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E9Q5F9

- SETD2_MOUSE

UniProt

E9Q5F9 - SETD2_MOUSE

Protein

Histone-lysine N-methyltransferase SETD2

Gene

Setd2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (05 Apr 2011)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate. Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation. Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A. Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction. H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A. H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase. Required during angiogenesis.2 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    Enzyme regulationi

    Specifically inhibited by sinefungin derivatives.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1599 – 15991InhibitorBy similarity
    Binding sitei1650 – 16501Inhibitor; alternateBy similarity
    Binding sitei1650 – 16501S-adenosyl-L-methionine; alternatePROSITE-ProRule annotation
    Binding sitei1653 – 16531Inhibitor; via amide nitrogen; alternateBy similarity
    Binding sitei1653 – 16531S-adenosyl-L-methionine; via amide nitrogen; alternatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. cell migration involved in vasculogenesis Source: MGI
    3. coronary vasculature morphogenesis Source: MGI
    4. embryonic cranial skeleton morphogenesis Source: MGI
    5. embryonic organ development Source: MGI
    6. embryonic placenta morphogenesis Source: MGI
    7. forebrain development Source: MGI
    8. histone H3-K36 methylation Source: MGI
    9. histone H3-K36 trimethylation Source: UniProtKB
    10. mesoderm morphogenesis Source: MGI
    11. mismatch repair Source: UniProtKB
    12. morphogenesis of a branching structure Source: MGI
    13. neural tube closure Source: MGI
    14. nucleosome organization Source: UniProtKB
    15. peptidyl-lysine trimethylation Source: MGI
    16. pericardium development Source: MGI
    17. regulation of gene expression Source: MGI
    18. regulation of mRNA export from nucleus Source: Ensembl
    19. regulation of transcription, DNA-templated Source: UniProtKB-KW
    20. stem cell development Source: MGI
    21. transcription elongation from RNA polymerase II promoter Source: UniProtKB
    22. vasculogenesis Source: MGI

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SETD2 (EC:2.1.1.43)
    Alternative name(s):
    Lysine N-methyltransferase 3A
    SET domain-containing protein 2
    Gene namesi
    Name:Setd2
    Synonyms:Kiaa1732, Kmt3a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1918177. Setd2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethality at E10.5-E11.5. Embryos show severe vascular defects in embryo, yolk sac and placenta. Capillaries are abnormally dilated in embryos and yolk sacs and cannot be remodeled into large blood vessels or intricate networks. The embryonic vessels fail to invade the labyrinthine layer of placenta, which impair the embryonic-maternal vascular connection. Defects are not caused by the extraembryonic tissues. Impaired H3K36me3, but not H3K36me2 or H3K36me1.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25372537Histone-lysine N-methyltransferase SETD2PRO_0000423553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321PhosphoserineBy similarity
    Modified residuei322 – 3221PhosphoserineBy similarity
    Modified residuei324 – 3241PhosphoserineBy similarity
    Modified residuei624 – 6241PhosphoserineBy similarity
    Modified residuei707 – 7071PhosphoserineBy similarity
    Modified residuei743 – 7431PhosphoserineBy similarity
    Modified residuei753 – 7531PhosphoserineBy similarity
    Modified residuei1201 – 12011PhosphoserineBy similarity
    Modified residuei1387 – 13871Phosphoserine1 Publication
    Modified residuei1389 – 13891Phosphoserine1 Publication
    Modified residuei1391 – 13911Phosphoserine1 Publication
    Modified residuei1846 – 18461PhosphothreonineBy similarity
    Modified residuei2053 – 20531PhosphoserineBy similarity
    Modified residuei2055 – 20551PhosphoserineBy similarity

    Post-translational modificationi

    May be automethylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiE9Q5F9.

    Expressioni

    Gene expression databases

    ArrayExpressiE9Q5F9.
    BgeeiE9Q5F9.

    Interactioni

    Subunit structurei

    Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad. Interacts with HTT and IWS1. Interacts with p53/TP53; leading to regulate p53/TP53 target genes. Component of a complex with HNRNPL By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000116313.

