BL1S1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BL1S1_HUMAN
• UniProt AC: P78537
• Protein Name: Biogenesis of lysosome-related organelles complex 1 subunit 1
• Gene Name: BLOC1S1
• Organism: Homo sapiens (Human).
• Sequence Length: 153
• Subcellular Localization: Mitochondrion intermembrane space . Mitochondrion matrix . Cytoplasm, cytosol . Lysosome membrane .
• 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. [PubMed: 17182842 As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor]
• Protein Sequence: MAPGSRGERSSFRSRRGPGVPSPQPDVTMLSRLLKEHQAKQNERKELQEKRRREAITAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS

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
10	Phosphorylation	PGSRGERSSFRSRRG CCCCCCCCCCCCCCC	29.53	20068231
11	Phosphorylation	GSRGERSSFRSRRGP CCCCCCCCCCCCCCC	30.79	20068231
14	Phosphorylation	GERSSFRSRRGPGVP CCCCCCCCCCCCCCC	25.07	20068231
22	Phosphorylation	RRGPGVPSPQPDVTM CCCCCCCCCCCCHHH	33.49	21815630
35	Ubiquitination	TMLSRLLKEHQAKQN HHHHHHHHHHHHHHH	58.71	29967540
40	Ubiquitination	LLKEHQAKQNERKEL HHHHHHHHHHHHHHH	47.27	24816145
128	Phosphorylation	DVENWARSIELDMRT CHHHHHHHHHCHHHH	16.81	24719451
135	Phosphorylation	SIELDMRTIATALEY HHHCHHHHHHHHHHH	14.34	21406692
138	Phosphorylation	LDMRTIATALEYVYK CHHHHHHHHHHHHHH	28.11	21406692
142	Phosphorylation	TIATALEYVYKGQLQ HHHHHHHHHHHCCCC	15.21	21406692
144	Phosphorylation	ATALEYVYKGQLQSA HHHHHHHHHCCCCCC	14.43	21406692
145	Ubiquitination	TALEYVYKGQLQSAP HHHHHHHHCCCCCCC	30.09	21906983

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

Oops, there are no upstream regulatory protein records of BL1S1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BL1S1_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 BL1S1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BL1S6_HUMAN	BLOC1S6	physical	15102850
BL1S2_HUMAN	BLOC1S2	physical	15102850
SNAPN_HUMAN	SNAPIN	physical	15102850
PTN_HUMAN	PTN	physical	16169070
MTA1_HUMAN	MTA1	physical	12639951
HDAC2_HUMAN	HDAC2	physical	12639951
ESR1_HUMAN	ESR1	physical	12639951
A4_HUMAN	APP	physical	21832049
CLH1_HUMAN	CLTC	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, AND MASSSPECTROMETRY.
PubMed: 18187866