Q9BYW2 (SETD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SETD2
Synonyms:	HIF1, HYPB, KIAA1732, KMT3A, SET2
ORF Names:	HSPC069

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2564 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression. Ref.6
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subunit structure	Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Binds specifically to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad. Interacts with HTT. Ref.4 Ref.6 Ref.11 Ref.12 Ref.19
Subcellular location	Nucleus Probable. Chromosome Probable.
Tissue specificity	Ubiquitously expressed. Ref.4
Domain	The low charge region mediates the transcriptional activation activity.
Post-translational modification	May be automethylated. Ref.6
Sequence similarities	Belongs to the histone-lysine methyltransferase family. SET2 subfamily. Contains 1 AWS domain. Contains 1 post-SET domain. Contains 1 SET domain. Contains 1 WW domain.
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 process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	DNA-binding S-adenosyl-L-methionine
Molecular function	Activator Chromatin regulator Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara cell migration involved in vasculogenesis Inferred from electronic annotation. Source: Compara coronary vasculature morphogenesis Inferred from electronic annotation. Source: Compara embryonic cranial skeleton morphogenesis Inferred from electronic annotation. Source: Compara embryonic placenta morphogenesis Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara histone H3-K36 methylation Inferred from electronic annotation. Source: Compara mesoderm morphogenesis Inferred from electronic annotation. Source: Compara morphogenesis of a branching structure Inferred from electronic annotation. Source: Compara neural tube closure Inferred from electronic annotation. Source: Compara peptidyl-lysine trimethylation Inferred from electronic annotation. Source: Compara pericardium development Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW stem cell development Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC oxidoreductase activity Inferred from electronic annotation. Source: InterPro transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD3	P84022	2	EBI-945869,EBI-347161

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2564

2564

Histone-lysine N-methyltransferase SETD2

PRO_0000252367

Regions

Domain

1494 – 1548

55

AWS

Domain

1549 – 1671

123

SET

Domain

1674 – 1690

17

Post-SET

Domain

2389 – 2422

34

WW

Region

2137 – 2366

230

Low charge region

Region

2457 – 2564

108

Interaction with POLR2A

Coiled coil

2117 – 2146

30

Potential

Compositional bias

166 – 247

82

Pro-rich

Compositional bias

385 – 456

72

Arg-rich

Compositional bias

2149 – 2232

84

Pro-rich

Compositional bias

2266 – 2365

100

Gln-rich

Amino acid modifications

Modified residue

131

1

Phosphoserine Ref.16

Modified residue

321

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18

Modified residue

323

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18

Modified residue

624

1

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

708

1

Phosphoserine Ref.16

Modified residue

744

1

Phosphoserine Ref.16

Modified residue

754

1

Phosphoserine Ref.15 Ref.16 Ref.18

Modified residue

1228

1

Phosphoserine Ref.14 Ref.15

Modified residue

1872

1

Phosphothreonine Ref.15 Ref.17

Modified residue

2080

1

Phosphoserine Ref.15

Modified residue

2082

1

Phosphoserine Ref.15 Ref.18

Natural variations

Alternative sequence

1573 – 2564

992

Missing in isoform 3.

VSP_020914

Alternative sequence

1715 – 2564

850

Missing in isoform 2.

VSP_020915

Natural variant

768

1

V → L.
Corresponds to variant rs9311404 [ dbSNP | Ensembl ].

VAR_027839

Natural variant

902

1

E → Q.
Corresponds to variant rs58906143 [ dbSNP | Ensembl ].

VAR_061216

Natural variant

1868

1

A → D.
Corresponds to variant rs11721074 [ dbSNP | Ensembl ].

VAR_027840

Natural variant

1962

1

P → L. Ref.5 Ref.8
Corresponds to variant rs4082155 [ dbSNP | Ensembl ].

VAR_027841

Experimental info

Mutagenesis

1625

1

R → H: Loss of methyltransferase activity. Ref.6

Mutagenesis

2475

1

R → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2476

1

K → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2480

1

Q → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2481

1

F → A: Does not affect interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2483

