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Q8K4B0

- MTA1_MOUSE

UniProt

Q8K4B0 - MTA1_MOUSE

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Protein

Metastasis-associated protein MTA1

Gene

Mta1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri393 – 42028GATA-type; atypicalAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. core promoter binding Source: UniProtKB
  3. core promoter sequence-specific DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. transcription coactivator activity Source: UniProtKB
  6. transcription corepressor activity Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. circadian regulation of gene expression Source: UniProtKB
  2. double-strand break repair Source: UniProtKB
  3. entrainment of circadian clock by photoperiod Source: UniProtKB
  4. locomotor rhythm Source: UniProtKB
  5. positive regulation of protein autoubiquitination Source: UniProtKB
  6. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. regulation of gene expression, epigenetic Source: UniProtKB
  8. regulation of inflammatory response Source: UniProtKB
  9. response to ionizing radiation Source: UniProtKB
  10. response to lipopolysaccharide Source: UniProtKB
  11. secretory granule organization Source: Ensembl
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Metastasis-associated protein MTA1
Gene namesi
Name:Mta1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:2150037. Mta1.

Subcellular locationi

Nucleus. Nucleus envelope PROSITE-ProRule annotation. Cytoplasm. Cytoplasmcytoskeleton By similarity
Note: Associated with microtubules. Primarily localized in the cytoplasm in embryonic tissues. Localization at the nuclear envelope is TPR-dependent.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: Ensembl
  3. microtubule Source: UniProtKB
  4. nuclear envelope Source: UniProtKB
  5. nucleus Source: MGI
  6. NuRD complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice exhibit a disruption of the free-running period of circadian rhythms under constant light and normal entrainment of behavior to light-dark (LD) cycles.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi322 – 3221S → A: Reduction in the ability of MTA1S to repress ER transactivation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Metastasis-associated protein MTA1PRO_0000083494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei386 – 3861PhosphoserineBy similarity
Modified residuei449 – 4491PhosphoserineBy similarity
Cross-linki509 – 509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)By similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei564 – 5641Phosphothreonine1 Publication
Modified residuei576 – 5761PhosphoserineBy similarity
Modified residuei578 – 5781PhosphothreonineBy similarity
Modified residuei626 – 6261N6-acetyllysineBy similarity
Cross-linki626 – 626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei639 – 6391PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER).2 Publications
Acetylation is essential for its transcriptional coactivator activity.By similarity
Sumoylation positively regulates its transcriptional corepressor activity but does not affect the protein stability. Sumoylated preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of PIAS1/3/4. Desumoylated by SENP1 (By similarity).By similarity
Ubiquitinated by RFWD2, which leads to proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8K4B0.
PaxDbiQ8K4B0.
PRIDEiQ8K4B0.

PTM databases

PhosphoSiteiQ8K4B0.

Expressioni

Tissue specificityi

Widely expressed but not in skeletal muscle. Highly expressed in the brain, liver, kidney and cardiac muscle and in mammary tumors.2 Publications

Developmental stagei

Expressed at high levels in embryonic nerve tissues, such as the brain, eyes, and spinal cord.

Inductioni

By lipopolyssacharide (LPS).1 Publication

Gene expression databases

BgeeiQ8K4B0.
CleanExiMM_MTA1.
ExpressionAtlasiQ8K4B0. baseline and differential.
GenevestigatoriQ8K4B0.

Interactioni

Subunit structurei

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR (By similarity). Binds to CSNK1G2 in the cytoplasm. Interacts with NACC2. Interacts with EP300, TFAP2C, IFI16, TPR, UBE2I/UBC9, PIAS1, PIAS3, PIAS4, MDM2, RFWD2, SUMO1, SUMO2, SENP1 and SENP2 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK. Interacts with p53/TP53 and HDAC2. Interacts with SIX3; facilitates the binding of SIX3 to the core DNA motif of SIX3 promoter.By similarity6 Publications

Protein-protein interaction databases

DIPiDIP-38226N.
IntActiQ8K4B0. 9 interactions.
MINTiMINT-1350646.
STRINGi10090.ENSMUSP00000105349.

