dbPTM

SQSTM_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SQSTM_MOUSE
UniProt AC	Q64337
Protein Name	Sequestosome-1
Gene Name	Sqstm1
Organism	Mus musculus (Mouse).
Sequence Length	442
Subcellular Localization	Cytoplasm, cytosol . Late endosome . Nucleus . Endoplasmic reticulum . Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus, PML body . Cytoplasm, myofibril, sarcomere. In cardiac muscles, localizes to the sarcomeric band. May also localize to the h
Protein Description	Autophagy receptor required for selective macroautophagy (aggrephagy). Functions as a bridge between polyubiquitinated cargo and autophagosomes. Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD. [PubMed: 14960283]
Protein Sequence	MASFTVKAYLLGKEEATREIRRFSFCFSPEPEAEAQAAAGPGPCERLLSRVAVLFPTLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRREHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKLIFPNPFGHLSDSFSHSRWLRKLKHGHFGWPGWEMGPPGNWSPRPPRAGDGRPCPTAESASAPPEDPNVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPTTPESSSTGTEDKSNTQPSSCSSEVSKPDGAGEGPAQSLTEQMKKIALESVGQPEEQMESGNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASFTVKAY ------CCCEEEEEH	17.22	-
13	Ubiquitination	VKAYLLGKEEATREI EEEHHCCCHHHHHHH	52.96	22790023
24	Phosphorylation	TREIRRFSFCFSPEP HHHHHHHEEECCCCH	21.20	25521595
28	Phosphorylation	RRFSFCFSPEPEAEA HHHEEECCCCHHHHH	29.54	25521595
91	Ubiquitination	TMAMSYVKDDIFRIY HHHHHHHHHCHHHEE	41.26	-
113	S-palmitoylation	RREHRPPCAQEAPRN HHHHCCCCHHHCCCC	7.27	26165157
128	Glutathionylation	MVHPNVICDGCNGPV CCCCCEEECCCCCCC	2.99	24333276
131	Glutathionylation	PNVICDGCNGPVVGT CCEEECCCCCCCCCC	3.21	24333276
141	Ubiquitination	PVVGTRYKCSVCPDY CCCCCCEEEEECCCC	19.42	22790023
143	Phosphorylation	VGTRYKCSVCPDYDL CCCCEEEEECCCCCC	23.70	27742792
145	S-nitrosocysteine	TRYKCSVCPDYDLCS CCEEEEECCCCCCHH	0.91	-
145	S-nitrosylation	TRYKCSVCPDYDLCS CCEEEEECCCCCCHH	0.91	20925432
148	Phosphorylation	KCSVCPDYDLCSVCE EEEECCCCCCHHHCC	8.92	27742792
152	Phosphorylation	CPDYDLCSVCEGKGL CCCCCCHHHCCCCCC	36.78	24453211
157	Ubiquitination	LCSVCEGKGLHREHS CHHHCCCCCCCHHCC	35.69	22790023
165	Ubiquitination	GLHREHSKLIFPNPF CCCHHCCCCCCCCCC	47.73	22790023
176	Phosphorylation	PNPFGHLSDSFSHSR CCCCCCCCCCCCCHH	26.07	26239621
178	Phosphorylation	PFGHLSDSFSHSRWL CCCCCCCCCCCHHHH	25.85	26824392
180	Phosphorylation	GHLSDSFSHSRWLRK CCCCCCCCCHHHHHH	25.22	26745281
182	Phosphorylation	LSDSFSHSRWLRKLK CCCCCCCHHHHHHHC	24.77	26745281
207	Phosphorylation	MGPPGNWSPRPPRAG CCCCCCCCCCCCCCC	18.28	26745281
219	Glutathionylation	RAGDGRPCPTAESAS CCCCCCCCCCCCCCC	4.51	24333276
221	Phosphorylation	GDGRPCPTAESASAP CCCCCCCCCCCCCCC	50.18	25619855
224	Phosphorylation	RPCPTAESASAPPED CCCCCCCCCCCCCCC	25.67	28066266
226	Phosphorylation	CPTAESASAPPEDPN CCCCCCCCCCCCCCC	51.06	25619855
249	Phosphorylation	ESVAAALSPLGIEVD HHHHHHHCCCCEEEE	17.22	26643407
266	Phosphorylation	VEHGGKRSRLTPTTP CCCCCEECCCCCCCC	34.82	25521595
269	Phosphorylation	GGKRSRLTPTTPESS CCEECCCCCCCCCCC	19.92	27087446
271	Phosphorylation	KRSRLTPTTPESSST EECCCCCCCCCCCCC	50.15	25521595
272	Phosphorylation	RSRLTPTTPESSSTG ECCCCCCCCCCCCCC	26.68	27087446
275	Phosphorylation	LTPTTPESSSTGTED CCCCCCCCCCCCCCC	30.69	25521595
276	Phosphorylation	TPTTPESSSTGTEDK CCCCCCCCCCCCCCC	30.20	27742792
277	Phosphorylation	PTTPESSSTGTEDKS CCCCCCCCCCCCCCC	39.89	25521595
278	Phosphorylation	TTPESSSTGTEDKSN CCCCCCCCCCCCCCC	50.50	27742792
280	Phosphorylation	PESSSTGTEDKSNTQ CCCCCCCCCCCCCCC	40.89	28725479
284	Phosphorylation	STGTEDKSNTQPSSC CCCCCCCCCCCCCCC	58.39	25619855
286	Phosphorylation	GTEDKSNTQPSSCSS CCCCCCCCCCCCCCC	49.28	25619855
289	Phosphorylation	DKSNTQPSSCSSEVS CCCCCCCCCCCCCCC	33.87	25619855
290	Phosphorylation	KSNTQPSSCSSEVSK CCCCCCCCCCCCCCC	25.38	25619855
291	Glutathionylation	SNTQPSSCSSEVSKP CCCCCCCCCCCCCCC	6.43	24333276
292	Phosphorylation	NTQPSSCSSEVSKPD CCCCCCCCCCCCCCC	31.33	25619855
293	Phosphorylation	TQPSSCSSEVSKPDG CCCCCCCCCCCCCCC	46.47	25619855
296	Phosphorylation	SSCSSEVSKPDGAGE CCCCCCCCCCCCCCC	34.12	25619855
297	Ubiquitination	SCSSEVSKPDGAGEG CCCCCCCCCCCCCCC	52.91	22790023
308	Phosphorylation	AGEGPAQSLTEQMKK CCCCCCHHHHHHHHH	39.09	25521595
310	Phosphorylation	EGPAQSLTEQMKKIA CCCCHHHHHHHHHHH	29.44	25619855
314	Ubiquitination	QSLTEQMKKIALESV HHHHHHHHHHHHHHC	40.50	22790023
315	Ubiquitination	SLTEQMKKIALESVG HHHHHHHHHHHHHCC	28.06	22790023
320	Phosphorylation	MKKIALESVGQPEEQ HHHHHHHHCCCHHHH	32.19	25619855
330	Phosphorylation	QPEEQMESGNCSGGD CHHHHHHCCCCCCCC	29.93	24925903
334	Phosphorylation	QMESGNCSGGDDDWT HHHCCCCCCCCCCCH	50.22	24925903
341 (in isoform 2)	Phosphorylation	-	21.67	25266776
341	Phosphorylation	SGGDDDWTHLSSKEV CCCCCCCHHHCCCEE	21.67	24925903
344	Phosphorylation	DDDWTHLSSKEVDPS CCCCHHHCCCEECCC	31.59	24925903
345	Phosphorylation	DDWTHLSSKEVDPST CCCHHHCCCEECCCC	38.91	24925903
345 (in isoform 2)	Phosphorylation	-	38.91	25266776
351	Phosphorylation	SSKEVDPSTGELQSL CCCEECCCCCCCCCC	44.58	25168779
352	Phosphorylation	SKEVDPSTGELQSLQ CCEECCCCCCCCCCC	39.81	25619855
357	Phosphorylation	PSTGELQSLQMPESE CCCCCCCCCCCCCCC	32.94	27087446
363	Phosphorylation	QSLQMPESEGPSSLD CCCCCCCCCCCCCCC	41.82	27087446
367	Phosphorylation	MPESEGPSSLDPSQE CCCCCCCCCCCCCCC	55.15	27087446
368	Phosphorylation	PESEGPSSLDPSQEG CCCCCCCCCCCCCCC	39.67	27087446
372	Phosphorylation	GPSSLDPSQEGPTGL CCCCCCCCCCCCCCC	40.30	22942356
377	Phosphorylation	DPSQEGPTGLKEAAL CCCCCCCCCCHHHHH	67.03	25168779
384	Ubiquitination	TGLKEAALYPHLPPE CCCHHHHHCCCCCCC	9.84	27667366
405	Phosphorylation	ESLSQMLSMGFSDEG HHHHHHHHCCCCCCC	16.12	26643407
409	Phosphorylation	QMLSMGFSDEGGWLT HHHHCCCCCCCCHHH	29.08	26643407
422	Ubiquitination	LTRLLQTKNYDIGAA HHHHHHCCCCCHHHH	40.32	22790023
437	Ubiquitination	LDTIQYSKHPPPL-- HHHHHHCCCCCCC--	56.02	22790023

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
351	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
351	S	Phosphorylation	Kinase	MAP3K7	Q62073	GPS
351	S	Phosphorylation	Kinase	MTOR	P42345	PSP
351	S	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
405	S	Phosphorylation	Kinase	TBK1	Q9WUN2	Uniprot
405	S	Phosphorylation	Kinase	ULK1	O70405	Uniprot
409	S	Phosphorylation	Kinase	ULK1	O75385	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
29	K	ubiquitylation	-
Ubiquitinated via 'Lys-29' and 'Lys-33'-linked polyubiquitination leading to xenophagic targeting of bacteria and inhibition of their replication.
351	S	Phosphorylation	20173742
Phosphorylation at Ser-351 by MTOR promotes interaction with KEAP1 and inactivation of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes.
405	S	Phosphorylation	24011591
Phosphorylated at Ser-405 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity).
405	S	Phosphorylation	24011591
Phosphorylation at Ser-405 by ULK1 is stimulated by SESN2 (By similarity).
405	S	ubiquitylation	24011591
Phosphorylated at Ser-405 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity).
422	K	ubiquitylation	-
Ubiquitinated by the BCR(KEAP1) complex at Lys-422, increasing SQSTM1 sequestering activity and promoting its degradation.

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 SQSTM_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NTRK1_MOUSE	Ntrk1	physical	18598672
TR30A_MOUSE	Trim30a	physical	18598672
RIPK1_MOUSE	Ripk1	physical	19850933
KPCD_MOUSE	Prkcd	physical	19850933
CYLD_MOUSE	Cyld	physical	21878516
CUL3_MOUSE	Cul3	physical	22167182
A16L1_MOUSE	Atg16l1	physical	22167182
SQSTM_MOUSE	Sqstm1	physical	21715324
SODC_MOUSE	Sod1	physical	19765191
MLP3A_MOUSE	Map1lc3a	physical	19765191
MLP3A_MOUSE	Map1lc3a	physical	18083104
SODC_MOUSE	Sod1	physical	17296612
NRAM1_MOUSE	Slc11a1	physical	20206555
UBIM_MOUSE	Fau	physical	20206555
MLP3A_MOUSE	Map1lc3a	physical	18524774
KEAP1_MOUSE	Keap1	physical	20173742
MK01_MOUSE	Mapk1	physical	16517408
MK03_MOUSE	Mapk3	physical	20154642
ULK1_MOUSE	Ulk1	physical	17389358
TRAF6_MOUSE	Traf6	physical	17389358
ANDR_MOUSE	Ar	physical	23637164
MLP3A_MOUSE	Map1lc3a	physical	23637164
UBC_MOUSE	Ubc	physical	23637164
UBC_MOUSE	Ubc	physical	21715324
PELI3_MOUSE	Peli3	physical	25483963
CEP63_HUMAN	CEP63	physical	27869116
MLP3B_RAT	Map1lc3b	physical	27442348
SQSTM_MOUSE	Sqstm1	physical	27442348

Drug and Disease Associations

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

Regulatory Network of SQSTM_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-269 ANDTHR-272, AND MASS SPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASSSPECTROMETRY.	15345747 [Abstract]

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