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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9 (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi359 – 3591ZincBy similarity
Metal bindingi362 – 3621ZincBy similarity
Metal bindingi420 – 4201ZincBy similarity
Metal bindingi424 – 4241ZincBy similarity
Sitei515 – 5151Important for activityBy similarity
Active sitei1231 – 12311PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri650 – 69647CXXC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. DNA (cytosine-5-)-methyltransferase activity Source: RGD
  3. DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: RGD
  4. double-stranded DNA binding Source: RGD
  5. estrogen receptor binding Source: RGD
  6. histone deacetylase binding Source: RGD
  7. methyl-CpG binding Source: RGD
  8. protein domain specific binding Source: RGD
  9. S-adenosylmethionine-dependent methyltransferase activity Source: RGD
  10. unmethylated CpG binding Source: RGD
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. aging Source: RGD
  2. brain development Source: RGD
  3. cellular response to lead ion Source: RGD
  4. cellular response to nerve growth factor stimulus Source: RGD
  5. cellular response to platelet-derived growth factor stimulus Source: RGD
  6. cellular response to transforming growth factor beta stimulus Source: RGD
  7. chromatin modification Source: UniProtKB-KW
  8. DNA hypermethylation Source: RGD
  9. DNA methylation Source: RGD
  10. DNA methylation on cytosine Source: RGD
  11. DNA methylation on cytosine within a CG sequence Source: RGD
  12. maintenance of DNA methylation Source: RGD
  13. neuron differentiation Source: RGD
  14. regulation of transcription, DNA-templated Source: UniProtKB-KW
  15. response to activity Source: RGD
  16. response to antidepressant Source: RGD
  17. response to drug Source: RGD
  18. response to estradiol Source: RGD
  19. response to ethanol Source: RGD
  20. response to heat Source: RGD
  21. response to ionizing radiation Source: RGD
  22. response to lead ion Source: RGD
  23. response to lipopolysaccharide Source: RGD
  24. response to nutrient levels Source: RGD
  25. response to organic substance Source: RGD
  26. response to testosterone Source: RGD
  27. response to toxic substance Source: RGD
  28. response to vitamin A Source: RGD
  29. S-adenosylhomocysteine metabolic process Source: RGD
  30. S-adenosylmethioninamine metabolic process Source: RGD
  31. S-adenosylmethionine metabolic process Source: RGD
  32. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8581.

Protein family/group databases

REBASEi3019. M.RnoDnmt1.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
Short name:
Dnmt1
Alternative name(s):
DNA MTase RnoIP
Short name:
M.RnoIP
DNA methyltransferase I
MCMT
Gene namesi
Name:Dnmt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620979. Dnmt1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. neuronal cell body Source: RGD
  3. nucleus Source: RGD
  4. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16221622DNA (cytosine-5)-methyltransferase 1PRO_0000088036Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6,N6-dimethyllysine; by EHMT2By similarity
Modified residuei139 – 1391N6-methyllysine; by SETD7By similarity
Modified residuei140 – 1401Phosphoserine; by PKB/AKT1By similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei169 – 1691N6-acetyllysineBy similarity
Modified residuei372 – 3721N6-acetyllysineBy similarity
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei515 – 5151PhosphoserineBy similarity
Modified residuei718 – 7181PhosphoserineBy similarity
Modified residuei736 – 7361PhosphoserineBy similarity
Modified residuei753 – 7531N6-acetyllysineBy similarity
Modified residuei895 – 8951N6-acetyllysineBy similarity
Modified residuei961 – 9611N6-acetyllysineBy similarity
Modified residuei980 – 9801N6-acetyllysineBy similarity
Modified residuei1116 – 11161N6-acetyllysineBy similarity
Modified residuei1118 – 11181N6-acetyllysineBy similarity
Modified residuei1120 – 11201N6-acetyllysineBy similarity
Modified residuei1122 – 11221N6-acetyllysineBy similarity
Modified residuei1124 – 11241N6-acetyllysineBy similarity
Modified residuei1126 – 11261N6-acetyllysineBy similarity
Modified residuei1354 – 13541N6-acetyllysineBy similarity

Post-translational modificationi

Sumoylated.By similarity
Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1116 and Lys-1354 by SIRT1 increases methyltransferase activity (By similarity).By similarity
Phosphorylation of Ser-151 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-140 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability (By similarity).By similarity
Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal degradation.By similarity
Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9Z330.
PRIDEiQ9Z330.

PTM databases

PhosphoSiteiQ9Z330.

Expressioni

Tissue specificityi

Isoforms 0 and 8 are highly expressed in placenta, brain, lung, spleen, kidney, heart, and at much lower levels in liver. Isoform 1 is expressed in cerebellum, isoform 2 in muscle and testis, isoform 3 in lung, isoform 4 in spleen and brain, and isoform 5 in brain.

Gene expression databases

GenevestigatoriQ9Z330.

Interactioni

Subunit structurei

Homodimer. Interacts with HDAC1 and with PCNA. Forms a complex with DMAP1 and HDAC2, with direct interaction. Forms also a stable complex with E2F1, BB1 and HDAC1. Binds MBD2 and MBD3. Component of complexes containing SUV39H1. Interacts with DNMT3A and DNMT3B (By similarity). Binds annexin V (Potential). Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9 and BAZ2A/TIP5 (By similarity). Binds to CSNK1D. Interacts with BAZ2A/TIP5. Binds to CSNK1D. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination (By similarity).By similarityCurated

Protein-protein interaction databases

IntActiQ9Z330. 2 interactions.
STRINGi10116.ENSRNOP00000063029.

Structurei

3D structure databases

ProteinModelPortaliQ9Z330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10588DMAP-interactionAdd
BLAST
Domaini759 – 884126BAH 1PROSITE-ProRule annotationAdd
BLAST
Domaini977 – 1105129BAH 2PROSITE-ProRule annotationAdd
BLAST
Repeati1114 – 111521
Repeati1116 – 111722
Repeati1118 – 111923
Repeati1120 – 112124
Repeati1122 – 112325
Repeati1124 – 112526
Repeati1126 – 112727; approximate
Domaini1144 – 1603460SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni1 – 145145Interaction with DNMT3ABy similarityAdd
BLAST
Regioni146 – 21368Interaction with DNMT3BBy similarityAdd
BLAST
Regioni304 – 610307Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni327 – 556230DNA replication foci-targeting sequenceAdd
BLAST
Regioni697 – 75862Autoinhibitory linkerAdd
BLAST
Regioni1114 – 1127147 X 2 AA tandem repeats of K-GAdd
BLAST
Regioni1126 – 1622497Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
BLAST
Regioni1144 – 1622479CatalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi173 – 20028Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi149 – 1524Poly-Ser
Compositional biasi269 – 2746Poly-Asp
Compositional biasi726 – 7294Poly-Lys

Domaini

The N-terminal part is required for homodimerization and acts as a regulatory domain.
The CXXC-type zinc finger specifically binds to unmethylated CpG dinucleotides, positioning the autoinhibitory linker between the DNA and the active site, thus providing a mechanism to ensure that only hemimethylated CpG dinucleotides undergo methylation.By similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 2 BAH domains.PROSITE-ProRule annotation
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 DMAP-interaction domain.Curated
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri650 – 69647CXXC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0270.
HOGENOMiHOG000082497.
HOVERGENiHBG051384.
InParanoidiQ9Z330.
PhylomeDBiQ9Z330.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNMT1.
IPR029063. SAM-dependent_MTases.
IPR002857. Znf_CXXC.
[Graphical view]
PfamiPF01426. BAH. 2 hits.
PF06464. DMAP_binding. 1 hit.
PF12047. DNMT1-RFD. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF037404. DNMT1. 1 hit.
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 2 hits.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51038. BAH. 2 hits.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
PS51058. ZF_CXXC. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9Z330-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVKEKLNLLH
60 70 80 90 100
EFLQTEIKSQ LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT
110 120 130 140 150
QKANGCPANG SRPTWKAEMA DSNRSPRSRP KPRGPRRSKS DSETMIEASS
160 170 180 190 200
SSVATRRTTR QTTITSHFKG PAKRKPKEDS EKGNANESAA EERDQDKKRR
210 220 230 240 250
VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR PRRQTRELAS
260 270 280 290 300
RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV
310 320 330 340 350
EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA
360 370 380 390 400
IPKLNPPQCP ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS
410 420 430 440 450
WFETYDSSPM HKFTFFSVYC SRGHLCPVDT GLIEKNVELY FSGVAKAIHE
460 470 480 490 500
ENPSVEGGVN GKNLGPINQW WISGFDGGEK ALIGFSTAFA EYFLMEPSPE
510 520 530 540 550
YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT VPPSAINVNR
560 570 580 590 600
FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ
610 620 630 640 650
RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN
660 670 680 690 700
TMKRRRCGVC EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV
710 720 730 740 750
KEADEDEEAD DDIPELPSPK KLHQGKKKKQ NKDRISWLGE PVKIEENRTY
760 770 780 790 800
YWKVSIDEET LEVGDCVSVI PDDPSKPLYL ARVTALWEDK NGQMFHAHWF
810 820 830 840 850
CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR GPSPNWAMEG
860 870 880 890 900
GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC
910 920 930 940 950
IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF
960 970 980 990 1000
TFNIKMASPM KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR
1010 1020 1030 1040 1050
IKEIYCGKKK GGKVNEADIK IRLYKFYRPE NTHKSIQATY HADINLLYWS
1060 1070 1080 1090 1100
DEEAVVDFSD VQGRCTVEYG EDLLESIQDY SQGGPDRFYF LEAYNSKTKS
1110 1120 1130 1140 1150
FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK LPKLRTLDVF
1160 1170 1180 1190 1200
SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL
1210 1220 1230 1240 1250
KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN
1260 1270 1280 1290 1300
SLVVSFLSYC DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT
1310 1320 1330 1340 1350
FGVLQAGQYG VAQTRRRAII LAAAPGEKLP LFPEPLHVFA PRACQLSVVV
1360 1370 1380 1390 1400
DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP EIQNGASAPE ISYKWRATVL
1410 1420 1430 1440 1450
VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD WRDLPNIQVR
1460 1470 1480 1490 1500
LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI
1510 1520 1530 1540 1550
PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR
1560 1570 1580 1590 1600
VVSVRECARS QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL
1610 1620
LASAQESASA AVKGKEETTT ED
Length:1,622
Mass (Da):182,774
Last modified:February 21, 2002 - v2
Checksum:iFCFA4AAA69E234BA
GO
Isoform 2 (identifier: Q9Z330-2) [UniParc]FASTAAdd to Basket

