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Q9BYW2

- SETD2_HUMAN

UniProt

Q9BYW2 - SETD2_HUMAN

Protein

Histone-lysine N-methyltransferase SETD2

Gene

SETD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      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. 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

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    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: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18420. SETD2.

    Subcellular locationi

    Nucleus Curated. Chromosome Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Renal cell carcinoma (RCC) [MIM:144700]: Renal 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.3 Publications
    Note: 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).1 Publication
    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.
    PharmGKBiPA143485612.

    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 – 3211Phosphoserine4 Publications
    Modified residuei323 – 3231Phosphoserine4 Publications
    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 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

    ArrayExpressiQ9BYW2.
    BgeeiQ9BYW2.
    CleanExiHS_SETD2.
    GenevestigatoriQ9BYW2.

    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. 17 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 – 14503
    Helixi1451 – 14555
    Helixi1457 – 14659
    Beta strandi1480 – 14823
    Helixi1506 – 15116
    Helixi1523 – 15253
    Helixi1536 – 15383
    Turni1543 – 15475
    Beta strandi1552 – 15565
    Beta strandi1558 – 156811
    Beta strandi1575 – 15784
    Beta strandi1582 – 15843
    Helixi1586 – 159813
    Beta strandi1606 – 16105
    Beta strandi1613 – 16164
    Beta strandi1618 – 16214
    Helixi1623 – 16264
    Beta strandi1634 – 16429
    Beta strandi1645 – 165410
    Beta strandi1661 – 16644
    Turni1667 – 16693
    Beta strandi1687 – 16893
    Helixi2463 – 248624
    Turni2487 – 24893
    Beta strandi2495 – 24984
    Helixi2502 – 252423
    Helixi2527 – 25293
    Helixi2534 – 254815
    Turni2549 – 25513
    Helixi2557 – 25593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A7ONMR-A2457-2564[»]
    4FMUX-ray2.10A1434-1711[»]
    4H12X-ray1.99A1434-1711[»]
    ProteinModelPortaliQ9BYW2.
    SMRiQ9BYW2. Positions 1447-1691, 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.
    HOVERGENiHBG093939.
    InParanoidiQ9BYW2.
    KOiK11423.
    OMAiVMDDFRD.
    PhylomeDBiQ9BYW2.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA     50
    SSRFLPKGTK TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT 100
    PNPPAVPLQV DSTPKMKMEI GDTLSTAEES SPPKSRVELG KIHFKKHLLH 150
    VTSRPLLATT TAVASPPTHA APLPAVIAES TTVDSPPSSP PPPPPPAQAT 200
    TLSSPAPVTE PVALPHTPIT VLMAAPVPLP VDVAVRSLKE PPIIIVPESL 250
    EADTKQDTIS NSLEEHVTQI LNEQADISSK KEDSHIGKDE EIPDSSKISL 300
    SCKKTGSKKK SSQSEGIFLG SESDEDSVRT SSSQRSHDLK FSASIEKERD 350
    FKKSSAPLKS EDLGKPSRSK TDRDDKYFSY SKLERDTRYV SSRCRSERER 400
    RRSRSHSRSE RGSRTNLSYS RSERSHYYDS DRRYHRSSPY RERTRYSRPY 450
    TDNRARESSD SEEEYKKTYS RRTSSHSSSY RDLRTSSYSK SDRDCKTETS 500
    YLEMERRGKY SSKLERESKR TSENEAIKRC CSPPNELGFR RGSSYSKHDS 550
    SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL 600
    RMINKNPERE KAGSPAPSNR LNDSPTLKKL DELPIFKSEF ITHDSHDSIK 650
    ELDSLSKVKN DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD 700
    SVTGSELSPL VKACMLSSNG FQNISRCKEK DLDDTCMLHK KSESPFRETE 750
    PLVSPHQDKL MSMPVMTVDY SKTVVKEPVD TRVSCCKTKD SDIYCTLNDS 800
    NPSLCNSEAE NIEPSVMKIS SNSFMNVHLE SKPVICDSRN LTDHSKFACE 850
    EYKQSIGSTS SASVNHFDDL YQPIGSSGIA SSLQSLPPGI KVDSLTLLKC 900
    GENTSPVLDA VLKSKKSSEF LKHAGKETIV EVGSDLPDSG KGFASRENRR 950
    NNGLSGKCLQ EAQEEGNSIL PERRGRPEIS LDERGEGGHV HTSDDSEVVF 1000
    SSCDLNLTME DSDGVTYALK CDSSGHAPEI VSTVHEDYSG SSESSNDESD 1050
    SEDTDSDDSS IPRNRLQSVV VVPKNSTLPM EETSPCSSRS SQSYRHYSDH 1100
    WEDERLESRR HLYEEKFESI ASKACPQTDK FFLHKGTEKN PEISFTQSSR 1150
    KQIDNRLPEL SHPQSDGVDS TSHTDVKSDP LGHPNSEETV KAKIPSRQQE 1200
    ELPIYSSDFE DVPNKSWQQT TFQNRPDSRL GKTELSFSSS CEIPHVDGLH 1250
    SSEELRNLGW DFSQEKPSTT YQQPDSSYGA CGGHKYQQNA EQYGGTRDYW 1300
    QGNGYWDPRS GRPPGTGVVY DRTQGQVPDS LTDDREEEEN WDQQDGSHFS 1350
    DQSDKFLLSL QKDKGSVQAP EISSNSIKDT LAVNEKKDFS KNLEKNDIKD 1400
    RGPLKKRRQE IESDSESDGE LQDRKKVRVE VEQGETSVPP GSALVGPSCV 1450
    MDDFRDPQRW KECAKQGKMP CYFDLIEENV YLTERKKNKS HRDIKRMQCE 1500
    CTPLSKDERA QGEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA 1550
    DVEVILTEKK GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK ARVKEYARNK 1600
    NIHYYFMALK NDEIIDATQK GNCSRFMNHS CEPNCETQKW TVNGQLRVGF 1650
    FTTKLVPSGS ELTFDYQFQR YGKEAQKCFC GSANCRGYLG GENRVSIRAA 1700
    GGKMKKERSR KKDSVDGELE ALMENGEGLS DKNQVLSLSR LMVRIETLEQ 1750
    KLTCLELIQN THSQSCLKSF LERHGLSLLW IWMAELGDGR ESNQKLQEEI 1800
    IKTLEHLPIP TKNMLEESKV LPIIQRWSQT KTAVPPLSEG DGYSSENTSR 1850
    AHTPLNTPDP STKLSTEADT DTPKKLMFRR LKIISENSMD SAISDATSEL 1900
    EGKDGKEDLD QLENVPVEEE EELQSQQLLP QQLPECKVDS ETNIEASKLP 1950
    TSEPEADAEI EPKESNGTKL EEPINEETPS QDEEEGVSDV ESERSQEQPD 2000
    KTVDISDLAT KLLDSWKDLK EVYRIPKKSQ TEKENTTTER GRDAVGFRDQ 2050
    TPAPKTPNRS RERDPDKQTQ NKEKRKRRSS LSPPSSAYER GTKRPDDRYD 2100
    TPTSKKKVRI KDRNKLSTEE RRKLFEQEVA QREAQKQQQQ MQNLGMTSPL 2150
    PYDSLGYNAP HHPFAGYPPG YPMQAYVDPS NPNAGKVLLP TPSMDPVCSP 2200
    APYDHAQPLV GHSTEPLSAP PPVPVVPHVA APVEVSSSQY VAQSDGVVHQ 2250
    DSSVAVLPVP APGPVQGQNY SVWDSNQQSV SVQQQYSPAQ SQATIYYQGQ 2300
    TCPTVYGVTS PYSQTTPPIV QSYAQPSLQY IQGQQIFTAH PQGVVVQPAA 2350
    AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV LPPNWKTARD 2400
    PEGKIYYYHV ITRQTQWDPP TWESPGDDAS LEHEAEMDLG TPTYDENPMK 2450
    ASKKPKTAEA DTSSELAKKS KEVFRKEMSQ FIVQCLNPYR KPDCKVGRIT 2500
    TTEDFKHLAR KLTHGVMNKE LKYCKNPEDL ECNENVKHKT KEYIKKYMQK 2550
    FGAVYKPKED TELE 2564
    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 BAB15367.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAF29041.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAI17163.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAI17165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAT77612.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAT77613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15367.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC87131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAD38601.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH72440.1 differs from that shown. Reason: Erroneous termination at position 463. Translated as Glu.
    The sequence CAC28349.1 differs from that shown. Reason: Erroneous termination at position 385. Translated as Arg.

    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. 1 PublicationCurated
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi296452963.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2749.2. [Q9BYW2-1 ]
    RefSeqi NP_054878.5. NM_014159.6. [Q9BYW2-1 ]
    UniGenei Hs.517941.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A7O NMR - A 2457-2564 [» ]
    4FMU X-ray 2.10 A 1434-1711 [» ]
    4H12 X-ray 1.99 A 1434-1711 [» ]
    ProteinModelPortali Q9BYW2.
    SMRi Q9BYW2. Positions 1447-1691, 2462-2561.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118845. 17 interactions.
    IntActi Q9BYW2. 10 interactions.
    MINTi MINT-1537591.

    PTM databases

    PhosphoSitei Q9BYW2.

    Polymorphism databases

    DMDMi 296452963.

    2D gel databases

    OGPi Q9BYW2.

    Proteomic databases

    MaxQBi Q9BYW2.
    PaxDbi Q9BYW2.
    PRIDEi Q9BYW2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000409792 ; ENSP00000386759 ; ENSG00000181555 . [Q9BYW2-1 ]
    GeneIDi 29072.
    KEGGi hsa:29072.
    UCSCi uc003cqs.3. human. [Q9BYW2-1 ]

    Organism-specific databases

    CTDi 29072.
    GeneCardsi GC03M047033.
    H-InvDB HIX0021942.
    HIX0163343.
    HGNCi HGNC:18420. SETD2.
    HPAi HPA042451.
    MIMi 144700. phenotype.
    612778. gene.
    neXtProti NX_Q9BYW2.
    PharmGKBi PA143485612.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG093939.
    InParanoidi Q9BYW2.
    KOi K11423.
    OMAi VMDDFRD.
    PhylomeDBi Q9BYW2.
    TreeFami TF106477.

    Enzyme and pathway databases

    SignaLinki Q9BYW2.

    Miscellaneous databases

    ChiTaRSi SETD2. human.
    EvolutionaryTracei Q9BYW2.
    GeneWikii SETD2.
    GenomeRNAii 29072.
    NextBioi 52031.
    PROi Q9BYW2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYW2.
    Bgeei Q9BYW2.
    CleanExi HS_SETD2.
    Genevestigatori Q9BYW2.

    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. "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. "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.
    30. "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: October 1, 2014
    This is version 118 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