DNM3A_HUMAN - dbPTM
DNM3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNM3A_HUMAN
UniProt AC Q9Y6K1
Protein Name DNA (cytosine-5)-methyltransferase 3A
Gene Name DNMT3A
Organism Homo sapiens (Human).
Sequence Length 912
Subcellular Localization Nucleus . Cytoplasm . Accumulates in the major satellite repeats at pericentric heterochromatin..
Protein Description Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity..
Protein Sequence MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
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
6Phosphorylation--MPAMPSSGPGDTS
--CCCCCCCCCCCCC		34.5423401153
7Phosphorylation-MPAMPSSGPGDTSS
-CCCCCCCCCCCCCC		43.0423401153
12PhosphorylationPSSGPGDTSSSAAER
CCCCCCCCCCCHHHH		36.1023401153
13PhosphorylationSSGPGDTSSSAAERE
CCCCCCCCCCHHHHH		27.3423401153
14PhosphorylationSGPGDTSSSAAEREE
CCCCCCCCCHHHHHH		26.5328060719
15PhosphorylationGPGDTSSSAAEREED
CCCCCCCCHHHHHHH		31.1327732954
23MethylationAAEREEDRKDGEEQE
HHHHHHHHCCCCCCC		42.09-
62PhosphorylationRKHPPVESGDTPKDP
CCCCCCCCCCCCCCC		42.0528555341
65PhosphorylationPPVESGDTPKDPAVI
CCCCCCCCCCCCHHH		35.4525159151
75PhosphorylationDPAVISKSPSMAQDS
CCHHHCCCHHHHCCC		18.5430266825
77PhosphorylationAVISKSPSMAQDSGA
HHHCCCHHHHCCCCC		33.5630266825
82PhosphorylationSPSMAQDSGASELLP
CHHHHCCCCCCCCCC		24.9525850435
85PhosphorylationMAQDSGASELLPNGD
HHCCCCCCCCCCCCC		32.1025850435
97PhosphorylationNGDLEKRSEPQPEEG
CCCHHHCCCCCCCCC		65.7723403867
102PhosphorylationKRSEPQPEEGSPAGG
HCCCCCCCCCCCCCC		70.5118669648
105PhosphorylationEPQPEEGSPAGGQKG
CCCCCCCCCCCCCCC		18.1729255136
124PhosphorylationEGEGAAETLPEASRA
CCCCHHHHCHHHHHH		42.7726074081
138PhosphorylationAVENGCCTPKEGRGA
HHHCCCCCCCCCCCC		41.2825850435
144 (in isoform 2)Ubiquitination-46.9321890473
156PhosphorylationAGKEQKETNIESMKM
CCHHHHHHCHHHEEE		48.83-
162SumoylationETNIESMKMEGSRGR
HHCHHHEEEECCCCC		42.9828112733
171MethylationEGSRGRLRGGLGWES
ECCCCCCCCCCCCCH		35.45-
178PhosphorylationRGGLGWESSLRQRPM
CCCCCCCHHHCCCCC		28.3228555341
179PhosphorylationGGLGWESSLRQRPMP
CCCCCCHHHCCCCCC		18.96-
199PhosphorylationAGDPYYISKRKRDEW
CCCCEEECCCCHHHH		15.4127251275
200UbiquitinationGDPYYISKRKRDEWL
CCCEEECCCCHHHHH		52.9921890473
200 (in isoform 1)Ubiquitination-52.9921890473
236PhosphorylationENQGPGESQKVEEAS
HCCCCCCCCCCCCCC		41.0121406692
243PhosphorylationSQKVEEASPPAVQQP
CCCCCCCCCCCCCCC		34.3925159151
251PhosphorylationPPAVQQPTDPASPTV
CCCCCCCCCCCCCCC		50.7225159151
255PhosphorylationQQPTDPASPTVATTP
CCCCCCCCCCCCCCC		26.8823401153
257PhosphorylationPTDPASPTVATTPEP
CCCCCCCCCCCCCCC		21.9325159151
260PhosphorylationPASPTVATTPEPVGS
CCCCCCCCCCCCCCC		38.2525159151
261PhosphorylationASPTVATTPEPVGSD
CCCCCCCCCCCCCCC		18.8625159151
267PhosphorylationTTPEPVGSDAGDKNA
CCCCCCCCCCCCCCC		25.2330631047
275PhosphorylationDAGDKNATKAGDDEP
CCCCCCCCCCCCCCC		30.7125841592
276UbiquitinationAGDKNATKAGDDEPE
CCCCCCCCCCCCCCC		48.22-
299UbiquitinationIGELVWGKLRGFSWW
HHHHHHHCCCCCCCC		21.21-
367 (in isoform 1)Ubiquitination-22.9621890473
367UbiquitinationNKQPMYRKAIYEVLQ
CCCCHHHHHHHHHHH		22.9621890473
377PhosphorylationYEVLQVASSRAGKLF
HHHHHHHHHHCCCEE		22.85-
382UbiquitinationVASSRAGKLFPVCHD
HHHHHCCCEECCCCC		46.07-
390PhosphorylationLFPVCHDSDESDTAK
EECCCCCCCCCCCCH		21.4421406692
393PhosphorylationVCHDSDESDTAKAVE
