SGT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SGT1_MOUSE
• UniProt AC: Q9CX34
• Protein Name: Protein SGT1 homolog {ECO:0000250|UniProtKB:Q08446}
• Gene Name: Sugt1 {ECO:0000312|MGI:MGI:1915205}
• Organism: Mus musculus (Mouse).
• Sequence Length: 336
• Subcellular Localization: Cytoplasm. Nucleus. Translocates the to nucleus upon heat shock, requiring S100A6..
• Protein Description: May play a role in ubiquitination and subsequent proteasomal degradation of target proteins..
• Protein Sequence: MAAAAAGPASSQRLFQSFSDALIDGDPQAALEELTKALEQNPDDAQYYCQRAYCHILLGKYRDGIADVKKSLELNPNNCTALLRKGICEYHEKDYASALETFAEGQKLDSTDTNFDTWIKRCQEIQNGSESEVSASQRTQSKIKYDWYQTESHVIITLMIKSVQKNDVRVGFSERELSALVKIPAGEDYSLKLRLLHPIIPEQSTFKVLSTKIEIKMKKPEAVRWEKLEGQGDEPTPKQFTADVKNMYPSSSHYTRNWDKLVGEIKEEEKNEKLEGDAALNKLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTNWSDVGKRKVEINPPDDMEWKQY

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
2	Acetylation	------MAAAAAGPA ------CCCCCCCCH	63.17	-
10	Phosphorylation	AAAAGPASSQRLFQS CCCCCCHHHHHHHHH	5.11	29514104
11	Phosphorylation	AAAGPASSQRLFQSF CCCCCHHHHHHHHHH	27.45	29472430
47	Phosphorylation	QNPDDAQYYCQRAYC HCCCHHHHHHHHHHH	4.76	-
49	S-nitrosocysteine	PDDAQYYCQRAYCHI CCHHHHHHHHHHHHH	5.63	-
93	Acetylation	GICEYHEKDYASALE CHHHHHHHHHHHHHH	7.52	22826441
97	Phosphorylation	YHEKDYASALETFAE HHHHHHHHHHHHHHC	37.14	26525534
129	Phosphorylation	CQEIQNGSESEVSAS HHHHHCCCHHHCCHH	9.52	26525534
131	Phosphorylation	EIQNGSESEVSASQR HHHCCCHHHCCHHHH	40.28	26525534
192	Acetylation	AGEDYSLKLRLLHPI CCCCCEEEEHHHCCC	28.13	22826441
205	Phosphorylation	PIIPEQSTFKVLSTK CCCCCCCCEEEEEEE	15.94	29899451
207	Acetylation	IPEQSTFKVLSTKIE CCCCCCEEEEEEEEE	23.53	22826441
227	Acetylation	PEAVRWEKLEGQGDE CCCCCHHHCCCCCCC	5.88	22826441
236	Phosphorylation	EGQGDEPTPKQFTAD CCCCCCCCCCCCCCH	12.12	29899451
248	Phosphorylation	TADVKNMYPSSSHYT CCHHHHHCCCCCHHC	6.08	29514104
252	Phosphorylation	KNMYPSSSHYTRNWD HHHCCCCCHHCCCHH	12.65	-
254	Phosphorylation	MYPSSSHYTRNWDKL HCCCCCHHCCCHHHH	36.40	29514104
255	Phosphorylation	YPSSSHYTRNWDKLV CCCCCHHCCCHHHHH	53.52	28576409
270	Acetylation	GEIKEEEKNEKLEGD HHHCHHHHHHHCCHH	5.36	7614587
273	Ubiquitination	KEEEKNEKLEGDAAL CHHHHHHHCCHHHHH	3.63	22790023
288	Phosphorylation	NKLFQQIYSDGSDEV HHHHHHHHCCCCHHH	34.10	22817900
292	Phosphorylation	QQIYSDGSDEVKRAM HHHHCCCCHHHHHHH	21.18	25367039
302	Phosphorylation	VKRAMNKSFMESGGT HHHHHHHHHHHCCCE	5.13	-

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
302	S	Phosphorylation	Kinase	PLK1	P53350	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
252	S	Phosphorylation	Phosphorylated at Ser-252 and Ser-302, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex.	-
302	S	Phosphorylation	Phosphorylated at Ser-252 and Ser-302, dephosphorylation promotes nuclear translocation, most likely due to disruption of the SUGT1-HSP90 complex.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SGT1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITBP2_MOUSE	Itgb1bp2	physical	18474241

Drug and Disease Associations

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