SRGN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRGN_HUMAN
• UniProt AC: P10124
• Protein Name: Serglycin
• Gene Name: SRGN
• Organism: Homo sapiens (Human).
• Sequence Length: 158
• Subcellular Localization: Cytoplasmic granule . Secreted, extracellular space . Golgi apparatus . Found in mast cell granules and in cytoplasmic granules of cytolytic T lymphocytes from where it is secreted upon cell activation (By similarity). Secreted constitutively by endo
• Protein Description: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization..
• Protein Sequence: MMQKLLKCSRLVLALALILVLESSVQGYPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFML

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
9	Phosphorylation	MQKLLKCSRLVLALA HHHHHHHHHHHHHHH	27.36	24719451
23	Phosphorylation	ALILVLESSVQGYPT HHHHHHHHHHCCCCC	31.48	24719451
28	Phosphorylation	LESSVQGYPTRRARY HHHHHCCCCCCCCCE	5.59	24719451
64	Phosphorylation	FELLPGESNKIPRLR EEECCCCCCCCCCCC	49.71	28060719
94	O-linked_Glycosylation	FPLSEDYSGSGFGSG CCCCCCCCCCCCCCC	38.51	3402609
96	O-linked_Glycosylation	LSEDYSGSGFGSGSG CCCCCCCCCCCCCCC	25.63	3402609
100	O-linked_Glycosylation	YSGSGFGSGSGSGSG CCCCCCCCCCCCCCC	27.76	-
102	O-linked_Glycosylation	GSGFGSGSGSGSGSG CCCCCCCCCCCCCCC	31.33	-
104	O-linked_Glycosylation	GFGSGSGSGSGSGSG CCCCCCCCCCCCCCC	31.33	-
106	O-linked_Glycosylation	GSGSGSGSGSGSGFL CCCCCCCCCCCCCCC	31.33	-
108	O-linked_Glycosylation	GSGSGSGSGSGFLTE CCCCCCCCCCCCCHH	31.33	-
110	O-linked_Glycosylation	GSGSGSGSGFLTEME CCCCCCCCCCCHHHH	28.24	-
142	Phosphorylation	SLDRNLPSDSQDLGQ HHHHCCCCCCCCHHH	53.73	23532336
144	Phosphorylation	DRNLPSDSQDLGQHG HHCCCCCCCCHHHCC	29.90	28450419

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SRGN_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 SRGN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SGTA_HUMAN	SGTA	physical	16189514
PSRC1_HUMAN	PSRC1	physical	21900206
BAG6_HUMAN	BAG6	physical	21900206
CEP70_HUMAN	CEP70	physical	21900206
UBR4_HUMAN	UBR4	physical	21900206
SGTA_HUMAN	SGTA	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	25416956

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

O-linked Glycosylation

"Complete amino acid sequence of a human platelet proteoglycan.";
Alliel P.M., Perin J.-P., Maillet P., Bonnet F., Rosa J.-P.,Jolles P.;
FEBS Lett. 236:123-126(1988).
Cited for: PROTEIN SEQUENCE OF 28-158, NUCLEOTIDE SEQUENCE [MRNA] OF 34-158, ANDGLYCOSYLATION AT SER-94 AND SER-96.
PubMed: 3402609