CALR_HUMAN - dbPTM
CALR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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
7Ubiquitination-MLLSVPLLLGLLGL
-CCCHHHHHHHHHHH
6.0521890473
22PhosphorylationAVAEPAVYFKEQFLD
HHHCCCCCCCCCCCC
15.84-
24UbiquitinationAEPAVYFKEQFLDGD
HCCCCCCCCCCCCCC
32.6821890473
24SumoylationAEPAVYFKEQFLDGD
HCCCCCCCCCCCCCC
32.68-
34PhosphorylationFLDGDGWTSRWIESK
CCCCCCHHHHHHHHC
17.5921712546
35PhosphorylationLDGDGWTSRWIESKH
CCCCCHHHHHHHHCC
21.0721712546
41AcetylationTSRWIESKHKSDFGK
HHHHHHHCCHHHCCE
42.1125953088
412-HydroxyisobutyrylationTSRWIESKHKSDFGK
HHHHHHHCCHHHCCE
42.11-
41UbiquitinationTSRWIESKHKSDFGK
HHHHHHHCCHHHCCE
42.11-
43SuccinylationRWIESKHKSDFGKFV
HHHHHCCHHHCCEEE
56.2923954790
432-HydroxyisobutyrylationRWIESKHKSDFGKFV
HHHHHCCHHHCCEEE
56.29-
44PhosphorylationWIESKHKSDFGKFVL
HHHHCCHHHCCEEEE
37.5824719451
48AcetylationKHKSDFGKFVLSSGK
CCHHHCCEEEECCCC
32.0919608861
48UbiquitinationKHKSDFGKFVLSSGK
CCHHHCCEEEECCCC
32.0921890473
48SuccinylationKHKSDFGKFVLSSGK
CCHHHCCEEEECCCC
32.0923954790
482-HydroxyisobutyrylationKHKSDFGKFVLSSGK
CCHHHCCEEEECCCC
32.09-
48UbiquitinationKHKSDFGKFVLSSGK
CCHHHCCEEEECCCC
32.0921890473
52PhosphorylationDFGKFVLSSGKFYGD
HCCEEEECCCCCCCC
31.5723911959
53PhosphorylationFGKFVLSSGKFYGDE
CCEEEECCCCCCCCC
41.6723911959
55UbiquitinationKFVLSSGKFYGDEEK
EEEECCCCCCCCCHH
37.0421890473
55AcetylationKFVLSSGKFYGDEEK
EEEECCCCCCCCCHH
37.0426822725
55UbiquitinationKFVLSSGKFYGDEEK
EEEECCCCCCCCCHH
37.0421890473
57PhosphorylationVLSSGKFYGDEEKDK
EECCCCCCCCCHHCC
27.4428152594
62MalonylationKFYGDEEKDKGLQTS
CCCCCCHHCCCCCCC
63.7926320211
622-HydroxyisobutyrylationKFYGDEEKDKGLQTS
CCCCCCHHCCCCCCC
63.79-
62AcetylationKFYGDEEKDKGLQTS
CCCCCCHHCCCCCCC
63.7927178108
62UbiquitinationKFYGDEEKDKGLQTS
CCCCCCHHCCCCCCC
63.79-
64AcetylationYGDEEKDKGLQTSQD
CCCCHHCCCCCCCHH
73.0026822725
64UbiquitinationYGDEEKDKGLQTSQD
CCCCHHCCCCCCCHH
73.00-
73MethylationLQTSQDARFYALSAS
CCCCHHHHHEEEEEE
33.14-
75PhosphorylationTSQDARFYALSASFE
CCHHHHHEEEEEEEE
10.9028152594
78PhosphorylationDARFYALSASFEPFS
HHHHEEEEEEEECCC
17.4428152594
80PhosphorylationRFYALSASFEPFSNK
HHEEEEEEEECCCCC
27.1121712546
85PhosphorylationSASFEPFSNKGQTLV
EEEEECCCCCCCEEE
48.6321712546
105S-nitrosylationKHEQNIDCGGGYVKL
ECCCCCCCCCCEEEE
4.9025040305
105GlutathionylationKHEQNIDCGGGYVKL
ECCCCCCCCCCEEEE
4.9022555962
109PhosphorylationNIDCGGGYVKLFPNS
CCCCCCCEEEECCCC
9.5528152594
111MethylationDCGGGYVKLFPNSLD
CCCCCEEEECCCCCC
35.61-
122SulfoxidationNSLDQTDMHGDSEYN
CCCCCCCCCCCCCEE
4.2930846556
131SulfoxidationGDSEYNIMFGPDICG
CCCCEEEEECCCCCC
2.5730846556
142UbiquitinationDICGPGTKKVHVIFN
CCCCCCCCEEEEEEE
59.73-
142AcetylationDICGPGTKKVHVIFN
CCCCCCCCEEEEEEE
59.732374799
143AcetylationICGPGTKKVHVIFNY
CCCCCCCEEEEEEEE
37.0926051181
143UbiquitinationICGPGTKKVHVIFNY
CCCCCCCEEEEEEEE
37.0921906983
143MalonylationICGPGTKKVHVIFNY
CCCCCCCEEEEEEEE
37.0926320211
150PhosphorylationKVHVIFNYKGKNVLI
EEEEEEEECCCEEEE
15.46-
151UbiquitinationVHVIFNYKGKNVLIN
EEEEEEECCCEEEEC
65.59-
151AcetylationVHVIFNYKGKNVLIN
EEEEEEECCCEEEEC
65.5921466224
151SuccinylationVHVIFNYKGKNVLIN
EEEEEEECCCEEEEC
65.5923954790
153AcetylationVIFNYKGKNVLINKD
EEEEECCCEEEECCC
39.4718795239
153UbiquitinationVIFNYKGKNVLINKD
EEEEECCCEEEECCC
39.4721890473
1532-HydroxyisobutyrylationVIFNYKGKNVLINKD
EEEEECCCEEEECCC
39.47-
153UbiquitinationVIFNYKGKNVLINKD
EEEEECCCEEEECCC
39.4721890473
159MalonylationGKNVLINKDIRCKDD
CCEEEECCCCCCCCC
47.7626320211
159AcetylationGKNVLINKDIRCKDD
CCEEEECCCCCCCCC
47.7619608861
159UbiquitinationGKNVLINKDIRCKDD
CCEEEECCCCCCCCC
47.7621890473
1592-HydroxyisobutyrylationGKNVLINKDIRCKDD
CCEEEECCCCCCCCC
47.76-
159UbiquitinationGKNVLINKDIRCKDD
CCEEEECCCCCCCCC
47.7621890473
164AcetylationINKDIRCKDDEFTHL
ECCCCCCCCCCCEEE
59.3626051181
169PhosphorylationRCKDDEFTHLYTLIV
CCCCCCCEEEEEEEE
14.66-
172PhosphorylationDDEFTHLYTLIVRPD
CCCCEEEEEEEECCC
7.5928152594
173PhosphorylationDEFTHLYTLIVRPDN
CCCEEEEEEEECCCC
19.1728152594
181PhosphorylationLIVRPDNTYEVKIDN
EEECCCCEEEEEECC
28.5628152594
182PhosphorylationIVRPDNTYEVKIDNS
EECCCCEEEEEECCC
25.6128152594
189PhosphorylationYEVKIDNSQVESGSL
EEEEECCCCCCCCCC
31.6728450419
193PhosphorylationIDNSQVESGSLEDDW
ECCCCCCCCCCCCCC
34.5229507054
195PhosphorylationNSQVESGSLEDDWDF
CCCCCCCCCCCCCCC
37.5529507054
2062-HydroxyisobutyrylationDWDFLPPKKIKDPDA
CCCCCCCCCCCCCCC
66.25-
206AcetylationDWDFLPPKKIKDPDA
CCCCCCCCCCCCCCC
66.2526051181
206UbiquitinationDWDFLPPKKIKDPDA
CCCCCCCCCCCCCCC
66.2521890473
207UbiquitinationWDFLPPKKIKDPDAS
CCCCCCCCCCCCCCC
61.84-
207AcetylationWDFLPPKKIKDPDAS
CCCCCCCCCCCCCCC
61.8418795239
209UbiquitinationFLPPKKIKDPDASKP
CCCCCCCCCCCCCCC
72.5819608861
209AcetylationFLPPKKIKDPDASKP
CCCCCCCCCCCCCCC
72.5819608861
214PhosphorylationKIKDPDASKPEDWDE
CCCCCCCCCCCCHHH
57.0023401153
215AcetylationIKDPDASKPEDWDER
CCCCCCCCCCCHHHH
54.8925038526
222MethylationKPEDWDERAKIDDPT
CCCCHHHHHCCCCCC
38.41-
229PhosphorylationRAKIDDPTDSKPEDW
HHCCCCCCCCCCCCC
60.9626471730
231PhosphorylationKIDDPTDSKPEDWDK
CCCCCCCCCCCCCCC
53.2226657352
238AcetylationSKPEDWDKPEHIPDP
CCCCCCCCCCCCCCC
48.3127178108
238MethylationSKPEDWDKPEHIPDP
CCCCCCCCCCCCCCC
48.31-
249AcetylationIPDPDAKKPEDWDEE
CCCCCCCCCCCCCHH
56.1926051181
257SulfoxidationPEDWDEEMDGEWEPP
CCCCCHHCCCCCCCC
8.2530846556
271PhosphorylationPVIQNPEYKGEWKPR
CCCCCCCCCCCCCCC
26.08-
2722-HydroxyisobutyrylationVIQNPEYKGEWKPRQ
CCCCCCCCCCCCCCC
49.01-
285PhosphorylationRQIDNPDYKGTWIHP
CCCCCCCCCCCEECC
16.7525884760
285NitrationRQIDNPDYKGTWIHP
CCCCCCCCCCCEECC
16.75-
299PhosphorylationPEIDNPEYSPDPSIY
CCCCCCCCCCCCCEE
27.10-
300PhosphorylationEIDNPEYSPDPSIYA
CCCCCCCCCCCCEEE
22.59-
325O-linked_GlycosylationLWQVKSGTIFDNFLI
EEEEECCEEEECEEE
26.0932119511
333PhosphorylationIFDNFLITNDEAYAE
EEECEEECCCHHHHH
38.47-
344N-linked_GlycosylationAYAEEFGNETWGVTK
HHHHHHCCCCHHHHH
49.1719159218
351UbiquitinationNETWGVTKAAEKQMK
CCCHHHHHHHHHHHC
43.10-
357SulfoxidationTKAAEKQMKDKQDEE
HHHHHHHHCCHHHHH
10.0630846556
366MethylationDKQDEEQRLKEEEED
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 Domain-Domain Interactions
TPA_HUMANPLATphysical
9359841
PDIA3_HUMANPDIA3physical
10436013
CALX_HUMANCANXphysical
10436013
PERF_HUMANPRF1physical
9671507
A4_HUMANAPPphysical
11378243
APOB_HUMANAPOBphysical
10513896
TPSN_HUMANTAPBPphysical
8769474
VWF_HUMANVWFphysical
10887119
FA5_HUMANF5physical
9525969
TRFE_HUMANTFphysical
9312001
NKX21_HUMANNKX2-1physical
9988700
GTR1_HUMANSLC2A1physical
8662691
LRIF1_HUMANLRIF1physical
21900206
SNF5_HUMANSMARCB1physical
21900206
KCNH2_HUMANKCNH2physical
22242185
GLU2B_HUMANPRKCSHphysical
22939629
GANAB_HUMANGANABphysical
22939629
K1C17_HUMANKRT17physical
22939629
ENPL_HUMANHSP90B1physical
22939629
PDIA1_HUMANP4HBphysical
22939629
HLAE_HUMANHLA-Ephysical
9427624
ITA3_HUMANITGA3physical
8006073
HLAE_HUMANHLA-Ephysical
15383281
1A02_HUMANHLA-Aphysical
15383281
1A03_HUMANHLA-Aphysical
15383281
1A01_HUMANHLA-Aphysical
15383281
1A26_HUMANHLA-Aphysical
15383281
CALR_HUMANCALRphysical
15383281
PDIA3_HUMANPDIA3physical
12052826
AASD1_HUMANAARSD1physical
22863883
ARP2_HUMANACTR2physical
22863883
AN32B_HUMANANP32Bphysical
22863883
ARC1B_HUMANARPC1Bphysical
22863883
ARPC3_HUMANARPC3physical
22863883
NSUN2_HUMANNSUN2physical
22863883
PFD5_HUMANPFDN5physical
22863883
KAPCA_HUMANPRKACAphysical
22863883
RFA1_HUMANRPA1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
THG1_HUMANTHG1Lphysical
22863883
TPD54_HUMANTPD52L2physical
22863883
MARE3_HUMANMAPRE3physical
26344197
NACA2_HUMANNACA2physical
26344197
PDIA1_HUMANP4HBphysical
26344197
PCNA_HUMANPCNAphysical
26344197
TSHR_HUMANTSHRphysical
12383251
A4_HUMANAPPphysical
25241761
FA8_HUMANF8physical
25241761
B2MG_HUMANB2Mphysical
25241761
TECT2_HUMANTCTN2physical
27173435
1B07_HUMANHLA-Bphysical
11823531
1B18_HUMANHLA-Bphysical
11823531
TPSN_HUMANTAPBPphysical
11823531
TAP1_HUMANTAP1physical
11823531
PDIA3_HUMANPDIA3physical
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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
N-linked Glycosylation
ReferencePubMed
"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.

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