CCCCCCCCCCCHHEE		45.3021406692
395PhosphorylationHDSDESDTAKAVEVQ
CCCCCCCCCHHEEEC		39.0621406692
420UbiquitinationGFQPSGPKGLEPPEE
CCCCCCCCCCCCCHH		78.60-
437PhosphorylationNPYKEVYTDMWVEPE
CCCCEEECCCCCCHH		25.2627642862
448PhosphorylationVEPEAAAYAPPPPAK
CCHHHHHCCCCCCCC		18.2127642862
468SumoylationTAEKPKVKEIIDERT
CCCCCCHHHHHCHHH		49.69-
468SumoylationTAEKPKVKEIIDERT
CCCCCCHHHHHCHHH		49.69-
638PhosphorylationRKPIRVLSLFDGIAT
CCCCEEEECCCCCHH		24.92-
645PhosphorylationSLFDGIATGLLVLKD
ECCCCCHHHHHHHHH		26.83-
721UbiquitinationSIVNPARKGLYEGTG
CCCCCCCCCCCCCCC		56.21-
783UbiquitinationNPVMIDAKEVSAAHR
CCEEEEHHHHHHHHH		55.70-
812UbiquitinationLASTVNDKLELQECL
CHHHHCHHHHHHHHH		38.36-
839PhosphorylationTITTRSNSIKQGKDQ
EEECCCCCHHCCCCC		32.2024719451
844UbiquitinationSNSIKQGKDQHFPVF
CCCHHCCCCCCCCEE		52.28-
882MethylationTDVSNMSRLARQRLL
CCHHHHHHHHHHHHH		22.92-
894PhosphorylationRLLGRSWSVPVIRHL
HHHCCCCHHHHHHHH		20.1427251275
906UbiquitinationRHLFAPLKEYFACV-
HHHHHHHHHHHCCC-		49.67-
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
255SPhosphorylationKinaseERK2P28482
PSP
390SPhosphorylationKinaseCK2A1P68400
PSP
393SPhosphorylationKinaseCK2A1P68400
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNM3A_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 DNM3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
14752048
MYC_HUMANMYCphysical
15616584
ZBT17_HUMANZBTB17physical
15616584
PIAS1_HUMANPIAS1physical
14752048
PIAS2_HUMANPIAS2physical
14752048
DNM3B_HUMANDNMT3Bphysical
14752048
DNM3B_HUMANDNMT3Bphysical
12867029
CBX5_HUMANCBX5physical
12867029
SUV91_HUMANSUV39H1physical
12711675
CBX1_HUMANCBX1physical
12711675
ZBT18_MOUSEZbtb18physical
11350943
ZBT18_HUMANZBTB18physical
11350943
HDAC1_HUMANHDAC1physical
11350943
RB_HUMANRB1physical
11350943
DNM3B_HUMANDNMT3Bphysical
12145218
TDG_MOUSETdgphysical
17175537
H31_HUMANHIST1H3Aphysical
19834512
UHRF1_HUMANUHRF1physical
19798101
EZH2_HUMANEZH2physical
16357870
CBX4_HUMANCBX4physical
17439403
UBP7_HUMANUSP7physical
21745816
UHRF1_HUMANUHRF1physical
21745816
UHRF1_HUMANUHRF1physical
22064703
UHRF2_HUMANUHRF2physical
22064703
SALL3_HUMANSALL3physical
19139273
F8I2_HUMANF8A1physical
19139273
MYC_HUMANMYCphysical
19786833
IRF9_HUMANIRF9physical
19786833
AP2A_HUMANTFAP2Aphysical
19786833
HDAC1_HUMANHDAC1physical
19786833
MPP8_HUMANMPHOSPH8physical
22086334
DNM3L_HUMANDNMT3Lphysical
15105426
NRIP1_HUMANNRIP1physical
17972916
RPAB3_HUMANPOLR2Hphysical
21406692
RPB3_HUMANPOLR2Cphysical
21406692
RPB1_HUMANPOLR2Aphysical
21406692
RTF1_HUMANRTF1physical
21406692
LEO1_HUMANLEO1physical
21406692
CTR9_HUMANCTR9physical
21406692
PAF1_HUMANPAF1physical
21406692
CDC73_HUMANCDC73physical
21406692
DNMT1_HUMANDNMT1physical
21406692
TEBP_HUMANPTGES3physical
8772199
SP100_HUMANSP100physical
25416956
TCL1A_HUMANTCL1Aphysical
25416956
DNM3B_HUMANDNMT3Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615879Tatton-Brown-Rahman syndrome (TBRS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNM3A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-105, AND MASSSPECTROMETRY.
"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-105, AND MASSSPECTROMETRY.
"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-105, AND MASSSPECTROMETRY.

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