SGTA_RAT - dbPTM
SGTA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGTA_RAT
UniProt AC O70593
Protein Name Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Gene Name Sgta
Organism Rattus norvegicus (Rat).
Sequence Length 314
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 (By similarity). Binds directly to HSC70 and HSP70 and regulates their ATPase activity. [PubMed: 12878599]
Protein Sequence MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE
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 Orthologous
Protein Cluster
81PhosphorylationDPRGPDRTPPSEEDS
CCCCCCCCCCCHHHH
47.1019700791
84PhosphorylationGPDRTPPSEEDSAEA
CCCCCCCCHHHHHHH
55.6225403869
88PhosphorylationTPPSEEDSAEAERLK
CCCCHHHHHHHHHHH
31.1525403869
95AcetylationSAEAERLKTEGNEQM
HHHHHHHHCCCCHHH
51.2322902405
137AcetylationNRAAAYSKLGNYVGA
HHHHHHHHHHCHHHH
47.97-
137UbiquitinationNRAAAYSKLGNYVGA
HHHHHHHHHHCHHHH
47.97-
160AcetylationGIDPGYSKAYGRMGL
CCCCCCHHHHHHHHH
36.8222902405
160UbiquitinationGIDPGYSKAYGRMGL
CCCCCCHHHHHHHHH
36.82-
200UbiquitinationDTYKSNLKIAELKLR
CHHHHHHHHHEEEEC
44.09-
211PhosphorylationLKLREAPSPTGGVGS
EEECCCCCCCCCCCC
41.9930240740
297PhosphorylationEFVEQIRSQVVRSRT
HHHHHHHHHHHHHCC
29.0225575281
302PhosphorylationIRSQVVRSRTPSASH
HHHHHHHHCCCCCCH
28.9729779826
304PhosphorylationSQVVRSRTPSASHEE
HHHHHHCCCCCCHHH
23.8821738781
306PhosphorylationVVRSRTPSASHEEQQ
HHHHCCCCCCHHHHC
41.6223712012
308PhosphorylationRSRTPSASHEEQQE-
HHCCCCCCHHHHCC-
35.4527097102

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGTA_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGTA_RATSgtaphysical
9557704

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGTA_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND MASSSPECTROMETRY.

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