Also known as: SF1

The sequence of this isoform differs from the canonical sequence as follows:
     1323-1403: Missing.

Show »
Length:1,541
Mass (Da):173,853
Checksum:i9F1B86D1D13B45AB
GO
Isoform 3 (identifier: Q9Z330-3) [UniParc]FASTAAdd to Basket

Also known as: SF2

The sequence of this isoform differs from the canonical sequence as follows:
     1252-1482: Missing.

Show »
Length:1,391
Mass (Da):156,880
Checksum:i7F92F4E446BBD358
GO
Isoform 4 (identifier: Q9Z330-4) [UniParc]FASTAAdd to Basket

Also known as: SF3

The sequence of this isoform differs from the canonical sequence as follows:
     1226-1477: Missing.

Show »
Length:1,370
Mass (Da):154,529
Checksum:i9137E151ED3EED0B
GO
Isoform 5 (identifier: Q9Z330-5) [UniParc]FASTAAdd to Basket

Also known as: SF4

The sequence of this isoform differs from the canonical sequence as follows:
     1218-1430: QKGDVEMLCG...VHERAGGCRM → VC

Show »
Length:1,411
Mass (Da):159,119
Checksum:i961F53E307E2447E
GO
Isoform 6 (identifier: Q9Z330-6) [UniParc]FASTAAdd to Basket

Also known as: SF5

The sequence of this isoform differs from the canonical sequence as follows:
     1202-1410: Missing.

Show »
Length:1,413
Mass (Da):159,421
Checksum:iAE3F0037058D8167
GO
Isoform 7 (identifier: Q9Z330-7) [UniParc]FASTAAdd to Basket

Also known as: SF6

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1481: Missing.

Show »
Length:1,399
Mass (Da):157,713
Checksum:i28C6F61C3085A7ED
GO
Isoform 8 (identifier: Q9Z330-8) [UniParc]FASTAAdd to Basket

Also known as: SF7

The sequence of this isoform differs from the canonical sequence as follows:
     1216-1504: Missing.

