dbPTM

SQSTM_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SQSTM_RAT
UniProt AC	O08623
Protein Name	Sequestosome-1
Gene Name	Sqstm1
Organism	Rattus norvegicus (Rat).
Sequence Length	439
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. Localizes to late endosomes.
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 (By similarity). Involved in midbody ring degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. [PubMed: 11244088]
Protein Sequence	MASLTVKAYLLGKEEAAREIRRFSFCFSPEPEAEAAAGPGPCERLLSRVAVLFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRREHRPPCAQEARSMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKLIFPNPFGHLSDSFSHSRWLRKLKHGHFGWPGWEMGPPGNWSPRPPRAGDGRPCPTAESASAPSEDPNVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPTSAESSSTGTEDKSGTQPSSCSSEVSKPDGAGEGPAQSLTEQMKKIALESVGQPEELMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASLTVKAY ------CCCHHHHHH	17.16	-
24	Phosphorylation	AREIRRFSFCFSPEP HHHHHHHCEECCCCH	21.20	29779826
28	Phosphorylation	RRFSFCFSPEPEAEA HHHCEECCCCHHHHH	29.54	27097102
145	Phosphorylation	KCSVCPDYDLCSVCE EEEECCCCCCHHHCC	8.92	-
149	Phosphorylation	CPDYDLCSVCEGKGL CCCCCCHHHCCCCCC	36.78	23984901
173	Phosphorylation	PNPFGHLSDSFSHSR CCCCCCCCCCCCCHH	26.07	23984901
175	Phosphorylation	PFGHLSDSFSHSRWL CCCCCCCCCCCHHHH	25.85	23984901
177	Phosphorylation	GHLSDSFSHSRWLRK CCCCCCCCCHHHHHH	25.22	23984901
179	Phosphorylation	LSDSFSHSRWLRKLK CCCCCCCHHHHHHHC	24.77	23984901
204	Phosphorylation	MGPPGNWSPRPPRAG CCCCCCCCCCCCCCC	18.28	27097102
226	Phosphorylation	AESASAPSEDPNVNF CCCCCCCCCCCCCCH	55.11	28689409
246	Phosphorylation	ESVAAALSPLGIEVD HHHHHHHCCCCEEEE	17.22	-
263	Phosphorylation	VEHGGKRSRLTPTSA CCCCCEECCCCCCCC	34.82	30240740
266	Phosphorylation	GGKRSRLTPTSAESS CCEECCCCCCCCCCC	24.34	28689409
268	Phosphorylation	KRSRLTPTSAESSST EECCCCCCCCCCCCC	35.02	23298284
269	Phosphorylation	RSRLTPTSAESSSTG ECCCCCCCCCCCCCC	31.10	22108457
272	Phosphorylation	LTPTSAESSSTGTED CCCCCCCCCCCCCCC	29.34	27097102
273	Phosphorylation	TPTSAESSSTGTEDK CCCCCCCCCCCCCCC	24.35	27097102
274	Phosphorylation	PTSAESSSTGTEDKS CCCCCCCCCCCCCCC	39.89	27097102
275	Phosphorylation	TSAESSSTGTEDKSG CCCCCCCCCCCCCCC	50.50	28432305
277	Phosphorylation	AESSSTGTEDKSGTQ CCCCCCCCCCCCCCC	40.89	28432305
281	Phosphorylation	STGTEDKSGTQPSSC CCCCCCCCCCCCCCC	60.43	27097102
283	Phosphorylation	GTEDKSGTQPSSCSS CCCCCCCCCCCCCCC	44.38	27097102
286	Phosphorylation	DKSGTQPSSCSSEVS CCCCCCCCCCCCCCC	33.87	27097102
287	Phosphorylation	KSGTQPSSCSSEVSK CCCCCCCCCCCCCCC	25.38	27097102
289	Phosphorylation	GTQPSSCSSEVSKPD CCCCCCCCCCCCCCC	31.33	27097102
290	Phosphorylation	TQPSSCSSEVSKPDG CCCCCCCCCCCCCCC	46.47	27097102
293	Phosphorylation	SSCSSEVSKPDGAGE CCCCCCCCCCCCCCC	34.12	27097102
305	Phosphorylation	AGEGPAQSLTEQMKK CCCCCCHHHHHHHHH	39.09	27097102
307	Phosphorylation	EGPAQSLTEQMKKIA CCCCHHHHHHHHHHH	29.44	27097102
317	Phosphorylation	MKKIALESVGQPEEL HHHHHHHHCCCHHHH	32.19	28551015
327	Phosphorylation	QPEELMESDNCSGGD CHHHHHHCCCCCCCC	21.84	27097102
331	Phosphorylation	LMESDNCSGGDDDWT HHHCCCCCCCCCCCH	52.65	27097102
338	Phosphorylation	SGGDDDWTHLSSKEV CCCCCCCHHHCCCEE	21.67	27097102
341	Phosphorylation	DDDWTHLSSKEVDPS CCCCHHHCCCEECCC	31.59	27097102
342	Phosphorylation	DDWTHLSSKEVDPST CCCHHHCCCEECCCC	38.91	27097102
348	Phosphorylation	SSKEVDPSTGELQSL CCCEECCCCCCCCCC	44.58	27097102
349	Phosphorylation	SKEVDPSTGELQSLQ CCEECCCCCCCCCCC	39.81	27097102
354	Phosphorylation	PSTGELQSLQMPESE CCCCCCCCCCCCCCC	32.94	27097102
360	Phosphorylation	QSLQMPESEGPSSLD CCCCCCCCCCCCCCC	41.82	27097102
364	Phosphorylation	MPESEGPSSLDPSQE CCCCCCCCCCCCCCC	55.15	27097102
365	Phosphorylation	PESEGPSSLDPSQEG CCCCCCCCCCCCCCC	39.67	23712012
369	Phosphorylation	GPSSLDPSQEGPTGL CCCCCCCCCCCCCCC	40.30	27097102
374	Phosphorylation	DPSQEGPTGLKEAAL CCCCCCCCCCHHHHH	67.03	27097102
402	Phosphorylation	ESLSQMLSMGFSDEG HHHHHHHHCCCCCCC	16.12	-

