MARH6_HUMAN - dbPTM
MARH6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARH6_HUMAN
UniProt AC O60337
Protein Name E3 ubiquitin-protein ligase MARCH6
Gene Name 6-Mar
Organism Homo sapiens (Human).
Sequence Length 910
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1..
Protein Sequence MDTAEEDICRVCRSEGTPEKPLYHPCVCTGSIKFIHQECLVQWLKHSRKEYCELCKHRFAFTPIYSPDMPSRLPIQDIFAGLVTSIGTAIRYWFHYTLVAFAWLGVVPLTACRIYKCLFTGSVSSLLTLPLDMLSTENLLADCLQGCFVVTCTLCAFISLVWLREQIVHGGAPIWLEHAAPPFNAAGHHQNEAPAGGNGAENVAADQPANPPAENAVVGENPDAQDDQAEEEEEDNEEEDDAGVEDAADANNGAQDDMNWNALEWDRAAEELTWERMLGLDGSLVFLEHVFWVVSLNTLFILVFAFCPYHIGHFSLVGLGFEEHVQASHFEGLITTIVGYILLAITLIICHGLATLVKFHRSRRLLGVCYIVVKVSLLVVVEIGVFPLICGWWLDICSLEMFDATLKDRELSFQSAPGTTMFLHWLVGMVYVFYFASFILLLREVLRPGVLWFLRNLNDPDFNPVQEMIHLPIYRHLRRFILSVIVFGSIVLLMLWLPIRIIKSVLPNFLPYNVMLYSDAPVSELSLELLLLQVVLPALLEQGHTRQWLKGLVRAWTVTAGYLLDLHSYLLGDQEENENSANQQVNNNQHARNNNAIPVVGEGLHAAHQAILQQGGPVGFQPYRRPLNFPLRIFLLIVFMCITLLIASLICLTLPVFAGRWLMSFWTGTAKIHELYTAACGLYVCWLTIRAVTVMVAWMPQGRRVIFQKVKEWSLMIMKTLIVAVLLAGVVPLLLGLLFELVIVAPLRVPLDQTPLFYPWQDWALGVLHAKIIAAITLMGPQWWLKTVIEQVYANGIRNIDLHYIVRKLAAPVISVLLLSLCVPYVIASGVVPLLGVTAEMQNLVHRRIYPFLLMVVVLMAILSFQVRQFKRLYEHIKNDKYLVGQRLVNYERKSGKQGSSPPPPQSSQE
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
1Acetylation-------MDTAEEDI
-------CCCHHHHH		10.4922814378
14PhosphorylationDICRVCRSEGTPEKP
HHHHHHHCCCCCCCC		34.9421712546
17PhosphorylationRVCRSEGTPEKPLYH
HHHHCCCCCCCCCCC		24.9921712546
20UbiquitinationRSEGTPEKPLYHPCV
HCCCCCCCCCCCCEE		41.3421963094
23PhosphorylationGTPEKPLYHPCVCTG
CCCCCCCCCCEEECC		16.5522210691
29PhosphorylationLYHPCVCTGSIKFIH
CCCCEEECCCCEEEC		17.3625159151
31PhosphorylationHPCVCTGSIKFIHQE
CCEEECCCCEEECHH		12.4025159151
33UbiquitinationCVCTGSIKFIHQECL
EEECCCCEEECHHHH		39.7121963094
45UbiquitinationECLVQWLKHSRKEYC
HHHHHHHHHCHHHHH		36.2521963094
49UbiquitinationQWLKHSRKEYCELCK
HHHHHCHHHHHHHHC		56.9321963094
56UbiquitinationKEYCELCKHRFAFTP
HHHHHHHCCCCCCCC		50.9023000965
150UbiquitinationCLQGCFVVTCTLCAF
HHHHCHHHHHHHHHH		1.5027667366
309UbiquitinationLVFAFCPYHIGHFSL
HHHHHCCHHHCCCHH		13.7821963094
311UbiquitinationFAFCPYHIGHFSLVG
HHHCCHHHCCCHHHC		3.6522817900
437PhosphorylationVYVFYFASFILLLRE
HHHHHHHHHHHHHHH		11.70-
445UbiquitinationFILLLREVLRPGVLW
HHHHHHHHHCHHHHH		4.4327667366
474PhosphorylationEMIHLPIYRHLRRFI
HHHHHHHHHHHHHHH		7.0517053785
478UbiquitinationLPIYRHLRRFILSVI
HHHHHHHHHHHHHHH		25.9121963094
481UbiquitinationYRHLRRFILSVIVFG
HHHHHHHHHHHHHHH		2.3827667366
482UbiquitinationRHLRRFILSVIVFGS
HHHHHHHHHHHHHHH		2.8427667366
494UbiquitinationFGSIVLLMLWLPIRI
HHHHHHHHHHHHHHH		1.8922817900
497UbiquitinationIVLLMLWLPIRIIKS
HHHHHHHHHHHHHHH		1.9122817900
502UbiquitinationLWLPIRIIKSVLPNF
HHHHHHHHHHHCCCC		1.6327667366
502UbiquitinationLWLPIRIIKSVLPNF
HHHHHHHHHHHCCCC		1.6321890473
502UbiquitinationLWLPIRIIKSVLPNF
HHHHHHHHHHHCCCC		1.6321890473
550UbiquitinationGHTRQWLKGLVRAWT
CCHHHHHHHHHHHHH		47.4421890473
550UbiquitinationGHTRQWLKGLVRAWT
