CSDE1_MOUSE - dbPTM
CSDE1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSDE1_MOUSE
UniProt AC Q91W50
Protein Name Cold shock domain-containing protein E1
Gene Name Csde1
Organism Mus musculus (Mouse).
Sequence Length 798
Subcellular Localization Cytoplasm.
Protein Description RNA-binding protein. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity)..
Protein Sequence MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAIKLVKIKPEIHPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTSEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQGVVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDPLPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNISTDRRDKLERATNIEVLSNTFQFTNEAREMGVIAAMRDGFGFIKCVDRDARMFFHFSEILDGNQLHIADEVEFTVVPDMLSAQRNHAIRIKKLPKGTVSFHSHSDHRFLGTVEKEATFSNPKTTSPNKGKDKEAEDGIIAYDDCGVKLTIAFQAKDVEGSTSPQIGDKVEFSISDKQRPGQQIATCVRLLGRNSNSKRLLGYVATLKDNFGFIETANHDKEIFFHYSEFSGDVDSLELGDMVEYSLSKGKGNKVSAEKVNKAHSVNGITEEANPTIYSGKVIRPLRGVDPTQIEYQGMIEIVEEGDMKGEVYPFGIVGMANKGDCLQKGESVKFQLCVLGQNAQTMAYNITPLRRATVECVKDQFGFINYEVGDSKKLFFHVKEVQDGVELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID
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
2Phosphorylation------MSFDPNLLH
------CCCCCCCCC
38.0526643407
32UbiquitinationRETGVIEKLLTSYGF
HHHCHHHHHHHHCCC
37.36-
81AcetylationSSDRRTGKPIAIKLV
ECCCCCCCEEEEEEE
32.41-
81UbiquitinationSSDRRTGKPIAIKLV
ECCCCCCCEEEEEEE
32.41-
91UbiquitinationAIKLVKIKPEIHPEE
EEEEEEECCCCCHHH
30.77-
106GlutathionylationRMNGQVVCAVPHNLE
HCCCEEEEECCCCCC
3.1224333276
114PhosphorylationAVPHNLESKSPAAPG
ECCCCCCCCCCCCCC
41.4123984901
116PhosphorylationPHNLESKSPAAPGQS
CCCCCCCCCCCCCCC
29.1125619855
123PhosphorylationSPAAPGQSPTGSVCY
CCCCCCCCCCCCEEE
30.2825521595
125PhosphorylationAAPGQSPTGSVCYER
CCCCCCCCCCEEEEE
47.5425619855
127PhosphorylationPGQSPTGSVCYERNG
CCCCCCCCEEEEECC
16.1125619855
129S-nitrosylationQSPTGSVCYERNGEV
CCCCCCEEEEECCEE
2.9021278135
129S-nitrosocysteineQSPTGSVCYERNGEV
CCCCCCEEEEECCEE
2.90-
130PhosphorylationSPTGSVCYERNGEVF
CCCCCEEEEECCEEE
18.7723984901
166UbiquitinationNFVIDNNKHTGAVSA
EEEEECCCCCCCCCH
49.12-
239UbiquitinationTIKDRNGKEVATDVR
EEECCCCCEEEEEEE
53.19-
276PhosphorylationKVIPKVPSKNQNDPL
EEECCCCCCCCCCCC
47.4221183079
277UbiquitinationVIPKVPSKNQNDPLP
EECCCCCCCCCCCCC
57.38-
288UbiquitinationDPLPGRIKVDFVIPK
CCCCCCEEEEEEECC
34.10-
364UbiquitinationRDGFGFIKCVDRDAR
ECCCCEEEEEECCCC
26.41-
424PhosphorylationTVSFHSHSDHRFLGT
EEEEEECCCCCEEEE
37.8223684622
444PhosphorylationTFSNPKTTSPNKGKD
ECCCCCCCCCCCCCC
48.6025338131
445PhosphorylationFSNPKTTSPNKGKDK
CCCCCCCCCCCCCCC
31.5419060867
452AcetylationSPNKGKDKEAEDGII
CCCCCCCCCCCCCEE
63.41-
469PhosphorylationDDCGVKLTIAFQAKD
ECCCCEEEEEEEEEC
12.4422802335
480PhosphorylationQAKDVEGSTSPQIGD
EEECCCCCCCCCCCC
16.5329472430
481PhosphorylationAKDVEGSTSPQIGDK
EECCCCCCCCCCCCE
56.1129472430
482PhosphorylationKDVEGSTSPQIGDKV
ECCCCCCCCCCCCEE
19.2625521595
488UbiquitinationTSPQIGDKVEFSISD
CCCCCCCEEEEECCC
38.15-
492PhosphorylationIGDKVEFSISDKQRP
CCCEEEEECCCCCCC
14.0022802335
494PhosphorylationDKVEFSISDKQRPGQ
CEEEEECCCCCCCHH
37.2422802335
506GlutathionylationPGQQIATCVRLLGRN
CHHHHHHHHHHHCCC
0.9324333276
514PhosphorylationVRLLGRNSNSKRLLG
HHHHCCCCCCHHHHE
40.9125266776
516PhosphorylationLLGRNSNSKRLLGYV
HHCCCCCCHHHHEEE
20.9726745281
584PhosphorylationEKVNKAHSVNGITEE
HHHCCCCCCCCCCCC
23.3325521595
589PhosphorylationAHSVNGITEEANPTI
CCCCCCCCCCCCCCE
29.2223984901
682UbiquitinationRATVECVKDQFGFIN
CCEEHHHHHHCCCEE
58.43-
682AcetylationRATVECVKDQFGFIN
CCEEHHHHHHCCCEE
58.43-
695PhosphorylationINYEVGDSKKLFFHV
EEEEECCCEEEEEEE
26.26-
696UbiquitinationNYEVGDSKKLFFHVK
EEEECCCEEEEEEEE
59.23-
729UbiquitinationILNQRTGKCSACNVW
EEECCCCCCCCCCEE
25.14-
743UbiquitinationWRVCEGPKAVAAPRP
EEEECCCCCEECCCH
67.37-
758AcetylationDRLVNRLKNITLDDA
HHHHHHHCCCCCCCC
42.96-
758UbiquitinationDRLVNRLKNITLDDA
HHHHHHHCCCCCCCC
42.96-
761PhosphorylationVNRLKNITLDDASAP
HHHHCCCCCCCCCCC
33.2622324799

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 CSDE1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSDE1_MOUSE !!

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 CSDE1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4H_HUMANEIF4Hphysical
26496610
ABHGA_HUMANABHD16Aphysical
26496610
DUS11_HUMANDUSP11physical
26496610
TXND9_HUMANTXNDC9physical
26496610
STRAP_HUMANSTRAPphysical
26496610
TM131_HUMANTMEM131physical
26496610
DDX41_HUMANDDX41physical
26496610
PKHA3_HUMANPLEKHA3physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSDE1_MOUSE

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Related Literatures of Post-Translational Modification

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