Conserved Protein Domain Family
DMAP1

?
pfam05499: DMAP1 
DNA methyltransferase 1-associated protein 1 (DMAP1)
DNA methylation can contribute to transcriptional silencing through several transcriptionally repressive complexes, which include methyl-CpG binding domain proteins (MBDs) and histone deacetylases (HDACs). The chief enzyme that maintains mammalian DNA methylation, DNMT1, can also establish a repressive transcription complex. The non-catalytic amino terminus of DNMT1 binds to HDAC2 and DMAP1 (for DNMT1 associated protein), and can mediate transcriptional repression. DMAP1 has intrinsic transcription repressive activity, and binds to the transcriptional co-repressor TSG101. DMAP1 is targeted to replication foci through interaction with the far N terminus of DNMT1 throughout S phase, whereas HDAC2 joins DNMT1 and DMAP1 only during late S phase, providing a platform for how histones may become deacetylated in heterochromatin following replication.
Statistics
?
PSSM-Id: 398903
Aligned: 24 rows
Threshold Bit Score: 194.811
Created: 22-Mar-2022
Updated: 17-Oct-2022
Structure
?
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
XP_015789967 239 EEQKLLEELRKIEMRKKEREKKTQDLQKLIAAADKN-----------SDGskadtpganknpgpgrpgpgRGRKKTS--- 304
XP_003144340 236 EEEMLIAELKKIEVRKRERERKAQDLQKLITAGERT-----------PAS--------------------PSTSTASvvp 284
CAP28526     224 EEEDLIAEMRRIDQRKKEREKKAHDLQKLINMSEQP----------------------------------ASPSTAGfsg 269
EKC31208     246 EEEHLIAELKKIELRKKEREKKTQDLQKLITAADSN-----------FDA--------------------RRSEKKQ--- 291
ESO12570     239 EEERLVQELKKIEQRKKEREKKAMDLQKLITAADNN-----------SDS--------------------RRSERKI--- 284
XP_008184506 238 EEQMLIQEMRKIEARKRDRDRKTQDLQKLISAVDKQ-----------NDS--------------------RKSLKID--- 283
XP_004926554 242 EEQMLLAELKKIEARKRERERKTQDLQKLISRADSGtitpstptnhnTEPpgtpss---------maanmRRHDRKL--- 309
XP_001997784   3 EEQMLINEMKKIEARKKERERKTQDLQKLISQADQQ-----------NEHaast-------------pstRKYEKKL--- 55 
XP_011139450 233 EEQTLLAELRKIEQRKKERDRKTQDLQKLITAADHQ-----------ADP--------------------RKSERKS--- 278
XP_002115417 299 EEEMLMVELKAIEAQRKERVKGQEGLVRLMTANEKK------------EAkhpp-------------sgrKSAKKKS--- 350
XP_015789967 305 --HLKLNAVGKGSDPSTPNAtnv------leSVGIKFPEIKSSGVSLRSHKMKLPGSVGTKKAKAIEQLLIELNVDlKPM 376
XP_003144340 285 ssNMKKSHKSRLLKTASISNpsisa-syiqdHSNLRFPEFRSAGAHLRSQEMKLPTNIGQKKLKNIETVIEKLKLDlVPF 363
CAP28526     270 aaAGKRNKQFRTKAGSISMApgplfnpldisVTALRFSEFKSSGVHMRGQEMKLPTNIGQKKLKNIEVVLEKCKMEmNPV 349
EKC31208     292 --TKKKIHTPHQKINPTVSTp---------ePSGIKFADFKTSGVSLRSQRMKLPASIGQKKLKAIEQVLEELGIEySPI 360
ESO12570     285 ---SKKIVPYKTRESNVAPE-----------STSIKFPDFKQSGVYLRSQKMKLPISLGQKKTKAIEQMLEEFAIEpNPV 350
XP_008184506 284 ---KKTTHHRKRVTVPVRPTrvdp---nnfeATTIKFPDIKNSGVSTRSQRMKIPANVSQKKVKNVEQALESLKIKlNPI 357
XP_004926554 310 --HKKKITTQQRPMRAVENVtv--------eWSGIKFPEARGTGVWLRSQRMKLPPGVGQRKTKAIEQELRLMNIDiAPT 379
XP_001997784  56 --HKKKV-HHQPRPSKVDSVvnai----eigSSGIKFADLRGSGVSLRSQKMKLPANIGQRKVKALEQAIQEFKVDpGPP 128
XP_011139450 279 ---SKKNSNSRNRPNKTDTSha-------veSTGIKFPDFKNSGVTLRSQRIKLPSSLGQKKMKGIEQMLNELRLElNPP 348
XP_002115417 351 --LKKKGDHNQSSTD----------------TAIIKFPE-KSSGVWLRSSRMKLPLSIGQKKTKAVEQFLSEYDLPpAPM 411
XP_015789967 377 PTEEICQHFNELRSDMVLLYELKMALASSEFELQTLKHQFEAL 419
XP_003144340 364 GVADIVKGYNEFRARIVLLQELKHSLHSAEFELESLRTRYNAL 406
CAP28526     350 ASESIMKVYNDFRSQIMLAQELKSAMQTAEFELESLRTKLQeq 392
EKC31208     361 PTEDTVTHFNELRQDIVLLYELKIALATCDYELESLKHRFETL 403
ESO12570     351 PTQEIVNSFNDLRQDMVLLYELKIALANSEYELQTLRHRYETL 393
XP_008184506 358 PTEDICQNYNDLRNEIVLLNELKAACSSSDFELQTLKHQYETL 400
XP_004926554 380 PTEPICKHFNELRSDLALSIDLKNALASCEFELQALRHQYEAL 422
XP_001997784 129 PTEDICTSFNELRSDMVLLCELRTALSTCIYEMESLKHQYEAA 171
XP_011139450 349 PTEQICQQFNELRSDIVLHYELRSALSTCDYELQSLRHQYEAL 391
XP_002115417 412 PTEEICQAFNDLREKILLLLNLRQLADNCEYEAQTLKHKLEAI 454
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap