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Protein

Histone-lysine N-methyltransferase SETD2

Gene

SETD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.7 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. N-propyl sinefungin (Pr-SNF) interacts preferentially with SETD2.1 Publication

Kineticsi

Kcat is 0.14 min(-1).

  1. KM=1.21 µM for S-adenosyl-L-methionine1 Publication
  2. KM=0.42 µM for histone H31 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1625 – 16251Inhibitor
    Binding sitei1676 – 16761Inhibitor; alternate
    Binding sitei1676 – 16761S-adenosyl-L-methionine; alternate
    Binding sitei1679 – 16791Inhibitor; via amide nitrogen; alternate
    Binding sitei1679 – 16791S-adenosyl-L-methionine; via amide nitrogen; alternate

    GO - Molecular functioni

    • histone-lysine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • angiogenesis Source: Ensembl
    • cell migration involved in vasculogenesis Source: Ensembl
    • chromatin organization Source: Reactome
    • coronary vasculature morphogenesis Source: Ensembl
    • embryonic cranial skeleton morphogenesis Source: Ensembl
    • embryonic placenta morphogenesis Source: Ensembl
    • forebrain development Source: Ensembl
    • histone H3-K36 trimethylation Source: UniProtKB
    • mesoderm morphogenesis Source: Ensembl
    • mismatch repair Source: UniProtKB
    • morphogenesis of a branching structure Source: Ensembl
    • neural tube closure Source: Ensembl
    • nucleosome organization Source: UniProtKB
    • pericardium development Source: Ensembl
    • regulation of mRNA export from nucleus Source: UniProtKB
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • stem cell development Source: Ensembl
    • transcription elongation from RNA polymerase II promoter Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 2681.
    ReactomeiREACT_268728. PKMTs methylate histone lysines.
    SignaLinkiQ9BYW2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase SETD2 (EC:2.1.1.43)
    Alternative name(s):
    HIF-1
    Huntingtin yeast partner B
    Huntingtin-interacting protein 1
    Short name:
    HIP-1
    Huntingtin-interacting protein B
    Lysine N-methyltransferase 3A
    SET domain-containing protein 2
    Short name:
    hSET2
    p231HBP
    Gene namesi
    Name:SETD2
    Synonyms:HIF1, HYPB, KIAA1732, KMT3A, SET2
    ORF Names:HSPC069
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18420. SETD2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Renal cell carcinoma (RCC)3 Publications

    The disease may be caused by mutations affecting the gene represented in this entry. Defects of SETD2 are associated with loss of DNA methylation at non-promoter regions (PubMed:23792563).

    Disease descriptionRenal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.

    See also OMIM:144700
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1733 – 17331N → D in RCC cell line; defects in recruitment of the MutS alpha complex. 1 Publication
    VAR_069812
    Natural varianti1769 – 17691S → P in RCC cell line; defects in recruitment of the MutS alpha complex. 1 Publication
    VAR_069813

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1625 – 16251R → H: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi1668 – 16681F → A: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi1669 – 16691Q → A: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi1670 – 16701R → A, V, L, I or F: Impaired methyltransferase activity. 1 Publication
    Mutagenesisi1670 – 16701R → P, W, K or Q: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi1671 – 16711Y → A: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi2475 – 24751R → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2476 – 24761K → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2480 – 24801Q → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2481 – 24811F → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2483 – 24831V → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2505 – 25051F → L: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2506 – 25061K → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2510 – 25101R → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2514 – 25141H → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2515 – 25151G → A or T: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication
    Mutagenesisi2528 – 25281E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531. 1 Publication
    Mutagenesisi2531 – 25311E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528. 1 Publication

    Organism-specific databases

    MIMi144700. phenotype.
    Orphaneti821. Sotos syndrome.
    PharmGKBiPA143485612.

    Polymorphism and mutation databases

    BioMutaiSETD2.
    DMDMi296452963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25642564Histone-lysine N-methyltransferase SETD2PRO_0000252367Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei321 – 3211Phosphoserine5 Publications
    Modified residuei323 – 3231Phosphoserine4 Publications
    Modified residuei614 – 6141Phosphoserine1 Publication
    Modified residuei624 – 6241Phosphoserine3 Publications
    Modified residuei708 – 7081Phosphoserine1 Publication
    Modified residuei744 – 7441Phosphoserine1 Publication
    Modified residuei754 – 7541Phosphoserine3 Publications
    Modified residuei1228 – 12281Phosphoserine2 Publications
    Modified residuei1413 – 14131PhosphoserineBy similarity
    Modified residuei1415 – 14151PhosphoserineBy similarity
    Modified residuei1417 – 14171PhosphoserineBy similarity
    Modified residuei1853 – 18531Phosphothreonine1 Publication
    Modified residuei1872 – 18721Phosphothreonine2 Publications
    Modified residuei2080 – 20801Phosphoserine1 Publication
    Modified residuei2082 – 20821Phosphoserine2 Publications

    Post-translational modificationi

    May be automethylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BYW2.
    PaxDbiQ9BYW2.
    PRIDEiQ9BYW2.

