CSDE1_HUMAN - dbPTM
CSDE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSDE1_HUMAN
UniProt AC O75534
Protein Name Cold shock domain-containing protein E1
Gene Name CSDE1
Organism Homo sapiens (Human).
Sequence Length 798
Subcellular Localization Cytoplasm.
Protein Description RNA-binding protein. Required for internal initiation of translation of human rhinovirus RNA. 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..
Protein Sequence MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAVKLVKIKQEILPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTPEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQGVVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDPLPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNISTDRRDKLERATNIEVLSNTFQFTNEAREMGVIAAMRDGFGFIKCVDRDVRMFFHFSEILDGNQLHIADEVEFTVVPDMLSAQRNHAIRIKKLPKGTVSFHSHSDHRFLGTVEKEATFSNPKTTSPNKGKEKEAEDGIIAYDDCGVKLTIAFQAKDVEGSTSPQIGDKVEFSISDKQRPGQQVATCVRLLGRNSNSKRLLGYVATLKDNFGFIETANHDKEIFFHYSEFSGDVDSLELGDMVEYSLSKGKGNKVSAEKVNKTHSVNGITEEADPTIYSGKVIRPLRSVDPTQTEYQGMIEIVEEGDMKGEVYPFGIVGMANKGDCLQKGESVKFQLCVLGQNAQTMAYNITPLRRATVECVKDQFGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID
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		38.0525159151
6 (in isoform 3)Phosphorylation-58.0121955146
6 (in isoform 4)Phosphorylation-58.0121955146
8 (in isoform 3)Phosphorylation-5.3021955146
8 (in isoform 4)Phosphorylation-5.3021955146
9 (in isoform 3)Phosphorylation-28.9521955146
9 (in isoform 4)Phosphorylation-28.9521955146
14 (in isoform 3)Phosphorylation-53.7621955146
14 (in isoform 4)Phosphorylation-53.7621955146
16PhosphorylationHNNGHNGYPNGTSAA
CCCCCCCCCCCHHHH		9.9921955146
20PhosphorylationHNGYPNGTSAALRET
CCCCCCCHHHHHHHH		23.1021955146
20 (in isoform 3)Phosphorylation-23.1021955146
20 (in isoform 4)Phosphorylation-23.1021955146
21PhosphorylationNGYPNGTSAALRETG
CCCCCCHHHHHHHHC		16.9721955146
22 (in isoform 3)Phosphorylation-15.4521955146
22 (in isoform 4)Phosphorylation-15.4521955146
26 (in isoform 3)Phosphorylation-51.2521955146
26 (in isoform 4)Phosphorylation-51.2521955146
27O-linked_GlycosylationTSAALRETGVIEKLL
HHHHHHHHCHHHHHH		30.2523301498
27PhosphorylationTSAALRETGVIEKLL
HHHHHHHHCHHHHHH		30.2521955146
27 (in isoform 3)Phosphorylation-30.2521955146
27 (in isoform 4)Phosphorylation-30.2521955146
28 (in isoform 3)Phosphorylation-17.4121955146
28 (in isoform 4)Phosphorylation-17.4121955146
29 (in isoform 3)Phosphorylation-7.1521955146
29 (in isoform 4)Phosphorylation-7.1521955146
30 (in isoform 3)Phosphorylation-4.0121955146
30 (in isoform 4)Phosphorylation-4.0121955146
31 (in isoform 3)Phosphorylation-34.9321955146
31 (in isoform 4)Phosphorylation-34.9321955146
32UbiquitinationRETGVIEKLLTSYGF
HHHCHHHHHHHHCCC		37.36-
32 (in isoform 3)Phosphorylation-37.3621955146
32 (in isoform 4)Phosphorylation-37.3621955146
34 (in isoform 3)Phosphorylation-4.4121955146
34 (in isoform 4)Phosphorylation-4.4121955146
35PhosphorylationGVIEKLLTSYGFIQC
CHHHHHHHHCCCEEC		30.2728152594
36PhosphorylationVIEKLLTSYGFIQCS
HHHHHHHHCCCEECC		24.1928152594
37PhosphorylationIEKLLTSYGFIQCSE
HHHHHHHCCCEECCH		15.7228152594
40 (in isoform 3)Phosphorylation-3.3322798277
40 (in isoform 4)Phosphorylation-3.3322798277
42 (in isoform 3)Phosphorylation-3.7922798277
42 (in isoform 4)Phosphorylation-3.7922798277
42GlutathionylationTSYGFIQCSERQARL
HHCCCEECCHHHHHH		3.7922555962
46 (in isoform 3)Phosphorylation-27.1226437602
46 (in isoform 4)Phosphorylation-27.1226437602
48PhosphorylationQCSERQARLFFHCSQ
ECCHHHHHHHEEHHH		24.5627251275
48 (in isoform 3)Phosphorylation-24.5622496350
48 (in isoform 4)Phosphorylation-24.5622496350
54PhosphorylationARLFFHCSQYNGNLQ
HHHHEEHHHCCCCCC		27.4227067055
81AcetylationSSDRRTGKPIAVKLV
ECCCCCCCEEEEEEE		32.4119608861
81UbiquitinationSSDRRTGKPIAVKLV
ECCCCCCCEEEEEEE		32.4121906983
81 (in isoform 2)Acetylation-32.41-
81 (in isoform 1)Ubiquitination-32.4121890473
81 (in isoform 2)Ubiquitination-32.4121890473
86UbiquitinationTGKPIAVKLVKIKQE
CCCEEEEEEEEECCH		38.24-
86AcetylationTGKPIAVKLVKIKQE
CCCEEEEEEEEECCH		38.2426051181
91SumoylationAVKLVKIKQEILPEE
EEEEEEECCHHCCHH		35.84-
91UbiquitinationAVKLVKIKQEILPEE
EEEEEEECCHHCCHH		35.84-
91SumoylationAVKLVKIKQEILPEE
EEEEEEECCHHCCHH		35.8428112733
114PhosphorylationAVPHNLESKSPAAPG
ECCCCCCCCCCCCCC		41.4122199227
116PhosphorylationPHNLESKSPAAPGQS
CCCCCCCCCCCCCCC		29.1119664994
123PhosphorylationSPAAPGQSPTGSVCY
CCCCCCCCCCCCEEE		30.2825159151
125PhosphorylationAAPGQSPTGSVCYER
CCCCCCCCCCEEEEE		47.5425850435
127PhosphorylationPGQSPTGSVCYERNG
CCCCCCCCEEEEECC		16.1128450419
127UbiquitinationPGQSPTGSVCYERNG
CCCCCCCCEEEEECC		16.11-
127AcetylationPGQSPTGSVCYERNG
CCCCCCCCEEEEECC		16.1119608861
127UbiquitinationPGQSPTGSVCYERNG
CCCCCCCCEEEEECC		16.1119608861
130PhosphorylationSPTGSVCYERNGEVF
CCCCCEEEEECCEEE		18.7730576142
135 (in isoform 2)Ubiquitination-32.7621890473
137 (in isoform 2)Phosphorylation-3.44-
137UbiquitinationYERNGEVFYLTYTPE
EEECCEEEEEEECHH		3.44-
138PhosphorylationERNGEVFYLTYTPED
EECCEEEEEEECHHH		11.87-
149 (in isoform 2)Ubiquitination-12.5921890473