Show »
Length:1,333
Mass (Da):150,479
Checksum:iD8713CC5B748BFC2
GO
Isoform 9 (identifier: Q9Z330-9) [UniParc]FASTAAdd to Basket

Also known as: short

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Show »
Length:1,504
Mass (Da):169,645
Checksum:iC880386135929522
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 259AGSLPDHVR → RQARPRPCP in BAA20854. (PubMed:8667030)Curated
Sequence conflicti189 – 1891A → V in BAA20854. (PubMed:8667030)Curated
Sequence conflicti1276 – 12761F → S in BAA37118. (PubMed:9878564)Curated
Sequence conflicti1300 – 13001T → I in AAD28102. (PubMed:9722504)Curated
Sequence conflicti1372 – 13721M → V in BAA37118. (PubMed:9878564)Curated
Sequence conflicti1394 – 142835KWRAT…RAGGC → NGEPQSWFQRQLRGSHYQPI LRDHICKDMSALVAA in BAA37118. (PubMed:9878564)CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 9. CuratedVSP_005620Add
BLAST
Alternative sequencei1202 – 1410209Missing in isoform 6. CuratedVSP_005622Add
BLAST
Alternative sequencei1216 – 1504289Missing in isoform 8. CuratedVSP_005623Add
BLAST
Alternative sequencei1218 – 1430213QKGDV…GGCRM → VC in isoform 5. CuratedVSP_005621Add
BLAST
Alternative sequencei1226 – 1477252Missing in isoform 4. CuratedVSP_005624Add
BLAST
Alternative sequencei1252 – 1482231Missing in isoform 3. CuratedVSP_005625Add
BLAST
Alternative sequencei1259 – 1481223Missing in isoform 7. CuratedVSP_005626Add
BLAST
Alternative sequencei1323 – 140381Missing in isoform 2. CuratedVSP_005627Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012214 mRNA. Translation: BAA37118.1.
AF116344 mRNA. Translation: AAD32541.1.
AF116345 Genomic DNA. Translation: AAD32542.1.
D64060 mRNA. Translation: BAA20854.1.
AH007612 Genomic DNA. Translation: AAD28102.1.
PIRiJE0378.
UniGeneiRn.6955.

Genome annotation databases

UCSCiRGD:620979. rat. [Q9Z330-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012214 mRNA. Translation: BAA37118.1.
AF116344 mRNA. Translation: AAD32541.1.
AF116345 Genomic DNA. Translation: AAD32542.1.
D64060 mRNA. Translation: BAA20854.1.
AH007612 Genomic DNA. Translation: AAD28102.1.
PIRiJE0378.
UniGeneiRn.6955.

3D structure databases

ProteinModelPortaliQ9Z330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z330. 2 interactions.
STRINGi10116.ENSRNOP00000063029.

Protein family/group databases

REBASEi3019. M.RnoDnmt1.

PTM databases

PhosphoSiteiQ9Z330.

Proteomic databases

PaxDbiQ9Z330.
PRIDEiQ9Z330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620979. rat. [Q9Z330-1]

Organism-specific databases

RGDi620979. Dnmt1.

Phylogenomic databases

eggNOGiCOG0270.
HOGENOMiHOG000082497.
HOVERGENiHBG051384.
InParanoidiQ9Z330.
PhylomeDBiQ9Z330.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8581.

Miscellaneous databases

PROiQ9Z330.

Gene expression databases

GenevestigatoriQ9Z330.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNMT1.
IPR029063. SAM-dependent_MTases.
IPR002857. Znf_CXXC.
[Graphical view]
PfamiPF01426. BAH. 2 hits.
PF06464. DMAP_binding. 1 hit.
PF12047. DNMT1-RFD. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF037404. DNMT1. 1 hit.
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 2 hits.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51038. BAH. 2 hits.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
PS51058. ZF_CXXC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Expression of rat DNA (cytosine-5) methyltransferase (DNA MTase) in rodent trophoblast giant cells: molecular cloning and characterization of rat DNA MTase."
    Kimura H., Takeda T., Tanaka S., Ogawa T., Shiota K.
    Biochem. Biophys. Res. Commun. 253:495-501(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Brain and Placenta.
  2. "Multiple N-terminal isoforms of DNA (cytosine-5-)-methyltransferase in vivo."
    Deng J., Szyf M.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 9).
    Tissue: Brain.
  3. "Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."
    Ohsawa K., Imai Y., Ito D., Kohsaka S.
    J. Neurochem. 67:89-97(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-356, IN VITRO BINDING TO ANNEXIN V.
    Strain: Wistar.
    Tissue: Brain.
  4. "Multiple isoforms of DNA methyltransferase are encoded by the vertebrate cytosine DNA methyltransferase gene."
    Deng J., Szyf M.
    J. Biol. Chem. 273:22869-22872(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1169-1517 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8).

Entry informationi

Entry nameiDNMT1_RAT
AccessioniPrimary (citable) accession number: Q9Z330
Secondary accession number(s): P70487
, Q9R252, Q9WTX3, Q9WU57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: February 21, 2002
Last modified: February 4, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.