SIR4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIR4_HUMAN
• UniProt AC: Q9Y6E7
• Protein Name: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000303|PubMed:25525879}
• Gene Name: SIRT4 {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000312|HGNC:HGNC:14932}
• Organism: Homo sapiens (Human).
• Sequence Length: 314
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. [PubMed: 25525879 Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest]
• Protein Sequence: MKMSFALTFRSAKGRWIANPSQPCSKASIGLFVPASPPLDPEKVKELQRFITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFVRSAPIRQRYWARNFVGWPQFSSHQPNPAHWALSTWEKLGKLYWLVTQNVDALHTKAGSRRLTELHGCMDRVLCLDCGEQTPRGVLQERFQVLNPTWSAEAHGLAPDGDVFLSEEQVRSFQVPTCVQCGGHLKPDVVFFGDTVNPDKVDFVHKRVKEADSLLVVGSSLQVYSGYRFILTAWEKKLPIAILNIGPTRSDDLACLKLNSRCGELLPLIDPC

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
13	Acetylation	ALTFRSAKGRWIANP EEEEECCCCCEEECC	50.70	12432727
26	Acetylation	NPSQPCSKASIGLFV CCCCCCCCCEEEEEE	53.52	12432737
43	Acetylation	SPPLDPEKVKELQRF CCCCCHHHHHHHHHH	65.09	12432745
61	Phosphorylation	SKRLLVMTGAGISTE HHHHHHHCCCCCCCC	19.19	23532336
69	Phosphorylation	GAGISTESGIPDYRS CCCCCCCCCCCCHHH	41.95	23532336
78	Ubiquitination	IPDYRSEKVGLYART CCCHHHHCCEEEEEC	42.73	-
255	Phosphorylation	KRVKEADSLLVVGSS HHHHHCCEEEEECCE	30.56	17924679
261	Phosphorylation	DSLLVVGSSLQVYSG CEEEEECCEEEEECC	19.10	17924679
262	Phosphorylation	SLLVVGSSLQVYSGY EEEEECCEEEEECCC	19.52	17924679
299	Ubiquitination	SDDLACLKLNSRCGE CCHHHHHHCCCCCCC	45.57	29967540

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

Oops, there are no upstream regulatory protein records of SIR4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIR4_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 SIR4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR3_HUMAN	SIRT3	physical	17715127
IDE_HUMAN	IDE	physical	17715127
ADT2_HUMAN	SLC25A5	physical	17715127
ADT3_HUMAN	SLC25A6	physical	17715127
DHE3_MOUSE	Glud1	physical	16959573
CH60_HUMAN	HSPD1	physical	26186194
SNX3_HUMAN	SNX3	physical	26186194
CH60_HUMAN	HSPD1	physical	28514442
SNX3_HUMAN	SNX3	physical	28514442
FANCA_HUMAN	FANCA	physical	28215707

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

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-261 ANDSER-262, AND MASS SPECTROMETRY.
PubMed: 17924679