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
293	S	Phosphorylation	Kinase	PRKAA1	P54645	GPS
402	S	Phosphorylation	Kinase	ULK1	-	Uniprot
402	S	Phosphorylation	Kinase	TBK1	-	Uniprot

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.
348	S	Phosphorylation	9177193
Phosphorylation at Ser-348 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 (By similarity).
402	S	Phosphorylation	9177193
Phosphorylated at Ser-402 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity).
402	S	Phosphorylation	9177193
Phosphorylation at Ser-402 by ULK1 is stimulated by SESN2 (By similarity).
402	S	ubiquitylation	9177193
Phosphorylated at Ser-402 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity).
419	K	ubiquitylation	-
Ubiquitinated by the BCR(KEAP1) complex at Lys-419, 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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_RAT	Sqstm1	physical	12431995
KPCZ_RAT	Prkcz	physical	12431995
KCAB2_RAT	Kcnab2	physical	12431995
TRAF6_RAT	Traf6	physical	16252010
NRIF1_RAT	Zfp110	physical	16252010
IRS1_RAT	Irs1	physical	22761437
SUMO1_BOVIN	SUMO1	physical	21707618
SPART_BOVIN	SPG20	physical	21707618
SPART_MOUSE	Spg20	physical	21707618
KPCZ_HUMAN	PRKCZ	physical	20979579
KPCZ_RAT	Prkcz	physical	20979579
KPCZ_RAT	Prkcz	physical	9177193
SQSTM_RAT	Sqstm1	physical	9177193
KPCI_RAT	Prkci	physical	11500922

Drug and Disease Associations

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

Regulatory Network of SQSTM_RAT

Related Literatures of Post-Translational Modification

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