DMAP1_HUMAN - dbPTM
DMAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DMAP1_HUMAN
UniProt AC Q9NPF5
Protein Name DNA methyltransferase 1-associated protein 1
Gene Name DMAP1
Organism Homo sapiens (Human).
Sequence Length 467
Subcellular Localization Nucleus. Cytoplasm. Targeted to replication foci throughout S phase by DNMT1.
Protein Description Involved in transcription repression and activation. Its interaction with HDAC2 may provide a mechanism for histone deacetylation in heterochromatin following replication of DNA at late firing origins. Can also repress transcription independently of histone deacetylase activity. May specifically potentiate DAXX-mediated repression of glucocorticoid receptor-dependent transcription. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Participates in the nuclear localization of URI1 and increases its transcriptional corepressor activity..
Protein Sequence MATGADVRDILELGGPEGDAASGTISKKDIINPDKKKSKKSSETLTFKRPEGMHREVYALLYSDKKDAPPLLPSDTGQGYRTVKAKLGSKKVRPWKWMPFTNPARKDGAMFFHWRRAAEEGKDYPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQFKKRSVEDLKERYYHICAKLANVRAVPGTDLKIPVFDAGHERRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPETAGIKFPDFKSAGVTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALARAGVLGGPATPASGPGPASAEPAVTEPGLGPDPKDTIIDVVGAPLTPNSRKRRESASSSSSVKKAKKP
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
22PhosphorylationGPEGDAASGTISKKD
CCCCCCCCCCCCHHH		37.8820068231
24PhosphorylationEGDAASGTISKKDII
CCCCCCCCCCHHHCC		21.4124173317
26PhosphorylationDAASGTISKKDIINP
CCCCCCCCHHHCCCC		33.2320068231
27UbiquitinationAASGTISKKDIINPD
CCCCCCCHHHCCCCC		51.0929967540
27SumoylationAASGTISKKDIINPD
CCCCCCCHHHCCCCC		51.0928112733
27AcetylationAASGTISKKDIINPD
CCCCCCCHHHCCCCC		51.0925953088
28AcetylationASGTISKKDIINPDK
CCCCCCHHHCCCCCC		47.5869543
35AcetylationKDIINPDKKKSKKSS
HHCCCCCCCCCCCCC		64.4619608861
36AcetylationDIINPDKKKSKKSSE
HCCCCCCCCCCCCCC		70.4369547
41PhosphorylationDKKKSKKSSETLTFK
CCCCCCCCCCCEEEE		36.8230266825
42PhosphorylationKKKSKKSSETLTFKR
CCCCCCCCCCEEEEC		43.4030266825
44PhosphorylationKSKKSSETLTFKRPE
CCCCCCCCEEEECCC		32.8030108239
46PhosphorylationKKSSETLTFKRPEGM
CCCCCCEEEECCCCC		34.2330108239
48AcetylationSSETLTFKRPEGMHR
CCCCEEEECCCCCHH		62.9025953088
58PhosphorylationEGMHREVYALLYSDK
CCCHHHHHHHHHCCC		6.1829978859
62PhosphorylationREVYALLYSDKKDAP
HHHHHHHHCCCCCCC		18.7029083192
63PhosphorylationEVYALLYSDKKDAPP
HHHHHHHCCCCCCCC		42.8121815630
65UbiquitinationYALLYSDKKDAPPLL
HHHHHCCCCCCCCCC		46.76-
66UbiquitinationALLYSDKKDAPPLLP
HHHHCCCCCCCCCCC		65.2029967540
80PhosphorylationPSDTGQGYRTVKAKL
CCCCCCCCCEEEEEC		8.6728555341
106UbiquitinationPFTNPARKDGAMFFH
CCCCCCCCCCCEEEE		63.72-
122UbiquitinationRRAAEEGKDYPFARF
HHHHHCCCCCCCCCC		58.32-
122AcetylationRRAAEEGKDYPFARF
HHHHHCCCCCCCCCC		58.3226051181
131UbiquitinationYPFARFNKTVQVPVY
CCCCCCCCEEEEECC		47.5729967540
192UbiquitinationKRSVEDLKERYYHIC
HCCHHHHHHHHHHHH		53.09-
201AcetylationRYYHICAKLANVRAV
HHHHHHHHHHCCCCC		43.6625953088
201UbiquitinationRYYHICAKLANVRAV
HHHHHHHHHHCCCCC		43.6629967540
214UbiquitinationAVPGTDLKIPVFDAG
CCCCCCCCCCCCCCC		48.0129967540
214SumoylationAVPGTDLKIPVFDAG
CCCCCCCCCCCCCCC		48.0128112733
222UbiquitinationIPVFDAGHERRRKEQ
CCCCCCCCHHHHHHH		27.4124816145
234PhosphorylationKEQLERLYNRTPEQV
HHHHHHHHHCCHHHH		14.6022817900
237PhosphorylationLERLYNRTPEQVAEE
HHHHHHCCHHHHHHH		27.7824247654
246PhosphorylationEQVAEEEYLLQELRK
HHHHHHHHHHHHHHH		18.9122817900
270UbiquitinationKRSQDLQKLITAADT
HHHHHHHHHHHHHHH		49.5124816145
273PhosphorylationQDLQKLITAADTTAE
HHHHHHHHHHHHHHH		26.6520068231
277PhosphorylationKLITAADTTAEQRRT
HHHHHHHHHHHHHHH		24.1521406692
278PhosphorylationLITAADTTAEQRRTE
