dbPTM

MMSA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MMSA_MOUSE
UniProt AC	Q9EQ20
Protein Name	Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
Gene Name	Aldh6a1
Organism	Mus musculus (Mouse).
Sequence Length	535
Subcellular Localization	Mitochondrion.
Protein Description	Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity)..
Protein Sequence	MAAAVAAAAAMRSRILQVSSKVNATWYPASSFSSSSVPTVKLFIDGKFVESKSDKWIDIHNPATNEVVGRVPQSTKAEMDAAVESCKRAFPAWADTSILSRQQVLLRYQQLIKENLKEIARLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHDAVNFICDHPDIKAISFVGSNQAGEYIFERGSRNGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGEAKKWLPELVDRAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRRIKVKGYENGNFVGPTIISNVKPSMTCYKEEIFGPVLVVLETETLDEAIKIVNDNPYGNGTAIFTTNGATARKYAHMVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Acetylation	SSSVPTVKLFIDGKF CCCCCEEEEEECCEE	39.91	23576753
47	Malonylation	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	26073543
47	Acetylation	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	23576753
47	Glutarylation	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	24703693
47	Succinylation	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	-
47	Succinylation	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	23806337
47	Ubiquitination	VKLFIDGKFVESKSD EEEEECCEEEECCCC	42.35	-
52	Glutarylation	DGKFVESKSDKWIDI CCEEEECCCCCEEEE	49.52	24703693
52	Acetylation	DGKFVESKSDKWIDI CCEEEECCCCCEEEE	49.52	23576753
52	Succinylation	DGKFVESKSDKWIDI CCEEEECCCCCEEEE	49.52	23806337
52	Succinylation	DGKFVESKSDKWIDI CCEEEECCCCCEEEE	49.52	-
55	Malonylation	FVESKSDKWIDIHNP EEECCCCCEEEECCC	53.81	26073543
55	Glutarylation	FVESKSDKWIDIHNP EEECCCCCEEEECCC	53.81	24703693
55	Succinylation	FVESKSDKWIDIHNP EEECCCCCEEEECCC	53.81	23806337
55	Succinylation	FVESKSDKWIDIHNP EEECCCCCEEEECCC	53.81	-
55	Acetylation	FVESKSDKWIDIHNP EEECCCCCEEEECCC	53.81	23576753
76	Succinylation	GRVPQSTKAEMDAAV CCCCCCCHHHHHHHH	47.82	23806337
76	Ubiquitination	GRVPQSTKAEMDAAV CCCCCCCHHHHHHHH	47.82	-
76	Succinylation	GRVPQSTKAEMDAAV CCCCCCCHHHHHHHH	47.82	-
76	Acetylation	GRVPQSTKAEMDAAV CCCCCCCHHHHHHHH	47.82	23576753
76	Glutarylation	GRVPQSTKAEMDAAV CCCCCCCHHHHHHHH	47.82	24703693
86	S-palmitoylation	MDAAVESCKRAFPAW HHHHHHHHHHHCCCH	1.88	28526873
86	S-nitrosylation	MDAAVESCKRAFPAW HHHHHHHHHHHCCCH	1.88	21278135
86	S-nitrosocysteine	MDAAVESCKRAFPAW HHHHHHHHHHHCCCH	1.88	-
87	Glutarylation	DAAVESCKRAFPAWA HHHHHHHHHHCCCHH	56.92	24703693
87	Malonylation	DAAVESCKRAFPAWA HHHHHHHHHHCCCHH	56.92	25418362
87	Acetylation	DAAVESCKRAFPAWA HHHHHHHHHHCCCHH	56.92	23576753
100	Phosphorylation	WADTSILSRQQVLLR HHCCHHHHHHHHHHH	26.77	23567750
113	Malonylation	LRYQQLIKENLKEIA HHHHHHHHHHHHHHH	49.49	26073543
113	Ubiquitination	LRYQQLIKENLKEIA HHHHHHHHHHHHHHH	49.49	-
113	Glutarylation	LRYQQLIKENLKEIA HHHHHHHHHHHHHHH	49.49	24703693
113	Acetylation	LRYQQLIKENLKEIA HHHHHHHHHHHHHHH	49.49	23864654
117	Succinylation	QLIKENLKEIARLIT HHHHHHHHHHHHHHH	59.67	23806337
117	Glutarylation	QLIKENLKEIARLIT HHHHHHHHHHHHHHH	59.67	24703693
117	Acetylation	QLIKENLKEIARLIT HHHHHHHHHHHHHHH	59.67	23576753
117	Malonylation	QLIKENLKEIARLIT HHHHHHHHHHHHHHH	59.67	26320211
117	Succinylation	QLIKENLKEIARLIT HHHHHHHHHHHHHHH	59.67	-
129	Acetylation	LITLEQGKTLADAEG HHHHHCCCCHHHCCC	39.81	23576753
129	Succinylation	LITLEQGKTLADAEG HHHHHCCCCHHHCCC	39.81	23806337
129	Malonylation	LITLEQGKTLADAEG HHHHHCCCCHHHCCC	39.81	26073543
129	Ubiquitination	LITLEQGKTLADAEG HHHHHCCCCHHHCCC	39.81	-
129	Succinylation	LITLEQGKTLADAEG HHHHHCCCCHHHCCC	39.81	-
130	Phosphorylation	ITLEQGKTLADAEGD HHHHCCCCHHHCCCC	33.72	55446217
149	S-nitrosylation	LQVVEHACSVTSLML HHHHHHHHHHHHHHC	3.47	21278135
149	S-nitrosocysteine	LQVVEHACSVTSLML HHHHHHHHHHHHHHC	3.47	-
209	Malonylation	CGNTFLMKPSERVPG HCCCEECCHHHCCCC	47.76	26073543
262	Phosphorylation	KAISFVGSNQAGEYI EEEEEECCCCCCCCC	22.07	-
268	Phosphorylation	GSNQAGEYIFERGSR CCCCCCCCCCCCCCC	15.25	25195567
287	Malonylation	VQANMGAKNHGVVMP EECCCCCCCCCEECC	43.69	25418362
298	Acetylation	VVMPDANKENTLNQL EECCCCCCCCHHHHH	54.80	23576753
298	Malonylation	VVMPDANKENTLNQL EECCCCCCCCHHHHH	54.80	26073543
317	S-palmitoylation	FGAAGQRCMALSTAI HHHHHHHHHHHHHHH	1.12	26165157
330	Malonylation	AILVGEAKKWLPELV HHHHHHHHHHHHHHH	39.93	25418362
330	Acetylation	AILVGEAKKWLPELV HHHHHHHHHHHHHHH	39.93	23576753
331	Ubiquitination	ILVGEAKKWLPELVD HHHHHHHHHHHHHHH	62.10	-
331	Glutarylation	ILVGEAKKWLPELVD HHHHHHHHHHHHHHH	62.10	24703693
331	Acetylation	ILVGEAKKWLPELVD HHHHHHHHHHHHHHH	62.10	23576753
331	Malonylation	ILVGEAKKWLPELVD HHHHHHHHHHHHHHH	62.10	26073543
364	Ubiquitination	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	-
364	Acetylation	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	23576753
364	Succinylation	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	-
364	Malonylation	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	26073543
364	Succinylation	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	23806337
364	Glutarylation	PLITPQAKERVCNLI CCCCHHHHHHHHHHH	40.58	24703693
368	S-nitrosocysteine	PQAKERVCNLIDSGT HHHHHHHHHHHHCCC	4.25	-
368	S-palmitoylation	PQAKERVCNLIDSGT HHHHHHHHHHHHCCC	4.25	28526873
368	S-nitrosylation	PQAKERVCNLIDSGT HHHHHHHHHHHHCCC	4.25	21278135
376	Succinylation	NLIDSGTKEGASILL HHHHCCCCCCCEEEE	58.64	23806337
376	Succinylation	NLIDSGTKEGASILL HHHHCCCCCCCEEEE	58.64	-
376	Malonylation	NLIDSGTKEGASILL HHHHCCCCCCCEEEE	58.64	26073543
376	Acetylation	NLIDSGTKEGASILL HHHHCCCCCCCEEEE	58.64	23576753
376	Ubiquitination	NLIDSGTKEGASILL HHHHCCCCCCCEEEE	58.64	-
380	Phosphorylation	SGTKEGASILLDGRR CCCCCCCEEEECCCE	25.32	-
391	Succinylation	DGRRIKVKGYENGNF CCCEEEEEEEECCCE	51.26	23806337
391	Succinylation	DGRRIKVKGYENGNF CCCEEEEEEEECCCE	51.26	-
391	Acetylation	DGRRIKVKGYENGNF CCCEEEEEEEECCCE	51.26	23806337
391	Ubiquitination	DGRRIKVKGYENGNF CCCEEEEEEEECCCE	51.26	-
408	Ubiquitination	PTIISNVKPSMTCYK CEECCCCCCCCEEEC	35.31	-
408	Malonylation	PTIISNVKPSMTCYK CEECCCCCCCCEEEC	35.31	26073543
413	S-nitrosylation	NVKPSMTCYKEEIFG CCCCCCEEECCHHCC	3.23	21278135
413	S-nitrosocysteine	NVKPSMTCYKEEIFG CCCCCCEEECCHHCC	3.23	-
485	Phosphorylation	PLPMFSFTGSRSSFR CCCCEEEECCCCCCC	32.80	51459437
487	Phosphorylation	PMFSFTGSRSSFRGD CCEEEECCCCCCCCC	26.40	46162115
489	Phosphorylation	FSFTGSRSSFRGDTN EEEECCCCCCCCCCC	35.21	23684622
490	Phosphorylation	SFTGSRSSFRGDTNF EEECCCCCCCCCCCC	20.18	51459449
500	Ubiquitination	GDTNFYGKQGIQFYT CCCCCCCCCCHHHEE	33.69	-
500	Acetylation	GDTNFYGKQGIQFYT CCCCCCCCCCHHHEE	33.69	23576753
500	Malonylation	GDTNFYGKQGIQFYT CCCCCCCCCCHHHEE	33.69	26073543
517	Succinylation	KTITSQWKEEDATLS HHHHHHHHHHCCCCC	43.52	23806337
517	Acetylation	KTITSQWKEEDATLS HHHHHHHHHHCCCCC	43.52	23864654
517	Succinylation	KTITSQWKEEDATLS HHHHHHHHHHCCCCC	43.52	-
517	Malonylation	KTITSQWKEEDATLS HHHHHHHHHHCCCCC	43.52	26073543

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 MMSA_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
55	K	Acetylation	23806337
Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice.
117	K	Acetylation	23806337
Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice.
331	K	Acetylation	23576753
Acetylation of Lys-55; Lys-117 and Lys-331 is observed in liver mitochondria from fasted mice but not from fed mice.

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 MMSA_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of MMSA_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-55; LYS-117 AND LYS-331, ANDMASS SPECTROMETRY.	16916647 [Abstract]

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