CCHHHHHHHHHHHHH		47.4427667366
604UbiquitinationIPVVGEGLHAAHQAI
CCCCCCHHHHHHHHH		1.8521963094
606UbiquitinationVVGEGLHAAHQAILQ
CCCCHHHHHHHHHHH		16.2222817900
641UbiquitinationFLLIVFMCITLLIAS
HHHHHHHHHHHHHHH		1.1421963094
643UbiquitinationLIVFMCITLLIASLI
HHHHHHHHHHHHHHH		15.5822817900
661UbiquitinationLPVFAGRWLMSFWTG
HHHHHHHHHHHHHHC		8.7621963094
663UbiquitinationVFAGRWLMSFWTGTA
HHHHHHHHHHHHCCH		2.1722817900
709UbiquitinationGRRVIFQKVKEWSLM
CCCCHHHHHHHHHHH		44.5221963094
711UbiquitinationRVIFQKVKEWSLMIM
CCHHHHHHHHHHHHH		61.5722817900
773UbiquitinationGVLHAKIIAAITLMG
HHHHHHHHHHHHHHC		1.7727667366
776UbiquitinationHAKIIAAITLMGPQW
HHHHHHHHHHHCCHH		1.9427667366
789UbiquitinationQWWLKTVIEQVYANG
HHHHHHHHHHHHHCC		3.5722817900
792UbiquitinationLKTVIEQVYANGIRN
HHHHHHHHHHCCCCC		2.9433845483
810UbiquitinationHYIVRKLAAPVISVL
HHHHHHHHHHHHHHH		16.8621963094
813UbiquitinationVRKLAAPVISVLLLS
HHHHHHHHHHHHHHH		4.3427667366
826UbiquitinationLSLCVPYVIASGVVP
HHHHHHHHHHCCCHH		2.1122817900
829UbiquitinationCVPYVIASGVVPLLG
HHHHHHHCCCHHHCC		22.4622817900
830UbiquitinationVPYVIASGVVPLLGV
HHHHHHCCCHHHCCC		18.5427667366
833UbiquitinationVIASGVVPLLGVTAE
HHHCCCHHHCCCCHH		21.3327667366
833UbiquitinationVIASGVVPLLGVTAE
HHHCCCHHHCCCCHH		21.3321890473
833UbiquitinationVIASGVVPLLGVTAE
HHHCCCHHHCCCCHH		21.3321890473
846UbiquitinationAEMQNLVHRRIYPFL
HHHHHHHHHCHHHHH		19.2322817900
849UbiquitinationQNLVHRRIYPFLLMV
HHHHHHCHHHHHHHH		5.3033845483
850PhosphorylationNLVHRRIYPFLLMVV
HHHHHCHHHHHHHHH		6.01-
874PhosphorylationVRQFKRLYEHIKNDK
HHHHHHHHHHHHCCC		14.97-
878UbiquitinationKRLYEHIKNDKYLVG
HHHHHHHHCCCHHHH		62.0927667366
881UbiquitinationYEHIKNDKYLVGQRL
HHHHHCCCHHHHHHH		50.2927667366
8812-HydroxyisobutyrylationYEHIKNDKYLVGQRL
HHHHHCCCHHHHHHH		50.29-
881UbiquitinationYEHIKNDKYLVGQRL
HHHHHCCCHHHHHHH		50.2921890473
882PhosphorylationEHIKNDKYLVGQRLV
HHHHCCCHHHHHHHH		14.96-
891PhosphorylationVGQRLVNYERKSGKQ
HHHHHHCCCCCCCCC		15.0522210691
894UbiquitinationRLVNYERKSGKQGSS
HHHCCCCCCCCCCCC		52.1722817900
895PhosphorylationLVNYERKSGKQGSSP
HHCCCCCCCCCCCCC		58.4022210691
897UbiquitinationNYERKSGKQGSSPPP
CCCCCCCCCCCCCCC		59.5922817900
907PhosphorylationSSPPPPQSSQE----
CCCCCCCCCCC----		39.5024719451
908PhosphorylationSPPPPQSSQE-----
CCCCCCCCCC-----		32.8325627689
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 MARH6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARH6_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 MARH6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IOD2_HUMANDIO2physical
19651899
UB2G2_MOUSEUbe2g2physical
19103148
ERG1_HUMANSQLEphysical
24449766
UBC_HUMANUBCphysical
15673284
UB2G1_HUMANUBE2G1physical
15673284
ERG1_HUMANSQLEphysical
24840124
UB2D2_HUMANUBE2D2physical
17848550
MARH6_HUMANMARCH6physical
17848550
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 MARH6_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-474, AND MASSSPECTROMETRY.

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