1

V → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2505

1

F → L: Impairs interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2506

1

K → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2510

1

R → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2514

1

H → A: Impairs interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2515

1

G → A or T: Does not affect interaction with hyperphosphorylated POLR2A. Ref.19

Mutagenesis

2528

1

E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531. Ref.19

Mutagenesis

2531

1

E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528. Ref.19

Sequence conflict

448

1

R → Q in BAD18522. Ref.2

Sequence conflict

455

1

A → V in CAD38601. Ref.3

Sequence conflict

912

1

L → P in BAB15367. Ref.2

Sequence conflict

964

1

E → K in CAC28349. Ref.4

Sequence conflict

964

1

E → K in AAT77612. Ref.6

Sequence conflict

964

1

E → K in AAT77613. Ref.7

Sequence conflict

1080

1

M → I in BAC87131. Ref.2

Sequence conflict

1080

1

M → T in CAD38601. Ref.3

Sequence conflict

1212

1

V → F in BAD18522. Ref.2

Sequence conflict

1269

1

T → A in CAC28349. Ref.4

Sequence conflict

1269

1

T → A in AAT77612. Ref.6

Sequence conflict

1269

1

T → A in AAT77613. Ref.7

Sequence conflict

1338

1

E → G in BAB15367. Ref.2

Sequence conflict

1498

1

Q → R in CAD38601. Ref.3

Sequence conflict

1706

1

K → N in AAF29041. Ref.10

Sequence conflict

1736

1

L → P in CAC28349. Ref.4

Sequence conflict

1736

1

L → P in AAT77612. Ref.6

Secondary structure

1

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2564

Helix Strand Turn

Details...

Beta strand

1448 – 1450

3

Helix

1451 – 1455

5

Helix

1457 – 1465

9

Beta strand

1480 – 1482

3

Helix

1506 – 1511

6

Helix

1523 – 1525

3

Helix

1536 – 1538

3

Turn

1543 – 1547

5

Beta strand

1552 – 1556

5

Beta strand

1558 – 1568

11

Beta strand

1575 – 1578

4

Beta strand

1582 – 1584

3

Helix

1586 – 1598

13

Beta strand

1606 – 1610

5

Beta strand

1613 – 1616

4

Beta strand

1618 – 1621

4

Helix

1623 – 1626

4

Beta strand

1634 – 1642

9

Beta strand

1645 – 1654

10

Beta strand

1661 – 1664

4

Turn

1667 – 1669

3

Beta strand

1687 – 1689

3

Helix

2463 – 2486

24

Turn

2487 – 2489

3

Beta strand

2495 – 2498

4

Helix

2502 – 2524

23

Helix

2527 – 2529

3

Helix

2534 – 2548

15

Turn

2549 – 2551

3

Helix

2557 – 2559

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 2B1BAE5867AB8EAB	FASTA	2,564	287,597
	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
	Isoform 2 [UniParc]. Checksum: BD566E360FCF0E9B	FASTA	1,714	192,342
	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 GSANCRGYLG GENRVSIRAA GGKMKKERSR KKDS
	Isoform 3 [UniParc]. Checksum: 1FAC3FE752C0777C	FASTA	1,572	175,982
	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 GWGLRAAKDL PS

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, POSSIBLE METHYLATION, 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]	"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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
+	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.

IPI

IPI00307733.
IPI00442150.
IPI00796144.

RefSeq

NP_054878.5. NM_014159.6.

UniGene

Hs.517941.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9BYW2.

SMR

Q9BYW2. Positions 1447-1691, 2462-2561.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BYW2. 8 interactions.

MINT

MINT-1537591.

PTM databases

PhosphoSite

Q9BYW2.

Polymorphism databases

DMDM

296452963.

2D gel databases

OGP

Q9BYW2.

Proteomic databases

PaxDb

Q9BYW2.

PRIDE

Q9BYW2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000409792; ENSP00000386759; ENSG00000181555.

GeneID

29072.

KEGG

hsa:29072.

UCSC

uc003cqs.3. human.

Organism-specific databases

CTD

29072.

GeneCards

GC03M047033.

H-InvDB

HIX0021942.
HIX0163343.

HGNC

HGNC:18420. SETD2.

HPA

HPA042451.

MIM

612778. gene.

neXtProt

NX_Q9BYW2.

PharmGKB

PA143485612.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2940.

HOVERGEN

HBG093939.

InParanoid

Q9BYW2.

KO

K11423.

OMA

VMDDFRD.

Gene expression databases

ArrayExpress

Q9BYW2.

Bgee

Q9BYW2.

CleanEx

HS_SETD2.

Genevestigator

Q9BYW2.

GermOnline

ENSG00000181555. Homo sapiens.

Family and domain databases

InterPro

IPR006560. AWS.
IPR009078. Ferritin-like_SF.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR013257. SRI.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00856. SET. 1 hit.
PF08236. SRI. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]

SMART

SM00570. AWS. 1 hit.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.
SSF51045. WW_Rsp5_WWP. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

SETD2. human.

EvolutionaryTrace

Q9BYW2.

GenomeRNAi

29072.

NextBio

52031.

SOURCE

Search...

Entry information

Entry name

SETD2_HUMAN

Accession

Primary (citable) accession number: Q9BYW2
Secondary accession number(s): O75397 , 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:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.