162PhosphorylationGDKINFVIDNNKHTG
CCEEEEEEECCCCCC		4.0327251275
166UbiquitinationNFVIDNNKHTGAVSA
EEEEECCCCCCCCCH		49.1221890473
166AcetylationNFVIDNNKHTGAVSA
EEEEECCCCCCCCCH		49.1227452117
166 (in isoform 1)Ubiquitination-49.1221890473
168PhosphorylationVIDNNKHTGAVSARN
EEECCCCCCCCCHHH		28.5720068231
169PhosphorylationIDNNKHTGAVSARNI
EECCCCCCCCCHHHH		24.5727251275
172PhosphorylationNKHTGAVSARNIMLL
CCCCCCCCHHHHHHH		22.4520068231
176 (in isoform 2)Ubiquitination-1.3921890473
177SulfoxidationAVSARNIMLLKKKQA
CCCHHHHHHHHHHHH		4.0221406390
180UbiquitinationARNIMLLKKKQARCQ
HHHHHHHHHHHHHCC		54.7021906983
180 (in isoform 1)Ubiquitination-54.7021890473
181UbiquitinationRNIMLLKKKQARCQG
HHHHHHHHHHHHCCC		50.52-
181UbiquitinationRNIMLLKKKQARCQG
HHHHHHHHHHHHCCC		50.5221890473
194UbiquitinationQGVVCAMKEAFGFIE
CCCEEEHHHHHCCCC		27.63-
207UbiquitinationIERGDVVKEIFFHYS
CCCCHHHHHHEEEHH		44.9621890473
207 (in isoform 1)Ubiquitination-44.9621890473
208 (in isoform 2)Ubiquitination-33.1621890473
212UbiquitinationVVKEIFFHYSEFKGD
HHHHHEEEHHHCCCC		17.92-
222UbiquitinationEFKGDLETLQPGDDV
HCCCCCCCCCCCCCE		37.6821890473
227UbiquitinationLETLQPGDDVEFTIK
CCCCCCCCCEEEEEE		64.56-
234UbiquitinationDDVEFTIKDRNGKEV
CCEEEEEECCCCCEE		47.80-
239AcetylationTIKDRNGKEVATDVR
EEECCCCCEEEEEEE		53.1923749302
239UbiquitinationTIKDRNGKEVATDVR
EEECCCCCEEEEEEE		53.1921906983
239 (in isoform 1)Ubiquitination-53.1921890473
240UbiquitinationIKDRNGKEVATDVRL
EECCCCCEEEEEEEE		38.49-
246 (in isoform 2)Ubiquitination-33.0621890473
253UbiquitinationRLLPQGTVIFEDISI
EECCCCEEEEEECCE		6.37-
257 (in isoform 2)Ubiquitination-29.2321890473
264 (in isoform 2)Ubiquitination-56.7321890473
273UbiquitinationTVTKVIPKVPSKNQN
EEEEEECCCCCCCCC		56.50-
276PhosphorylationKVIPKVPSKNQNDPL
EEECCCCCCCCCCCC		47.4230266825
276 (in isoform 2)Ubiquitination-47.4221890473
277UbiquitinationVIPKVPSKNQNDPLP
EECCCCCCCCCCCCC		57.3820972266
277 (in isoform 1)Ubiquitination-57.3821890473
285UbiquitinationNQNDPLPGRIKVDFV
CCCCCCCCCEEEEEE		52.18-
288UbiquitinationDPLPGRIKVDFVIPK
CCCCCCEEEEEEECC		34.1021906983
288 (in isoform 1)Ubiquitination-34.1021890473
295UbiquitinationKVDFVIPKELPFGDK
EEEEEECCCCCCCCC		61.8421890473
295 (in isoform 1)Ubiquitination-61.8421890473
302UbiquitinationKELPFGDKDTKSKVT
CCCCCCCCCCCCCEE		68.62-
307UbiquitinationGDKDTKSKVTLLEGD
CCCCCCCCEEEEECC		40.5721906983
3072-HydroxyisobutyrylationGDKDTKSKVTLLEGD
CCCCCCCCEEEEECC		40.57-
307 (in isoform 1)Ubiquitination-40.5721890473
310UbiquitinationDTKSKVTLLEGDHVR
CCCCCEEEEECCEEE		4.6121890473
322PhosphorylationHVRFNISTDRRDKLE
EEEEECCCCCHHHHH		29.7221210654
323UbiquitinationVRFNISTDRRDKLER
EEEECCCCCHHHHHH		36.51-
324MethylationRFNISTDRRDKLERA
EEECCCCCHHHHHHH		49.11-
334UbiquitinationKLERATNIEVLSNTF
HHHHHHCCHHHCCCE		3.17-
353UbiquitinationEAREMGVIAAMRDGF
HHHHHCCEEEEECCC		1.35-
364AcetylationRDGFGFIKCVDRDVR
ECCCCEEEEEECCCE		26.4123749302
364UbiquitinationRDGFGFIKCVDRDVR
ECCCCEEEEEECCCE		26.41-
379UbiquitinationMFFHFSEILDGNQLH
EEEEHHHCCCCCCEE		4.0421890473
410UbiquitinationQRNHAIRIKKLPKGT
HHCCEEEEEECCCCE		3.64-
413 (in isoform 2)Phosphorylation-4.50-
414 (in isoform 2)Phosphorylation-41.74-
415UbiquitinationIRIKKLPKGTVSFHS
EEEEECCCCEEEEEE		77.10-
419PhosphorylationKLPKGTVSFHSHSDH
ECCCCEEEEEECCCC		19.6529214152
422PhosphorylationKGTVSFHSHSDHRFL
CCEEEEEECCCCCEE		23.7527251275
424PhosphorylationTVSFHSHSDHRFLGT
EEEEEECCCCCEEEE		37.8227251275
431PhosphorylationSDHRFLGTVEKEATF
CCCCEEEEEEEEEEC		27.8626074081
434AcetylationRFLGTVEKEATFSNP
CEEEEEEEEEECCCC		48.6026051181
434UbiquitinationRFLGTVEKEATFSNP
CEEEEEEEEEECCCC		48.60-
437PhosphorylationGTVEKEATFSNPKTT
EEEEEEEECCCCCCC		28.7826074081
439PhosphorylationVEKEATFSNPKTTSP
EEEEEECCCCCCCCC		48.1126074081
442UbiquitinationEATFSNPKTTSPNKG
EEECCCCCCCCCCCC		69.55-
443PhosphorylationATFSNPKTTSPNKGK
EECCCCCCCCCCCCC		33.4926074081
444PhosphorylationTFSNPKTTSPNKGKE
ECCCCCCCCCCCCCC		48.6028176443
445PhosphorylationFSNPKTTSPNKGKEK
CCCCCCCCCCCCCCC		31.5430278072
450 (in isoform 2)Phosphorylation-68.19-
452UbiquitinationSPNKGKEKEAEDGII
CCCCCCCCCCCCCEE		66.75-
461 (in isoform 2)Phosphorylation-11.25-
464GlutathionylationGIIAYDDCGVKLTIA
CEEEECCCCCEEEEE		6.5322555962
465PhosphorylationIIAYDDCGVKLTIAF
EEEECCCCCEEEEEE		26.9627251275
480PhosphorylationQAKDVEGSTSPQIGD
EEECCCCCCCCCCCC		16.5321815630
481PhosphorylationAKDVEGSTSPQIGDK
EECCCCCCCCCCCCE		56.1129255136
482PhosphorylationKDVEGSTSPQIGDKV
ECCCCCCCCCCCCEE		19.2629255136
483 (in isoform 2)Phosphorylation-29.87-
488UbiquitinationTSPQIGDKVEFSISD
CCCCCCCEEEEECCC		38.15-
492PhosphorylationIGDKVEFSISDKQRP
CCCEEEEECCCCCCC		14.0020068231
494PhosphorylationDKVEFSISDKQRPGQ
CEEEEECCCCCCCCH		37.2420068231
496UbiquitinationVEFSISDKQRPGQQV
EEEECCCCCCCCHHH		41.22-
496AcetylationVEFSISDKQRPGQQV
EEEECCCCCCCCHHH		41.2226051181
514PhosphorylationVRLLGRNSNSKRLLG
HHHHCCCCCHHHHHE		40.9121955146
516PhosphorylationLLGRNSNSKRLLGYV
HHCCCCCHHHHHEEE		20.9725849741
522PhosphorylationNSKRLLGYVATLKDN
CHHHHHEEEEEEECC		6.2021406692
525PhosphorylationRLLGYVATLKDNFGF
HHHEEEEEEECCEEE		25.0521406692
527UbiquitinationLGYVATLKDNFGFIE
HEEEEEEECCEEEEE		46.39-
535PhosphorylationDNFGFIETANHDKEI
CCEEEEEECCCCCEE		28.1328555341
547PhosphorylationKEIFFHYSEFSGDVD
CEEEEEEEEECCCCC		24.4822210691
550PhosphorylationFFHYSEFSGDVDSLE
EEEEEEECCCCCEEE		29.9922210691
555PhosphorylationEFSGDVDSLELGDMV
EECCCCCEEEHHHHE		24.4822210691
560PhosphorylationVDSLELGDMVEYSLS
CCEEEHHHHEEEECC		51.0527251275
571PhosphorylationYSLSKGKGNKVSAEK
EECCCCCCCCCCHHH		48.1127251275
578UbiquitinationGNKVSAEKVNKTHSV
CCCCCHHHCCCCCCC		51.31-
578AcetylationGNKVSAEKVNKTHSV
CCCCCHHHCCCCCCC		51.3125953088
581UbiquitinationVSAEKVNKTHSVNGI
CCHHHCCCCCCCCCC		51.07-
582PhosphorylationSAEKVNKTHSVNGIT
CHHHCCCCCCCCCCC		17.7428450419
584PhosphorylationEKVNKTHSVNGITEE
HHCCCCCCCCCCCCC		23.6225159151
589PhosphorylationTHSVNGITEEADPTI
CCCCCCCCCCCCCCE		29.2228450419
595PhosphorylationITEEADPTIYSGKVI
CCCCCCCCEECCCEE		32.8523186163
597PhosphorylationEEADPTIYSGKVIRP
CCCCCCEECCCEEEE		17.5328152594
598PhosphorylationEADPTIYSGKVIRPL
CCCCCEECCCEEEEC		28.4323186163
600UbiquitinationDPTIYSGKVIRPLRS
CCCEECCCEEEECCC		28.66-
607PhosphorylationKVIRPLRSVDPTQTE
CEEEECCCCCCCCCE		38.2622210691
611PhosphorylationPLRSVDPTQTEYQGM
ECCCCCCCCCEEEEE		43.5922210691
613PhosphorylationRSVDPTQTEYQGMIE
CCCCCCCCEEEEEEE		38.8522210691
615PhosphorylationVDPTQTEYQGMIEIV
CCCCCCEEEEEEEEE		17.4722210691
617 (in isoform 2)Ubiquitination-20.3821890473
627UbiquitinationEIVEEGDMKGEVYPF
EEEECCCCCCCEEEC		9.87-
628PhosphorylationIVEEGDMKGEVYPFG
EEECCCCCCCEEECE		57.5727251275
628SumoylationIVEEGDMKGEVYPFG
EEECCCCCCCEEECE		57.57-
642UbiquitinationGIVGMANKGDCLQKG
EEEEEECCCCCCCCC		46.73-
646UbiquitinationMANKGDCLQKGESVK
EECCCCCCCCCCCEE		7.59-
648AcetylationNKGDCLQKGESVKFQ
CCCCCCCCCCCEEEE		52.2623749302
648UbiquitinationNKGDCLQKGESVKFQ
CCCCCCCCCCCEEEE		52.2621906983
648 (in isoform 1)Ubiquitination-52.2621890473
653PhosphorylationLQKGESVKFQLCVLG
CCCCCCEEEEEEEEC		36.3527251275
665 (in isoform 2)Ubiquitination-11.0221890473
677PhosphorylationITPLRRATVECVKDQ
CCCCCCCEEHHHHHH		18.2828985074
682AcetylationRATVECVKDQFGFIN
CCEEHHHHHHCCCEE		58.4323749302
682UbiquitinationRATVECVKDQFGFIN
CCEEHHHHHHCCCEE		58.43-
682MalonylationRATVECVKDQFGFIN
CCEEHHHHHHCCCEE		58.4326320211
690PhosphorylationDQFGFINYEVGDSKK
HHCCCEEEEECCCEE		13.7428796482
694UbiquitinationFINYEVGDSKKLFFH
CEEEEECCCEEEEEE		63.56-
696AcetylationNYEVGDSKKLFFHVK
EEEECCCEEEEEEEE		59.2326051181
696UbiquitinationNYEVGDSKKLFFHVK
EEEECCCEEEEEEEE		59.2321906983
6962-HydroxyisobutyrylationNYEVGDSKKLFFHVK
EEEECCCEEEEEEEE		59.23-
696 (in isoform 1)Ubiquitination-59.2321890473
697AcetylationYEVGDSKKLFFHVKE
