Q9SGH2 (MBD9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methyl-CpG-binding domain-containing protein 9
Short name=AtMBD9
Short name=MBD09
EC=2.3.1.48

Alternative name(s):
Histone acetyl tranferase MBD9
Methyl-CpG-binding protein MBD9

Gene names

Name:	MBD9
Ordered Locus Names:	At3g01460
ORF Names:	F4P13.1, T13O15.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	2176 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Probable transcriptional regulator that acts as a histone acetyltranferase. Mediates the acetylation of histone H3 and H4 of target loci (e.g. FLC). Involved in an auxin-independent regulation of shoot branching and flowering time. Ref.5 Ref.7
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with histone H4.
Subcellular location	Nucleus Ref.7.
Tissue specificity	Expressed in leaves, buds, flowers and stems. Ref.3 Ref.7
Domain	The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions By similarity.
Disruption phenotype	Over-methylated genomic DNA. Increased shoot branching and reduced transcription of FLC leading to early flowering, associated with a decrease in the acetylation level in histone H3 and H4 of FLC chromatin. Ref.5 Ref.7
Sequence similarities	Contains 1 bromo domain. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 1 MBD (methyl-CpG-binding) domain. Contains 2 PHD-type zinc fingers. Contains 1 pumilio repeat. Contains 2 RING-type zinc fingers.
Sequence caution	The sequence AAF01531.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Coiled coil Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 acetylation Inferred from mutant phenotype Ref.5. Source: UniProtKB histone H4 acetylation Inferred from mutant phenotype Ref.5. Source: UniProtKB photoperiodism, flowering Inferred from mutant phenotype Ref.5. Source: TAIR regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.5. Source: TAIR secondary shoot formation Inferred from mutant phenotype Ref.5. Source: TAIR transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.7. Source: UniProtKB plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR
Molecular_function	histone acetyltransferase activity Inferred from direct assay Ref.7. Source: UniProtKB methyl-CpG binding Inferred from sequence or structural similarity PubMed 12787239. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Isoform 1 (identifier: Q9SGH2-1)

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: Q9SGH2-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2176	2176	Methyl-CpG-binding domain-containing protein 9		PRO_0000405285
Regions
	Domain	258 – 327	70	MBD
	Domain	403 – 456	54	FYR N-terminal
	Domain	550 – 698	149	FYR C-terminal
	Repeat	1098 – 1137	40	Pumilio
	Domain	1157 – 1228	72	Bromo
	Zinc finger	83 – 133	51	PHD-type 1
	Zinc finger	86 – 131	46	RING-type 1; degenerate
	Zinc finger	1287 – 1337	51	PHD-type 2
	Zinc finger	1290 – 1335	46	RING-type 2; degenerate
	Coiled coil	491 – 511	21	Potential
	Coiled coil	1251 – 1273	23	Potential
	Coiled coil	1410 – 1437	28	Potential
	Coiled coil	1588 – 1628	41	Potential
	Motif	914 – 921	8	Nuclear localization signal By similarity
	Motif	1124 – 1131	8	Nuclear localization signal By similarity
	Motif	1256 – 1263	8	Nuclear localization signal By similarity
	Motif	1337 – 1344	8	Nuclear localization signal By similarity
	Motif	1761 – 1768	8	Nuclear localization signal By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 05DBD955D895C3D5	FASTA	2,176	240,431
	10 20 30 40 50 60 MEPTDSTNEQ LGDTKTAAVK EESRSFLGID LNEIPTGATL GGGCTAGQDD DGEYEPVEVV 70 80 90 100 110 120 RSIHDNPDPA PGAPAEVPEP DRDASCGACG RPESIELVVV CDACERGFHM SCVNDGVEAA 130 140 150 160 170 180 PSADWMCSDC RTGGERSKLW PLGVKSKLIL DMNASPPSDA EGYGAEETSD SRKHMLASSS 190 200 210 220 230 240 CIGNSFDYAM MHSSFSSLGR GHASLEASGL MSRNTKMSMD ALGSHNLGFG FPLNLNNSSL 250 260 270 280 290 300 PMRFPSLDPS ELFLQNLRHF ISERHGVLED GWRVEFRQPL NGYQLCAVYC APNGKTFSSI 310 320 330 340 350 360 QEVACYLGLA INGNYSCMDA EIRNENSLLQ ERLHTPKRRK TSRWPNNGFP EQKGSSVSAQ 370 380 390 400 410 420 LRRFPFNGQT MSPFAVKSGT HFQAGGSLSS GNNGCGCEEA KNGCPMQFED FFVLSLGRID 430 440 450 460 470 480 IRQSYHNVNV IYPIGYKSCW HDKITGSLFT CEVSDGNSGP IFKVTRSPCS KSFIPAGSTV 490 500 510 520 530 540 FSCPKIDEMV EQNSDKLSNR RDSTQERDDD ASVEILLSEH CPPLGDDILS CLREKSFSKT 550 560 570 580 590 600 VNSLRSEVDS SRVDFDKNLS YDQDHGVEIG DIVVEEDSLS DAWKKVSQKL VDACSIVLKQ 610 620 630 640 650 660 KGTLNFLCKH VDRETSEINW DTMNEKDNVI LSLSKFCCSL APCSVTCGEK DKSEFAAVVD 670 680 690 700 710 720 ALSRWLDQNR FGLDADFVQE MIEHMPGAES CTNYRTLKSR SSSSVPITVA EGALVVKPKG 730 740 750 760 770 780 GENVKDEVFG EISRKAKKPK LNGGHGVRNL HPPPGRPMCL RLPPGLVGDF LQVSEVFWRF 790 800 810 820 830 840 HEILGFEEAF SPENLEQELI NPVFDGLFLD KPGKDDKRSE INFTDKDSTA TKLFSLFDES 850 860 870 880 890 900 RQPFPAKNTS ASELKEKKAG DSSDFKISDS SRGSCVGALL TRAHISLLQV LICELQSKVA 910 920 930 940 950 960 AFVDPNFDSG ESRSRRGRKK DDSTLSAKRN KLHMLPVNEF TWPELARRYI LSLLSMDGNL 970 980 990 1000 1010 1020 ESAEIAARES GKVFRCLQGD GGLLCGSLTG VAGMEADSML LAEAIKKISG SLTSENDVLS 1030 1040 1050 1060 1070 1080 VEDDDSDGLD ATETNTCSGD IPEWAQVLEP VKKLPTNVGT RIRKCVYEAL ERNPPEWAKK 1090 1100 1110 1120 1130 1140 ILEHSISKEI YKGNASGPTK KAVLSLLADI RGGDLVQRSI KGTKKRTYIS VSDVIMKKCR 1150 1160 1170 1180 1190 1200 AVLRGVAAAD EDKVLCTLLG RKLLNSSDND DDGLLGSPAM VSRPLDFRTI DLRLAAGAYD 1210 1220 1230 1240 1250 1260 GSTEAFLEDV LELWSSIRVM YADQPDCVDL VATLSEKFKS LYEAEVVPLV QKLKDYRKLE 1270 1280 1290 1300 1310 1320 CLSAEMKKEI KDIVVSVNKL PKAPWDEGVC KVCGVDKDDD SVLLCDTCDA EYHTYCLNPP 1330 1340 1350 1360 1370 1380 LIRIPDGNWY CPSCVIAKRM AQEALESYKL VRRRKGRKYQ GELTRASMEL TAHLADVMEE 1390 1400 1410 1420 1430 1440 KDYWEFSAEE RILLLKLLCD ELLSSSLVHQ HLEQCAEAII EMQQKLRSLS SEWKNAKMRQ 1450 1460 1470 1480 1490 1500 EFLTAKLAKV EPSILKEVGE PHNSSYFADQ MGCDPQPQEG VGDGVTRDDE TSSTAYLNKN 1510 1520 1530 1540 1550 1560 QGKSPLETDT QPGESHVNFG ESKISSPETI SSPGRHELPI ADTSPLVTDN LPEKDTSETL 1570 1580 1590 1600 1610 1620 LKSVGRNHET HSPNSNAVEL PTAHDASSQA SQELQACQQD LSATSNEIQN LQQSIRSIES 1630 1640 1650 1660 1670 1680 QLLKQSIRRD FLGTDASGRL YWGCCFPDEN PRILVDGSIS LQKPVQADLI GSKVPSPFLH 1690 1700 1710 1720 1730 1740 TVDHGRLRLS PWTYYETETE ISELVQWLHD DDLKERDLRE SILWWKRLRY GDVQKEKKQA 1750 1760 1770 1780 1790 1800 QNLSAPVFAT GLETKAAMSM EKRYGPCIKL EMETLKKRGK KTKVAEREKL CRCECLESIL 1810 1820 1830 1840 1850 1860 PSMIHCLICH KTFASDDEFE DHTESKCIPY SLATEEGKDI SDSSKAKESL KSDYLNVKSS 1870 1880 1890 1900 1910 1920 AGKDVAEISN VSELDSGLIR YQEEESISPY HFEEICSKFV TKDCNRDLVK EIGLISSNGI 1930 1940 1950 1960 1970 1980 PTFLPSSSTH LNDSVLISAK SNKPDGGDSG DQVIFAGPET NVEGLNSESN MSFDRSVTDS 1990 2000 2010 2020 2030 2040 HGGPLDKPSG LGFGFSEQKN KKSSGSGLKS CCVVPQAALK RVTGKALPGF RFLKTNLLDM 2050 2060 2070 2080 2090 2100 DVALPEEALR PSKSHPNRRR AWRVFVKSSQ SIYELVQATI VVEDMIKTEY LKNEWWYWSS 2110 2120 2130 2140 2150 2160 LSAAAKISTL SALSVRIFSL DAAIIYDKPI TPSNPIDETK PIISLPDQKS QPVSDSQERS 2170 SRVRRSGKKR KEPEGS
	Isoform 2 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Ten members of the Arabidopsis gene family encoding methyl-CpG-binding domain proteins are transcriptionally active and at least one, AtMBD11, is crucial for normal development." Berg A., Meza T.J., Mahic M., Thorstensen T., Kristiansen K., Aalen R.B. Nucleic Acids Res. 31:5291-5304(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[4]	"Evolutionary divergence of monocot and dicot methyl-CpG-binding domain proteins." Springer N.M., Kaeppler S.M. Plant Physiol. 138:92-104(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY.
[5]	"AtMBD9: a protein with a methyl-CpG-binding domain regulates flowering time and shoot branching in Arabidopsis." Peng M., Cui Y., Bi Y.-M., Rothstein S.J. Plant J. 46:282-296(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Methyl-CpG-binding domain proteins in plants: interpreters of DNA methylation." Zemach A., Grafi G. Trends Plant Sci. 12:80-85(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[7]	"AtMBD9 modulates Arabidopsis development through the dual epigenetic pathways of DNA methylation and histone acetylation." Yaish M.W.F., Peng M., Rothstein S.J. Plant J. 59:123-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

