DYM_HUMAN - dbPTM
DYM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYM_HUMAN
UniProt AC Q7RTS9
Protein Name Dymeclin
Gene Name DYM
Organism Homo sapiens (Human).
Sequence Length 669
Subcellular Localization Cytoplasm. Golgi apparatus. Membrane
Lipid-anchor . Sequence analysis programs clearly predict 1 transmembrane region. However, PubMed:18996921 shows that it is not a stably anchored transmembrane protein but it weakly associates with the Golgi app
Protein Description Necessary for correct organization of Golgi apparatus. Involved in bone development..
Protein Sequence MGSNSSRIGDLPKNEYLKKLSGTESISENDPFWNQLLSFSFPAPTSSSELKLLEEATISVCRSLVENNPRTGNLGALIKVFLSRTKELKLSAECQNHIFIWQTHNALFIICCLLKVFICQMSEEELQLHFTYEEKSPGNYSSDSEDLLEELLCCLMQLITDIPLLDITYEISVEAISTMVVFLSCQLFHKEVLRQSISHKYLMRGPCLPYTSKLVKTLLYNFIRQEKPPPPGAHVFPQQSDGGGLLYGLASGVATGLWTVFTLGGVGSKAAASPELSSPLANQSLLLLLVLANLTDASDAPNPYRQAIMSFKNTQDSSPFPSSIPHAFQINFNSLYTALCEQQTSDQATLLLYTLLHQNSNIRTYMLARTDMENLVLPILEILYHVEERNSHHVYMALIILLILTEDDGFNRSIHEVILKNITWYSERVLTEISLGSLLILVVIRTIQYNMTRTRDKYLHTNCLAALANMSAQFRSLHQYAAQRIISLFSLLSKKHNKVLEQATQSLRGSLSSNDVPLPDYAQDLNVIEEVIRMMLEIINSCLTNSLHHNPNLVYALLYKRDLFEQFRTHPSFQDIMQNIDLVISFFSSRLLQAGAELSVERVLEIIKQGVVALPKDRLKKFPELKFKYVEEEQPEEFFIPYVWSLVYNSAVGLYWNPQDIQLFTMDSD
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
2Myristoylation------MGSNSSRIG
------CCCCCCCCC		35.2218996921
13UbiquitinationSRIGDLPKNEYLKKL
CCCCCCCCHHHHHHH		70.4829967540
83PhosphorylationALIKVFLSRTKELKL
HHHHHHHHCCCCCCC		26.8329978859
304 (in isoform 2)Ubiquitination-23.2321890473
308 (in isoform 2)Ubiquitination-1.4721890473
322O-linked_GlycosylationQDSSPFPSSIPHAFQ
CCCCCCCCCCCEEEE		41.0829351928
334O-linked_GlycosylationAFQINFNSLYTALCE
EEEECHHHHHHHHHH		20.7229351928
418 (in isoform 2)Ubiquitination-4.0621890473
434UbiquitinationERVLTEISLGSLLIL
HHHHHHCCHHHHHHH		22.0521890473
435UbiquitinationRVLTEISLGSLLILV
HHHHHCCHHHHHHHH		7.1122817900
438UbiquitinationTEISLGSLLILVVIR
HHCCHHHHHHHHHHH		3.0621890473
439UbiquitinationEISLGSLLILVVIRT
HCCHHHHHHHHHHHH		2.8122817900
442UbiquitinationLGSLLILVVIRTIQY
HHHHHHHHHHHHHHH		2.3921890473
446PhosphorylationLILVVIRTIQYNMTR
HHHHHHHHHHHCCCC		10.9920071362
449PhosphorylationVVIRTIQYNMTRTRD
HHHHHHHHCCCCCCC		11.75-
452PhosphorylationRTIQYNMTRTRDKYL
HHHHHCCCCCCCHHH		25.83-
454PhosphorylationIQYNMTRTRDKYLHT
HHHCCCCCCCHHHHH		33.7729083192
458PhosphorylationMTRTRDKYLHTNCLA
CCCCCCHHHHHHHHH		14.1717053785
461PhosphorylationTRDKYLHTNCLAALA
CCCHHHHHHHHHHHH		25.6529083192
471PhosphorylationLAALANMSAQFRSLH
HHHHHHHCHHHHHHH		20.8024719451
490PhosphorylationQRIISLFSLLSKKHN
HHHHHHHHHHHHHHH		33.4223186163
492UbiquitinationIISLFSLLSKKHNKV
HHHHHHHHHHHHHHH		7.3621890473
493UbiquitinationISLFSLLSKKHNKVL
HHHHHHHHHHHHHHH		44.9721890473
494 (in isoform 1)Ubiquitination-59.0021890473
494UbiquitinationSLFSLLSKKHNKVLE
HHHHHHHHHHHHHHH		59.0021890473
495UbiquitinationLFSLLSKKHNKVLEQ
HHHHHHHHHHHHHHH		49.3822817900
496UbiquitinationFSLLSKKHNKVLEQA
HHHHHHHHHHHHHHH		42.9821890473
497UbiquitinationSLLSKKHNKVLEQAT
HHHHHHHHHHHHHHH		45.0421890473
498 (in isoform 1)Ubiquitination-48.1721890473
498UbiquitinationLLSKKHNKVLEQATQ
HHHHHHHHHHHHHHH		48.1721890473
510PhosphorylationATQSLRGSLSSNDVP
HHHHHHHCCCCCCCC		20.7426657352
513PhosphorylationSLRGSLSSNDVPLPD
HHHHCCCCCCCCCCH		42.2026657352
545UbiquitinationIINSCLTNSLHHNPN
HHHHHHHHCCCCCHH		29.6221890473
546UbiquitinationINSCLTNSLHHNPNL
HHHHHHHCCCCCHHH		24.6821890473
547UbiquitinationNSCLTNSLHHNPNLV
HHHHHHCCCCCHHHH		5.3021890473
548UbiquitinationSCLTNSLHHNPNLVY
HHHHHCCCCCHHHHH		20.6421890473
552UbiquitinationNSLHHNPNLVYALLY
HCCCCCHHHHHHHHH		47.6721890473
560UbiquitinationLVYALLYKRDLFEQF
HHHHHHHCHHHHHHH		39.13-
572PhosphorylationEQFRTHPSFQDIMQN
HHHHHCCCHHHHHHH		28.1224719451
599PhosphorylationLQAGAELSVERVLEI
HHCCCCCCHHHHHHH		17.2824719451
606UbiquitinationSVERVLEIIKQGVVA
CHHHHHHHHHHCCCC		4.1121890473
607UbiquitinationVERVLEIIKQGVVAL
HHHHHHHHHHCCCCC		1.6721890473
608UbiquitinationERVLEIIKQGVVALP
HHHHHHHHHCCCCCC		46.8121906983
608 (in isoform 1)Ubiquitination-46.8121890473
616UbiquitinationQGVVALPKDRLKKFP
HCCCCCCHHHHHHCC		57.2229967540
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 DYM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of DYM_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
223800Dyggve-Melchior-Clausen syndrome (DMC)
607326Smith-McCort dysplasia 1 (SMC1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYM_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, AND MASSSPECTROMETRY.

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