Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E9Q5F9

- SETD2_MOUSE

UniProt

E9Q5F9 - SETD2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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-KW
  2. nucleus Source: MGI
Complete GO annotation...

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

MaxQBiE9Q5F9.
PRIDEiE9Q5F9.

Expressioni

Gene expression databases

BgeeiE9Q5F9.
ExpressionAtlasiE9Q5F9. baseline and differential.

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

GeneTreeiENSGT00760000118855.
InParanoidiE9Q5F9.
KOiK11423.
OMAiVMDDFRD.
OrthoDBiEOG7DFXBB.
TreeFamiTF106477.

Family and domain databases

InterProiIPR006560. AWS_dom.
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

        10         20         30         40         50
MKPLPSQQPP PKMGDFYDPE HPTPEEEENE AKIENVQKTG FIKGPVFKGV
60 70 80 90 100
ASSRFLPKGT KTKVNLEEQG RQKVSFSFSF TKKTLQNRFL TALSNEKQSD
110 120 130 140 150
SPNSPAPPLQ VDSNPKVKMD AGDTFPATEE SSPPKSRVEL GRIHFKKHLL
160 170 180 190 200
HVTSRPQLAA STTAASPLPP TTQLPAVLAE SMIDSPPSSP PPPPPPPQAS
210 220 230 240 250
SPSPPAQISE PVALPQPPAT ALMTSPPGPL PGDVAVRAQK ESPVKSGPEV
260 270 280 290 300
LEVDTKQDIV SNSLEEHTVQ TLKEQADHLL QKEDSHIGKE EEVSDGSKIS
310 320 330 340 350
LSSKKASSKK KSSQFEGTFL GSESDEDSVR TSSSQRSHDL KSSTSIDKER
360 370 380 390 400
DFKKSSAPSK SEDLGKSSRS KTERDDRYCS YSKLERDTRY VSSRCRSERD
410 420 430 440 450
RRRSRSRSRS DRASRTSLSY SRSERSHYYD SERRYHRSSP YRERTRYSRP
460 470 480 490 500
YTDNRARESS DSEDEYKKTY PRRTSAHSYR DLRTSSSYSK FDRDCKTETS
510 520 530 540 550
YLEMERRGKY TSKLERESKR TSEHETIKRC CSPPNELGFR RGSSYSKHDN
560 570 580 590 600
STSRYKSALS KSISKNDKFK NSFCCTELNE ENKQSHSFSL QTPCSKGSEL
610 620 630 640 650
RTINKISERE KTGSPTPSNQ LNDSPTFKKL DESPVLKPEF IGHDGRESIK
660 670 680 690 700
ELELSKVKND QLRNFCSIEL NVNGSPETEA DVATFCTSKT DAISMTSDDS
710 720 730 740 750
VTGSEVSPLI KACMLSSNGF QNVGRCRERD SDDTCRQHNT SKSPFREMEP
760 770 780 790 800
LLSPHHDKLM SLPVKTIDYP KTLIKEPVDK RHSCCKTKDS DIYCSPNENP
810 820 830 840 850
EAENAEPSAM TISSHSFVNV HLESKTVICD NREPTDRHSE NTCDEYKQSI
860 870 880 890 900
GSTSSASHNH FDGLYEPIGS SGISSLQSPP SGIRCEENTS PTLDAVESKK
910 920 930 940 950
GIDFLKYARK ETDVGSALPD SGKGFSWENR HNNVLSGQSL QEAQEEGNSI
960 970 980 990 1000
LHERRGRPEI PLDEEQRGHT HISDDSEVVF PYDLNLTMED SDGITYTLKC
1010 1020 1030 1040 1050
DSSGNAPEIV STVHEDYSGS SASSSDESDS EDTESDDSSI PRNRLQSVVV
1060 1070 1080 1090 1100
VPKNSTLPME ETSPCSSRSS QSYKHYSDRW EDGLETRRHA YEEEYESKGC
1110 1120 1130 1140 1150
SQTEKYFLHK GTERSAESCY SQFGRKADNH LPDIAHAQSD GVDSTSQTDS
1160 1170 1180 1190 1200
RSDHLGHLNP EDTLRAKTSR PQELPVYSDD FEDLPNKSRQ QMIFSNRPDS
1210 1220 1230 1240 1250
SRLGKTELSF SSSCDISRMD GLHSSEELRN LGWDFSQQER PTTTYQQPDS
1260 1270 1280 1290 1300
SYGTCGTHKY QQSTEHYGGT HNYWQGNGYW DPRSAGRPPG TGLAYDRIQG
1310 1320 1330 1340 1350
QVPDSLTDDR EEEEHWDQRS GSHFSSPSNK FFFHQKDKGS VQAPEISSNS
1360 1370 1380 1390 1400
IKDALVMNER KDFSKNFEKN DIKERGPPKK RRQELESDSE SDGELQARKK
1410 1420 1430 1440 1450
VRVEMEQGES SVPQHSELMG PSCAMDDFRD PQRWKEFAKL GKMPCYFDLI
1460 1470 1480 1490 1500
EENVYLTERK KNKSHRDIKR MQCECTPLSK DERAQGEVAC GEDCLNRLLM
1510 1520 1530 1540 1550
IECSSRCPNG DYCSNRRFQR KQHADVEVIL TEKKGWGLRA AKDLPSNTFV
1560 1570 1580 1590 1600
LEYCGEVLDH KEFKARVKEY ARNKNIHYYF MALKNDEIID ATQKGNCSRF
1610 1620 1630 1640 1650
MNHSCEPNCE TQKWTVNGQL RVGFFTTKLV PSGSELTFDY QFQRYGKEAQ
1660 1670 1680 1690 1700
KCFCGSANCR GYLGGENRVS IRAAGGKMKK ERSRKKDSVD GELEALMENG
1710 1720 1730 1740 1750
EGLSDKNQVL SLSRLMVRIE TLEQKLTCLK LIQNTHSQSC LKSFLERHGL
1760 1770 1780 1790 1800
SLLWIWMAEL GDGRESNQKL QEEIIKTLEH LPIPTKNMLE ESKVLPIIQR
1810 1820 1830 1840 1850
WSQTKTAVPQ LSEGDGYSSE NTSRAHTPLN TPDPSAKPST EMDTDTPKKL
1860 1870 1880 1890 1900
IFRRLKIISE NSMDSAVSDV TSELECKDGK EDLDQLETVT VEEDEELQSQ
1910 1920 1930 1940 1950
QLLPQQLCES KVESEATIEV SKLPTSEPEA DTETEPKDSN GTKLEETIAE
1960 1970 1980 1990 2000
ETPSQDEEEG VSDVESERSQ EPPDKTVDIS DLATKLLDSW KDLKEVYRIP
2010 2020 2030 2040 2050
KKSQTEKEST VAERGRDAAA FRDQTAPKTP NRSRERDPDK QSQNKEKRKR
2060 2070 2080 2090 2100
RGSLSPPSSA YERGTKRPDD RYDTPTSKKK VRIKDRNKLS TEERRKLFEQ
2110 2120 2130 2140 2150
EVAQREAQKQ QQQMQNLGMT SPLPFDSLGY NASHHPFAGY PPGYPMQAYV
2160 2170 2180 2190 2200
DPSNPNAGKV LLPTPSMDPV CSPAPYDHAQ PLVGHSTESL AAPPSVPVVP
2210 2220 2230 2240 2250
HVAASVEVSS SQYVAQNESV VHQDSNVPVM PVQAPGPVQG QNYNVWESNQ
2260 2270 2280 2290 2300
QSVSVQQQYS PAQSQTTIYY QGQTCSTVYS VTSPYSQTTP PIVQSYAQPS
2310 2320 2330 2340 2350
LQYIQGQQIF TAHPQGVVVQ PTAAVTSIVA PGQPQSLQPP EMVVTNNLLD
2360 2370 2380 2390 2400
LPPPSPPKPK TIVLPPNWKT ARDPEGKIYY YHVITRQTQW DPPTWESPGD
2410 2420 2430 2440 2450
DASLEHEAEM DLGTPTYDEN PMKTSKKPKT AEADTSSELA KKSKEVFRKE
2460 2470 2480 2490 2500
MSQFIVQCLN PYRKPDCKVG RITTTEDFKH LARKLTHGVM NKELKYCKNP
2510 2520 2530
EDLECNENVK HKTKEYIKKY MQKFGAVYKP KEDTELE
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

MaxQBi E9Q5F9.
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 ENSGT00760000118855.
InParanoidi E9Q5F9.
KOi K11423.
OMAi VMDDFRD.
OrthoDBi EOG7DFXBB.
TreeFami TF106477.

Miscellaneous databases

NextBioi 382803.
PROi E9Q5F9.
SOURCEi Search...

Gene expression databases

Bgeei E9Q5F9.
ExpressionAtlasi E9Q5F9. baseline and differential.

Family and domain databases

InterProi IPR006560. AWS_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 34 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