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Q9BYW2 (SETD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SETD2
Synonyms:HIF1, HYPB, KIAA1732, KMT3A, SET2
ORF Names:HSPC069
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.15 Ref.23 Ref.24 Ref.26 Ref.28 Ref.30

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.30

Enzyme regulation

Specifically inhibited by sinefungin derivatives. N-propyl sinefungin (Pr-SNF) interacts preferentially with SETD2. Ref.30

Subunit structure

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. Ref.4 Ref.6 Ref.11 Ref.12 Ref.14 Ref.15 Ref.19 Ref.29

Subcellular location

Nucleus Probable. Chromosome Probable.

Tissue specificity

Ubiquitously expressed. Ref.4

Domain

The low charge region mediates the transcriptional activation activity (Ref.6).

Post-translational modification

May be automethylated. Ref.6

Involvement in disease

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.
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 (Ref.27). Ref.21 Ref.26 Ref.27

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.

Contains 1 AWS domain.

Contains 1 post-SET domain.

Contains 1 SET domain.

Contains 1 WW domain.

Biophysicochemical properties

Kinetic parameters:

Kcat is 0.14 min(-1).

KM=1.21 µM for S-adenosyl-L-methionine Ref.30

KM=0.42 µM for histone H3

Sequence caution

The sequence AAF29041.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAH72440.1 differs from that shown. Reason: Erroneous termination at position 463. Translated as Glu.

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 BAB15367.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAC87131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC28349.1 differs from that shown. Reason: Erroneous termination at position 385. Translated as Arg.

The sequence CAD38601.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandS-adenosyl-L-methionine
   Molecular functionActivator
Chromatin regulator
Methyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: Ensembl

cell migration involved in vasculogenesis

Inferred from electronic annotation. Source: Ensembl

coronary vasculature morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic placenta morphogenesis

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

histone H3-K36 trimethylation

Inferred from direct assay Ref.30. Source: UniProtKB

mesoderm morphogenesis

Inferred from electronic annotation. Source: Ensembl

mismatch repair

Inferred from mutant phenotype Ref.26. Source: UniProtKB

morphogenesis of a branching structure

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

nucleosome organization

Inferred from mutant phenotype Ref.28. Source: UniProtKB

pericardium development

Inferred from electronic annotation. Source: Ensembl

regulation of mRNA export from nucleus

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

stem cell development

Inferred from electronic annotation. Source: Ensembl

transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype Ref.28. Source: UniProtKB

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone-lysine N-methyltransferase activity

Inferred from direct assay Ref.30. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYW2-1)

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.
Isoform 2 (identifier: Q9BYW2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1715-2564: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9BYW2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1573-2564: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25642564Histone-lysine N-methyltransferase SETD2
PRO_0000252367

Regions

Domain1494 – 154855AWS
Domain1550 – 1667118SET
Domain1674 – 169017Post-SET
Domain2389 – 242234WW
Region1560 – 15623Inhibitor binding
Region1560 – 15623S-adenosyl-L-methionine binding
Region1603 – 16053Inhibitor binding
Region1603 – 16053S-adenosyl-L-methionine binding
Region1628 – 16292Inhibitor binding
Region1628 – 16292S-adenosyl-L-methionine binding
Region2137 – 2366230Low charge region
Region2457 – 2564108Interaction with POLR2A
Coiled coil2117 – 214630 Potential
Compositional bias166 – 24782Pro-rich
Compositional bias385 – 45672Arg-rich
Compositional bias2149 – 223284Pro-rich
Compositional bias2266 – 2365100Gln-rich

Sites

Binding site16251Inhibitor
Binding site16761Inhibitor; alternate
Binding site16761S-adenosyl-L-methionine; alternate
Binding site16791Inhibitor; via amide nitrogen; alternate
Binding site16791S-adenosyl-L-methionine; via amide nitrogen; alternate

Amino acid modifications

Modified residue1311Phosphoserine Ref.20
Modified residue3211Phosphoserine Ref.17 Ref.20 Ref.22 Ref.25
Modified residue3231Phosphoserine Ref.17 Ref.20 Ref.22 Ref.25
Modified residue6241Phosphoserine Ref.17 Ref.22 Ref.25
Modified residue7081Phosphoserine Ref.20
Modified residue7441Phosphoserine Ref.20
Modified residue7541Phosphoserine Ref.17 Ref.20 Ref.25
Modified residue12281Phosphoserine Ref.16 Ref.17
Modified residue14131Phosphoserine By similarity
Modified residue14151Phosphoserine By similarity
Modified residue14171Phosphoserine By similarity
Modified residue18721Phosphothreonine Ref.17 Ref.22
Modified residue20801Phosphoserine Ref.17
Modified residue20821Phosphoserine Ref.17 Ref.25

Natural variations

Alternative sequence1573 – 2564992Missing in isoform 3.
VSP_020914
Alternative sequence1715 – 2564850Missing in isoform 2.
VSP_020915
Natural variant7681V → L.
Corresponds to variant rs9311404 [ dbSNP | Ensembl ].
VAR_027839
Natural variant9021E → Q.
Corresponds to variant rs58906143 [ dbSNP | Ensembl ].
VAR_061216
Natural variant17331N → D in RCC cell line; defects in recruitment of the MutS alpha complex. Ref.26
VAR_069812
Natural variant17691S → P in RCC cell line; defects in recruitment of the MutS alpha complex. Ref.26
VAR_069813
Natural variant18681A → D.
Corresponds to variant rs11721074 [ dbSNP | Ensembl ].
VAR_027840
Natural variant19621P → L. Ref.5 Ref.8
Corresponds to variant rs4082155 [ dbSNP | Ensembl ].
VAR_027841

Experimental info

Mutagenesis16251R → H: Loss of methyltransferase activity. Ref.6
Mutagenesis16681F → A: Loss of methyltransferase activity. Ref.30
Mutagenesis16691Q → A: Loss of methyltransferase activity. Ref.30
Mutagenesis16701R → A, V, L, I or F: Impaired methyltransferase activity. Ref.30
Mutagenesis16701R → P, W, K or Q: Loss of methyltransferase activity. Ref.30
Mutagenesis16711Y → A: Loss of methyltransferase activity. Ref.30
Mutagenesis24751R → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis24761K → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis24801Q → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis24811F → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis24831V → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25051F → L: Impairs interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25061K → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25101R → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25141H → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25151G → A or T: Does not affect interaction with hyperphosphorylated POLR2A. Ref.29
Mutagenesis25281E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531. Ref.29
Mutagenesis25311E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528. Ref.29
Sequence conflict4481R → Q in BAD18522. Ref.2
Sequence conflict4551A → V in CAD38601. Ref.3
Sequence conflict9121L → P in BAB15367. Ref.2
Sequence conflict9641E → K in CAC28349. Ref.4
Sequence conflict9641E → K in AAT77612. Ref.6
Sequence conflict9641E → K in AAT77613. Ref.7
Sequence conflict10801M → I in BAC87131. Ref.2
Sequence conflict10801M → T in CAD38601. Ref.3
Sequence conflict12121V → F in BAD18522. Ref.2
Sequence conflict12691T → A in CAC28349. Ref.4
Sequence conflict12691T → A in AAT77612. Ref.6
Sequence conflict12691T → A in AAT77613. Ref.7
Sequence conflict13381E → G in BAB15367. Ref.2
Sequence conflict14981Q → R in CAD38601. Ref.3
Sequence conflict17061K → N in AAF29041. Ref.10
Sequence conflict17361L → P in CAC28349. Ref.4
Sequence conflict17361L → P in AAT77612. Ref.6

Secondary structure

.......................................................... 2564
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 2B1BAE5867AB8EAB

FASTA2,564287,597
        10         20         30         40         50         60 
MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA SSRFLPKGTK 

        70         80         90        100        110        120 
TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT PNPPAVPLQV DSTPKMKMEI 

       130        140        150        160        170        180 
GDTLSTAEES SPPKSRVELG KIHFKKHLLH VTSRPLLATT TAVASPPTHA APLPAVIAES 

       190        200        210        220        230        240 
TTVDSPPSSP PPPPPPAQAT TLSSPAPVTE PVALPHTPIT VLMAAPVPLP VDVAVRSLKE 

       250        260        270        280        290        300 
PPIIIVPESL EADTKQDTIS NSLEEHVTQI LNEQADISSK KEDSHIGKDE EIPDSSKISL 

       310        320        330        340        350        360 
SCKKTGSKKK SSQSEGIFLG SESDEDSVRT SSSQRSHDLK FSASIEKERD FKKSSAPLKS 

       370        380        390        400        410        420 
EDLGKPSRSK TDRDDKYFSY SKLERDTRYV SSRCRSERER RRSRSHSRSE RGSRTNLSYS 

       430        440        450        460        470        480 
RSERSHYYDS DRRYHRSSPY RERTRYSRPY TDNRARESSD SEEEYKKTYS RRTSSHSSSY 

       490        500        510        520        530        540 
RDLRTSSYSK SDRDCKTETS YLEMERRGKY SSKLERESKR TSENEAIKRC CSPPNELGFR 

       550        560        570        580        590        600 
RGSSYSKHDS SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL 

       610        620        630        640        650        660 
RMINKNPERE KAGSPAPSNR LNDSPTLKKL DELPIFKSEF ITHDSHDSIK ELDSLSKVKN 

