CALX_SCHPO - dbPTM
CALX_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CALX_SCHPO
UniProt AC P36581
Protein Name Calnexin homolog
Gene Name cal1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 560
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein.
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..
Protein Sequence MKYGKVSFLALLCSLYVRGSLADPESEQEPLVFNPTEVKAPLVEQFQGAWSERWIPSHAKRFVNGIEEMSYVGEWTVEESSGPGALKGEAGLVMKDEAAHHAISYEFDEPINEPEKDLVVQYEVNPEEGLNCGGAYLKLLAEPTHGEMSNSIDYRIMFGPDKCGVNDRVHFIFKHKNPLTGEYSEKHLDSRPASLLKPGITNLYTLIVKPDQTFEVRINGDVVRQGSLFYDFIPPVLPPVEIYDPEDIKPADWVDEPEIPDPNAVKPDDWDEDAPRMIPDPDAVKPEDWLEDEPLYIPDPEAQKPEDWDDEEDGDWIPSEIINPKCIEGAGCGEWKPPMIRNPNYRGPWSPPMIPNPEFIGEWYPRKIPNPDYFDDDHPSHFGPLYGVGFELWTMQPNIRFSNIYVGHSIEDAERLGNETFLPKLKAERELLSKQESMEKQSMHVDEESNQILEKFLDVYDIIKAKLPPNVAEKVDYYVETIIETPEIGIAIVAVLGSLTAVILTCYFYFFASSSPASLSTGTTEAEKEQQEKFKQETETEKIDVSYAPETESPTAKNED
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
418N-linked_GlycosylationEDAERLGNETFLPKL
HHHHHHCCCCHHHHH
50.13-
546PhosphorylationETEKIDVSYAPETES
HCCCCCCCCCCCCCC
16.3024763107
551PhosphorylationDVSYAPETESPTAKN
CCCCCCCCCCCCCCC
40.4828889911
553PhosphorylationSYAPETESPTAKNED
CCCCCCCCCCCCCCC
34.6628889911
555PhosphorylationAPETESPTAKNED--
CCCCCCCCCCCCC--
60.5928889911

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 CALX_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRP78_SCHPObip1physical
9860839
PPA2_SCHPOpho4physical
9860839
GRP78_SCHPObip1physical
17230581

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-553 ANDTHR-555, AND MASS SPECTROMETRY.

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