dbPTM

SYUG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYUG_HUMAN
UniProt AC	O76070
Protein Name	Gamma-synuclein
Gene Name	SNCG
Organism	Homo sapiens (Human).
Sequence Length	127
Subcellular Localization	Cytoplasm, perinuclear region . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle.
Protein Description	Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity)..
Protein Sequence	MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MDVFKKGFSIAK ---CCCHHHCCCHHH	52.41	18530279
6	Methylation	--MDVFKKGFSIAKE --CCCHHHCCCHHHH	54.44	-
9	Phosphorylation	DVFKKGFSIAKEGVV CCHHHCCCHHHHCCH	30.24	28355574
21	Acetylation	GVVGAVEKTKQGVTE CCHHHHHHHCCCHHH	55.19	26051181
32	Acetylation	GVTEAAEKTKEGVMY CHHHHHHHHCCCEEE	61.24	26051181
34	2-Hydroxyisobutyrylation	TEAAEKTKEGVMYVG HHHHHHHCCCEEEEC	64.64	-
39	Phosphorylation	KTKEGVMYVGAKTKE HHCCCEEEECCCCHH	8.04	30576142
43	Acetylation	GVMYVGAKTKENVVQ CEEEECCCCHHHHHH	54.95	26051181
44	Phosphorylation	VMYVGAKTKENVVQS EEEECCCCHHHHHHH	42.95	23312004
44	O-linked_Glycosylation	VMYVGAKTKENVVQS EEEECCCCHHHHHHH	42.95	28657654
45	2-Hydroxyisobutyrylation	MYVGAKTKENVVQSV EEECCCCHHHHHHHH	46.73	-
51	Phosphorylation	TKENVVQSVTSVAEK CHHHHHHHHHHHHHH	18.76	20068231
53	O-linked_Glycosylation	ENVVQSVTSVAEKTK HHHHHHHHHHHHHHH	23.80	28657654
53	Phosphorylation	ENVVQSVTSVAEKTK HHHHHHHHHHHHHHH	23.80	30576142
54	Phosphorylation	NVVQSVTSVAEKTKE HHHHHHHHHHHHHHH	19.71	20068231
54	O-linked_Glycosylation	NVVQSVTSVAEKTKE HHHHHHHHHHHHHHH	19.71	28657654
58	Acetylation	SVTSVAEKTKEQANA HHHHHHHHHHHHHHH	55.98	23236377
59	O-linked_Glycosylation	VTSVAEKTKEQANAV HHHHHHHHHHHHHHH	31.17	28657654
67	O-linked_Glycosylation	KEQANAVSEAVVSSV HHHHHHHHHHHHHHH	19.89	28657654
67	Phosphorylation	KEQANAVSEAVVSSV HHHHHHHHHHHHHHH	19.89	-
72	O-linked_Glycosylation	AVSEAVVSSVNTVAT HHHHHHHHHHHHCCC	23.21	28657654
72	Phosphorylation	AVSEAVVSSVNTVAT HHHHHHHHHHHHCCC	23.21	27251275
73	Phosphorylation	VSEAVVSSVNTVATK HHHHHHHHHHHCCCC	14.05	27251275
81	O-linked_Glycosylation	VNTVATKTVEEAENI HHHCCCCCHHHHHHH	28.88	28657654
91	O-linked_Glycosylation	EAENIAVTSGVVRKE HHHHHEEEECCEEHH	15.67	28657654
91	Phosphorylation	EAENIAVTSGVVRKE HHHHHEEEECCEEHH	15.67	27251275
92	O-linked_Glycosylation	AENIAVTSGVVRKED HHHHEEEECCEEHHH	24.00	28657654
92	Phosphorylation	AENIAVTSGVVRKED HHHHEEEECCEEHHH	24.00	27251275
112	Phosphorylation	PQQEGEASKEKEEVA CCCCCCCHHHHHHHH	36.73	25159151
115	Acetylation	EGEASKEKEEVAEEA CCCCHHHHHHHHHHH	64.01	26051181
124	Phosphorylation	EVAEEAQSGGD---- HHHHHHHCCCC----	52.36	30278072

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
124	S	Phosphorylation	Kinase	ADRBK1	P25098	GPS
124	S	Phosphorylation	Kinase	CAMK2B	Q13554	GPS
124	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
124	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
124	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYUG_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 SYUG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYL1_HUMAN	DYNLL1	physical	17353931
MCM3_HUMAN	MCM3	physical	17353931
FUBP1_HUMAN	FUBP1	physical	17353931
BUB1B_HUMAN	BUB1B	physical	14576821
MK03_HUMAN	MAPK3	physical	12121974
MK01_HUMAN	MAPK1	physical	12121974
MK08_HUMAN	MAPK8	physical	12121974
SC6A4_HUMAN	SLC6A4	physical	19429025
JUPI1_HUMAN	HN1	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.

Regulatory Network of SYUG_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-124, AND MASSSPECTROMETRY.	18669648 [Abstract]