Q9R190 (MTA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metastasis-associated protein MTA2

Alternative name(s):
Metastasis-associated 1-like 1

Gene names

Name:	Mta2
Synonyms:	Mta1l1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	668 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.
Subunit structure	Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC7, p53/TP53, MINT and MBD3 By similarity. Ref.6 Ref.7
Subcellular location	Nucleus Ref.3.
Sequence similarities	Contains 1 BAH domain. Contains 1 ELM2 domain. Contains 1 GATA-type zinc finger. Contains 1 SANT domain.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation Inferred from mutant phenotype PubMed 20720167. Source: MGI DNA packaging Traceable author statement Ref.1. Source: MGI chromatin remodeling Traceable author statement PubMed 14645126. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.3. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.3. Source: MGI
Cellular_component	NuRD complex Inferred from direct assay PubMed 14645126. Source: MGI transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	chromatin binding Inferred from electronic annotation. Source: InterPro histone deacetylase activity Inferred from direct assay Ref.1. Source: MGI sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription factor binding transcription factor activity Inferred from direct assay PubMed 20636338. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay PubMed 20636338. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Esrrb	Q61539	2	EBI-904134,EBI-2312731
Pou5f1	P20263	6	EBI-904134,EBI-1606219
Sall4	Q8BX22	3	EBI-904134,EBI-2312582

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 668	668	Metastasis-associated protein MTA2		PRO_0000083497
Regions
	Domain	1 – 144	144	BAH
	Domain	145 – 256	112	ELM2
	Domain	263 – 315	53	SANT
	Zinc finger	367 – 394	28	GATA-type; atypical
Amino acid modifications
	Modified residue	152	1	N6-acetyllysine By similarity
	Modified residue	433	1	Phosphoserine By similarity
	Modified residue	435	1	Phosphoserine By similarity
	Modified residue	534	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	489	1	N → I in BAC40180. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9R190 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 88996F779BA6F4D1	FASTA	668	75,030
	10 20 30 40 50 60 MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD 70 80 90 100 110 120 SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILNQY 130 140 150 160 170 180 LDKEDCFFYS LVFDPVQKTL LADQGEIRVG CKFQAEIPDR LAEGESDNRN QQKMEMKVWD 190 200 210 220 230 240 PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR 250 260 270 280 290 300 NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL 310 320 330 340 350 360 ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG 370 380 390 400 410 420 FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGAARGTTEP 430 440 450 460 470 480 HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR 490 500 510 520 530 540 RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT 550 560 570 580 590 600 PINRNQLTQN RGLGGIMVKR SYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 610 620 630 640 650 660 APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLMTVRPPVP LPASSHPAST NEPIVLED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation." Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D. Genes Dev. 13:1924-1935(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sp1 and ETS family transcription factors regulate the mouse Mta2 gene expression." Xia L., Zhang Y. Gene 268:77-85(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"Characterization of mouse metastasis-associated gene 2: genomic structure, nuclear localization signal, and alternative potentials as transcriptional activator and repressor." Matsusue K., Takiguchi S., Toh Y., Kono A. DNA Cell Biol. 20:603-611(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBCELLULAR LOCATION. Strain: 129/SvJ. Tissue: Liver.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Amnion and Thymus.
[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]. Strain: C57BL/6. Tissue: Brain.
[6]	"Identification of a nuclear domain with deacetylase activity." Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M. Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC7.
[7]	"The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2." Saito M., Ishikawa F. J. Biol. Chem. 277:35434-35439(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MBD3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF159259 mRNA. Translation: AAD51281.1. AF348083 Genomic DNA. Translation: AAL30174.1. AB047977 Genomic DNA. Translation: BAB79231.1. AK088158 mRNA. Translation: BAC40180.1. AK147099 mRNA. Translation: BAE27675.1. AK159979 mRNA. Translation: BAE35530.1. BC079847 mRNA. Translation: AAH79847.1.
IPI	IPI00128230.
RefSeq	NP_035972.3. NM_011842.3.
UniGene	Mm.25339.
3D structure databases
ProteinModelPortal	Q9R190.
SMR	Q9R190. Positions 265-321, 364-406.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36630N.
IntAct	Q9R190. 12 interactions.
PTM databases
PhosphoSite	Q9R190.
2D gel databases
REPRODUCTION-2DPAGE	IPI00128230.
Proteomic databases
PaxDb	Q9R190.
PRIDE	Q9R190.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000096240; ENSMUSP00000093959; ENSMUSG00000071646.
GeneID	23942.
KEGG	mmu:23942.
UCSC	uc008gof.1. mouse.
Organism-specific databases
CTD	9219.
MGI	MGI:1346340. Mta2.
Phylogenomic databases
eggNOG	NOG252834.
GeneTree	ENSGT00580000081398.
HOGENOM	HOG000045387.
HOVERGEN	HBG002598.
InParanoid	Q9R190.
KO	K11660.
OMA	KVKPPLI.
OrthoDB	EOG4640BG.
Gene expression databases
ArrayExpress	Q9R190.
Bgee	Q9R190.
CleanEx	MM_MTA2.
Genevestigator	Q9R190.
GermOnline	ENSMUSG00000071646. Mus musculus.
Family and domain databases
InterPro	IPR001025. BAH_dom. IPR000949. ELM2_dom. IPR009057. Homeodomain-like. IPR001005. SANT/Myb. IPR017884. SANT_dom. IPR000679. Znf_GATA. [Graphical view]
Pfam	PF01426. BAH. 1 hit. PF01448. ELM2. 1 hit. PF00320. GATA. 1 hit. [Graphical view]
SMART	SM00439. BAH. 1 hit. SM00717. SANT. 1 hit. SM00401. ZnF_GATA. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS51038. BAH. 1 hit. PS51156. ELM2. 1 hit. PS00344. GATA_ZN_FINGER_1. False negative. PS50114. GATA_ZN_FINGER_2. False negative. PS51293. SANT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MTA2. mouse.
NextBio	303749.
SOURCE	Search...

Entry information

Entry name

MTA2_MOUSE

Accession

Primary (citable) accession number: Q9R190
Secondary accession number(s): Q3TVT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program