DMWD_HUMAN - dbPTM
DMWD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DMWD_HUMAN
UniProt AC Q09019
Protein Name Dystrophia myotonica WD repeat-containing protein
Gene Name DMWD
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Perikaryon . Cell projection, dendrite . Nucleus . In neurons, shows punctate expression throughout the cell body, nucleus and dendrites. Not detected in axons.
Protein Description
Protein Sequence MAAGGAEGGSGPGAAMGDCAEIKSQFRTREGFYKLLPGDGAARRSGPASAQTPVPPQPPQPPPGPASASGPGAAGPASSPPPAGPGPGPALPAVRLSLVRLGEPDSAGAGEPPATPAGLGSGGDRVCFNLGRELYFYPGCCRRGSQRSIDLNKPIDKRIYKGTQPTCHDFNQFTAATETISLLVGFSAGQVQYLDLIKKDTSKLFNEERLIDKTKVTYLKWLPESESLFLASHASGHLYLYNVSHPCASAPPQYSLLKQGEGFSVYAAKSKAPRNPLAKWAVGEGPLNEFAFSPDGRHLACVSQDGCLRVFHFDSMLLRGLMKSYFGGLLCVCWSPDGRYVVTGGEDDLVTVWSFTEGRVVARGHGHKSWVNAVAFDPYTTRAEEAATAAGADGERSGEEEEEEPEAAGTGSAGGAPLSPLPKAGSITYRFGSAGQDTQFCLWDLTEDVLYPHPPLARTRTLPGTPGTTPPAASSSRGGEPGPGPLPRSLSRSNSLPHPAGGGKAGGPGVAAEPGTPFSIGRFATLTLQERRDRGAEKEHKRYHSLGNISRGGSGGSGSGGEKPSGPVPRSRLDPAKVLGTALCPRIHEVPLLEPLVCKKIAQERLTVLLFLEDCIITACQEGLICTWARPGKAFTDEETEAQTGEGSWPRSPSKSVVEGISSQPGNSPSGTVV
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
2Acetylation------MAAGGAEGG
------CCCCCCCCC		18.1422814378
33PhosphorylationFRTREGFYKLLPGDG
HHCCCCCHHCCCCCC		16.1629496907
97PhosphorylationALPAVRLSLVRLGEP
CCCHHHEEEEECCCC		17.7924719451
148PhosphorylationCRRGSQRSIDLNKPI
CCCCCCCCCCCCCCC		16.9030266825
153UbiquitinationQRSIDLNKPIDKRIY
CCCCCCCCCCCCCHH		51.12-
157UbiquitinationDLNKPIDKRIYKGTQ
CCCCCCCCCHHCCCC		41.22-
199UbiquitinationQYLDLIKKDTSKLFN
HHHHHHHHHHHHHCC		60.28-
203UbiquitinationLIKKDTSKLFNEERL
HHHHHHHHHCCHHHH		60.22-
254PhosphorylationCASAPPQYSLLKQGE
CCCCCCCHHHHHCCC		13.6824719451
255PhosphorylationASAPPQYSLLKQGEG
CCCCCCHHHHHCCCC		23.2124719451
266PhosphorylationQGEGFSVYAAKSKAP
CCCCCEEEEECCCCC		10.31-
269UbiquitinationGFSVYAAKSKAPRNP
CCEEEEECCCCCCCC		44.30-
279UbiquitinationAPRNPLAKWAVGEGP
CCCCCHHHCCCCCCC		43.2821906983
388PhosphorylationTRAEEAATAAGADGE
CHHHHHHHHCCCCCC		24.8830108239
396DimethylationAAGADGERSGEEEEE
HCCCCCCCCCCCCCC		56.33-
397PhosphorylationAGADGERSGEEEEEE
CCCCCCCCCCCCCCC		46.3730576142
410PhosphorylationEEPEAAGTGSAGGAP
CCCCCCCCCCCCCCC		24.2030108239
412PhosphorylationPEAAGTGSAGGAPLS
CCCCCCCCCCCCCCC		24.4730108239
419PhosphorylationSAGGAPLSPLPKAGS
CCCCCCCCCCCCCCE		24.2728985074
459PhosphorylationPHPPLARTRTLPGTP
CCCCCCCCCCCCCCC		23.5422199227
461PhosphorylationPPLARTRTLPGTPGT
CCCCCCCCCCCCCCC		36.3721712546
465PhosphorylationRTRTLPGTPGTTPPA
CCCCCCCCCCCCCCC		19.3321712546
468PhosphorylationTLPGTPGTTPPAASS
CCCCCCCCCCCCCCC		37.0122199227
469PhosphorylationLPGTPGTTPPAASSS
CCCCCCCCCCCCCCC		32.9422199227
474PhosphorylationGTTPPAASSSRGGEP
CCCCCCCCCCCCCCC		30.8422199227
475PhosphorylationTTPPAASSSRGGEPG
CCCCCCCCCCCCCCC		21.2322199227
476PhosphorylationTPPAASSSRGGEPGP
CCCCCCCCCCCCCCC		32.2322199227
477MethylationPPAASSSRGGEPGPG
CCCCCCCCCCCCCCC		60.11-
491PhosphorylationGPLPRSLSRSNSLPH
CCCCCCCCCCCCCCC		34.6024670416
493PhosphorylationLPRSLSRSNSLPHPA
CCCCCCCCCCCCCCC		27.6530266825
495PhosphorylationRSLSRSNSLPHPAGG
CCCCCCCCCCCCCCC		44.5230266825
516PhosphorylationGVAAEPGTPFSIGRF
CCCCCCCCCCCCCCE		31.6925850435
519PhosphorylationAEPGTPFSIGRFATL
CCCCCCCCCCCEEEE		25.9025850435
525PhosphorylationFSIGRFATLTLQERR
CCCCCEEEEEHHHHH		19.9827050516
530PhosphorylationFATLTLQERRDRGAE
EEEEEHHHHHHHCCH		53.4415302935
538AcetylationRRDRGAEKEHKRYHS
HHHHCCHHHHHHHHC		65.667706941
543PhosphorylationAEKEHKRYHSLGNIS
CHHHHHHHHCCCCCC		10.6830266825
545PhosphorylationKEHKRYHSLGNISRG
HHHHHHHCCCCCCCC		29.1030266825
550PhosphorylationYHSLGNISRGGSGGS
HHCCCCCCCCCCCCC		28.9530108239
551MethylationHSLGNISRGGSGGSG
HCCCCCCCCCCCCCC		50.09-
554PhosphorylationGNISRGGSGGSGSGG
CCCCCCCCCCCCCCC		42.6928985074
557PhosphorylationSRGGSGGSGSGGEKP
CCCCCCCCCCCCCCC		33.0522468782
563UbiquitinationGSGSGGEKPSGPVPR
CCCCCCCCCCCCCCH		48.002190698
571PhosphorylationPSGPVPRSRLDPAKV
CCCCCCHHHCCHHHH		30.9922468782
577UbiquitinationRSRLDPAKVLGTALC
HHHCCHHHHHCEECC		43.30-
644PhosphorylationDEETEAQTGEGSWPR
CHHHCHHCCCCCCCC		44.2228348404
648PhosphorylationEAQTGEGSWPRSPSK
CHHCCCCCCCCCCCC		29.6124719451
652PhosphorylationGEGSWPRSPSKSVVE
CCCCCCCCCCCCCEE		29.4627050516
655UbiquitinationSWPRSPSKSVVEGIS
CCCCCCCCCCEECCC		51.13-
662PhosphorylationKSVVEGISSQPGNSP
CCCEECCCCCCCCCC		33.5030266825
663PhosphorylationSVVEGISSQPGNSPS
CCEECCCCCCCCCCC		38.1730266825
668PhosphorylationISSQPGNSPSGTVV-
CCCCCCCCCCCCCC-		26.7630266825
670PhosphorylationSQPGNSPSGTVV---
CCCCCCCCCCCC---		47.0930266825
672PhosphorylationPGNSPSGTVV-----
CCCCCCCCCC-----		23.5630266825
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 DMWD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DMWD_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 DMWD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALBU_HUMANALBphysical
19615732
CAPZB_HUMANCAPZBphysical
19615732
CATB_HUMANCTSBphysical
19615732
FA7_HUMANF7physical
19615732
FLNA_HUMANFLNAphysical
19615732
GALK1_HUMANGALK1physical
19615732
HBB_HUMANHBBphysical
19615732
HSPB1_HUMANHSPB1physical
19615732
IDH3A_HUMANIDH3Aphysical
19615732
NDUA5_HUMANNDUFA5physical
19615732
NDUS2_HUMANNDUFS2physical
19615732
OAT_HUMANOATphysical
19615732
PFKAL_HUMANPFKLphysical
19615732
PFKAP_HUMANPFKPphysical
19615732
S10A8_HUMANS100A8physical
19615732
SDF2_HUMANSDF2physical
19615732
SPEE_HUMANSRMphysical
19615732
TSNAX_HUMANTSNAXphysical
19615732
SYVC_HUMANVARSphysical
19615732
1433F_HUMANYWHAHphysical
19615732
SUCB2_HUMANSUCLG2physical
19615732
P4HA2_HUMANP4HA2physical
19615732
PSA_HUMANNPEPPSphysical
19615732
NU155_HUMANNUP155physical
19615732
CDC37_HUMANCDC37physical
19615732
PHLP1_HUMANPHLPP1physical
19615732
SCRIB_HUMANSCRIBphysical
19615732
TRM7_HUMANFTSJ1physical
19615732
TRM2A_HUMANTRMT2Aphysical
19615732
DCXR_HUMANDCXRphysical
19615732
SYSM_HUMANSARS2physical
19615732
WDR48_HUMANWDR48physical
19615732
UBP46_HUMANUSP46physical
19615732
UBP12_HUMANUSP12physical
19615732
FEM1B_HUMANFEM1Bphysical
26186194
GAK_HUMANGAKphysical
26186194
WDR6_HUMANWDR6physical
28514442
TKT_HUMANTKTphysical
28514442
GAK_HUMANGAKphysical
28514442
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 DMWD_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASSSPECTROMETRY.

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