[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). STRAIN=Sprague-Dawley; TISSUE=Brain, and Placenta; DOI=10.1006/bbrc.1998.9802; PubMed=9878564 [NCBI, ExPASy, EBI, Israel, Japan] Kimura H., Takeda T., Tanaka S., Ogawa T., Shiota K.; "Expression of rat DNA (cytosine-5) methyltransferase (DNA MTase) in rodent trophoblast giant cells: molecular cloning and characterization of rat DNA MTase."; Biochem. Biophys. Res. Commun. 253:495-501(1998).
[2]	NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 9). TISSUE=Brain; Deng J., Szyf M.; "Multiple N-terminal isoforms of DNA (cytosine-5-)-methyltransferase in vivo."; Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 17-356, AND IN VITRO BINDING TO ANNEXIN V. STRAIN=Wistar; TISSUE=Brain; PubMed=8667030 [NCBI, ExPASy, EBI, Israel, Japan] Ohsawa K., Imai Y., Ito D., Kohsaka S.; "Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."; J. Neurochem. 67:89-97(1996).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1169-1517 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8). DOI=10.1074/jbc.273.36.22869; PubMed=9722504 [NCBI, ExPASy, EBI, Israel, Japan] Deng J., Szyf M.; "Multiple isoforms of DNA methyltransferase are encoded by the vertebrate cytosine DNA methyltransferase gene."; J. Biol. Chem. 273:22869-22872(1998).

Comments

FUNCTION: Methylates CpG residues. Preferentially methylates hemimethylated DNA. 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 (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SUBUNIT: 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 (By similarity).
INTERACTION:
P08758:ANXA5 (xeno); NbExp=1; IntAct=EBI-78342, EBI-296601;
SUBCELLULAR LOCATION: Nucleus.

ALTERNATIVE PRODUCTS: 9 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	1
Isoform ID	Q9Z330-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	SF1
Isoform ID	Q9Z330-2
Features which should be applied to build the isoform sequence: VSP_005627.

Name	3
Synonyms	SF2
Isoform ID	Q9Z330-3
Features which should be applied to build the isoform sequence: VSP_005625.

Name	4
Synonyms	SF3
Isoform ID	Q9Z330-4
Features which should be applied to build the isoform sequence: VSP_005624.

Name	5
Synonyms	SF4
Isoform ID	Q9Z330-5
Features which should be applied to build the isoform sequence: VSP_005621.

Name	6
Synonyms	SF5
Isoform ID	Q9Z330-6
Features which should be applied to build the isoform sequence: VSP_005622.

Name	7
Synonyms	SF6
Isoform ID	Q9Z330-7
Features which should be applied to build the isoform sequence: VSP_005626.

Name	8
Synonyms	SF7
Isoform ID	Q9Z330-8
Features which should be applied to build the isoform sequence: VSP_005623.

Name	9
Synonyms	short
Isoform ID	Q9Z330-9
Features which should be applied to build the isoform sequence: VSP_005620.

TISSUE SPECIFICITY: 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.
SIMILARITY: Belongs to the C5-methyltransferase family.
SIMILARITY: Contains 2 BAH domains.
SIMILARITY: Contains 1 CXXC-type zinc finger.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB012214; BAA37118.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF116344; AAD32541.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF116345; AAD32542.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D64060; BAA20854.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083043; AAD28102.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083038; AAD28102.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083039; AAD28102.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083040; AAD28102.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083041; AAD28102.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083042; AAD28102.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JE0378; JE0378.

NP_445806.2; -.

3D structure databases

ModBase

Q9Z330.

Protein-protein interaction databases

IntAct

Q9Z330; -.

Protein family/group databases

REBASE

11410; M.RraDnmtI.

PTM databases

PhosphoSite

Q9Z330; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8581; -.

Organism-specific databases

RGD

620979; Dnmt1.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0008134;	Molecular function: transcription factor binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006306;	Biological process: DNA methylation (inferred from electronic annotation from InterPro).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001025; BAH.
IPR001525; C5_DNA_meth.
IPR010506; DMAP1_bd.
IPR017198; DNA_C5-MeTrfase_1.
IPR002857; Znf_CXXC.
Graphical view of domain structure.

PANTHER

PTHR10629; C5_DNA_meth; 1.

Pfam

PF01426; BAH; 2.
PF06464; DMAP_binding; 1.
PF00145; DNA_methylase; 3.
PF02008; zf-CXXC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037404; DNMT1; 1.

PRINTS

PR00105; C5METTRFRASE.

SMART

SM00439; BAH; 2.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00675; dcm; 1.

PROSITE

PS51038; BAH; 2.
PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; 1.
PS51058; ZF_CXXC; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9Z330.

Genome annotation databases

GeneID

84350; -.

KEGG

rno:84350; -.

Phylogenomic databases

HOVERGEN

Q9Z330; -.

Other

NextBio

616655; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Alternative splicing; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Repeat; Repressor; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1622`	`1622`	`DNA (cytosine-5)-methyltransferase 1.`	`PRO_0000088036`
`DOMAIN`	`759 884`	`126`	`BAH 1.`
`DOMAIN`	`977 1105`	`129`	`BAH 2.`
`REPEAT`	`1114 1115`	`2`	`1.`
`REPEAT`	`1116 1117`	`2`	`2.`
`REPEAT`	`1118 1119`	`2`	`3.`
`REPEAT`	`1120 1121`	`2`	`4.`
`REPEAT`	`1122 1123`	`2`	`5.`
`REPEAT`	`1124 1125`	`2`	`6.`
`REPEAT`	`1126 1127`	`2`	`7; approximate.`
`ZN_FING`	`650 696`	`47`	`CXXC-type.`
`REGION`	`1 342`	`342`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`1 145`	`145`	`Interaction with DNMT3A (By similarity).`
`REGION`	`146 213`	`68`	`Interaction with DNMT3B (By similarity).`
`REGION`	`304 610`	`307`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`327 556`	`230`	`DNA replication foci-targeting sequence.`
`REGION`	`1114 1127`	`14`	`7 X 2 AA tandem repeats of K-G.`
`REGION`	`1126 1622`	`497`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`1144 1622`	`479`	`Catalytic.`
`MOTIF`	`173 200`	`28`	`Nuclear localization signal (Potential).`
`COMPBIAS`	`149 152`	`4`	`Poly-Ser.`
`COMPBIAS`	`269 274`	`6`	`Poly-Asp.`
`COMPBIAS`	`726 729`	`4`	`Poly-Lys.`
`ACT_SITE`	`1231 1231`		`By similarity.`
`MOD_RES`	`151 151`		`Phosphoserine (By similarity).`
`MOD_RES`	`515 515`		`Phosphoserine (By similarity).`
`MOD_RES`	`718 718`		`Phosphoserine (By similarity).`
`MOD_RES`	`736 736`		`Phosphoserine (By similarity).`
`MOD_RES`	`958 958`		`Phosphoserine (By similarity).`
`MOD_RES`	`1110 1110`		`Phosphoserine (By similarity).`
`MOD_RES`	`1118 1118`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`1120 1120`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`1122 1122`		`N6-acetyllysine (By similarity).`
`VAR_SEQ`	`1 118`		`Missing (in isoform 9).`	`VSP_005620`
`VAR_SEQ`	`1202 1410`		`Missing (in isoform 6).`	`VSP_005622`
`VAR_SEQ`	`1216 1504`		`Missing (in isoform 8).`	`VSP_005623`
`VAR_SEQ`	`1218 1430`		`QKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFL` `SYCDYYRPRFFLLENVRNFVSFRRSMVLKLTLRCLVRMGY` `QCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLH` `VFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITMRDTMS` `DLPEIQNGASAPEISYKWRATVLVPEAAARVALPAHPQGP` `YPQVHERAGGCRM -> VC (in isoform 5).`	`VSP_005621`
`VAR_SEQ`	`1226 1477`		`Missing (in isoform 4).`	`VSP_005624`
`VAR_SEQ`	`1252 1482`		`Missing (in isoform 3).`	`VSP_005625`
`VAR_SEQ`	`1259 1481`		`Missing (in isoform 7).`	`VSP_005626`
`VAR_SEQ`	`1323 1403`		`Missing (in isoform 2).`	`VSP_005627`
`CONFLICT`	`17 25`		`AGSLPDHVR -> RQARPRPCP (in Ref. 3).`
`CONFLICT`	`189 189`		`A -> V (in Ref. 3; BAA20854).`
`CONFLICT`	`1276 1276`		`F -> S (in Ref. 1; BAA37118).`
`CONFLICT`	`1300 1300`		`T -> I (in Ref. 4; AAD28102).`
`CONFLICT`	`1372 1372`		`M -> V (in Ref. 1; BAA37118).`
`CONFLICT`	`1394 1428`		`KWRATVLVPEAAARVALPAHPQGPYPQVHERAGGC -> NGEPQSWFQRQLRGSHYQPILRDHICKDMSALVAA (in Ref. 1).`

