CALX_MOUSE - dbPTM
CALX_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CALX_MOUSE
UniProt AC P35564
Protein Name Calnexin
Gene Name Canx
Organism Mus musculus (Mouse).
Sequence Length 591
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein . Endoplasmic reticulum . Melanosome . The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). When bound to CD3 epsilon chains, calnexin's ER r
Protein Description Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse..
Protein Sequence MEGKWLLCLLLVLGTAAVEAHDGHDDDAIDIEDDLDDVIEEVEDSKSKSDASTPPSPKVTYKAPVPTGEVYFADSFDRGSLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTAELSLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIADPDAVKPDDWDEDAPSKIPDEEATKPEGWLDDEPEYIPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFKMTPFSAIGLELWSMTSDIFFDNFIISGDRRVVDDWANDGWGLKKAADGAAEPGVVLQMLEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQSNAMEYKKTDAPQPDVKDEEGKEEEKNKRDEEEEEEKLEEKQKSDAEEDGVTGSQDEEDSKPKAEEDEILNRSPRNRKPRRE
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
47PhosphorylationEEVEDSKSKSDASTP
HHHHHHCCCCCCCCC		41.1529899451
48AcetylationEVEDSKSKSDASTPP
HHHHHCCCCCCCCCC		56.9723806337
48SuccinylationEVEDSKSKSDASTPP
HHHHHCCCCCCCCCC		56.9723806337
49PhosphorylationVEDSKSKSDASTPPS
HHHHCCCCCCCCCCC		45.5630635358
52PhosphorylationSKSKSDASTPPSPKV
HCCCCCCCCCCCCCE		46.5727742792
53PhosphorylationKSKSDASTPPSPKVT
CCCCCCCCCCCCCEE		40.7227742792
56PhosphorylationSDASTPPSPKVTYKA
CCCCCCCCCCEEEEC		38.2627742792
67PhosphorylationTYKAPVPTGEVYFAD
EEECCCCCCEEEEEC		46.32-
82PhosphorylationSFDRGSLSGWILSKA
CCCCCCCHHHHHHHH		33.5022817900
104AcetylationEIAKYDGKWEVDEMK
HHHHHCCCEEHHHCH		36.9623954790
104SuccinylationEIAKYDGKWEVDEMK
HHHHHCCCEEHHHCH		36.9623954790
133PhosphorylationRAKHHAISAKLNKPF
CCHHHHHHHCCCCCC		21.8218779572
138SuccinylationAISAKLNKPFLFDTK
HHHHCCCCCCCCCCC		47.8123954790
138AcetylationAISAKLNKPFLFDTK
HHHHCCCCCCCCCCC		47.81-
171SuccinylationAYVKLLSKTAELSLD
HHHHHHHCCEECCHH		52.2923954790
171UbiquitinationAYVKLLSKTAELSLD
HHHHHHHCCEECCHH		52.29-
186PhosphorylationQFHDKTPYTIMFGPD
HHCCCCCEEEEECCC		17.7118779572
187PhosphorylationFHDKTPYTIMFGPDK
HCCCCCEEEEECCCC		13.7318779572
195S-palmitoylationIMFGPDKCGEDYKLH
EEECCCCCCCCEEEE		10.5926165157
218AcetylationKTGVYEEKHAKRPDA
CCCCCCHHHCCCCCC		36.6021728379
228SuccinylationKRPDADLKTYFTDKK
CCCCCCHHHHCCCCC		41.5523954790
459AcetylationANDGWGLKKAADGAA
HHCCCCCHHHHCCCC		36.11129529
459SuccinylationANDGWGLKKAADGAA
HHCCCCCHHHHCCCC		36.1123954790
460AcetylationNDGWGLKKAADGAAE
HCCCCCHHHHCCCCC		54.58156285
503S-palmitoylationVFLVILFCCSGKKQS
HHHHHHHHCCCCHHH		1.29-
504S-palmitoylationFLVILFCCSGKKQSN
HHHHHHHCCCCHHHC		4.75-
516AcetylationQSNAMEYKKTDAPQP
HHCCCHHCCCCCCCC		35.576566661
517UbiquitinationSNAMEYKKTDAPQPD
HCCCHHCCCCCCCCC		51.2222790023
517AcetylationSNAMEYKKTDAPQPD
HCCCHHCCCCCCCCC		51.226566727
526UbiquitinationDAPQPDVKDEEGKEE
CCCCCCCCCCCCHHH		67.7922790023
531UbiquitinationDVKDEEGKEEEKNKR
CCCCCCCHHHHHHHC		66.29-
535UbiquitinationEEGKEEEKNKRDEEE
CCCHHHHHHHCHHHH		71.6722790023
537UbiquitinationGKEEEKNKRDEEEEE
CHHHHHHHCHHHHHH		72.7522790023
546UbiquitinationDEEEEEEKLEEKQKS
HHHHHHHHHHHHHHH		65.5622790023
546AcetylationDEEEEEEKLEEKQKS
HHHHHHHHHHHHHHH		65.5623954790
550UbiquitinationEEEKLEEKQKSDAEE
HHHHHHHHHHHHHHH		54.3622790023
553PhosphorylationKLEEKQKSDAEEDGV
HHHHHHHHHHHHHCC		39.2924925903
561PhosphorylationDAEEDGVTGSQDEED
HHHHHCCCCCCCCCC		36.3227087446
563PhosphorylationEEDGVTGSQDEEDSK
HHHCCCCCCCCCCCC		25.7024925903
569PhosphorylationGSQDEEDSKPKAEED
CCCCCCCCCCCHHHH		54.8824925903
582PhosphorylationEDEILNRSPRNRKPR
HHHHHHCCCCCCCCC		27.4324925903
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
563SPhosphorylationKinaseMAPK3Q63844
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
563SPhosphorylation

17208939
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 CALX_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALX_MOUSECanxphysical
8798466
ACHA_MOUSEChrna1physical
8798466
ACHB_MOUSEChrnb1physical
8798466
ACHD_MOUSEChrndphysical
8798466
HA11_MOUSEH2-D1physical
9973410
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CALX_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-582, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-582, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 ANDSER-582, AND MASS SPECTROMETRY.
"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 SER-582, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563; SER-569AND SER-582, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; THR-561; SER-563AND SER-582, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; THR-561 ANDSER-563, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-563, ANDMASS SPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory