[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1093/nar/20.9.2287; PubMed=1594447 [NCBI, ExPASy, EBI, Israel, Japan] Yen R.-W.C., Vertino P.M., Nelkin B.D., Yu J.J., Deiry W.E., Cumaraswamy A., Lennon G.G., Trask B.J., Celano P., Baylin S.B.; "Isolation and characterization of the cDNA encoding human DNA methyltransferase."; Nucleic Acids Res. 20:2287-2291(1992).
[2]	SEQUENCE REVISION TO N-TERMINUS. DOI=10.1074/jbc.271.49.31092; PubMed=8940105 [NCBI, ExPASy, EBI, Israel, Japan] Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.; "New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase."; J. Biol. Chem. 271:31092-31097(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). TISSUE=Prostatic carcinoma; Li L.C., Au H., Chui R., Dahiya R.; "Human DNA methyltransferase (DNMT1) is alternatively spliced."; Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan] Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.; "The DNA sequence and biology of human chromosome 19."; Nature 428:529-535(2004).
[5]	PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). DOI=10.1073/pnas.96.17.9751; PubMed=10449766 [NCBI, ExPASy, EBI, Israel, Japan] Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J.; "Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues."; Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999).
[6]	PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). DOI=10.1074/jbc.275.15.10754; PubMed=10753866 [NCBI, ExPASy, EBI, Israel, Japan] Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R.; "Characterization of the human DNA methyltransferase splice variant Dnmt1b."; J. Biol. Chem. 275:10754-10760(2000).
[7]	INTERACTION WITH PCNA, AND MUTAGENESIS. DOI=10.1126/science.277.5334.1996; PubMed=9302295 [NCBI, ExPASy, EBI, Israel, Japan] Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.; "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1."; Science 277:1996-2000(1997).
[8]	INTERACTION WITH MBD2 AND MBD3. PubMed=10947852 [NCBI, ExPASy, EBI, Israel, Japan] Tatematsu K., Yamazaki T., Ishikawa F.; "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase."; Genes Cells 5:677-688(2000).
[9]	INTERACTION WITH HDAC2 AND DMAP1. DOI=10.1038/77023; PubMed=10888872 [NCBI, ExPASy, EBI, Israel, Japan] Rountree M.R., Bachman K.E., Baylin S.B.; "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."; Nat. Genet. 25:269-277(2000).
[10]	INTERACTION WITH RB1; E2F1 AND HDAC1. DOI=10.1038/77124; PubMed=10888886 [NCBI, ExPASy, EBI, Israel, Japan] Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.; "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters."; Nat. Genet. 25:338-342(2000).
[11]	TISSUE SPECIFICITY. DOI=10.1093/nar/27.11.2291; PubMed=10325416 [NCBI, ExPASy, EBI, Israel, Japan] Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A.; "The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors."; Nucleic Acids Res. 27:2291-2298(1999).
[12]	INTERACTION WITH DNMT3A AND DNMT3B, AND SUBCELLULAR LOCATION. DOI=10.1093/emboj/cdf401; PubMed=12145218 [NCBI, ExPASy, EBI, Israel, Japan] Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.; "Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases."; EMBO J. 21:4183-4195(2002).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714 AND SER-954, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-714 AND SER-1105, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[15]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1113; LYS-1115 AND LYS-1117, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).
[16]	FUNCTION, AND INTERACTION WITH EED AND EZH2. DOI=10.1038/nature04431; PubMed=16357870 [NCBI, ExPASy, EBI, Israel, Japan] Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.; "The Polycomb group protein EZH2 directly controls DNA methylation."; Nature 439:871-874(2006).
[17]	ERRATUM. Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.; Nature 446:824-824(2006).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-969, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[19]	DE NOVO DNA METHYLATION OF TARGET GENES. DOI=10.1038/ng1950; PubMed=17200670 [NCBI, ExPASy, EBI, Israel, Japan] Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.; "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."; Nat. Genet. 39:232-236(2007).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).

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.
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. Interacts with the PRC2/EED-EZH2 complex.
INTERACTION:
O75530:EED; NbExp=1; IntAct=EBI-719459, EBI-923794;
Q15910:EZH2; NbExp=3; IntAct=EBI-719459, EBI-530054;
Q96T88:UHRF1; NbExp=1; IntAct=EBI-719459, EBI-1548946;
SUBCELLULAR LOCATION: Nucleus.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P26358-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	Dnmt1b
Isoform ID	P26358-2
Features which should be applied to build the isoform sequence: VSP_005618.

Name	3
Isoform ID	P26358-3
Features which should be applied to build the isoform sequence: VSP_005617.

TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal tissues, heart, kidney, placenta, peripheral blood mononuclear cells, and expressed at lower levels in spleen, lung, brain, small intestine, colon, liver, and skeletal muscle. Isoform 2 is less expressed than isoform 1.
INDUCTION: Its abundance is reduced to non detectable levels at the G0 phase of the cell cycle and is dramatically induced upon entrance into the S-phase of the cell cycle.
SIMILARITY: Belongs to the C5-methyltransferase family.
SIMILARITY: Contains 2 BAH domains.
SIMILARITY: Contains 1 CXXC-type zinc finger.
SEQUENCE CAUTION:
- Sequence=AAD54507.1; Type=Erroneous gene model prediction;

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

X63692; CAA45219.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF180682; AAF23609.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010077; AAD54507.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC020931; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AF169120; AAD51619.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S22610; S22610.

NP_001370.1; -.

3D structure databases

ModBase

P26358.

Protein-protein interaction databases

IntAct

P26358; -.

Protein family/group databases

REBASE

1161; M.HsaDnmt1A.

PTM databases

PhosphoSite

P26358; -.

Organism-specific databases

HIX0027457; -.

HGNC:2976; DNMT1.

CAB005876; -.
HPA002694; -.

MIM

126375; gene. [NCBI / EBI]

PharmGKB

PA27443; -.

GeneCards

P26358.

Gene expression databases

ArrayExpress

P26358; -.

CleanEx

HS_DNMT1; -.

GermOnline

ENSG00000130816; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (traceable author statement from ProtInc).
GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (traceable author statement from ProtInc).
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 (traceable author statement from ProtInc).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
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).

Genome annotation databases

Ensembl

ENSG00000130816; Homo sapiens. [Contig view]

GeneID

1786; -.

KEGG

hsa:1786; -.

Phylogenomic databases

HOVERGEN

P26358; -.

Other

DrugBank

DB00928; Azacitidine.
DB01262; Decitabine.
DB01099; Flucytosine.
DB01181; Ifosfamide.
DB01035; Procainamide.

NextBio

7267; -.

SOURCE

DNMT1; Homo sapiens.

UniRef

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

Keywords

Acetylation; Alternative splicing; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; 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 1616`	`1616`	`DNA (cytosine-5)-methyltransferase 1.`	`PRO_0000088034`
`DOMAIN`	`755 880`	`126`	`BAH 1.`
`DOMAIN`	`972 1100`	`129`	`BAH 2.`
`REPEAT`	`1109 1110`	`2`	`1.`
`REPEAT`	`1111 1112`	`2`	`2.`
`REPEAT`	`1113 1114`	`2`	`3.`
`REPEAT`	`1115 1116`	`2`	`4.`
`REPEAT`	`1117 1118`	`2`	`5.`
`REPEAT`	`1119 1120`	`2`	`6; approximate.`
`ZN_FING`	`646 692`	`47`	`CXXC-type.`
`REGION`	`1 336`	`336`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`1 148`	`148`	`Interaction with DNMT3A.`
`REGION`	`1 120`	`120`	`Interaction with DMAP1.`
`REGION`	`149 217`	`69`	`Interaction with DNMT3B.`
`REGION`	`163 174`	`12`	`Interaction with PCNA.`
`REGION`	`308 606`	`299`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`331 550`	`220`	`DNA replication foci-targeting sequence (By similarity).`
`REGION`	`1109 1120`	`12`	`6 X 2 AA tandem repeats of K-G.`
`REGION`	`1121 1616`	`496`	`Interaction with the PRC2/EED-EZH2 complex (By similarity).`
`REGION`	`1139 1616`	`478`	`Catalytic.`
`MOTIF`	`177 205`	`29`	`Nuclear localization signal (Potential).`
`ACT_SITE`	`1226 1226`		`By similarity.`
`MOD_RES`	`127 127`		`Phosphoserine.`
`MOD_RES`	`154 154`		`Phosphoserine.`
`MOD_RES`	`509 509`		`Phosphoserine (By similarity).`
`MOD_RES`	`714 714`		`Phosphoserine.`
`MOD_RES`	`732 732`		`Phosphoserine.`
`MOD_RES`	`954 954`		`Phosphoserine.`
`MOD_RES`	`969 969`		`Phosphotyrosine.`
`MOD_RES`	`1105 1105`		`Phosphoserine.`
`MOD_RES`	`1113 1113`		`N6-acetyllysine.`
`MOD_RES`	`1115 1115`		`N6-acetyllysine.`
`MOD_RES`	`1117 1117`		`N6-acetyllysine.`
`VAR_SEQ`	`1 336`		`Missing (in isoform 3).`	`VSP_005617`
`VAR_SEQ`	`149 149`		`P -> RSRDPPASASQVTGIRA (in isoform 2).`	`VSP_005618`
`VARIANT`	`97 97`	`1`	`H -> R (in dbSNP:rs16999593 [NCBI]).`	`VAR_024605`
`MUTAGEN`	`163 163`		`R->A: Abolishes interaction with PCNA.`
`MUTAGEN`	`164 164`		`Q->A: Abolishes interaction with PCNA.`
`MUTAGEN`	`166 166`		`T->A: Abolishes interaction with PCNA.`
`MUTAGEN`	`167 167`		`I->A: Abolishes interaction with PCNA.`
`MUTAGEN`	`169 169`		`S->A: No loss of interaction with PCNA.`
`MUTAGEN`	`170 170`		`H->V: Abolishes interaction with PCNA.`
`MUTAGEN`	`171 171`		`F->V: Abolishes interaction with PCNA.`
`MUTAGEN`	`172 172`		`A->S: No loss of interaction with PCNA.`
`MUTAGEN`	`173 173`		`K->A: No loss of interaction with PCNA.`