    2D gel databases

    OGPiQ9BYW2.

    PTM databases

    PhosphoSiteiQ9BYW2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ9BYW2.
    CleanExiHS_SETD2.
    ExpressionAtlasiQ9BYW2. baseline and differential.
    GenevisibleiQ9BYW2. HS.

    Organism-specific databases

    HPAiHPA042451.

    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.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428584EBI-945869,EBI-466029
    SMAD3P840222EBI-945869,EBI-347161

    Protein-protein interaction databases

    BioGridi118845. 25 interactions.
    IntActiQ9BYW2. 10 interactions.
    MINTiMINT-1537591.

    Structurei

    Secondary structure

    1
    2564
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1448 – 14503Combined sources
    Helixi1451 – 14555Combined sources
    Helixi1457 – 14659Combined sources
    Beta strandi1480 – 14823Combined sources
    Helixi1506 – 15116Combined sources
    Helixi1523 – 15253Combined sources
    Helixi1536 – 15383Combined sources
    Turni1543 – 15475Combined sources
    Beta strandi1552 – 15565Combined sources
    Beta strandi1558 – 156811Combined sources
    Beta strandi1575 – 15784Combined sources
    Beta strandi1582 – 15843Combined sources
    Helixi1586 – 159813Combined sources
    Beta strandi1606 – 16105Combined sources
    Beta strandi1613 – 16164Combined sources
    Beta strandi1618 – 16214Combined sources
    Helixi1623 – 16264Combined sources
    Beta strandi1634 – 16429Combined sources
    Beta strandi1645 – 165410Combined sources
    Beta strandi1661 – 16644Combined sources
    Turni1667 – 16693Combined sources
    Beta strandi1687 – 16893Combined sources
    Beta strandi2377 – 23793Combined sources
    Helixi2386 – 23883Combined sources
    Beta strandi2392 – 23998Combined sources
    Turni2401 – 24033Combined sources
    Beta strandi2405 – 24095Combined sources
    Turni2410 – 24134Combined sources
    Beta strandi2414 – 24196Combined sources
    Beta strandi2424 – 24285Combined sources
    Helixi2463 – 248624Combined sources
    Turni2487 – 24893Combined sources
    Beta strandi2495 – 24984Combined sources
    Helixi2502 – 252423Combined sources
    Helixi2527 – 25293Combined sources
    Helixi2534 – 254815Combined sources
    Turni2549 – 25513Combined sources
    Helixi2557 – 25593Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A7ONMR-A2457-2564[»]
    2MDCNMR-A2385-2430[»]
    2MDINMR-A2377-2430[»]
    2MDJNMR-A2377-2430[»]
    4FMUX-ray2.10A1434-1711[»]
    4H12X-ray1.99A1434-1711[»]
    ProteinModelPortaliQ9BYW2.
    SMRiQ9BYW2. Positions 1447-1691, 2385-2430, 2462-2561.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYW2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1494 – 154855AWSPROSITE-ProRule annotationAdd
    BLAST
    Domaini1550 – 1667118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1674 – 169017Post-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini2389 – 242234WWPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1560 – 15623Inhibitor binding
    Regioni1560 – 15623S-adenosyl-L-methionine binding
    Regioni1603 – 16053Inhibitor binding
    Regioni1603 – 16053S-adenosyl-L-methionine binding
    Regioni1628 – 16292Inhibitor binding
    Regioni1628 – 16292S-adenosyl-L-methionine binding
    Regioni2137 – 2366230Low charge regionAdd
    BLAST
    Regioni2457 – 2564108Interaction with POLR2AAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2117 – 214630Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi166 – 24782Pro-richAdd
    BLAST
    Compositional biasi385 – 45672Arg-richAdd
    BLAST
    Compositional biasi2149 – 223284Pro-richAdd
    BLAST
    Compositional biasi2266 – 2365100Gln-richAdd
    BLAST

    Domaini

    The low charge region mediates the transcriptional activation activity.1 Publication

