EOMES_HUMAN - dbPTM
EOMES_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EOMES_HUMAN
UniProt AC O95936
Protein Name Eomesodermin homolog
Gene Name EOMES
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization Nucleus .
Protein Description Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes..
Protein Sequence MQLGEQLLVSSVNLPGAHFYPLESARGGSGGSAGHLPSAAPSPQKLDLDKASKKFSGSLSCEAVSGEPAAASAGAPAAMLSDTDAGDAFASAAAVAKPGPPDGRKGSPCGEEELPSAAAAAAAAAAAAAATARYSMDSLSSERYYLQSPGPQGSELAAPCSLFPYQAAAGAPHGPVYPAPNGARYPYGSMLPPGGFPAAVCPPGRAQFGPGAGAGSGAGGSSGGGGGPGTYQYSQGAPLYGPYPGAAAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSSHQIVPGGRYGVQSFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPGTNKLDISSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGSYQRKMAAGLPWTSRTSPTVFSEDQLSKEKVKEEIGSSWIETPPSIKSLDSNDSGVYTSACKRRRLSPSNSSNENSPSIKCEDINAEEYSKDTSKGMGGYYAFYTTP
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
32PhosphorylationARGGSGGSAGHLPSA
CCCCCCCCCCCCCCC		34.3030576142
38PhosphorylationGSAGHLPSAAPSPQK
CCCCCCCCCCCCCCC		43.3428348404
42PhosphorylationHLPSAAPSPQKLDLD
CCCCCCCCCCCCCHH		34.9230576142
52PhosphorylationKLDLDKASKKFSGSL
CCCHHHHHHHHCCCC		41.9628111955
107PhosphorylationPPDGRKGSPCGEEEL
CCCCCCCCCCCCCCC		21.7622617229
107 (in isoform 4)Phosphorylation-21.7627251275
116PhosphorylationCGEEELPSAAAAAAA
CCCCCCHHHHHHHHH		43.0728464451
148 (in isoform 4)Phosphorylation-29.2727251275
148PhosphorylationSERYYLQSPGPQGSE
CCEEEECCCCCCCCC		29.2727251275
154PhosphorylationQSPGPQGSELAAPCS
CCCCCCCCCCCCCCC		24.9627080861
161PhosphorylationSELAAPCSLFPYQAA
CCCCCCCCCCCCCCC		31.8027080861
165 (in isoform 3)Phosphorylation-11.9328634120
167 (in isoform 3)Phosphorylation-8.0828634120
174 (in isoform 2)Phosphorylation-16.5928634120
176 (in isoform 3)Phosphorylation-12.0827251275
176 (in isoform 2)Phosphorylation-12.0828634120
178 (in isoform 3)Phosphorylation-41.2822985185
185 (in isoform 2)Phosphorylation-10.5627251275
187 (in isoform 2)Phosphorylation-16.9522985185
216PhosphorylationGPGAGAGSGAGGSSG
CCCCCCCCCCCCCCC		25.57-
221PhosphorylationAGSGAGGSSGGGGGP
CCCCCCCCCCCCCCC		25.54-
291UbiquitinationQTEMIITKQGRRMFP
CCEEEEECCCCCEEC		40.11-
350PhosphorylationNMQGNKMYVHPESPN
CCCCCEEEECCCCCC		9.3822210691
355PhosphorylationKMYVHPESPNTGSHW
EEEECCCCCCCCCCC		28.0922210691
358PhosphorylationVHPESPNTGSHWMRQ
ECCCCCCCCCCCCCE		43.3722210691
360PhosphorylationPESPNTGSHWMRQEI
CCCCCCCCCCCCEEE		16.3722210691
385PhosphorylationKGANNNNTQMIVLQS
CCCCCCCCEEEEEHH		22.9523403867
392PhosphorylationTQMIVLQSLHKYQPR
CEEEEEHHHHHCCCC		28.4223403867
396PhosphorylationVLQSLHKYQPRLHIV
EEHHHHHCCCCEEEE		17.0122468782
460 (in isoform 4)Phosphorylation-21.2528634120
462 (in isoform 4)Phosphorylation-25.9128634120
471 (in isoform 4)Phosphorylation-15.0427251275
473 (in isoform 4)Phosphorylation-30.1122985185
578MethylationAMAGWGGRGSYQRKM
CCCCCCCCCHHHHHH		27.26-
583MethylationGGRGSYQRKMAAGLP
CCCCHHHHHHHCCCC		23.60-
595PhosphorylationGLPWTSRTSPTVFSE
CCCCCCCCCCCCCCH		38.5323401153
596PhosphorylationLPWTSRTSPTVFSED
CCCCCCCCCCCCCHH		19.9123911959
598PhosphorylationWTSRTSPTVFSEDQL
CCCCCCCCCCCHHHH		33.6730576142
601PhosphorylationRTSPTVFSEDQLSKE
CCCCCCCCHHHHCHH		35.6127080861
606PhosphorylationVFSEDQLSKEKVKEE
CCCHHHHCHHHHHHH		32.8927080861
615 (in isoform 4)Phosphorylation-20.9327251275
621PhosphorylationIGSSWIETPPSIKSL
HHHCCCCCCCCCCCC		31.2228348404
627PhosphorylationETPPSIKSLDSNDSG
CCCCCCCCCCCCCCC		35.42-
633PhosphorylationKSLDSNDSGVYTSAC
CCCCCCCCCCCCHHH		34.1129978859
636PhosphorylationDSNDSGVYTSACKRR
CCCCCCCCCHHHCCC		9.8629978859
637PhosphorylationSNDSGVYTSACKRRR
CCCCCCCCHHHCCCC		13.8729978859
638PhosphorylationNDSGVYTSACKRRRL
CCCCCCCHHHCCCCC		17.6229978859
641AcetylationGVYTSACKRRRLSPS
CCCCHHHCCCCCCCC		48.9725953088
646PhosphorylationACKRRRLSPSNSSNE
HHCCCCCCCCCCCCC		25.1923401153
648PhosphorylationKRRRLSPSNSSNENS
CCCCCCCCCCCCCCC		46.0726657352
650PhosphorylationRRLSPSNSSNENSPS
CCCCCCCCCCCCCCC		38.5930576142
651PhosphorylationRLSPSNSSNENSPSI
CCCCCCCCCCCCCCC		53.0326657352
655PhosphorylationSNSSNENSPSIKCED
CCCCCCCCCCCEEEE		17.5330576142
657PhosphorylationSSNENSPSIKCEDIN
CCCCCCCCCEEEECC		34.20-
665 (in isoform 4)Phosphorylation-16.0127251275
667 (in isoform 4)Phosphorylation-53.3427251275
668PhosphorylationEDINAEEYSKDTSKG
EECCHHHHCCCCCCC		16.7224719451
669 (in isoform 4)Phosphorylation-27.6027251275
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 EOMES_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EOMES_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 EOMES_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EOMES_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EOMES_HUMAN

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Related Literatures of Post-Translational Modification

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