dbPTM

SODM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SODM_MOUSE
UniProt AC	P09671
Protein Name	Superoxide dismutase [Mn], mitochondrial
Gene Name	Sod2
Organism	Mus musculus (Mouse).
Sequence Length	222
Subcellular Localization	Mitochondrion matrix.
Protein Description	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems..
Protein Sequence	MLCRAACSTGRRLGPVAGAAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVALQPALKFNGGGHINHTIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYTACKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Acetylation	GAAGSRHKHSLPDLP CCCCCCCCCCCCCCC	33.50	23576753
27	Phosphorylation	AGSRHKHSLPDLPYD CCCCCCCCCCCCCCC	46.53	21082442
33	Nitration	HSLPDLPYDYGALEP CCCCCCCCCCCCCCH	29.15	-
53	Acetylation	IMQLHHSKHHAAYVN HHHHHHHHHHHHHHC	34.74	23576753
58	Nitrated tyrosine	HSKHHAAYVNNLNAT HHHHHHHHHCCCCCC	12.42	-
58	Phosphorylation	HSKHHAAYVNNLNAT HHHHHHHHHCCCCCC	12.42	25195567
58	Nitration	HSKHHAAYVNNLNAT HHHHHHHHHCCCCCC	12.42	-
68	Succinylation	NLNATEEKYHEALAK CCCCCHHHHHHHHHC	45.75	23806337
68	Ubiquitination	NLNATEEKYHEALAK CCCCCHHHHHHHHHC	45.75	-
68	Succinylation	NLNATEEKYHEALAK CCCCCHHHHHHHHHC	45.75	-
68	Acetylation	NLNATEEKYHEALAK CCCCCHHHHHHHHHC	45.75	23576753
75	Ubiquitination	KYHEALAKGDVTTQV HHHHHHHCCCCHHHH	57.40	-
75	Succinylation	KYHEALAKGDVTTQV HHHHHHHCCCCHHHH	57.40	-
75	Acetylation	KYHEALAKGDVTTQV HHHHHHHCCCCHHHH	57.40	23576753
75	Succinylation	KYHEALAKGDVTTQV HHHHHHHCCCCHHHH	57.40	23806337
89	Acetylation	VALQPALKFNGGGHI HEECEEEEECCCCCC	38.60	23864654
108	Acetylation	FWTNLSPKGGGEPKG EEECCCCCCCCCCCH	67.80	23864654
114	Acetylation	PKGGGEPKGELLEAI CCCCCCCCHHHHHHH	61.79	23576753
114	Ubiquitination	PKGGGEPKGELLEAI CCCCCCCCHHHHHHH	61.79	-
114	Succinylation	PKGGGEPKGELLEAI CCCCCCCCHHHHHHH	61.79	23806337
122	Malonylation	GELLEAIKRDFGSFE HHHHHHHHHHHCCHH	53.62	26320211
122	Succinylation	GELLEAIKRDFGSFE HHHHHHHHHHHCCHH	53.62	23806337
122	Glutarylation	GELLEAIKRDFGSFE HHHHHHHHHHHCCHH	53.62	24703693
122	Succinylation	GELLEAIKRDFGSFE HHHHHHHHHHHCCHH	53.62	-
122	Acetylation	GELLEAIKRDFGSFE HHHHHHHHHHHCCHH	53.62	23576753
130	Glutarylation	RDFGSFEKFKEKLTA HHHCCHHHHHHHCEE	60.78	24703693
130	Succinylation	RDFGSFEKFKEKLTA HHHCCHHHHHHHCEE	60.78	23806337
130	Ubiquitination	RDFGSFEKFKEKLTA HHHCCHHHHHHHCEE	60.78	-
130	Succinylation	RDFGSFEKFKEKLTA HHHCCHHHHHHHCEE	60.78	-
130	Acetylation	RDFGSFEKFKEKLTA HHHCCHHHHHHHCEE	60.78	23806337
132	Succinylation	FGSFEKFKEKLTAVS HCCHHHHHHHCEEEE	66.07	23954790
132	Acetylation	FGSFEKFKEKLTAVS HCCHHHHHHHCEEEE	66.07	21728379
134	Acetylation	SFEKFKEKLTAVSVG CHHHHHHHCEEEEEE	52.29	21728379
136	Phosphorylation	EKFKEKLTAVSVGVQ HHHHHHCEEEEEEEC	35.76	23335269
139	Phosphorylation	KEKLTAVSVGVQGSG HHHCEEEEEEECCCC	15.64	23335269
145	Phosphorylation	VSVGVQGSGWGWLGF EEEEECCCCCCCCCC	17.80	23335269
154	Succinylation	WGWLGFNKEQGRLQI CCCCCCCCCCCEEEE	49.51	26388266
154	Acetylation	WGWLGFNKEQGRLQI CCCCCCCCCCCEEEE	49.51	21728379
164	S-nitrosylation	GRLQIAACSNQDPLQ CEEEEEEECCCCCCC	2.65	21278135
164	S-nitrosocysteine	GRLQIAACSNQDPLQ CEEEEEEECCCCCCC	2.65	-
202	Acetylation	NVRPDYLKAIWNVIN CCCHHHHHHHHHHHC	31.43	23576753
220	Glutathionylation	VTERYTACKK----- HHHHHHHCCC-----	4.44	24333276
221	Succinylation	TERYTACKK------ HHHHHHCCC------	60.08	26388266
221	Acetylation	TERYTACKK------ HHHHHHCCC------	60.08	23864654
222	Acetylation	ERYTACKK------- HHHHHCCC-------	66.51	2389583

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
122	K	Acetylation		21172655
Acetylation at Lys-122 decreases enzymatic activity.

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 SODM_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SODM_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SODM_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.	16916647 [Abstract]

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