HHHHHHHHHHHHHHH		28.8321406692
284PhosphorylationTTAEQRRTERKAPKK
HHHHHHHHHHCCCCC		42.1828555341
297AcetylationKKKLPQKKEAEKPAV
CCCCCCCHHCCCCCC		57.847826205
301AcetylationPQKKEAEKPAVPETA
CCCHHCCCCCCCCCC		45.3723749302
301UbiquitinationPQKKEAEKPAVPETA
CCCHHCCCCCCCCCC		45.3729967540
311AcetylationVPETAGIKFPDFKSA
CCCCCCCCCCCCHHC		50.3426051181
311UbiquitinationVPETAGIKFPDFKSA
CCCCCCCCCCCCHHC		50.3429967540
316MethylationGIKFPDFKSAGVTLR
CCCCCCCHHCCCCHH		46.94-
321PhosphorylationDFKSAGVTLRSQRMK
CCHHCCCCHHHCCCC		18.6124719451
336AcetylationLPSSVGQKKIKALEQ
CCCHHHHHHHHHHHH		51.0025953088
336UbiquitinationLPSSVGQKKIKALEQ
CCCHHHHHHHHHHHH		51.0029967540
353PhosphorylationLELGVELSPTPTEEL
HHHCCCCCCCCHHHH		17.14-
355PhosphorylationLGVELSPTPTEELVH
HCCCCCCCCHHHHHH		39.19-
357PhosphorylationVELSPTPTEELVHMF
CCCCCCCHHHHHHHH		44.57-
409PhosphorylationGVLGGPATPASGPGP
CCCCCCCCCCCCCCC		23.6327273156
412PhosphorylationGGPATPASGPGPASA
CCCCCCCCCCCCCCC		46.8829255136
418PhosphorylationASGPGPASAEPAVTE
CCCCCCCCCCCCCCC		35.9829255136
424PhosphorylationASAEPAVTEPGLGPD
CCCCCCCCCCCCCCC		38.2729978859
424O-linked_GlycosylationASAEPAVTEPGLGPD
CCCCCCCCCCCCCCC		38.2721740066
435PhosphorylationLGPDPKDTIIDVVGA
CCCCCCCCEEECCCC		26.4223927012
445PhosphorylationDVVGAPLTPNSRKRR
ECCCCCCCCCHHHHH		21.2629255136
448PhosphorylationGAPLTPNSRKRRESA
CCCCCCCHHHHHHHC		40.1429255136
450AcetylationPLTPNSRKRRESASS
CCCCCHHHHHHHCCC		56.4830588201
454PhosphorylationNSRKRRESASSSSSV
CHHHHHHHCCCCHHH		31.4725159151
456PhosphorylationRKRRESASSSSSVKK
HHHHHHCCCCHHHHC		39.7827794612
457PhosphorylationKRRESASSSSSVKKA
HHHHHCCCCHHHHCC		33.6830576142
458PhosphorylationRRESASSSSSVKKAK
HHHHCCCCHHHHCCC		24.9230576142
459PhosphorylationRESASSSSSVKKAKK
HHHCCCCHHHHCCCC		40.8930576142
460PhosphorylationESASSSSSVKKAKKP
HHCCCCHHHHCCCCC		39.6530576142
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
246YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DMAP1_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 DMAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNMT1_HUMANDNMT1physical
10888872
TS101_HUMANTSG101physical
10888872
PCNA_HUMANPCNAphysical
19845771
CAF1A_HUMANCHAF1Aphysical
19845771
H2AX_HUMANH2AFXphysical
19845771
RUVB1_HUMANRUVBL1physical
19845771
HDAC1_HUMANHDAC1physical
17371848
MAT1_HUMANMNAT1physical
17371848
TRRAP_HUMANTRRAPphysical
20946988
EP400_HUMANEP400physical
20946988
SRCAP_HUMANSRCAPphysical
20946988
BRD8_HUMANBRD8physical
20946988
EPC2_HUMANEPC2physical
20946988
EPC1_HUMANEPC1physical
20946988
KAT5_HUMANKAT5physical
20946988
VPS72_HUMANVPS72physical
20946988
ING3_HUMANING3physical
20946988
ACTB_HUMANACTBphysical
20946988
ACTG_HUMANACTG1physical
20946988
MYC_HUMANMYCphysical
20946988
TRRAP_HUMANTRRAPphysical
14966270
KAT5_HUMANKAT5physical
14966270
EPC1_HUMANEPC1physical
14966270
RUVB1_HUMANRUVBL1physical
14966270
ACL6A_HUMANACTL6Aphysical
14966270
MO4L1_HUMANMORF4L1physical
14966270
YETS4_HUMANYEATS4physical
14966270
RUVB2_HUMANRUVBL2physical
14966270
BRD8_HUMANBRD8physical
14966270
SRCAP_HUMANSRCAPphysical
14966270
ACTS_HUMANACTA1physical
14966270
DAXX_HUMANDAXXphysical
14978102
TS101_HUMANTSG101physical
15033475
RUVB2_HUMANRUVBL2physical
22939629
RUVB1_HUMANRUVBL1physical
22939629
VPS72_HUMANVPS72physical
22939629
SRCAP_HUMANSRCAPphysical
22939629
BRD3_HUMANBRD3physical
26344197
RUVB2_HUMANRUVBL2physical
26344197
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 DMAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445 AND SER-448, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, 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 THR-445, AND MASSSPECTROMETRY.

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