    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

    eggNOGiCOG2940.
    GeneTreeiENSGT00780000121845.
    HOVERGENiHBG093939.
    InParanoidiQ9BYW2.
    KOiK11423.
    OMAiVMDDFRD.
    PhylomeDBiQ9BYW2.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9BYW2-1) [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
    MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA
    60 70 80 90 100
    SSRFLPKGTK TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT
    110 120 130 140 150
    PNPPAVPLQV DSTPKMKMEI GDTLSTAEES SPPKSRVELG KIHFKKHLLH
    160 170 180 190 200
    VTSRPLLATT TAVASPPTHA APLPAVIAES TTVDSPPSSP PPPPPPAQAT
    210 220 230 240 250
    TLSSPAPVTE PVALPHTPIT VLMAAPVPLP VDVAVRSLKE PPIIIVPESL
    260 270 280 290 300
    EADTKQDTIS NSLEEHVTQI LNEQADISSK KEDSHIGKDE EIPDSSKISL
    310 320 330 340 350
    SCKKTGSKKK SSQSEGIFLG SESDEDSVRT SSSQRSHDLK FSASIEKERD
    360 370 380 390 400
    FKKSSAPLKS EDLGKPSRSK TDRDDKYFSY SKLERDTRYV SSRCRSERER
    410 420 430 440 450
    RRSRSHSRSE RGSRTNLSYS RSERSHYYDS DRRYHRSSPY RERTRYSRPY
    460 470 480 490 500
    TDNRARESSD SEEEYKKTYS RRTSSHSSSY RDLRTSSYSK SDRDCKTETS
    510 520 530 540 550
    YLEMERRGKY SSKLERESKR TSENEAIKRC CSPPNELGFR RGSSYSKHDS
    560 570 580 590 600
    SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL
    610 620 630 640 650
    RMINKNPERE KAGSPAPSNR LNDSPTLKKL DELPIFKSEF ITHDSHDSIK
    660 670 680 690 700
    ELDSLSKVKN DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD
    710 720 730 740 750
    SVTGSELSPL VKACMLSSNG FQNISRCKEK DLDDTCMLHK KSESPFRETE
    760 770 780 790 800
    PLVSPHQDKL MSMPVMTVDY SKTVVKEPVD TRVSCCKTKD SDIYCTLNDS
    810 820 830 840 850
    NPSLCNSEAE NIEPSVMKIS SNSFMNVHLE SKPVICDSRN LTDHSKFACE
    860 870 880 890 900
    EYKQSIGSTS SASVNHFDDL YQPIGSSGIA SSLQSLPPGI KVDSLTLLKC
    910 920 930 940 950
    GENTSPVLDA VLKSKKSSEF LKHAGKETIV EVGSDLPDSG KGFASRENRR
    960 970 980 990 1000
    NNGLSGKCLQ EAQEEGNSIL PERRGRPEIS LDERGEGGHV HTSDDSEVVF
    1010 1020 1030 1040 1050
    SSCDLNLTME DSDGVTYALK CDSSGHAPEI VSTVHEDYSG SSESSNDESD
    1060 1070 1080 1090 1100
    SEDTDSDDSS IPRNRLQSVV VVPKNSTLPM EETSPCSSRS SQSYRHYSDH
    1110 1120 1130 1140 1150
    WEDERLESRR HLYEEKFESI ASKACPQTDK FFLHKGTEKN PEISFTQSSR
    1160 1170 1180 1190 1200
    KQIDNRLPEL SHPQSDGVDS TSHTDVKSDP LGHPNSEETV KAKIPSRQQE
    1210 1220 1230 1240 1250
    ELPIYSSDFE DVPNKSWQQT TFQNRPDSRL GKTELSFSSS CEIPHVDGLH
    1260 1270 1280 1290 1300
    SSEELRNLGW DFSQEKPSTT YQQPDSSYGA CGGHKYQQNA EQYGGTRDYW
    1310 1320 1330 1340 1350
    QGNGYWDPRS GRPPGTGVVY DRTQGQVPDS LTDDREEEEN WDQQDGSHFS
    1360 1370 1380 1390 1400
    DQSDKFLLSL QKDKGSVQAP EISSNSIKDT LAVNEKKDFS KNLEKNDIKD
