BL1S3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BL1S3_HUMAN
• UniProt AC: Q6QNY0
• Protein Name: Biogenesis of lysosome-related organelles complex 1 subunit 3
• Gene Name: BLOC1S3
• Organism: Homo sapiens (Human).
• Sequence Length: 202
• Subcellular Localization: Cytoplasm.
• 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. Plays a role in intracellular vesicle trafficking..
• Protein Sequence: MASQGRRRRPLRRPETVVPGEATETDSERSASSSEEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPEPTAAPRDLPPLVVQRESAEEAWGTEEAPAPAPARSLLQLRLAESQARLDHDVAAAVSGVYRRAGRDVAALASRLAAAQAAGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGTEPEKDPGPRA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASQGRRRRP -----CCCCCCCCCC	31.69	24719451
16	Phosphorylation	RPLRRPETVVPGEAT CCCCCCCCCCCCCCC	29.50	20873877
23	Phosphorylation	TVVPGEATETDSERS CCCCCCCCCCCCCCC	34.81	23927012
25	Phosphorylation	VPGEATETDSERSAS CCCCCCCCCCCCCCC	40.23	29255136
27	Phosphorylation	GEATETDSERSASSS CCCCCCCCCCCCCCC	42.18	29255136
30	Phosphorylation	TETDSERSASSSEEE CCCCCCCCCCCCCCH	28.57	23663014
32	Phosphorylation	TDSERSASSSEEEEL CCCCCCCCCCCCHHH	35.33	23663014
33	Phosphorylation	DSERSASSSEEEELY CCCCCCCCCCCHHHH	41.29	23663014
34	Phosphorylation	SERSASSSEEEELYL CCCCCCCCCCHHHHC	46.67	23663014
40	Phosphorylation	SSEEEELYLGPSGPT CCCCHHHHCCCCCCC	16.94	-
63	Phosphorylation	VAGEAAETDSEPEPE ECCHHCCCCCCCCCC	39.85	29255136
65	Phosphorylation	GEAAETDSEPEPEPE CHHCCCCCCCCCCCC	63.57	29255136
74	Phosphorylation	PEPEPEPTAAPRDLP CCCCCCCCCCCCCCC	33.51	22167270
89	Phosphorylation	PLVVQRESAEEAWGT CEEEECCHHHHHHCC	43.07	22210691
159	Phosphorylation	AGLAAAHSVRLARGD HHHHHHHHHHHHCCC	12.28	28555341
196	Ubiquitination	VPGTEPEKDPGPRA- CCCCCCCCCCCCCC-	78.80	30230243

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BL1S3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BL1S3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BL1S3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BL1S1_HUMAN	BLOC1S1	physical	15102850
BL1S2_HUMAN	BLOC1S2	physical	15102850
SNAPN_HUMAN	SNAPIN	physical	15102850
BL1S6_HUMAN	BLOC1S6	physical	15102850
BL1S5_HUMAN	BLOC1S5	physical	15102850

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614077: Hermansky-Pudlak syndrome 8 (HPS8)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-63 AND SER-65, AND MASSSPECTROMETRY.
PubMed: 19690332

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND MASSSPECTROMETRY.
PubMed: 19369195

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND SER-65, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 THR-63 AND SER-65, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32; SER-33;SER-34; THR-63 AND SER-65, AND MASS SPECTROMETRY.
PubMed: 17081983