Sequence information

Length: 1622 AA [This is the length of the unprocessed precursor]

Molecular weight: 182774 Da [This is the MW of the unprocessed precursor]

CRC64: FCFA4AAA69E234BA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVKEKLNLLH EFLQTEIKSQ 

        70         80         90        100        110        120 
LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT QKANGCPANG SRPTWKAEMA 

       130        140        150        160        170        180 
DSNRSPRSRP KPRGPRRSKS DSETMIEASS SSVATRRTTR QTTITSHFKG PAKRKPKEDS 

       190        200        210        220        230        240 
EKGNANESAA EERDQDKKRR VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR 

       250        260        270        280        290        300 
PRRQTRELAS RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV 

       310        320        330        340        350        360 
EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA IPKLNPPQCP 

       370        380        390        400        410        420 
ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS WFETYDSSPM HKFTFFSVYC 

       430        440        450        460        470        480 
SRGHLCPVDT GLIEKNVELY FSGVAKAIHE ENPSVEGGVN GKNLGPINQW WISGFDGGEK 

       490        500        510        520        530        540 
ALIGFSTAFA EYFLMEPSPE YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT 

       550        560        570        580        590        600 
VPPSAINVNR FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ 

       610        620        630        640        650        660 
RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN TMKRRRCGVC 

       670        680        690        700        710        720 
EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV KEADEDEEAD DDIPELPSPK 

       730        740        750        760        770        780 
KLHQGKKKKQ NKDRISWLGE PVKIEENRTY YWKVSIDEET LEVGDCVSVI PDDPSKPLYL 

       790        800        810        820        830        840 
ARVTALWEDK NGQMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR 

       850        860        870        880        890        900 
GPSPNWAMEG GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC 

       910        920        930        940        950        960 
IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKMASPM 

       970        980        990       1000       1010       1020 
KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR IKEIYCGKKK GGKVNEADIK 

      1030       1040       1050       1060       1070       1080 
IRLYKFYRPE NTHKSIQATY HADINLLYWS DEEAVVDFSD VQGRCTVEYG EDLLESIQDY 

      1090       1100       1110       1120       1130       1140 
SQGGPDRFYF LEAYNSKTKS FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK 

      1150       1160       1170       1180       1190       1200 
LPKLRTLDVF SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL 

      1210       1220       1230       1240       1250       1260 
KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN SLVVSFLSYC 

      1270       1280       1290       1300       1310       1320 
DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT FGVLQAGQYG VAQTRRRAII 

      1330       1340       1350       1360       1370       1380 
LAAAPGEKLP LFPEPLHVFA PRACQLSVVV DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP 

      1390       1400       1410       1420       1430       1440 
EIQNGASAPE ISYKWRATVL VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD 

      1450       1460       1470       1480       1490       1500 
WRDLPNIQVR LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI 

      1510       1520       1530       1540       1550       1560 
PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR VVSVRECARS 

      1570       1580       1590       1600       1610       1620 
QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL LASAQESASA AVKGKEETTT 


ED

Q9Z330 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools