O94776 (MTA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metastasis-associated protein MTA2

Alternative name(s):
Metastasis-associated 1-like 1
Short name=MTA1-L1 protein
p53 target protein in deacetylase complex

Gene names

Name:	MTA2
Synonyms:	MTA1L1, PID

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	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.4
Subcellular location	Nucleus By similarity.
Tissue specificity	Widely expressed.
Sequence similarities	Contains 1 BAH domain. Contains 1 ELM2 domain. Contains 1 GATA-type zinc finger. Contains 1 SANT domain.
Sequence caution	The sequence AAH23656.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

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 electronic annotation. Source: Compara chromatin assembly or disassembly Traceable author statement PubMed 10444591. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	NuRD complex Inferred from direct assay PubMed 19644445. Source: UniProtKB transcription factor complex Inferred from direct assay PubMed 15920471. Source: BHF-UCL
Molecular_function	chromatin binding Inferred from electronic annotation. Source: InterPro histone deacetylase activity Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PARK7	Q99497	3	EBI-1783035,EBI-1164361

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 668	668	Metastasis-associated protein MTA2		PRO_0000083496
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 Ref.10
	Modified residue	433	1	Phosphoserine Ref.8
	Modified residue	435	1	Phosphoserine Ref.8 Ref.9 Ref.11
	Modified residue	534	1	Phosphothreonine Ref.11
	Modified residue	548	1	Phosphoserine Ref.13
Experimental info
	Sequence conflict	75	1	V → M in BAA36707. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O94776 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 65087AF798BA64EC	FASTA	668	75,023
	10 20 30 40 50 60 MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD 70 80 90 100 110 120 SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILSQY 130 140 150 160 170 180 LEKEDCFFYS LVFDPVQKTL LADQGEIRVG CKYQAEIPDR LVEGESDNRN 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 EGATRGTTEP 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 PINRNQLSQN RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 610 620 630 640 650 660 APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP LPAPSHPAST NEPIVLED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1." Futamura M., Nishimori H., Shiratsuchi T., Saji S., Nakamura Y., Tokino T. J. Hum. Genet. 44:52-56(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Deacetylation of p53 modulates its effect on cell growth and apoptosis." Luo J., Su F., Chen D., Shiloh A., Gu W. Nature 408:377-381(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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]. Tissue: Brain and Uterus.
[4]	"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation." Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M. Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MINT.
[5]	"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.
[6]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"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-433 AND SER-435, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-435, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, MASS SPECTROMETRY.
[11]	"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-435 AND THR-534, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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-548, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012922 Genomic DNA. Translation: BAA36562.1. AB016591 mRNA. Translation: BAA36707.1. AF295807 mRNA. Translation: AAG02241.1. BC023656 mRNA. Translation: AAH23656.1. Sequence problems. BC053650 mRNA. Translation: AAH53650.1.
IPI	IPI00171798.
RefSeq	NP_004730.2. NM_004739.3.
UniGene	Hs.173043.
3D structure databases
ProteinModelPortal	O94776.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46519N.
IntAct	O94776. 21 interactions.
STRING	9606.ENSP00000278823.
PTM databases
PhosphoSite	O94776.
Proteomic databases
PaxDb	O94776.
PeptideAtlas	O94776.
PRIDE	O94776.
Protocols and materials databases
DNASU	9219.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278823; ENSP00000278823; ENSG00000149480.
GeneID	9219.
KEGG	hsa:9219.
UCSC	uc001ntq.2. human.
Organism-specific databases
CTD	9219.
GeneCards	GC11M062360.
HGNC	HGNC:7411. MTA2.
HPA	CAB005315. CAB017522. HPA006214.
MIM	603947. gene.
neXtProt	NX_O94776.
PharmGKB	PA31219.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG252834.
HOGENOM	HOG000045387.
HOVERGEN	HBG002598.
InParanoid	O94776.
KO	K11660.
OMA	KVKPPLI.
OrthoDB	EOG4640BG.
PhylomeDB	O94776.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I.
Gene expression databases
ArrayExpress	O94776.
Bgee	O94776.
CleanEx	HS_MTA2.
Genevestigator	O94776.
GermOnline	ENSG00000149480. Homo sapiens.
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. human.
GenomeRNAi	9219.
NextBio	34563.
SOURCE	Search...

Entry information

Entry name

MTA2_HUMAN

Accession

Primary (citable) accession number: O94776
Secondary accession number(s): Q9UQB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 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.