       670        680        690        700        710        720 
DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD SVTGSELSPL VKACMLSSNG 

       730        740        750        760        770        780 
FQNISRCKEK DLDDTCMLHK KSESPFRETE PLVSPHQDKL MSMPVMTVDY SKTVVKEPVD 

       790        800        810        820        830        840 
TRVSCCKTKD SDIYCTLNDS NPSLCNSEAE NIEPSVMKIS SNSFMNVHLE SKPVICDSRN 

       850        860        870        880        890        900 
LTDHSKFACE EYKQSIGSTS SASVNHFDDL YQPIGSSGIA SSLQSLPPGI KVDSLTLLKC 

       910        920        930        940        950        960 
GENTSPVLDA VLKSKKSSEF LKHAGKETIV EVGSDLPDSG KGFASRENRR NNGLSGKCLQ 

       970        980        990       1000       1010       1020 
EAQEEGNSIL PERRGRPEIS LDERGEGGHV HTSDDSEVVF SSCDLNLTME DSDGVTYALK 

      1030       1040       1050       1060       1070       1080 
CDSSGHAPEI VSTVHEDYSG SSESSNDESD SEDTDSDDSS IPRNRLQSVV VVPKNSTLPM 

      1090       1100       1110       1120       1130       1140 
EETSPCSSRS SQSYRHYSDH WEDERLESRR HLYEEKFESI ASKACPQTDK FFLHKGTEKN 

      1150       1160       1170       1180       1190       1200 
PEISFTQSSR KQIDNRLPEL SHPQSDGVDS TSHTDVKSDP LGHPNSEETV KAKIPSRQQE 

      1210       1220       1230       1240       1250       1260 
ELPIYSSDFE DVPNKSWQQT TFQNRPDSRL GKTELSFSSS CEIPHVDGLH SSEELRNLGW 

      1270       1280       1290       1300       1310       1320 
DFSQEKPSTT YQQPDSSYGA CGGHKYQQNA EQYGGTRDYW QGNGYWDPRS GRPPGTGVVY 

      1330       1340       1350       1360       1370       1380 
DRTQGQVPDS LTDDREEEEN WDQQDGSHFS DQSDKFLLSL QKDKGSVQAP EISSNSIKDT 

      1390       1400       1410       1420       1430       1440 
LAVNEKKDFS KNLEKNDIKD RGPLKKRRQE IESDSESDGE LQDRKKVRVE VEQGETSVPP 

      1450       1460       1470       1480       1490       1500 
GSALVGPSCV MDDFRDPQRW KECAKQGKMP CYFDLIEENV YLTERKKNKS HRDIKRMQCE 

      1510       1520       1530       1540       1550       1560 
CTPLSKDERA QGEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA DVEVILTEKK 

      1570       1580       1590       1600       1610       1620 
GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK ARVKEYARNK NIHYYFMALK NDEIIDATQK 

      1630       1640       1650       1660       1670       1680 
GNCSRFMNHS CEPNCETQKW TVNGQLRVGF FTTKLVPSGS ELTFDYQFQR YGKEAQKCFC 

      1690       1700       1710       1720       1730       1740 
GSANCRGYLG GENRVSIRAA GGKMKKERSR KKDSVDGELE ALMENGEGLS DKNQVLSLSR 

      1750       1760       1770       1780       1790       1800 
LMVRIETLEQ KLTCLELIQN THSQSCLKSF LERHGLSLLW IWMAELGDGR ESNQKLQEEI 

      1810       1820       1830       1840       1850       1860 
IKTLEHLPIP TKNMLEESKV LPIIQRWSQT KTAVPPLSEG DGYSSENTSR AHTPLNTPDP 

      1870       1880       1890       1900       1910       1920 
STKLSTEADT DTPKKLMFRR LKIISENSMD SAISDATSEL EGKDGKEDLD QLENVPVEEE 

      1930       1940       1950       1960       1970       1980 
EELQSQQLLP QQLPECKVDS ETNIEASKLP TSEPEADAEI EPKESNGTKL EEPINEETPS 

      1990       2000       2010       2020       2030       2040 
QDEEEGVSDV ESERSQEQPD KTVDISDLAT KLLDSWKDLK EVYRIPKKSQ TEKENTTTER 

      2050       2060       2070       2080       2090       2100 
GRDAVGFRDQ TPAPKTPNRS RERDPDKQTQ NKEKRKRRSS LSPPSSAYER GTKRPDDRYD 

      2110       2120       2130       2140       2150       2160 
TPTSKKKVRI KDRNKLSTEE RRKLFEQEVA QREAQKQQQQ MQNLGMTSPL PYDSLGYNAP 

      2170       2180       2190       2200       2210       2220 
HHPFAGYPPG YPMQAYVDPS NPNAGKVLLP TPSMDPVCSP APYDHAQPLV GHSTEPLSAP 