    1410 1420 1430 1440 1450
    RGPLKKRRQE IESDSESDGE LQDRKKVRVE VEQGETSVPP GSALVGPSCV
    1460 1470 1480 1490 1500
    MDDFRDPQRW KECAKQGKMP CYFDLIEENV YLTERKKNKS HRDIKRMQCE
    1510 1520 1530 1540 1550
    CTPLSKDERA QGEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA
    1560 1570 1580 1590 1600
    DVEVILTEKK GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK ARVKEYARNK
    1610 1620 1630 1640 1650
    NIHYYFMALK NDEIIDATQK GNCSRFMNHS CEPNCETQKW TVNGQLRVGF
    1660 1670 1680 1690 1700
    FTTKLVPSGS ELTFDYQFQR YGKEAQKCFC GSANCRGYLG GENRVSIRAA
    1710 1720 1730 1740 1750
    GGKMKKERSR KKDSVDGELE ALMENGEGLS DKNQVLSLSR LMVRIETLEQ
    1760 1770 1780 1790 1800
    KLTCLELIQN THSQSCLKSF LERHGLSLLW IWMAELGDGR ESNQKLQEEI
    1810 1820 1830 1840 1850
    IKTLEHLPIP TKNMLEESKV LPIIQRWSQT KTAVPPLSEG DGYSSENTSR
    1860 1870 1880 1890 1900
    AHTPLNTPDP STKLSTEADT DTPKKLMFRR LKIISENSMD SAISDATSEL
    1910 1920 1930 1940 1950
    EGKDGKEDLD QLENVPVEEE EELQSQQLLP QQLPECKVDS ETNIEASKLP
    1960 1970 1980 1990 2000
    TSEPEADAEI EPKESNGTKL EEPINEETPS QDEEEGVSDV ESERSQEQPD
    2010 2020 2030 2040 2050
    KTVDISDLAT KLLDSWKDLK EVYRIPKKSQ TEKENTTTER GRDAVGFRDQ
    2060 2070 2080 2090 2100
    TPAPKTPNRS RERDPDKQTQ NKEKRKRRSS LSPPSSAYER GTKRPDDRYD
    2110 2120 2130 2140 2150
    TPTSKKKVRI KDRNKLSTEE RRKLFEQEVA QREAQKQQQQ MQNLGMTSPL
    2160 2170 2180 2190 2200
    PYDSLGYNAP HHPFAGYPPG YPMQAYVDPS NPNAGKVLLP TPSMDPVCSP
    2210 2220 2230 2240 2250
    APYDHAQPLV GHSTEPLSAP PPVPVVPHVA APVEVSSSQY VAQSDGVVHQ
    2260 2270 2280 2290 2300
    DSSVAVLPVP APGPVQGQNY SVWDSNQQSV SVQQQYSPAQ SQATIYYQGQ
    2310 2320 2330 2340 2350
    TCPTVYGVTS PYSQTTPPIV QSYAQPSLQY IQGQQIFTAH PQGVVVQPAA
    2360 2370 2380 2390 2400
    AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV LPPNWKTARD
    2410 2420 2430 2440 2450
    PEGKIYYYHV ITRQTQWDPP TWESPGDDAS LEHEAEMDLG TPTYDENPMK
    2460 2470 2480 2490 2500
    ASKKPKTAEA DTSSELAKKS KEVFRKEMSQ FIVQCLNPYR KPDCKVGRIT
    2510 2520 2530 2540 2550
    TTEDFKHLAR KLTHGVMNKE LKYCKNPEDL ECNENVKHKT KEYIKKYMQK
    2560
    FGAVYKPKED TELE
    Length:2,564
    Mass (Da):287,597
    Last modified:May 18, 2010 - v3
    Checksum:i2B1BAE5867AB8EAB
    GO
    Isoform 2 (identifier: Q9BYW2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1715-2564: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:1,714
    Mass (Da):192,342
    Checksum:iBD566E360FCF0E9B
    GO
    Isoform 3 (identifier: Q9BYW2-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1573-2564: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:1,572
    Mass (Da):175,982
    Checksum:i1FAC3FE752C0777C
    GO

