Reviewed, UniProtKB/Swiss-Prot Q9VW15 (ASH1_DROME)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase ash1
    EC=2.1.1.43
Alternative name(s):
    Absent small and homeotic disks protein 1
    Lysine N-methyltransferase 2H

Gene names

Name:	ash1
Synonyms:	KMT2H
ORF Names:	CG8887

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	2226 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Trithorax group (TrxG) protein that has histone methyltransferase activity. Specifically trimethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation. May also trimethylate H3 'Lys-9' and H4 'Lys-20'; however the relevance of this activity is unclear in vivo. TrxG protein are generally required to maintain the transcriptionally active state of homeotic genes throughout development. Does not act as a coactivator required for transcriptional activation, but specifically prevent inappropriate Polycomb Group (PcG) silencing of homeotic genes in cells in which they must stay transcriptionally active. Binds non-coding RNAs of trithorax response element (TRE), leading to its recruitment to the corresponding TRE in chromatin. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.10 Ref.11
Subunit structure	Component of a large multiprotein complex disting from complexes containing ash2 or brm. Interacts with trx via its SET domain. Interacts with nej/cbp. Ref.6 Ref.7 Ref.8 Ref.9
Subcellular location	Nucleus. Note: Localizes at the promoter of active genes. Ref.13 Ref.7 Ref.1
Tissue specificity	Expressed throughout development but is present at higher levels during the embryonic and pupal stages than during the larval stages. During the larval stages it accumulates primarily in imaginal disks. Ref.5
Developmental stage	Expressed both maternally and zygotically. During oogenesis it accumulates in the nurse cells of developing egg chambers. Ref.5
Domain	The SET domain is sufficient for methyltransferase activity. Ref.11
Sequence similarities	Belongs to the histone-lysine methyltransferase family. SET2 subfamily. Contains 3 A.T hook DNA-binding domains. Contains 1 AWS domain. Contains 1 BAH domain. Contains 1 PHD-type zinc finger. Contains 1 post-SET domain. Contains 1 SET domain.
Sequence caution	The sequence AAB01100.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAF49140.2 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAM52758.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Activator Chromatin regulator Developmental protein Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin-mediated maintenance of transcription Inferred from mutant phenotype. Source: FlyBase embryonic development via the syncytial blastoderm Ref.5 Inferred from mutant phenotype. Source: FlyBase histone methylation Ref.14 Inferred from direct assay. Source: FlyBase oogenesis Ref.5 Inferred from mutant phenotype. Source: FlyBase oviposition Ref.5 Inferred from mutant phenotype. Source: FlyBase transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred by curator. Source: FlyBase
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro histone methyltransferase activity (H3-K4 specific) Non-traceable author statement. Source: FlyBase histone methyltransferase activity (H3-K9 specific) Non-traceable author statement. Source: FlyBase histone methyltransferase activity (H4-K20 specific) Non-traceable author statement. Source: FlyBase identical protein binding Ref.9 Inferred from physical interaction. Source: IntAct single-stranded RNA binding Ref.14 Inferred from direct assay. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-124480,EBI-124480
Ctr1A	Q9W3X9	1	EBI-124480,EBI-171893

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2226	2226	Histone-lysine N-methyltransferase ash1		PRO_0000259518
Regions
	Domain	1339 – 1387	49	AWS
	Domain	1389 – 1510	122	SET
	Domain	1514 – 1530	17	Post-SET
	Domain	1952 – 2072	121	BAH
	DNA binding	261 – 273	13	A.T hook 1
	DNA binding	1065 – 1077	13	A.T hook 2
	DNA binding	1095 – 1107	13	A.T hook 3
	Zinc finger	1857 – 1903	47	PHD-type
Amino acid modifications
	Modified residue	135	1	Phosphoserine Ref.15
	Modified residue	136	1	Phosphoserine Ref.15
	Modified residue	138	1	Phosphoserine Ref.15
	Modified residue	200	1	Phosphothreonine Ref.15
	Modified residue	201	1	Phosphothreonine Ref.15
	Modified residue	740	1	Phosphoserine Ref.15
	Modified residue	831	1	Phosphoserine Ref.15
	Modified residue	977	1	Phosphoserine Ref.15
Experimental info
	Mutagenesis	1284	1	E → K in ash1-21; induces lethality between prepupae and lae pupae stage. Abolishes histone methyltransferase activity. Ref.10 Ref.1
	Mutagenesis	1473	1	N → I in ash1-10; induces lethality between prepupae and lae pupae stage. Abolishes histone methyltransferase activity. Ref.10 Ref.1
	Sequence conflict	163	1	A → G in AAB01100. Ref.1
	Sequence conflict	166	1	A → G in AAB01100. Ref.1
	Sequence conflict	320	1	P → T in AAB01100. Ref.1
	Sequence conflict	324 – 325	2	SS → RR in AAB01100. Ref.1
	Sequence conflict	457	1	A → P in AAB01100. Ref.1
	Sequence conflict	1001	1	Q → K in AAM52758. Ref.4
	Sequence conflict	1191	1	L → V in AAB01100. Ref.1
	Sequence conflict	1246	1	F → L in AAB01100. Ref.1
	Sequence conflict	1993	1	H → Q in AAB01100. Ref.1
	Sequence conflict	2031	1	R → P in AAB01100. Ref.1
	Sequence conflict	2034	1	V → L in AAB01100. Ref.1
	Sequence conflict	2038	1	T → P in AAB01100. Ref.1
	Sequence conflict	2041	1	C → S in AAB01100. Ref.1
	Sequence conflict	2044	1	R → P in AAB01100. Ref.1
	Sequence conflict	2145	1	R → C in AAB01100. Ref.1
	Sequence conflict	2169	1	L → H in AAB01100. Ref.1
	Sequence conflict	2181	1	I → V in AAB01100. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VW15-1 [UniParc]. Last modified October 31, 2006. Version 3. Checksum: 0ACBB0BF404848F2	FASTA	2,226	246,266
	10 20 30 40 50 60 MSCSQNETAA AKVLETQRAQ ESGSENEETD SITDQSSQSK SIKSATQFSV QRSDTDGLRM 70 80 90 100 110 120 RISAIRPTLG VVATKKPPKS RKMSTQDTES GCSEAKNRAV SKKVKVKRKK LASSSGISKS 130 140 150 160 170 180 DKVSKSKKSQ ISAFSSDSED DLPLKVHQQR APRVLLSAII QAAQSASKPT LDIGISSSDN 190 200 210 220 230 240 ELPNLVQAAI KRVESDTEDT TVEGSFRKAA KDKNLPQYQS TLLQDFMEKT QMLGQTVNAK 250 260 270 280 290 300 LAEEKVAKAK EETLVQTAVP RKRRGRPKKV VPTVPAPGNS GPAINESADS GVISTTSTTQ 310 320 330 340 350 360 STTPSPKMQN ENAVPTGSLP IASSSKPKID MAYLDKRMYA TERVLYPPPR SKRRQNNKKT 370 380 390 400 410 420 ACSSSNKEEL QLDPLWREID VNKKFRLRSM SVGAASGTGA STTICSKVLA AKSGYVSDYG 430 440 450 460 470 480 SVRHQRSSHN HNSGYKSDAS CKSRYSTKSC MSRRSRAKSC GYRSDCKESG KSGLRMRRKR 490 500 510 520 530 540 RASMLLKSSA DDTVEDQDIL QLAGLSLGQS SEESNEYISK PSLKSLPTTS ASKKYGEINR 550 560 570 580 590 600 YVTTGQYFGR GGSLSATNPD NFISKMMNQR KETPAPSKSS CKIKSRRSSA ASMCSSYVSG 610 620 630 640 650 660 VSRMRRRHRR KSFSHNKSLN IDSKLLTEIE IITSTFNSRC RIQDDRLTGS SGKEKLLADA 670 680 690 700 710 720 NKLQATLAAP SPAQQLTLNG GGPASTLSKP LKRGLKKRKL SEPLVDFAML SASASGTPNG 730 740 750 760 770 780 SGSSNGNTKR RHKKSQSNDS SSPDDHKLPL KKRHYLLTPG ERPPAEVAFA NGKLNAEAWA 790 800 810 820 830 840 AAAAAAKSTA STKSQAQFNA RSVKSALTPK KRHLLEQPTS VSGAGSSASN SPLRIVVDNN 850 860 870 880 890 900 SISGGKLLDI SPSSLCSLKQ QRRGGAAKQK VSAAKDLVQL QSPAGSYPPP GVFEPSVELE 910 920 930 940 950 960 IQIPLSKLNE SVITKAEVES PLLSALDIKE DTKKEVGQRV VETLLHKTGG NLLLKRKRKK 970 980 990 1000 1010 1020 INRTGFPTVR RKKRKVSVEQ QTTAVIDEHE PEFDPDDEPL QSLRETRSSN NVNVQAAPNP 1030 1040 1050 1060 1070 1080 PLDCERVPQA GEARETFVAR TNQKAPRLSV VALERLQRPQ TPARGRPRGR KPKNREQAEA 1090 1100 1110 1120 1130 1140 APQPPPKSEP EIRPAKKRGR QPKQPVLEEP PPTPPPQQKK NKMEPNIRLP DGIDPNTNFS 1150 1160 1170 1180 1190 1200 CKIRLKRRKN LEAGTQPKKE KPVQPVTVEE IPPEIPVSQE EIDAEAEAKR LDSIPTEHDP 1210 1220 1230 1240 1250 1260 LPASESHNPG PQDYASCSES SEDKASTTSL RKLSKVKKTY LVAGLFSNHY KQSLMPPPAK 1270 1280 1290 1300 1310 1320 VNKKPGLEEQ VGPASLLPPP PYCEKYLRRT EMDFELPYDI WWAYTNSKLP TRNVVPSWNY 1330 1340 1350 1360 1370 1380 RKIRTNVYAE SVRPNLAGFD HPTCNCKNQG EKSCLDNCLN RMVYTECSPS NCPAGEKCRN 1390 1400 1410 1420 1430 1440 QKIQRHAVAP GVERFMTADK GWGVRTKLPI AKGTYILEYV GEVVTEKEFK QRMASIYLND 1450 1460 1470 1480 1490 1500 THHYCLHLDG GLVIDGQRMG SDCRFVNHSC EPNCEMQKWS VNGLSRMVLF AKRAIEEGEE 1510 1520 1530 1540 1550 1560 LTYDYNFSLF NPSEGQPCRC NTPQCRGVIG GKSQRVKPLP AVEAKPSGEG LSGRNGRQRK 1570 1580 1590 1600 1610 1620 QKAKKHAQRQ AGKDISSAVA VAKLQPLSEK EKKLVRQFNT FLVRNFEKIR RCKAKRASDA 1630 1640 1650 1660 1670 1680 AATASSPALG TTNGDIPGRR PSTPSSPSLA AQISALCSPR NIKTRGLTQA VHDPELEKMA 1690 1700 1710 1720 1730 1740 KMAVVLRDIC SAMETLKMSD LLTTVSSKKK KPIKTTLSGK LGSTAATSKV EFRSIQAQVE 1750 1760 1770 1780 1790 1800 QGHYKTPQEF DDHMQQLFVE AKQQHGDDEG KEKALQSLKD SYEQQKIASY VQLVEILGDS 1810 1820 1830 1840 1850 1860 ESLQSFKPKE VLSSEEEPGK IAVKKSPGAK ERDSPIVPLK VTPPPLLPIE ASPDEDVIRC 1870 1880 1890 1900 1910 1920 ICGLYKDEGL MIQCSKCMVW QHTECTKADI DADNYQCERC EPREVDREIP LEEFTEEGHR 1930 1940 1950 1960 1970 1980 YYLSLMRGDL QVRQGDAVYV LRDIPIKDES GKVLPTKKHT YETIGAIDYQ ECDIFRVEHL 1990 2000 2010 2020 2030 2040 WKNELGKRFI FGHHFLRPHE TFHEPSRRFY PNEVVRVSLY EVVPIELVIG RCWVLDRTTF 2050 2060 2070 2080 2090 2100 CKGRPMECND EDHCYICELR VDKTARFFSK AKANHPACTK SYAFRKFPEK IKISKSYAPH 2110 2120 2130 2140 2150 2160 DVDPSLLKTR KQKTELDVGA GPTTMHKVSG RQEQHQAKMV GRKPRGISAP ADATAVHVVT 2170 2180 2190 2200 2210 2220 PVAPNKQMLK KRKSRLENVL ITMKLKCLDA QTAQEQPIDL SYLLSGRGAR QRKTQQSSSS STANST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila ash1 gene product, which is localized at specific sites on polytene chromosomes, contains a SET domain and a PHD finger." Tripoulas N., LaJeunesse D., Gildea J., Shearn A. Genetics 143:913-928(1996) [PubMed: 8725238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-1284 AND ASN-1473.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1120. Strain: Berkeley. Tissue: Embryo.
[5]	"Molecular genetic analysis of the Drosophila melanogaster gene absent, small or homeotic discs1 (ash1)." Tripoulas N.A., Hersperger E., La Jeunesse D., Shearn A. Genetics 137:1027-1038(1994) [PubMed: 7982557] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]	"The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes." Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M., Shearn A., Tamkun J.W. Development 125:3955-3966(1998) [PubMed: 9735357] [Abstract] Cited for: SUBUNIT.
[7]	"Trithorax and ASH1 interact directly and associate with the trithorax group-responsive bxd region of the Ultrabithorax promoter." Rozovskaia T., Tillib S., Smith S., Sedkov Y., Rozenblatt-Rosen O., Petruk S., Yano T., Nakamura T., Ben-Simchon L., Gildea J., Croce C.M., Shearn A., Canaani E., Mazo A. Mol. Cell. Biol. 19:6441-6447(1999) [PubMed: 10454589] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TRX.
[8]	"Functional interaction between the coactivator Drosophila CREB-binding protein and ASH1, a member of the trithorax group of chromatin modifiers." Bantignies F., Goodman R.H., Smolik S.M. Mol. Cell. Biol. 20:9317-9330(2000) [PubMed: 11094082] [Abstract] Cited for: INTERACTION WITH NEJ.
[9]	"Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins." Rozovskaia T., Rozenblatt-Rosen O., Sedkov Y., Burakov D., Yano T., Nakamura T., Petruck S., Ben-Simchon L., Croce C.M., Mazo A., Canaani E. Oncogene 19:351-357(2000) [PubMed: 10656681] [Abstract] Cited for: INTERACTION WITH TRX.
[10]	"Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1." Beisel C., Imhof A., Greene J., Kremmer E., Sauer F. Nature 419:857-862(2002) [PubMed: 12397363] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, MUTAGENESIS OF GLU-1284 AND ASN-1473.
[11]	"ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3." Byrd K.N., Shearn A. Proc. Natl. Acad. Sci. U.S.A. 100:11535-11540(2003) [PubMed: 13679578] [Abstract] Cited for: FUNCTION, SET DOMAIN, ENZYME ACTIVITY.
[12]	"The histone methyltransferases Trithorax and Ash1 prevent transcriptional silencing by Polycomb group proteins." Klymenko T., Mueller J. EMBO Rep. 5:373-377(2004) [PubMed: 15031712] [Abstract] Cited for: FUNCTION.
[13]	"Histone trimethylation and the maintenance of transcriptional ON and OFF states by trxG and PcG proteins." Papp B., Mueller J. Genes Dev. 20:2041-2054(2006) [PubMed: 16882982] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Noncoding RNAs of trithorax response elements recruit Drosophila Ash1 to Ultrabithorax." Sanchez-Elsner T., Gou D., Kremmer E., Sauer F. Science 311:1118-1123(2006) [PubMed: 16497925] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[15]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-136; SER-138; THR-200; THR-201; SER-740; SER-831 AND SER-977, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49439 Genomic DNA. Translation: AAB01100.1. Sequence problems. AE014296 Genomic DNA. Translation: AAF49140.2. Sequence problems. AY122246 mRNA. Translation: AAM52758.1. Sequence problems.
PIR	S71490.
RefSeq	NP_524160.1.
UniGene	Dm.7698
3D structure databases
HSSP	HSSP built from PDB template 1PEG based on UniProtKB Q8X225.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VW15. 5 interactions.
Genome annotation databases
Ensembl	FBgn0005386. Drosophila melanogaster. [Contig view]
GeneID	40133.
KEGG	dme:Dmel_CG8887.
Organism-specific databases
FlyBase	FBgn0005386. ash1.
Enzyme and pathway databases
BRENDA	2.1.1.43. 48.
Gene expression databases
ArrayExpress	Q9VW15.
GermOnline	CG8887. Drosophila melanogaster.
Family and domain databases
InterPro	IPR017956. AT_hook_DNA-bd_CS. IPR006560. AWS. IPR001025. BAH. IPR003616. Post-SET_Zn_bd. IPR001214. SET. IPR019786. Zinc_finger_PHD-type_CS. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. [Graphical view]
Pfam	PF01426. BAH. 1 hit. PF00628. PHD. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00384. AT_hook. 3 hits. SM00570. AWS. 1 hit. SM00439. BAH. 1 hit. SM00249. PHD. 1 hit. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
PROSITE	PS51215. AWS. 1 hit. PS51038. BAH. 1 hit. PS50868. POST_SET. 1 hit. PS50280. SET. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	817161.

Entry information

Entry name

ASH1_DROME

Accession

Primary (citable) accession number: Q9VW15
Secondary accession number(s): Q24189, Q8MQX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	June 16, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project