dbPTM

CALR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CALR_HUMAN
UniProt AC	P27797
Protein Name	Calreticulin
Gene Name	CALR
Organism	Homo sapiens (Human).
Sequence Length	417
Subcellular Localization	Endoplasmic reticulum lumen . Cytoplasm, cytosol . Secreted, extracellular space, extracellular matrix . Cell surface . Sarcoplasmic reticulum lumen . Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). Associate
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	MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MLLSVPLLLGLLGL -CCCHHHHHHHHHHH	6.05	21890473
22	Phosphorylation	AVAEPAVYFKEQFLD HHHCCCCCCCCCCCC	15.84	-
24	Ubiquitination	AEPAVYFKEQFLDGD HCCCCCCCCCCCCCC	32.68	21890473
24	Sumoylation	AEPAVYFKEQFLDGD HCCCCCCCCCCCCCC	32.68	-
34	Phosphorylation	FLDGDGWTSRWIESK CCCCCCHHHHHHHHC	17.59	21712546
35	Phosphorylation	LDGDGWTSRWIESKH CCCCCHHHHHHHHCC	21.07	21712546
41	Acetylation	TSRWIESKHKSDFGK HHHHHHHCCHHHCCE	42.11	25953088
41	2-Hydroxyisobutyrylation	TSRWIESKHKSDFGK HHHHHHHCCHHHCCE	42.11	-
41	Ubiquitination	TSRWIESKHKSDFGK HHHHHHHCCHHHCCE	42.11	-
43	Succinylation	RWIESKHKSDFGKFV HHHHHCCHHHCCEEE	56.29	23954790
43	2-Hydroxyisobutyrylation	RWIESKHKSDFGKFV HHHHHCCHHHCCEEE	56.29	-
44	Phosphorylation	WIESKHKSDFGKFVL HHHHCCHHHCCEEEE	37.58	24719451
48	Acetylation	KHKSDFGKFVLSSGK CCHHHCCEEEECCCC	32.09	19608861
48	Ubiquitination	KHKSDFGKFVLSSGK CCHHHCCEEEECCCC	32.09	21890473
48	Succinylation	KHKSDFGKFVLSSGK CCHHHCCEEEECCCC	32.09	23954790
48	2-Hydroxyisobutyrylation	KHKSDFGKFVLSSGK CCHHHCCEEEECCCC	32.09	-
48	Ubiquitination	KHKSDFGKFVLSSGK CCHHHCCEEEECCCC	32.09	21890473
52	Phosphorylation	DFGKFVLSSGKFYGD HCCEEEECCCCCCCC	31.57	23911959
53	Phosphorylation	FGKFVLSSGKFYGDE CCEEEECCCCCCCCC	41.67	23911959
55	Ubiquitination	KFVLSSGKFYGDEEK EEEECCCCCCCCCHH	37.04	21890473
55	Acetylation	KFVLSSGKFYGDEEK EEEECCCCCCCCCHH	37.04	26822725
55	Ubiquitination	KFVLSSGKFYGDEEK EEEECCCCCCCCCHH	37.04	21890473
57	Phosphorylation	VLSSGKFYGDEEKDK EECCCCCCCCCHHCC	27.44	28152594
62	Malonylation	KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC	63.79	26320211
62	2-Hydroxyisobutyrylation	KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC	63.79	-
62	Acetylation	KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC	63.79	27178108
62	Ubiquitination	KFYGDEEKDKGLQTS CCCCCCHHCCCCCCC	63.79	-
64	Acetylation	YGDEEKDKGLQTSQD CCCCHHCCCCCCCHH	73.00	26822725
64	Ubiquitination	YGDEEKDKGLQTSQD CCCCHHCCCCCCCHH	73.00	-
73	Methylation	LQTSQDARFYALSAS CCCCHHHHHEEEEEE	33.14	-
75	Phosphorylation	TSQDARFYALSASFE CCHHHHHEEEEEEEE	10.90	28152594
78	Phosphorylation	DARFYALSASFEPFS HHHHEEEEEEEECCC	17.44	28152594
80	Phosphorylation	RFYALSASFEPFSNK HHEEEEEEEECCCCC	27.11	21712546
85	Phosphorylation	SASFEPFSNKGQTLV EEEEECCCCCCCEEE	48.63	21712546
105	S-nitrosylation	KHEQNIDCGGGYVKL ECCCCCCCCCCEEEE	4.90	25040305
105	Glutathionylation	KHEQNIDCGGGYVKL ECCCCCCCCCCEEEE	4.90	22555962
109	Phosphorylation	NIDCGGGYVKLFPNS CCCCCCCEEEECCCC	9.55	28152594
111	Methylation	DCGGGYVKLFPNSLD CCCCCEEEECCCCCC	35.61	-
122	Sulfoxidation	NSLDQTDMHGDSEYN CCCCCCCCCCCCCEE	4.29	30846556
131	Sulfoxidation	GDSEYNIMFGPDICG CCCCEEEEECCCCCC	2.57	30846556
142	Ubiquitination	DICGPGTKKVHVIFN CCCCCCCCEEEEEEE	59.73	-
142	Acetylation	DICGPGTKKVHVIFN CCCCCCCCEEEEEEE	59.73	2374799
143	Acetylation	ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE	37.09	26051181
143	Ubiquitination	ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE	37.09	21906983
143	Malonylation	ICGPGTKKVHVIFNY CCCCCCCEEEEEEEE	37.09	26320211
150	Phosphorylation	KVHVIFNYKGKNVLI EEEEEEEECCCEEEE	15.46	-
151	Ubiquitination	VHVIFNYKGKNVLIN EEEEEEECCCEEEEC	65.59	-
151	Acetylation	VHVIFNYKGKNVLIN EEEEEEECCCEEEEC	65.59	21466224
151	Succinylation	VHVIFNYKGKNVLIN EEEEEEECCCEEEEC	65.59	23954790
153	Acetylation	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	18795239
153	Ubiquitination	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	21890473
153	2-Hydroxyisobutyrylation	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	-
153	Ubiquitination	VIFNYKGKNVLINKD EEEEECCCEEEECCC	39.47	21890473
159	Malonylation	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	26320211
159	Acetylation	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	19608861
159	Ubiquitination	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	21890473
159	2-Hydroxyisobutyrylation	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	-
159	Ubiquitination	GKNVLINKDIRCKDD CCEEEECCCCCCCCC	47.76	21890473
164	Acetylation	INKDIRCKDDEFTHL ECCCCCCCCCCCEEE	59.36	26051181
169	Phosphorylation	RCKDDEFTHLYTLIV CCCCCCCEEEEEEEE	14.66	-
172	Phosphorylation	DDEFTHLYTLIVRPD CCCCEEEEEEEECCC	7.59	28152594
173	Phosphorylation	DEFTHLYTLIVRPDN CCCEEEEEEEECCCC	19.17	28152594
181	Phosphorylation	LIVRPDNTYEVKIDN EEECCCCEEEEEECC	28.56	28152594
182	Phosphorylation	IVRPDNTYEVKIDNS EECCCCEEEEEECCC	25.61	28152594
189	Phosphorylation	YEVKIDNSQVESGSL EEEEECCCCCCCCCC	31.67	28450419
193	Phosphorylation	IDNSQVESGSLEDDW ECCCCCCCCCCCCCC	34.52	29507054
195	Phosphorylation	NSQVESGSLEDDWDF CCCCCCCCCCCCCCC	37.55	29507054
206	2-Hydroxyisobutyrylation	DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC	66.25	-
206	Acetylation	DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC	66.25	26051181
206	Ubiquitination	DWDFLPPKKIKDPDA CCCCCCCCCCCCCCC	66.25	21890473
207	Ubiquitination	WDFLPPKKIKDPDAS CCCCCCCCCCCCCCC	61.84	-
207	Acetylation	WDFLPPKKIKDPDAS CCCCCCCCCCCCCCC	61.84	18795239
209	Ubiquitination	FLPPKKIKDPDASKP CCCCCCCCCCCCCCC	72.58	19608861
209	Acetylation	FLPPKKIKDPDASKP CCCCCCCCCCCCCCC	72.58	19608861
214	Phosphorylation	KIKDPDASKPEDWDE CCCCCCCCCCCCHHH	57.00	23401153
215	Acetylation	IKDPDASKPEDWDER CCCCCCCCCCCHHHH	54.89	25038526
222	Methylation	KPEDWDERAKIDDPT CCCCHHHHHCCCCCC	38.41	-
229	Phosphorylation	RAKIDDPTDSKPEDW HHCCCCCCCCCCCCC	60.96	26471730
231	Phosphorylation	KIDDPTDSKPEDWDK CCCCCCCCCCCCCCC	53.22	26657352
238	Acetylation	SKPEDWDKPEHIPDP CCCCCCCCCCCCCCC	48.31	27178108
238	Methylation	SKPEDWDKPEHIPDP CCCCCCCCCCCCCCC	48.31	-
249	Acetylation	IPDPDAKKPEDWDEE CCCCCCCCCCCCCHH	56.19	26051181
257	Sulfoxidation	PEDWDEEMDGEWEPP CCCCCHHCCCCCCCC	8.25	30846556
271	Phosphorylation	PVIQNPEYKGEWKPR CCCCCCCCCCCCCCC	26.08	-
272	2-Hydroxyisobutyrylation	VIQNPEYKGEWKPRQ CCCCCCCCCCCCCCC	49.01	-
285	Phosphorylation	RQIDNPDYKGTWIHP CCCCCCCCCCCEECC	16.75	25884760
285	Nitration	RQIDNPDYKGTWIHP CCCCCCCCCCCEECC	16.75	-
299	Phosphorylation	PEIDNPEYSPDPSIY CCCCCCCCCCCCCEE	27.10	-
300	Phosphorylation	EIDNPEYSPDPSIYA CCCCCCCCCCCCEEE	22.59	-
325	O-linked_Glycosylation	LWQVKSGTIFDNFLI EEEEECCEEEECEEE	26.09	32119511
333	Phosphorylation	IFDNFLITNDEAYAE EEECEEECCCHHHHH	38.47	-
344	N-linked_Glycosylation	AYAEEFGNETWGVTK HHHHHHCCCCHHHHH	49.17	19159218
351	Ubiquitination	NETWGVTKAAEKQMK CCCHHHHHHHHHHHC	43.10	-
357	Sulfoxidation	TKAAEKQMKDKQDEE HHHHHHHHCCHHHHH	10.06	30846556
366	Methylation	DKQDEEQRLKEEEED CHHHHHHHHHHHHHH	51.51	-

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 CALR_HUMAN !!

Functions of PTM Sites

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

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 CALR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TPA_HUMAN	PLAT	physical	9359841
PDIA3_HUMAN	PDIA3	physical	10436013
CALX_HUMAN	CANX	physical	10436013
PERF_HUMAN	PRF1	physical	9671507
A4_HUMAN	APP	physical	11378243
APOB_HUMAN	APOB	physical	10513896
TPSN_HUMAN	TAPBP	physical	8769474
VWF_HUMAN	VWF	physical	10887119
FA5_HUMAN	F5	physical	9525969
TRFE_HUMAN	TF	physical	9312001
NKX21_HUMAN	NKX2-1	physical	9988700
GTR1_HUMAN	SLC2A1	physical	8662691
LRIF1_HUMAN	LRIF1	physical	21900206
SNF5_HUMAN	SMARCB1	physical	21900206
KCNH2_HUMAN	KCNH2	physical	22242185
GLU2B_HUMAN	PRKCSH	physical	22939629
GANAB_HUMAN	GANAB	physical	22939629
K1C17_HUMAN	KRT17	physical	22939629
ENPL_HUMAN	HSP90B1	physical	22939629
PDIA1_HUMAN	P4HB	physical	22939629
HLAE_HUMAN	HLA-E	physical	9427624
ITA3_HUMAN	ITGA3	physical	8006073
HLAE_HUMAN	HLA-E	physical	15383281
1A02_HUMAN	HLA-A	physical	15383281
1A03_HUMAN	HLA-A	physical	15383281
1A01_HUMAN	HLA-A	physical	15383281
1A26_HUMAN	HLA-A	physical	15383281
CALR_HUMAN	CALR	physical	15383281
PDIA3_HUMAN	PDIA3	physical	12052826
AASD1_HUMAN	AARSD1	physical	22863883
ARP2_HUMAN	ACTR2	physical	22863883
AN32B_HUMAN	ANP32B	physical	22863883
ARC1B_HUMAN	ARPC1B	physical	22863883
ARPC3_HUMAN	ARPC3	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
PFD5_HUMAN	PFDN5	physical	22863883
KAPCA_HUMAN	PRKACA	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
THG1_HUMAN	THG1L	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
MARE3_HUMAN	MAPRE3	physical	26344197
NACA2_HUMAN	NACA2	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
PCNA_HUMAN	PCNA	physical	26344197
TSHR_HUMAN	TSHR	physical	12383251
A4_HUMAN	APP	physical	25241761
FA8_HUMAN	F8	physical	25241761
B2MG_HUMAN	B2M	physical	25241761
TECT2_HUMAN	TCTN2	physical	27173435
1B07_HUMAN	HLA-B	physical	11823531
1B18_HUMAN	HLA-B	physical	11823531
TPSN_HUMAN	TAPBP	physical	11823531
TAP1_HUMAN	TAP1	physical	11823531
PDIA3_HUMAN	PDIA3	physical	11823531

Drug and Disease Associations

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

Regulatory Network of CALR_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-159 AND LYS-209, ANDMASS SPECTROMETRY.	19608861 [Abstract]
N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344, AND MASSSPECTROMETRY.	19159218 [Abstract]