EEECCCEEEEEEEEE		55.2526051181
697UbiquitinationYEVGDSKKLFFHVKE
EEECCCEEEEEEEEE		55.25-
723PhosphorylationEVEFSVILNQRTGKC
EEEEEEEEECCCCCC		4.1327251275
727 (in isoform 2)Ubiquitination-31.0921890473
728UbiquitinationVILNQRTGKCSACNV
EEEECCCCCCCCCCE		31.03-
729UbiquitinationILNQRTGKCSACNVW
EEECCCCCCCCCCEE		25.14-
729AcetylationILNQRTGKCSACNVW
EEECCCCCCCCCCEE		25.1426051181
743UbiquitinationWRVCEGPKAVAAPRP
EEEECCCCCEECCCH		67.37-
743UbiquitinationWRVCEGPKAVAAPRP
EEEECCCCCEECCCH		67.37-
743AcetylationWRVCEGPKAVAAPRP
EEEECCCCCEECCCH		67.3726051181
744UbiquitinationRVCEGPKAVAAPRPD
EEECCCCCEECCCHH		10.1821890473
749MethylationPKAVAAPRPDRLVNR
CCCEECCCHHHHHHH		40.81-
752MethylationVAAPRPDRLVNRLKN
EECCCHHHHHHHHCC		43.12-
758UbiquitinationDRLVNRLKNITLDDA
HHHHHHHCCCCCCCC		42.9621890473
758AcetylationDRLVNRLKNITLDDA
HHHHHHHCCCCCCCC		42.9627452117
758 (in isoform 1)Ubiquitination-42.9621890473
761PhosphorylationVNRLKNITLDDASAP
HHHHCCCCCCCCCCC		33.2629255136
773UbiquitinationSAPRLMVLRQPRGPD
CCCEEEEEECCCCCC		2.3421890473
775UbiquitinationPRLMVLRQPRGPDNS
CEEEEEECCCCCCCC		28.07-
782PhosphorylationQPRGPDNSMGFGAER
CCCCCCCCCCCCCHH		27.88-
783SulfoxidationPRGPDNSMGFGAERK
CCCCCCCCCCCCHHH		6.9028465586
789UbiquitinationSMGFGAERKIRQAGV
CCCCCCHHHHHHCCC		38.88-
804UbiquitinationID-------------
CC-------------		-
807Phosphorylation----------------
----------------		27251275
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSDE1_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 CSDE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STT3A_HUMANSTT3Aphysical
16169070
CUL1_HUMANCUL1physical
22863883
GANAB_HUMANGANABphysical
22863883
GMPPB_HUMANGMPPBphysical
22863883
PLAK_HUMANJUPphysical
22863883
PLOD2_HUMANPLOD2physical
22863883
SPT5H_HUMANSUPT5Hphysical
22863883
TRM1_HUMANTRMT1physical
22863883
UGPA_HUMANUGP2physical
22863883
VASN_HUMANVASNphysical
22863883
FAM9B_HUMANFAM9Bphysical
25416956
HID1_HUMANHID1physical
25416956
NU188_HUMANNUP188physical
26344197
CK068_HUMANC11orf68physical
21516116
PPIA_HUMANPPIAphysical
26496610
STRAP_HUMANSTRAPphysical
26496610
HTR5A_HUMANHEATR5Aphysical
26496610
PKHA3_HUMANPLEKHA3physical
26496610
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 CSDE1_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-81, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-123, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444 AND SER-445, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-481, AND MASSSPECTROMETRY.

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