The Chromatin Database (ChromDB)

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC009325 Genomic DNA. Translation: AAF01531.1. Sequence problems. AC010870 Genomic DNA. Translation: AAF24616.1. CP002686 Genomic DNA. Translation: AEE73669.1.
IPI	IPI00538023.
RefSeq	NP_186795.1. NM_111012.3.
UniGene	At.41275. At.47815.
3D structure databases
HSSP	HSSP built from PDB template 1MM2 based on UniProtKB Q14839.
ProteinModelPortal	Q9SGH2.
SMR	Q9SGH2. Positions 85-131, 1290-1334.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT3G01460.1-P.
Proteomic databases
PaxDb	Q9SGH2.
PRIDE	Q9SGH2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G01460.1; AT3G01460.1; AT3G01460.
GeneID	821132.
KEGG	ath:AT3G01460.
Organism-specific databases
TAIR	At3g01460.
Phylogenomic databases
eggNOG	NOG79337.
HOGENOM	HOG000153462.
InParanoid	Q9SGH2.
OMA	GTRIRKC.
PhylomeDB	Q9SGH2.
ProtClustDB	CLSN2684998.
Gene expression databases
Genevestigator	Q9SGH2.
Family and domain databases
Gene3D	3.30.40.10. 2 hits.
InterPro	IPR016177. DNA-bd_integrase-typ. IPR003889. FYrich_C. IPR003888. FYrich_N. IPR001739. Methyl_CpG_DNA-bd. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF01429. MBD. 1 hit. PF00628. PHD. 2 hits. [Graphical view]
SMART	SM00249. PHD. 2 hits. SM00184. RING. 2 hits. [Graphical view]
SUPFAM	SSF54171. DNA-binding_integrase-type. 1 hit. SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	PS00633. BROMODOMAIN_1. False negative. PS50014. BROMODOMAIN_2. False negative. PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS50982. MBD. 1 hit. PS50302. PUM. False negative. PS01359. ZF_PHD_1. 2 hits. PS50016. ZF_PHD_2. 2 hits. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MBD9_ARATH

Accession

Primary (citable) accession number: Q9SGH2
Secondary accession number(s): Q9SSA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program