    Structurei

    3D structure databases

    ProteinModelPortaliE9Q5F9.
    SMRiE9Q5F9. Positions 1421-1665, 2435-2534.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1468 – 152255AWSPROSITE-ProRule annotationAdd
    BLAST
    Domaini1524 – 1641118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1648 – 166417Post-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini2362 – 239534WWPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1534 – 15363Inhibitor bindingBy similarity
    Regioni1534 – 15363S-adenosyl-L-methionine bindingBy similarity
    Regioni1577 – 15793Inhibitor bindingBy similarity
    Regioni1577 – 15793S-adenosyl-L-methionine bindingBy similarity
    Regioni1602 – 16032Inhibitor bindingBy similarity
    Regioni1602 – 16032S-adenosyl-L-methionine bindingBy similarity
    Regioni2110 – 2339230Low charge regionBy similarityAdd
    BLAST
    Regioni2430 – 2537108Interaction with POLR2ABy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2090 – 211930Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi167 – 23165Pro-richAdd
    BLAST
    Compositional biasi294 – 439146Ser-richAdd
    BLAST
    Compositional biasi369 – 45789Arg-richAdd
    BLAST
    Compositional biasi2233 – 2338106Gln-richAdd
    BLAST

    Domaini

    The low charge region mediates the transcriptional activation activity.By similarity

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.PROSITE-ProRule annotation
    Contains 1 AWS domain.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation
    Contains 1 WW domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    GeneTreeiENSGT00750000117355.
    KOiK11423.
    OMAiVMDDFRD.
    OrthoDBiEOG7DFXBB.
    TreeFamiTF106477.

    Family and domain databases

    InterProiIPR006560. AWS.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR013257. SRI.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00856. SET. 1 hit.
    PF08236. SRI. 1 hit.
    PF00397. WW. 1 hit.
    [Graphical view]
    SMARTiSM00570. AWS. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00456. WW. 1 hit.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 1 hit.
    PROSITEiPS51215. AWS. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: E9Q5F9-1) [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