    Sequence cautioni

    The sequence AAF29041.1 differs from that shown. Reason: Frameshift at several positions. Curated
    The sequence AAH72440.1 differs from that shown. Reason: Erroneous termination at position 463. Translated as Glu.Curated
    The sequence AAI17163.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAI17165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAT77612.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAT77613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAB15367.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
    The sequence BAB15367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC87131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAC28349.1 differs from that shown. Reason: Erroneous termination at position 385. Translated as Arg.Curated
    The sequence CAD38601.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti448 – 4481R → Q in BAD18522 (PubMed:14702039).Curated
    Sequence conflicti455 – 4551A → V in CAD38601 (PubMed:17974005).Curated
    Sequence conflicti912 – 9121L → P in BAB15367 (PubMed:14702039).Curated
    Sequence conflicti964 – 9641E → K in CAC28349 (PubMed:11461154).Curated
    Sequence conflicti964 – 9641E → K in AAT77612 (PubMed:16118227).Curated
    Sequence conflicti964 – 9641E → K in AAT77613 (Ref. 7) Curated
    Sequence conflicti1080 – 10801M → I in BAC87131 (PubMed:14702039).Curated
    Sequence conflicti1080 – 10801M → T in CAD38601 (PubMed:17974005).Curated
    Sequence conflicti1212 – 12121V → F in BAD18522 (PubMed:14702039).Curated
    Sequence conflicti1269 – 12691T → A in CAC28349 (PubMed:11461154).Curated
    Sequence conflicti1269 – 12691T → A in AAT77612 (PubMed:16118227).Curated
    Sequence conflicti1269 – 12691T → A in AAT77613 (Ref. 7) Curated
    Sequence conflicti1338 – 13381E → G in BAB15367 (PubMed:14702039).Curated
    Sequence conflicti1498 – 14981Q → R in CAD38601 (PubMed:17974005).Curated
    Sequence conflicti1706 – 17061K → N in AAF29041 (PubMed:11042152).Curated
    Sequence conflicti1736 – 17361L → P in CAC28349 (PubMed:11461154).Curated
    Sequence conflicti1736 – 17361L → P in AAT77612 (PubMed:16118227).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti768 – 7681V → L.
    Corresponds to variant rs9311404 [ dbSNP | Ensembl ].
    VAR_027839
    Natural varianti902 – 9021E → Q.
    Corresponds to variant rs58906143 [ dbSNP | Ensembl ].
    VAR_061216
    Natural varianti1733 – 17331N → D in RCC cell line; defects in recruitment of the MutS alpha complex. 1 Publication
    VAR_069812
    Natural varianti1769 – 17691S → P in RCC cell line; defects in recruitment of the MutS alpha complex. 1 Publication
    VAR_069813
    Natural varianti1868 – 18681A → D.
    Corresponds to variant rs11721074 [ dbSNP | Ensembl ].
    VAR_027840
    Natural varianti1962 – 19621P → L.2 Publications
    Corresponds to variant rs4082155 [ dbSNP | Ensembl ].
    VAR_027841

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1573 – 2564992Missing in isoform 3. 1 PublicationVSP_020914Add
    BLAST
    Alternative sequencei1715 – 2564850Missing in isoform 2. 1 PublicationVSP_020915Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC094020 Genomic DNA. No translation available.
    AC127430 Genomic DNA. No translation available.
    AK026125 mRNA. Translation: BAB15367.1. Sequence problems.
    AK127782 mRNA. Translation: BAC87131.1. Different initiation.
    AK131371 mRNA. Translation: BAD18522.1.
    AL713692 mRNA. Translation: CAD28492.1.
    AL831959 mRNA. Translation: CAD38601.2. Different initiation.
    AL833394 mRNA. Translation: CAH10589.1.
    AJ238403 mRNA. Translation: CAC28349.1. Sequence problems.
    BC072440 mRNA. Translation: AAH72440.1. Sequence problems.
    BC090954 mRNA. Translation: AAH90954.1.
    BC117162 mRNA. Translation: AAI17163.1. Different initiation.
    BC117164 mRNA. Translation: AAI17165.1. Different initiation.
    AY576987 mRNA. Translation: AAT77612.1. Different initiation.
    AY576988 mRNA. Translation: AAT77613.1. Different initiation.
    AB051519 mRNA. Translation: BAB21823.2.
    AF161554 mRNA. Translation: AAF29041.1. Frameshift.
    AF049103 mRNA. Translation: AAC26194.1.
    AF049610 mRNA. Translation: AAC26846.1.
    CCDSiCCDS2749.2. [Q9BYW2-1]
    RefSeqiNP_054878.5. NM_014159.6. [Q9BYW2-1]
    UniGeneiHs.517941.

    Genome annotation databases

    EnsembliENST00000409792; ENSP00000386759; ENSG00000181555. [Q9BYW2-1]
    GeneIDi29072.
    KEGGihsa:29072.
    UCSCiuc003cqs.3. human. [Q9BYW2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC094020 Genomic DNA. No translation available.
    AC127430 Genomic DNA. No translation available.
    AK026125 mRNA. Translation: BAB15367.1. Sequence problems.
    AK127782 mRNA. Translation: BAC87131.1. Different initiation.
    AK131371 mRNA. Translation: BAD18522.1.
    AL713692 mRNA. Translation: CAD28492.1.
    AL831959 mRNA. Translation: CAD38601.2. Different initiation.
    AL833394 mRNA. Translation: CAH10589.1.
    AJ238403 mRNA. Translation: CAC28349.1. Sequence problems.
    BC072440 mRNA. Translation: AAH72440.1. Sequence problems.
    BC090954 mRNA. Translation: AAH90954.1.
    BC117162 mRNA. Translation: AAI17163.1. Different initiation.
    BC117164 mRNA. Translation: AAI17165.1. Different initiation.
    AY576987 mRNA. Translation: AAT77612.1. Different initiation.
    AY576988 mRNA. Translation: AAT77613.1. Different initiation.
    AB051519 mRNA. Translation: BAB21823.2.
    AF161554 mRNA. Translation: AAF29041.1. Frameshift.
    AF049103 mRNA. Translation: AAC26194.1.
    AF049610 mRNA. Translation: AAC26846.1.
    CCDSiCCDS2749.2. [Q9BYW2-1]
    RefSeqiNP_054878.5. NM_014159.6. [Q9BYW2-1]
    UniGeneiHs.517941.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A7ONMR-A2457-2564[»]
    2MDCNMR-A2385-2430[»]
    2MDINMR-A2377-2430[»]
    2MDJNMR-A2377-2430[»]
    4FMUX-ray2.10A1434-1711[»]
    4H12X-ray1.99A1434-1711[»]
    ProteinModelPortaliQ9BYW2.
    SMRiQ9BYW2. Positions 1447-1691, 2385-2430, 2462-2561.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi118845. 25 interactions.
    IntActiQ9BYW2. 10 interactions.
    MINTiMINT-1537591.

    Chemistry

    ChEMBLiCHEMBL3108647.

    PTM databases

    PhosphoSiteiQ9BYW2.

    Polymorphism and mutation databases

    BioMutaiSETD2.
    DMDMi296452963.

    2D gel databases

    OGPiQ9BYW2.

    Proteomic databases

    MaxQBiQ9BYW2.
    PaxDbiQ9BYW2.
    PRIDEiQ9BYW2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000409792; ENSP00000386759; ENSG00000181555. [Q9BYW2-1]
    GeneIDi29072.
    KEGGihsa:29072.
    UCSCiuc003cqs.3. human. [Q9BYW2-1]

    Organism-specific databases

    CTDi29072.
    GeneCardsiGC03M047033.
    H-InvDBHIX0021942.
    HIX0163343.
    HGNCiHGNC:18420. SETD2.
    HPAiHPA042451.
    MIMi144700. phenotype.
    612778. gene.
    neXtProtiNX_Q9BYW2.
    Orphaneti821. Sotos syndrome.
    PharmGKBiPA143485612.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2940.
    GeneTreeiENSGT00780000121845.
    HOVERGENiHBG093939.
    InParanoidiQ9BYW2.
    KOiK11423.
    OMAiVMDDFRD.
    PhylomeDBiQ9BYW2.
    TreeFamiTF106477.

    Enzyme and pathway databases

    BRENDAi2.1.1.43. 2681.
    ReactomeiREACT_268728. PKMTs methylate histone lysines.
    SignaLinkiQ9BYW2.

    Miscellaneous databases

    ChiTaRSiSETD2. human.
    EvolutionaryTraceiQ9BYW2.
    GeneWikiiSETD2.
    GenomeRNAii29072.
    NextBioi52031.
    PROiQ9BYW2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9BYW2.
    CleanExiHS_SETD2.
    ExpressionAtlasiQ9BYW2. baseline and differential.
    GenevisibleiQ9BYW2. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1390.
      Tissue: Brain and Cerebellum.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-2564 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 927-1482 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2228-2564 (ISOFORM 1).
      Tissue: Adipose tissue.
    4. "Identification of the full-length huntingtin-interacting protein p231HBP/HYPB as a DNA-binding factor."
      Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W., Marquitan G., Puetzer B.M.
      Mol. Cell. Neurosci. 18:68-79(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-2564 (ISOFORM 1), DNA-BINDING, TISSUE SPECIFICITY, INTERACTION WITH HTT.
    5. "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 388-2564 (ISOFORM 1), VARIANT LEU-1962.
      Tissue: Cerebellum, Duodenum and Testis.
    6. "Identification and characterization of a novel human histone H3 lysine 36 specific methyltransferase."
      Sun X.-J., Wei J., Wu X.-Y., Hu M., Wang L., Wang H.-H., Zhang Q.-H., Chen S.-J., Huang Q.-H., Chen Z.
      J. Biol. Chem. 280:35261-35271(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 481-2564 (ISOFORM 1), FUNCTION, AUTOMETHYLATION, MUTAGENESIS OF ARG-1625, INTERACTION WITH POLR2A.
    7. "Identification of a human histone H3-K36-specific methyltransferase that is orthologous to Saccharomyces cerevisiae SET2 protein."
      Sun X.J., Wei J., Wu X.Y., Hu M., Wang H.H., Zhang Q.H., Huang Q.H., Chen Z.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 481-2564 (ISOFORM 2).
    8. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 650-2564 (ISOFORM 1), VARIANT LEU-1962.
      Tissue: Brain.
    9. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    10. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1402-2069.
      Tissue: Umbilical cord blood.
    11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2378-2564, INTERACTION WITH HTT.
      Tissue: Frontal cortex.
    12. "Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis."
      Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H., Gusella J.F., Vonsattel J.-P., MacDonald M.E.
      Hum. Mol. Genet. 9:2175-2182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTT.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes."
      Xie P., Tian C., An L., Nie J., Lu K., Xing G., Zhang L., He F.
      Cell. Signal. 20:1671-1678(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    15. "The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylation."
      Yoh S.M., Lucas J.S., Jones K.A.
      Genes Dev. 22:3422-3434(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IWS1.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624; SER-754; SER-1228; THR-1872; SER-2080 AND SER-2082, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo."
      Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y., Tempst P., Chen S., Zhu B., Reinberg D.
      J. Biol. Chem. 284:15701-15707(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRNPL.
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-321; SER-323; SER-708; SER-744 AND SER-754, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. Cited for: INVOLVEMENT IN RCC.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624 AND THR-1872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36."
      de Almeida S.F., Grosso A.R., Koch F., Fenouil R., Carvalho S., Andrade J., Levezinho H., Gut M., Eick D., Gut I., Andrau J.C., Ferrier P., Carmo-Fonseca M.
      Nat. Struct. Mol. Biol. 18:977-983(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Relationship between gene body DNA methylation and intragenic H3K9me3 and H3K36me3 chromatin marks."
      Hahn M.A., Wu X., Li A.X., Hahn T., Pfeifer G.P.
      PLoS ONE 6:E18844-E18844(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624; SER-754 AND SER-2082, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha."
      Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.
      Cell 153:590-600(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INVOLVEMENT IN RCC, VARIANTS ASP-1733 AND PRO-1769, CHARACTERIZATION OF VARIANTS ASP-1733 AND PRO-1769.
    27. "Comprehensive molecular characterization of clear cell renal cell carcinoma."
      Creighton C.J., Morgan M., Gunaratne P.H., Wheeler D.A., Gibbs R.A., Gordon Robertson A., Chu A., Beroukhim R., Cibulskis K., Signoretti S., Vandin Hsin-Ta Wu F., Raphael B.J., Verhaak R.G., Tamboli P., Torres-Garcia W., Akbani R., Weinstein J.N., Reuter V.
