CALR_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CALR_MOUSE
• UniProt AC: P14211
• Protein Name: Calreticulin
• Gene Name: Calr
• Organism: Mus musculus (Mouse).
• Sequence Length: 416
• Subcellular Localization: Endoplasmic reticulum lumen . Cytoplasmic granule . Sarcoplasmic reticulum lumen . Associated with the lytic granules in the cytolytic T-lymphocytes.
• Protein Description: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity)..
• Protein Sequence: MLLSVPLLLGLLGLAAADPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDLEKDKGLQTSQDARFYALSAKFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPSGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDDDRDEDEDEEDEKEEDEEESPGQAKDEL

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
43	Acetylation	RWVESKHKSDFGKFV HHHHHCCHHHCHHEE	56.29	22826441
48	Acetylation	KHKSDFGKFVLSSGK CCHHHCHHEEECCCE	32.09	23806337
48	Succinylation	KHKSDFGKFVLSSGK CCHHHCHHEEECCCE	32.09	23954790
52	Phosphorylation	DFGKFVLSSGKFYGD HCHHEEECCCEEECC	31.57	26239621
53	Phosphorylation	FGKFVLSSGKFYGDL CHHEEECCCEEECCC	41.67	26239621
55	Succinylation	KFVLSSGKFYGDLEK HEEECCCEEECCCCC	37.04	23806337
55	Acetylation	KFVLSSGKFYGDLEK HEEECCCEEECCCCC	37.04	23806337
55	Ubiquitination	KFVLSSGKFYGDLEK HEEECCCEEECCCCC	37.04	-
57	Phosphorylation	VLSSGKFYGDLEKDK EECCCEEECCCCCCC	17.14	26239621
62	Ubiquitination	KFYGDLEKDKGLQTS EEECCCCCCCCCCCC	72.53	-
62	Succinylation	KFYGDLEKDKGLQTS EEECCCCCCCCCCCC	72.53	23954790
62	Acetylation	KFYGDLEKDKGLQTS EEECCCCCCCCCCCC	72.53	23864654
64	Acetylation	YGDLEKDKGLQTSQD ECCCCCCCCCCCCHH	73.00	23806337
64	Succinylation	YGDLEKDKGLQTSQD ECCCCCCCCCCCCHH	73.00	23806337
68	Phosphorylation	EKDKGLQTSQDARFY CCCCCCCCCHHHHHE	33.14	30635358
69	Phosphorylation	KDKGLQTSQDARFYA CCCCCCCCHHHHHEE	17.07	30635358
75	Phosphorylation	TSQDARFYALSAKFE CCHHHHHEEEEEEEE	10.90	29514104
80	Succinylation	RFYALSAKFEPFSNK HHEEEEEEEECCCCC	47.05	23954790
80	Ubiquitination	RFYALSAKFEPFSNK HHEEEEEEEECCCCC	47.05	-
80	Acetylation	RFYALSAKFEPFSNK HHEEEEEEEECCCCC	47.05	22733758
98	Acetylation	LVVQFTVKHEQNIDC EEEEEEEECCCCCCC	38.06	22826441
105	S-palmitoylation	KHEQNIDCGGGYVKL ECCCCCCCCCEEEEE	4.90	26165157
105	Glutathionylation	KHEQNIDCGGGYVKL ECCCCCCCCCEEEEE	4.90	24333276
105	S-nitrosylation	KHEQNIDCGGGYVKL ECCCCCCCCCEEEEE	4.90	24926564
109	Phosphorylation	NIDCGGGYVKLFPSG CCCCCCEEEEECCCC	9.55	30635358
111	Acetylation	DCGGGYVKLFPSGLD CCCCEEEEECCCCCC	35.61	23576753
115	Phosphorylation	GYVKLFPSGLDQKDM EEEEECCCCCCCCCC	44.66	24899341
137	Glutathionylation	IMFGPDICGPGTKKV EEECCCCCCCCCCEE	7.59	24333276
142	Acetylation	DICGPGTKKVHVIFN CCCCCCCCEEEEEEE	59.73	2372771
143	Acetylation	ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE	37.09	22826441
150	Phosphorylation	KVHVIFNYKGKNVLI EEEEEEEECCCEEEE	15.46	22817900
151	Acetylation	VHVIFNYKGKNVLIN EEEEEEECCCEEEEC	65.59	23864654
151	Succinylation	VHVIFNYKGKNVLIN EEEEEEECCCEEEEC	65.59	23954790
153	Acetylation	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	23806337
153	Succinylation	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	23806337
159	Acetylation	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	23806337
163	Glutathionylation	LINKDIRCKDDEFTH EECCCCCCCCCCCEE	6.07	24333276
163	S-nitrosylation	LINKDIRCKDDEFTH EECCCCCCCCCCCEE	6.07	22178444
164	Acetylation	INKDIRCKDDEFTHL ECCCCCCCCCCCEEE	59.36	23201123
189	Phosphorylation	YEVKIDNSQVESGSL EEEEECCCCCCCCCC	31.67	25293948
193	Phosphorylation	IDNSQVESGSLEDDW ECCCCCCCCCCCCCC	34.52	25293948
195	Phosphorylation	NSQVESGSLEDDWDF CCCCCCCCCCCCCCC	37.55	25293948
206	Succinylation	DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC	66.25	23954790
207	Acetylation	WDFLPPKKIKDPDAA CCCCCCCCCCCCCCC	61.84	22826441
209	Succinylation	FLPPKKIKDPDAAKP CCCCCCCCCCCCCCC	72.58	23806337
209	Acetylation	FLPPKKIKDPDAAKP CCCCCCCCCCCCCCC	72.58	23806337
215	Acetylation	IKDPDAAKPEDWDER CCCCCCCCCCCCCHH	51.14	23864654
215	Succinylation	IKDPDAAKPEDWDER CCCCCCCCCCCCCHH	51.14	23954790
229	Phosphorylation	RAKIDDPTDSKPEDW HHCCCCCCCCCCCCC	60.96	21743459
231	Phosphorylation	KIDDPTDSKPEDWDK CCCCCCCCCCCCCCC	53.22	21743459
232	Acetylation	IDDPTDSKPEDWDKP CCCCCCCCCCCCCCC	56.06	23864654
238	Acetylation	SKPEDWDKPEHIPDP CCCCCCCCCCCCCCC	48.31	23806337
248	Acetylation	HIPDPDAKKPEDWDE CCCCCCCCCCCCCCH	76.01	23864654
285	Phosphorylation	RQIDNPDYKGTWIHP CCCCCCCCCCCCCCC	16.75	28464351
338	Phosphorylation	LITNDEAYAEEFGNE EECCCHHHHHHHCCC	16.70	22817900
360	Acetylation	AEKQMKDKQDEEQRL HHHHHCCHHHHHHHH	54.88	23864654
360	Succinylation	AEKQMKDKQDEEQRL HHHHHCCHHHHHHHH	54.88	23954790
368	Acetylation	QDEEQRLKEEEEDKK HHHHHHHHHHHHHHH	66.33	23201123
368	Succinylation	QDEEQRLKEEEEDKK HHHHHHHHHHHHHHH	66.33	23954790
374	Acetylation	LKEEEEDKKRKEEEE HHHHHHHHHHHHHHH	58.73	23864654
375	Acetylation	KEEEEDKKRKEEEEA HHHHHHHHHHHHHHH	79.58	2381003
408	Phosphorylation	KEEDEEESPGQAKDE HHHHHCCCCCCCCCC	37.30	25195567

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CALR_MOUSE !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of CALR_MOUSE !!

Drug and Disease Associations

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