    MKPLPSQQPP PKMGDFYDPE HPTPEEEENE AKIENVQKTG FIKGPVFKGV     50
    ASSRFLPKGT KTKVNLEEQG RQKVSFSFSF TKKTLQNRFL TALSNEKQSD 100
    SPNSPAPPLQ VDSNPKVKMD AGDTFPATEE SSPPKSRVEL GRIHFKKHLL 150
    HVTSRPQLAA STTAASPLPP TTQLPAVLAE SMIDSPPSSP PPPPPPPQAS 200
    SPSPPAQISE PVALPQPPAT ALMTSPPGPL PGDVAVRAQK ESPVKSGPEV 250
    LEVDTKQDIV SNSLEEHTVQ TLKEQADHLL QKEDSHIGKE EEVSDGSKIS 300
    LSSKKASSKK KSSQFEGTFL GSESDEDSVR TSSSQRSHDL KSSTSIDKER 350
    DFKKSSAPSK SEDLGKSSRS KTERDDRYCS YSKLERDTRY VSSRCRSERD 400
    RRRSRSRSRS DRASRTSLSY SRSERSHYYD SERRYHRSSP YRERTRYSRP 450
    YTDNRARESS DSEDEYKKTY PRRTSAHSYR DLRTSSSYSK FDRDCKTETS 500
    YLEMERRGKY TSKLERESKR TSEHETIKRC CSPPNELGFR RGSSYSKHDN 550
    STSRYKSALS KSISKNDKFK NSFCCTELNE ENKQSHSFSL QTPCSKGSEL 600
    RTINKISERE KTGSPTPSNQ LNDSPTFKKL DESPVLKPEF IGHDGRESIK 650
    ELELSKVKND QLRNFCSIEL NVNGSPETEA DVATFCTSKT DAISMTSDDS 700
    VTGSEVSPLI KACMLSSNGF QNVGRCRERD SDDTCRQHNT SKSPFREMEP 750
    LLSPHHDKLM SLPVKTIDYP KTLIKEPVDK RHSCCKTKDS DIYCSPNENP 800
    EAENAEPSAM TISSHSFVNV HLESKTVICD NREPTDRHSE NTCDEYKQSI 850
    GSTSSASHNH FDGLYEPIGS SGISSLQSPP SGIRCEENTS PTLDAVESKK 900
    GIDFLKYARK ETDVGSALPD SGKGFSWENR HNNVLSGQSL QEAQEEGNSI 950
    LHERRGRPEI PLDEEQRGHT HISDDSEVVF PYDLNLTMED SDGITYTLKC 1000
    DSSGNAPEIV STVHEDYSGS SASSSDESDS EDTESDDSSI PRNRLQSVVV 1050
    VPKNSTLPME ETSPCSSRSS QSYKHYSDRW EDGLETRRHA YEEEYESKGC 1100
    SQTEKYFLHK GTERSAESCY SQFGRKADNH LPDIAHAQSD GVDSTSQTDS 1150
    RSDHLGHLNP EDTLRAKTSR PQELPVYSDD FEDLPNKSRQ QMIFSNRPDS 1200
    SRLGKTELSF SSSCDISRMD GLHSSEELRN LGWDFSQQER PTTTYQQPDS 1250
    SYGTCGTHKY QQSTEHYGGT HNYWQGNGYW DPRSAGRPPG TGLAYDRIQG 1300
    QVPDSLTDDR EEEEHWDQRS GSHFSSPSNK FFFHQKDKGS VQAPEISSNS 1350
    IKDALVMNER KDFSKNFEKN DIKERGPPKK RRQELESDSE SDGELQARKK 1400
    VRVEMEQGES SVPQHSELMG PSCAMDDFRD PQRWKEFAKL GKMPCYFDLI 1450
    EENVYLTERK KNKSHRDIKR MQCECTPLSK DERAQGEVAC GEDCLNRLLM 1500
    IECSSRCPNG DYCSNRRFQR KQHADVEVIL TEKKGWGLRA AKDLPSNTFV 1550
    LEYCGEVLDH KEFKARVKEY ARNKNIHYYF MALKNDEIID ATQKGNCSRF 1600
    MNHSCEPNCE TQKWTVNGQL RVGFFTTKLV PSGSELTFDY QFQRYGKEAQ 1650
    KCFCGSANCR GYLGGENRVS IRAAGGKMKK ERSRKKDSVD GELEALMENG 1700
    EGLSDKNQVL SLSRLMVRIE TLEQKLTCLK LIQNTHSQSC LKSFLERHGL 1750
    SLLWIWMAEL GDGRESNQKL QEEIIKTLEH LPIPTKNMLE ESKVLPIIQR 1800
    WSQTKTAVPQ LSEGDGYSSE NTSRAHTPLN TPDPSAKPST EMDTDTPKKL 1850
    IFRRLKIISE NSMDSAVSDV TSELECKDGK EDLDQLETVT VEEDEELQSQ 1900
    QLLPQQLCES KVESEATIEV SKLPTSEPEA DTETEPKDSN GTKLEETIAE 1950
    ETPSQDEEEG VSDVESERSQ EPPDKTVDIS DLATKLLDSW KDLKEVYRIP 2000
    KKSQTEKEST VAERGRDAAA FRDQTAPKTP NRSRERDPDK QSQNKEKRKR 2050
    RGSLSPPSSA YERGTKRPDD RYDTPTSKKK VRIKDRNKLS TEERRKLFEQ 2100
    EVAQREAQKQ QQQMQNLGMT SPLPFDSLGY NASHHPFAGY PPGYPMQAYV 2150
    DPSNPNAGKV LLPTPSMDPV CSPAPYDHAQ PLVGHSTESL AAPPSVPVVP 2200
    HVAASVEVSS SQYVAQNESV VHQDSNVPVM PVQAPGPVQG QNYNVWESNQ 2250
    QSVSVQQQYS PAQSQTTIYY QGQTCSTVYS VTSPYSQTTP PIVQSYAQPS 2300
    LQYIQGQQIF TAHPQGVVVQ PTAAVTSIVA PGQPQSLQPP EMVVTNNLLD 2350
    LPPPSPPKPK TIVLPPNWKT ARDPEGKIYY YHVITRQTQW DPPTWESPGD 2400
    DASLEHEAEM DLGTPTYDEN PMKTSKKPKT AEADTSSELA KKSKEVFRKE 2450
    MSQFIVQCLN PYRKPDCKVG RITTTEDFKH LARKLTHGVM NKELKYCKNP 2500
    EDLECNENVK HKTKEYIKKY MQKFGAVYKP KEDTELE 2537
    Length:2,537
    Mass (Da):285,663
    Last modified:April 5, 2011 - v1
    Checksum:i4ED47D778291DA9D
    GO
    Isoform 2 (identifier: E9Q5F9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2011-2011: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,536
    Mass (Da):285,564
    Checksum:i990ECF2CD8D56008
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2011 – 20111Missing in isoform 2. 1 PublicationVSP_047946

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC132103 Genomic DNA. No translation available.
    BC031601 mRNA. Translation: AAH31601.1.
    BC059049 mRNA. Translation: AAH59049.1.
    AK173246 mRNA. Translation: BAD32524.1.
    CCDSiCCDS40781.2. [E9Q5F9-1]
    RefSeqiNP_001074809.2. NM_001081340.2. [E9Q5F9-1]
    UniGeneiMm.288949.

    Genome annotation databases

    EnsembliENSMUST00000153838; ENSMUSP00000116313; ENSMUSG00000044791. [E9Q5F9-1]
    GeneIDi235626.
    KEGGimmu:235626.
    UCSCiuc009rug.2. mouse. [E9Q5F9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC132103 Genomic DNA. No translation available.
    BC031601 mRNA. Translation: AAH31601.1 .
    BC059049 mRNA. Translation: AAH59049.1 .
    AK173246 mRNA. Translation: BAD32524.1 .
    CCDSi CCDS40781.2. [E9Q5F9-1 ]
    RefSeqi NP_001074809.2. NM_001081340.2. [E9Q5F9-1 ]
    UniGenei Mm.288949.

    3D structure databases

    ProteinModelPortali E9Q5F9.
    SMRi E9Q5F9. Positions 1421-1665, 2435-2534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000116313.

    Proteomic databases

    PRIDEi E9Q5F9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000153838 ; ENSMUSP00000116313 ; ENSMUSG00000044791 . [E9Q5F9-1 ]
    GeneIDi 235626.
    KEGGi mmu:235626.
    UCSCi uc009rug.2. mouse. [E9Q5F9-1 ]

    Organism-specific databases

    CTDi 29072.
    MGIi MGI:1918177. Setd2.
    Rougei Search...

    Phylogenomic databases

    GeneTreei ENSGT00750000117355.
    KOi K11423.
    OMAi VMDDFRD.
    OrthoDBi EOG7DFXBB.
    TreeFami TF106477.

    Miscellaneous databases

    NextBioi 382803.
    PROi E9Q5F9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi E9Q5F9.
    Bgeei E9Q5F9.

    Family and domain databases

    InterProi IPR006560. AWS.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR013257. SRI.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00856. SET. 1 hit.
    PF08236. SRI. 1 hit.
    PF00397. WW. 1 hit.
    [Graphical view ]
    SMARTi SM00570. AWS. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    SM00456. WW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 1 hit.
    PROSITEi PS51215. AWS. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2121-2537 AND 1800-2537 (ISOFORM 2).
      Tissue: Mammary tumor.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1834-2537 (ISOFORM 1).
      Tissue: Thymus.
    4. "Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation."
      Edmunds J.W., Mahadevan L.C., Clayton A.L.
      EMBO J. 27:406-420(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1389 AND SER-1391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Histone H3 lysine 36 methyltransferase Hypb/Setd2 is required for embryonic vascular remodeling."
      Hu M., Sun X.J., Zhang Y.L., Kuang Y., Hu C.Q., Wu W.L., Shen S.H., Du T.T., Li H., He F., Xiao H.S., Wang Z.G., Liu T.X., Lu H., Huang Q.H., Chen S.J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 107:2956-2961(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiSETD2_MOUSE
    AccessioniPrimary (citable) accession number: E9Q5F9
    Secondary accession number(s): Q69ZC0, Q6PCY9, Q8K0F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 18, 2013
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 33 of the entry and version 1 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3