dbPTM

SSRA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSRA_MOUSE
UniProt AC	Q9CY50
Protein Name	Translocon-associated protein subunit alpha
Gene Name	Ssr1
Organism	Mus musculus (Mouse).
Sequence Length	286
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein.
Protein Description	TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins..
Protein Sequence	MRLLPRLLLLFLLAFPAAVLLRGGPGGSLALAQDPTEDEEIVEDSIIEDEDDEAEVEEDEPTDLAEDKEEEDVSSEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVVVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRQPRKRAQKRSVGSDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
75	Phosphorylation	KEEEDVSSEPEASPS CCCCCCCCCCCCCCC	57.95	25195567
112	Phosphorylation	VGFTNKGTEDFIVES HCCCCCCCCCEEEEE	33.71	23140645
119	Phosphorylation	TEDFIVESLDASFRY CCCEEEEECCHHCCC	22.21	23140645
123	Phosphorylation	IVESLDASFRYPQDY EEEECCHHCCCCCCC	15.21	23140645
126	Phosphorylation	SLDASFRYPQDYQFY ECCHHCCCCCCCEEE	11.84	23140645
130	Phosphorylation	SFRYPQDYQFYIQNF HCCCCCCCEEEEEEE	8.69	23140645
133	Phosphorylation	YPQDYQFYIQNFTAL CCCCCEEEEEEEEEE	6.00	23140645
136	N-linked_Glycosylation	DYQFYIQNFTALPLN CCEEEEEEEEEEECC	27.03	19656770
138	Phosphorylation	QFYIQNFTALPLNTV EEEEEEEEEEECCCC	34.53	23140645
143	N-linked_Glycosylation	NFTALPLNTVVPPQR EEEEEECCCCCCCCC	28.96	19656770
191	N-linked_Glycosylation	VFQDAVFNQTVTVIE CCCHHHHCCEEEEEE	29.98	-
245	Phosphorylation	IQKVEMGTSSQNDVD CCEEECCCCCCCCCC	24.72	25619855
246	Phosphorylation	QKVEMGTSSQNDVDM CEEECCCCCCCCCCH	24.97	25619855
247	Phosphorylation	KVEMGTSSQNDVDMS EEECCCCCCCCCCHH	32.61	25619855
254	Phosphorylation	SQNDVDMSWIPQETL CCCCCCHHHCCHHHH	19.86	25619855
260	Phosphorylation	MSWIPQETLNQINKA HHHCCHHHHHHHHHC	26.26	25521595
268	Phosphorylation	LNQINKASPRRQPRK HHHHHHCCCCCCCCH	22.13	27087446
281	Phosphorylation	RKRAQKRSVGSDE-- CHHHHHCCCCCCC--	37.55	22324799
284	Phosphorylation	AQKRSVGSDE----- HHHCCCCCCC-----	36.09	28066266

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 SSRA_MOUSE !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SSRA_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SSRA_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-143, AND MASSSPECTROMETRY.	19656770 [Abstract]
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-268, 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-260, AND MASSSPECTROMETRY.	18630941 [Abstract]