      , Hsieh J.J., Rose Brannon A., Ari Hakimi A., Jacobsen A., Ciriello G., Reva B., Ricketts C.J., Marston Linehan W., Stuart J.M., Kimryn Rathmell W., Shen H., Laird P.W., Muzny D., Davis C., Morgan M., Xi L., Chang K., Kakkar N., Trevino L.R., Benton S., Reid J.G., Morton D., Doddapaneni H., Han Y., Lewis L., Dinh H., Kovar C., Zhu Y., Santibanez J., Wang M., Hale W., Kalra D., Creighton C.J., Wheeler D.A., Gibbs R.A., Getz G., Cibulskis K., Lawrence M.S., Sougnez C., Carter S.L., Sivachenko A., Lichtenstein L., Stewart C., Voet D., Fisher S., Gabriel S.B., Lander E., Beroukhim R., Schumacher S.E., Tabak B., Saksena G., Onofrio R.C., Carter S.L., Cherniack A.D., Gentry J., Ardlie K., Sougnez C., Getz G., Gabriel S.B., Meyerson M., Gordon Robertson A., Chu A., Chun H.J., Mungall A.J., Sipahimalani P., Stoll D., Ally A., Balasundaram M., Butterfield Y.S., Carlsen R., Carter C., Chuah E., Coope R.J., Dhalla N., Gorski S., Guin R., Hirst C., Hirst M., Holt R.A., Lebovitz C., Lee D., Li H.I., Mayo M., Moore R.A., Pleasance E., Plettner P., Schein J.E., Shafiei A., Slobodan J.R., Tam A., Thiessen N., Varhol R.J., Wye N., Zhao Y., Birol I., Jones S.J., Marra M.A., Auman J.T., Tan D., Jones C.D., Hoadley K.A., Mieczkowski P.A., Mose L.E., Jefferys S.R., Topal M.D., Liquori C., Turman Y.J., Shi Y., Waring S., Buda E., Walsh J., Wu J., Bodenheimer T., Hoyle A.P., Simons J.V., Soloway M.G., Balu S., Parker J.S., Neil Hayes D., Perou C.M., Kucherlapati R., Park P., Shen H., Triche T. Jr., Weisenberger D.J., Lai P.H., Bootwalla M.S., Maglinte D.T., Mahurkar S., Berman B.P., Van Den Berg D.J., Cope L., Baylin S.B., Laird P.W., Creighton C.J., Wheeler D.A., Getz G., Noble M.S., Dicara D., Zhang H., Cho J., Heiman D.I., Gehlenborg N., Voet D., Mallard W., Lin P., Frazer S., Stojanov P., Liu Y., Zhou L., Kim J., Lawrence M.S., Chin L., Vandin F., Wu H.T., Raphael B.J., Benz C., Yau C., Reynolds S.M., Shmulevich I., Verhaak R.G., Torres-Garcia W., Vegesna R., Kim H., Zhang W., Cogdell D., Jonasch E., Ding Z., Lu Y., Akbani R., Zhang N., Unruh A.K., Casasent T.D., Wakefield C., Tsavachidou D., Chin L., Mills G.B., Weinstein J.N., Jacobsen A., Rose Brannon A., Ciriello G., Schultz N., Ari Hakimi A., Reva B., Antipin Y., Gao J., Cerami E., Gross B., Arman Aksoy B., Sinha R., Weinhold N., Onur Sumer S., Taylor B.S., Shen R., Ostrovnaya I., Hsieh J.J., Berger M.F., Ladanyi M., Sander C., Fei S.S., Stout A., Spellman P.T., Rubin D.L., Liu T.T., Stuart J.M., Ng S., Paull E.O., Carlin D., Goldstein T., Waltman P., Ellrott K., Zhu J., Haussler D., Gunaratne P.H., Xiao W., Shelton C., Gardner J., Penny R., Sherman M., Mallery D., Morris S., Paulauskis J., Burnett K., Shelton T., Signoretti S., Kaelin W.G., Choueiri T., Atkins M.B., Penny R., Burnett K., Mallery D., Curley E., Tickoo S., Reuter V., Kimryn Rathmell W., Thorne L., Boice L., Huang M., Fisher J.C., Marston Linehan W., Vocke C.D., Peterson J., Worrell R., Merino M.J., Schmidt L.S., Tamboli P., Czerniak B.A., Aldape K.D., Wood C.G., Boyd J., Weaver J., Iacocca M.V., Petrelli N., Witkin G., Brown J., Czerwinski C., Huelsenbeck-Dill L., Rabeno B., Myers J., Morrison C., Bergsten J., Eckman J., Harr J., Smith C., Tucker K., Anne Zach L., Bshara W., Gaudioso C., Morrison C., Dhir R., Maranchie J., Nelson J., Parwani A., Potapova O., Fedosenko K., Cheville J.C., Houston Thompson R., Signoretti S., Kaelin W.G., Atkins M.B., Tickoo S., Reuter V., Marston Linehan W., Vocke C.D., Peterson J., Merino M.J., Schmidt L.S., Tamboli P., Mosquera J.M., Rubin M.A., Blute M.L., Kimryn Rathmell W., Pihl T., Jensen M., Sfeir R., Kahn A., Chu A., Kothiyal P., Snyder E., Pontius J., Ayala B., Backus M., Walton J., Baboud J., Berton D., Nicholls M., Srinivasan D., Raman R., Girshik S., Kigonya P., Alonso S., Sanbhadti R., Barletta S., Pot D., Sheth M., Demchok J.A., Davidsen T., Wang Z., Yang L., Tarnuzzer R.W., Zhang J., Eley G., Ferguson M.L., Mills Shaw K.R., Guyer M.S., Ozenberger B.A., Sofia H.J.
      Nature 499:43-49(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RCC.
    28. "Histone methyltransferase SETD2 coordinates FACT recruitment with nucleosome dynamics during transcription."
      Carvalho S., Raposo A.C., Martins F.B., Grosso A.R., Sridhara S.C., Rino J., Carmo-Fonseca M., de Almeida S.F.
      Nucleic Acids Res. 41:2881-2893(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-614 AND THR-1853, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    30. "Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1."
      Li M., Phatnani H.P., Guan Z., Sage H., Greenleaf A.L., Zhou P.
      Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2457-2564, INTERACTION WITH POLR2A, MUTAGENESIS OF ARG-2475; LYS-2476; GLN-2480; PHE-2481; VAL-2483; PHE-2505; LYS-2506; ARG-2510; HIS-2514; GLY-2515; GLU-2528 AND GLU-2531.
    31. "Sinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2."
      Zheng W., Ibanez G., Wu H., Blum G., Zeng H., Dong A., Li F., Hajian T., Allali-Hassani A., Amaya M.F., Siarheyeva A., Yu W., Brown P.J., Schapira M., Vedadi M., Min J., Luo M.
      J. Am. Chem. Soc. 134:18004-18014(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1434-1711 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE OR N-PROPYL SINEFUNGIN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF PHE-1668; GLN-1669; ARG-1670 AND TYR-1671.

    Entry informationi

    Entry nameiSETD2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYW2
    Secondary accession number(s): O75397
    , O75405, Q17RW8, Q5BKS9, Q5QGN2, Q69YI5, Q6IN64, Q6ZN53, Q6ZS25, Q8N3R0, Q8TCN0, Q9C0D1, Q9H696, Q9NZW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: May 18, 2010
    Last modified: June 24, 2015
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.