      2230       2240       2250       2260       2270       2280 
PPVPVVPHVA APVEVSSSQY VAQSDGVVHQ DSSVAVLPVP APGPVQGQNY SVWDSNQQSV 

      2290       2300       2310       2320       2330       2340 
SVQQQYSPAQ SQATIYYQGQ TCPTVYGVTS PYSQTTPPIV QSYAQPSLQY IQGQQIFTAH 

      2350       2360       2370       2380       2390       2400 
PQGVVVQPAA AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV LPPNWKTARD 

      2410       2420       2430       2440       2450       2460 
PEGKIYYYHV ITRQTQWDPP TWESPGDDAS LEHEAEMDLG TPTYDENPMK ASKKPKTAEA 

      2470       2480       2490       2500       2510       2520 
DTSSELAKKS KEVFRKEMSQ FIVQCLNPYR KPDCKVGRIT TTEDFKHLAR KLTHGVMNKE 

      2530       2540       2550       2560 
LKYCKNPEDL ECNENVKHKT KEYIKKYMQK FGAVYKPKED TELE 

« Hide

Isoform 2 [UniParc].

Checksum: BD566E360FCF0E9B
Show »

FASTA1,714192,342
Isoform 3 [UniParc].

Checksum: 1FAC3FE752C0777C
Show »

FASTA1,572175,982

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Huntingtin interacts with a family of WW domain proteins."
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E.
Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes."
Dalgliesh G.L., Furge K., Greenman C., Chen L., Bignell G., Butler A., Davies H., Edkins S., Hardy C., Latimer C., Teague J., Andrews J., Barthorpe S., Beare D., Buck G., Campbell P.J., Forbes S., Jia M. expand/collapse author list , Jones D., Knott H., Kok C.Y., Lau K.W., Leroy C., Lin M.L., McBride D.J., Maddison M., Maguire S., McLay K., Menzies A., Mironenko T., Mulderrig L., Mudie L., O'Meara S., Pleasance E., Rajasingham A., Shepherd R., Smith R., Stebbings L., Stephens P., Tang G., Tarpey P.S., Turrell K., Dykema K.J., Khoo S.K., Petillo D., Wondergem B., Anema J., Kahnoski R.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 463:360-363(2010) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2749.2. [Q9BYW2-1]
RefSeqNP_054878.5. NM_014159.6. [Q9BYW2-1]
UniGeneHs.517941.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7ONMR-A2457-2564[»]
4FMUX-ray2.10A1434-1711[»]
4H12X-ray1.99A1434-1711[»]
ProteinModelPortalQ9BYW2.
SMRQ9BYW2. Positions 1447-1691, 2462-2561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118845. 17 interactions.
IntActQ9BYW2. 10 interactions.
MINTMINT-1537591.

PTM databases

PhosphoSiteQ9BYW2.

Polymorphism databases

DMDM296452963.

2D gel databases

OGPQ9BYW2.

Proteomic databases

MaxQBQ9BYW2.
PaxDbQ9BYW2.
PRIDEQ9BYW2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000409792; ENSP00000386759; ENSG00000181555. [Q9BYW2-1]
GeneID29072.
KEGGhsa:29072.
UCSCuc003cqs.3. human. [Q9BYW2-1]

Organism-specific databases

CTD29072.
GeneCardsGC03M047033.
H-InvDBHIX0021942.
HIX0163343.
HGNCHGNC:18420. SETD2.
HPAHPA042451.
MIM144700. phenotype.
612778. gene.
neXtProtNX_Q9BYW2.
PharmGKBPA143485612.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG093939.
InParanoidQ9BYW2.
KOK11423.
OMAVMDDFRD.
PhylomeDBQ9BYW2.
TreeFamTF106477.

Enzyme and pathway databases

SignaLinkQ9BYW2.

Gene expression databases

ArrayExpressQ9BYW2.
BgeeQ9BYW2.
CleanExHS_SETD2.
GenevestigatorQ9BYW2.

Family and domain databases

InterProIPR006560. AWS.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS51215. 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]
ProtoNetSearch...

Other

ChiTaRSSETD2. human.
EvolutionaryTraceQ9BYW2.
GeneWikiSETD2.
GenomeRNAi29072.
NextBio52031.
PROQ9BYW2.
SOURCESearch...

Entry information

Entry nameSETD2_HUMAN
AccessionPrimary (citable) accession number: Q9BYW2
Secondary accession number(s): O75397 expand/collapse secondary AC list , O75405, Q17RW8, Q5BKS9, Q5QGN2, Q69YI5, Q6IN64, Q6ZN53, Q6ZS25, Q8N3R0, Q8TCN0, Q9C0D1, Q9H696, Q9NZW9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM