 | Phosphorylation | DGGEDSDS------- CCCCCCCC------- | 46.18 | 30242111 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DTBP1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DTBP1_HUMAN !! | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-33 AND LYS-35, ANDMASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, ANDMASS SPECTROMETRY. | |
| "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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, ANDMASS SPECTROMETRY. | |
