CALR1_ARATH - dbPTM
CALR1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CALR1_ARATH
UniProt AC O04151
Protein Name Calreticulin-1
Gene Name CRT1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 425
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity)..
Protein Sequence MAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDAKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNPEFKDDPELYVFPKLKYVGVELWQVKSGSLFDNVLVSDDPEYAKKLAEETWGKHKDAEKAAFDEAEKKREEEESKDAPAESDAEEEAEDDDNEGDDSDNESKSEETKEAEETKEAEETDAAHDEL
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
59N-linked_GlycosylationEWKHTAGNWSGDAND
CCEECCCCCCCCCCC
27.55-
154N-linked_GlycosylationVHAILTYNGTNHLIK
EEEEEEECCCCCEEE
45.65-
337PhosphorylationLFDNVLVSDDPEYAK
CCCCEEECCCHHHHH
31.9419880383
374PhosphorylationKKREEEESKDAPAES
HHHHHHHHCCCCCCC
38.8323776212
381PhosphorylationSKDAPAESDAEEEAE
HCCCCCCCCHHHHHC
44.2024601666
397PhosphorylationDDNEGDDSDNESKSE
CCCCCCCCCCCCHHH
47.2619880383
399N-linked_GlycosylationNEGDDSDNESKSEET
CCCCCCCCCCHHHHH
60.43-
401PhosphorylationGDDSDNESKSEETKE
CCCCCCCCHHHHHHH
47.9723776212
403PhosphorylationDSDNESKSEETKEAE
CCCCCCHHHHHHHHH
50.3623776212
406PhosphorylationNESKSEETKEAEETK
CCCHHHHHHHHHHHH
30.0823776212
412PhosphorylationETKEAEETKEAEETD
HHHHHHHHHHHHHHH
26.2023660473
418PhosphorylationETKEAEETDAAHDEL
HHHHHHHHHHHHHCC
23.5730407730

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 CALR1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CALR1_ARATH !!

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 CALR1_ARATH !!

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

Oops, there are no PPI records of CALR1_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CALR1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-397, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASSSPECTROMETRY.

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