Structurei

3D structure databases

ProteinModelPortaliQ8K4B0.
SMRiQ8K4B0. Positions 165-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 164164BAHPROSITE-ProRule annotationAdd
BLAST
Domaini165 – 276112ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini283 – 33553SANTPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi545 – 5528SH3-bindingSequence Analysis
Motifi696 – 70510SH3-bindingSequence Analysis
Motifi711 – 7155SUMO interaction motif 1 (SIM); crucial for efficient sumoylationBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi700 – 7056Poly-Pro

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation
Contains 1 ELM2 domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.Curated
Contains 1 SANT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri393 – 42028GATA-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG252834.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000045387.
HOVERGENiHBG002598.
InParanoidiQ8K4B0.
KOiK11660.
OMAiDKHATLS.
OrthoDBiEOG780RM1.
PhylomeDBiQ8K4B0.
TreeFamiTF106444.

Family and domain databases

InterProiIPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K4B0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD
60 70 80 90 100
ISSSLIALAD KHATLSVCYR AGPGADTGEE GEVEEEVENP EMVDLPEKLK
110 120 130 140 150
HQLRHRELFL SRQLESLPAT HIRGKCSVTL LNETESLKSY LEREDFFFYS
160 170 180 190 200
LVYDPQQKTL LADKGEIRVG NRYQADITDL LKEGEEDGRD QSKLETKVWE
210 220 230 240 250
AHNPLVDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM SAAAASRDIT
260 270 280 290 300
LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL
310 320 330 340 350
EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK
360 370 380 390 400
LKQVYIPNYN KPNPNQISAS SVKATVVNGT GTPGQSPGAG RACESCYTTQ
410 420 430 440 450
SYQWYSWGPP NMQCRLCASC WTYWKKYGGL KMPTRLDGER PGPNRNNMSP
460 470 480 490 500
HGIPARSSGS PKFAMKTRQA FYLHTTKLTR IARRLCREIL RPWHAARHPY
510 520 530 540 550
MPINSAAIKA ECTARLPEAS QSPLVLKQVV RKPLEAVLRY LETHPRPPKP
560 570 580 590 600
DPVKSSSSVL SSLTPAKSAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL
610 620 630 640 650
MPSRGLANHG QTRHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW
660 670 680 690 700
IDAPDDVFYM ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPLRP
710
PPPAPVNDEP IVIED
Length:715
Mass (Da):80,798
Last modified:October 1, 2002 - v1
Checksum:i135152CD3554278D
GO

Sequence cautioni

The sequence BAC57413.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641T → R in AAK83044. (PubMed:11483358)Curated
Sequence conflicti65 – 8117Missing in AAK83044. (PubMed:11483358)CuratedAdd
BLAST
Sequence conflicti420 – 4201C → W in AAK83044. (PubMed:11483358)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF463504 mRNA. Translation: AAM97588.1.
AF450245 Genomic DNA. Translation: AAM97587.1.
AF288137 mRNA. Translation: AAK83044.1.
AB039744 Genomic DNA. Translation: BAC57413.1. Different initiation.
RefSeqiXP_006515485.1. XM_006515422.1.
XP_006536382.1. XM_006536319.1.
UniGeneiMm.212577.

Genome annotation databases

EnsembliENSMUST00000009099; ENSMUSP00000009099; ENSMUSG00000021144.
GeneIDi116870.
KEGGimmu:116870.
UCSCiuc007pfw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF463504 mRNA. Translation: AAM97588.1 .
AF450245 Genomic DNA. Translation: AAM97587.1 .
AF288137 mRNA. Translation: AAK83044.1 .
AB039744 Genomic DNA. Translation: BAC57413.1 . Different initiation.
RefSeqi XP_006515485.1. XM_006515422.1.
XP_006536382.1. XM_006536319.1.
UniGenei Mm.212577.

3D structure databases

ProteinModelPortali Q8K4B0.
SMRi Q8K4B0. Positions 165-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-38226N.
IntActi Q8K4B0. 9 interactions.
MINTi MINT-1350646.
STRINGi 10090.ENSMUSP00000105349.

PTM databases

PhosphoSitei Q8K4B0.

Proteomic databases

MaxQBi Q8K4B0.
PaxDbi Q8K4B0.
PRIDEi Q8K4B0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000009099 ; ENSMUSP00000009099 ; ENSMUSG00000021144 .
GeneIDi 116870.
KEGGi mmu:116870.
UCSCi uc007pfw.1. mouse.

Organism-specific databases

CTDi 9112.
MGIi MGI:2150037. Mta1.

Phylogenomic databases

eggNOGi NOG252834.
GeneTreei ENSGT00580000081398.
HOGENOMi HOG000045387.
HOVERGENi HBG002598.
InParanoidi Q8K4B0.
KOi K11660.
OMAi DKHATLS.
OrthoDBi EOG780RM1.
PhylomeDBi Q8K4B0.
TreeFami TF106444.

Miscellaneous databases

ChiTaRSi MTA1. mouse.
PROi Q8K4B0.
SOURCEi Search...

Gene expression databases

Bgeei Q8K4B0.
CleanExi MM_MTA1.
ExpressionAtlasi Q8K4B0. baseline and differential.
Genevestigatori Q8K4B0.

Family and domain databases

InterProi IPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view ]
Pfami PF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view ]
SMARTi SM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The origin of a developmentally regulated Igh replicon is located near the border of regulatory domains for Igh replication and expression."
    Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R., Schildkraut C.L., Birshtein B.K.
    Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: BALB/c.
  2. "Differential expression and subcellular distribution of the mouse metastasis-associated proteins Mta1 and Mta3."
    Simpson A., Uitto J., Rodeck U., Mahoney M.G.
    Gene 273:29-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Strain: 129/Sv.
  3. Takiguchi S.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  4. "Metastatic tumor antigen 1 short form (MTA1s) associates with casein kinase I-gamma2, an estrogen-responsive kinase."
    Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.
    Oncogene 23:4422-4429(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSNK1G2/CK1, MUTAGENESIS OF SER-322, INTERACTION WITH CSNK1G2, SUBCELLULAR LOCATION.
  5. Cited for: TISSUE SPECIFICITY.
  6. Erratum
    Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.
    Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013)
  7. Cited for: FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: INTERACTION WITH SIX3.
  10. Cited for: FUNCTION, INTERACTION WITH TP53.
  11. Cited for: FUNCTION.
  12. "Metastasis-associated protein 1 and its short form variant stimulates Wnt1 transcription through promoting its derepression from Six3 corepressor."
    Kumar R., Balasenthil S., Manavathi B., Rayala S.K., Pakala S.B.
    Cancer Res. 70:6649-6658(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Revelation of p53-independent function of MTA1 in DNA damage response via modulation of the p21 WAF1-proliferating cell nuclear antigen pathway."
    Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y., Fu S.W., Kumar R.
    J. Biol. Chem. 285:10044-10052(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Regulation of NF-kappaB circuitry by a component of the nucleosome remodeling and deacetylase complex controls inflammatory response homeostasis."
    Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K., Behringer R.R., Kumar R.
    J. Biol. Chem. 285:23590-23597(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDAC2, INDUCTION.
  15. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Metastasis-associated protein 1 is an integral component of the circadian molecular machinery."
    Li D.Q., Pakala S.B., Reddy S.D., Peng S., Balasenthil S., Deng C.X., Lee C.C., Rea M.A., Kumar R.
    Nat. Commun. 4:2545-2545(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CLOCK AND ARNTL.
  17. "The subcellular distribution and function of MTA1 in cancer differentiation."
    Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C., Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.
    Oncotarget 5:5153-5164(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMTA1_MOUSE
AccessioniPrimary (citable) accession number: Q8K4B0
Secondary accession number(s): Q80UI1, Q8K4D4, Q924K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3