dbPTM

SGTA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SGTA_MOUSE
UniProt AC	Q8BJU0
Protein Name	Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Gene Name	Sgta
Organism	Mus musculus (Mouse).
Sequence Length	315
Subcellular Localization	Cytoplasm . Nucleus . Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis.
Protein Description	Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex. Binds directly to HSC70 and HSP70 and regulates their ATPase activity..
Protein Sequence	MDNRKRLAYAIIQFLHGQLRHGGLSCDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATSSKQEMPQDPRAPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQQSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
81 (in isoform 2)	Phosphorylation	-	48.34	30352176
82	Phosphorylation	DPRAPDRTPPSEEDS CCCCCCCCCCCHHHH	47.10	27087446
85	Phosphorylation	APDRTPPSEEDSAEA CCCCCCCCHHHHHHH	55.62	25521595
89	Phosphorylation	TPPSEEDSAEAERLK CCCCHHHHHHHHHHH	31.15	25619855
104	Acetylation	TEGNEQMKLENFEAA CCCCHHHHHHHHHHH	52.95	23236377
104	Ubiquitination	TEGNEQMKLENFEAA CCCCHHHHHHHHHHH	52.95	22790023
130	Glutathionylation	PANAVYFCNRAAAYS HHHHHHHHHHHHHHH	1.52	24333276
130	S-nitrosylation	PANAVYFCNRAAAYS HHHHHHHHHHHHHHH	1.52	21278135
130	S-nitrosocysteine	PANAVYFCNRAAAYS HHHHHHHHHHHHHHH	1.52	-
138	Malonylation	NRAAAYSKLGNYVGA HHHHHHHHHHCHHHH	47.97	26320211
138	Ubiquitination	NRAAAYSKLGNYVGA HHHHHHHHHHCHHHH	47.97	-
138	Acetylation	NRAAAYSKLGNYVGA HHHHHHHHHHCHHHH	47.97	23806337
149	S-nitrosocysteine	YVGAVQDCERAIGID HHHHHHHHHHHHCCC	1.82	-
149	S-nitrosylation	YVGAVQDCERAIGID HHHHHHHHHHHHCCC	1.82	21278135
159	Phosphorylation	AIGIDPGYSKAYGRM HHCCCCCCHHHHHHH	16.64	-
161	Acetylation	GIDPGYSKAYGRMGL CCCCCCHHHHHHHHH	36.82	23236377
161	Ubiquitination	GIDPGYSKAYGRMGL CCCCCCHHHHHHHHH	36.82	-
161	Malonylation	GIDPGYSKAYGRMGL CCCCCCHHHHHHHHH	36.82	26320211
175	Ubiquitination	LALSSLNKHAEAVAY HHHHHHHHHHHHHHH	49.86	22790023
185	Ubiquitination	EAVAYYKKALELDPD HHHHHHHHHHHCCCC	41.92	22790023
197	Ubiquitination	DPDNDTYKSNLKIAE CCCCCHHHHHHHHEE	34.65	22790023
201	Ubiquitination	DTYKSNLKIAELKLR CHHHHHHHHEEEEEC	44.09	22790023
206	Ubiquitination	NLKIAELKLREAPSP HHHHEEEEECCCCCC	36.68	22790023
212	Phosphorylation	LKLREAPSPTGGVGS EEECCCCCCCCCCCC	41.99	23649490
298	Phosphorylation	EFVEQIRSQVVRSRT HHHHHHHHHHHHHCC	29.02	22324799
303	Phosphorylation	IRSQVVRSRTPSASH HHHHHHHHCCCCCCH	28.97	25521595
305	Phosphorylation	SQVVRSRTPSASHEE HHHHHHCCCCCCHHH	23.88	27087446
307	Phosphorylation	VVRSRTPSASHEEQQ HHHHCCCCCCHHHHC	41.62	27087446
309	Phosphorylation	RSRTPSASHEEQQE- HHCCCCCCHHHHCC-	35.45	25521595

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 SGTA_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SGTA_MOUSE !!

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 SGTA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNP25_MOUSE	Snap25	physical	21151134
HSP7C_MOUSE	Hspa8	physical	21151134
DNJC5_MOUSE	Dnajc5	physical	21151134
SGTA_MOUSE	Sgta	physical	21151134

Drug and Disease Associations

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

Regulatory Network of SGTA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82 AND SER-307, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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 THR-82, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASSSPECTROMETRY.	18630941 [Abstract]