Sequence information

Length: 1616 AA [This is the length of the unprocessed precursor]

Molecular weight: 183165 Da [This is the MW of the unprocessed precursor]

CRC64: 1E833192D22AFA5B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLQTEIKNQ 

        70         80         90        100        110        120 
LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN REVNGRLENG NQARSEARRV 

       130        140        150        160        170        180 
GMADANSPPK PLSKPRTPRR SKSDGEAKPE PSPSPRITRK STRQTTITSH FAKGPAKRKP 

       190        200        210        220        230        240 
QEESERAKSD ESIKEEDKDQ DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK 

       250        260        270        280        290        300 
EEKRLRSQTK EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE 

       310        320        330        340        350        360 
EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP PKCIQCGQYL 

       370        380        390        400        410        420 
DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE ALPQHKLTCF SVYCKHGHLC 

       430        440        450        460        470        480 
PIDTGLIEKN IELFFSGSAK PIYDDDPSLE GGVNGKNLGP INEWWITGFD GGEKALIGFS 

       490        500        510        520        530        540 
TSFAEYILMD PSPEYAPIFG LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL 

       550        560        570        580        590        600 
NLNRFTEDSL LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR 

       610        620        630        640        650        660 
RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR RRCGVCEVCQ 

       670        680        690        700        710        720 
QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD DDEEVDDNIP EMPSPKKMHQ 

       730        740        750        760        770        780 
GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV CIDAETLEVG DCVSVIPDDS SKPLYLARVT 

       790        800        810        820        830        840 
ALWEDSSNGQ MFHAHWFCAG TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS 

       850        860        870        880        890        900 
ENWAMEGGMD PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA 

       910        920        930        940        950        960 
EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI KLSSPVKRPR 

       970        980        990       1000       1010       1020 
KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF CPKKSNGRPN ETDIKIRVNK 

      1030       1040       1050       1060       1070       1080 
FYRPENTHKS TPASYHADIN LLYWSDEEAV VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP 

      1090       1100       1110       1120       1130       1140 
NRFYFLEAYN AKSKSFEDPP NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR 

      1150       1160       1170       1180       1190       1200 
TLDVFSGCGG LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA 

      1210       1220       1230       1240       1250       1260 
GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS FLSYCDYYRP 

      1270       1280       1290       1300       1310       1320 
RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ AGQYGVAQTR RRAIILAAAP 

      1330       1340       1350       1360       1370       1380 
GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF VSNITRLSSG PFRTITVRDT MSDLPEVRNG 

      1390       1400       1410       1420       1430       1440 
ASALEISYNG EPQSWFQRQL RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP 

      1450       1460       1470       1480       1490       1500 
NIEVRLSDGT MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL 

      1510       1520       1530       1540       1550       1560 
PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV RECARSQGFP 

      1570       1580       1590       1600       1610 
DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA RESASAKIKE EEAAKD

P26358 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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