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Q9BTC8

- MTA3_HUMAN

UniProt

Q9BTC8 - MTA3_HUMAN

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Protein

Metastasis-associated protein MTA3

Gene

MTA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels. Contributes to transcriptional repression by BCL6.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri379 – 40628GATA-type; atypicalAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. sequence-specific DNA binding Source: InterPro
  3. sequence-specific DNA binding transcription factor activity Source: InterPro
  4. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_228222. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Metastasis-associated protein MTA3
Gene namesi
Name:MTA3
Synonyms:KIAA1266
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:23784. MTA3.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134953540.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Metastasis-associated protein MTA3PRO_0000083498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei455 – 4551Phosphothreonine1 Publication
Modified residuei457 – 4571Phosphoserine1 Publication
Modified residuei519 – 5191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BTC8.
PaxDbiQ9BTC8.
PRIDEiQ9BTC8.

PTM databases

PhosphoSiteiQ9BTC8.

Expressioni

Tissue specificityi

Expressed in germinal centers of lymphoid tissues. No expression in nonepithelial cells.1 Publication

Inductioni

By estrogen.1 Publication

Gene expression databases

BgeeiQ9BTC8.
CleanExiHS_MTA3.
ExpressionAtlasiQ9BTC8. baseline and differential.
GenevestigatoriQ9BTC8.

Organism-specific databases

HPAiHPA039433.

Interactioni

Subunit structurei

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with BCL6. Interacts with NACC2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033723EBI-2461787,EBI-78473

Protein-protein interaction databases

BioGridi121568. 39 interactions.
DIPiDIP-47460N.
IntActiQ9BTC8. 17 interactions.
MINTiMINT-4538323.
STRINGi9606.ENSP00000385045.

Structurei

3D structure databases

ProteinModelPortaliQ9BTC8.
SMRiQ9BTC8. Positions 148-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 147147BAHPROSITE-ProRule annotationAdd
BLAST
Domaini148 – 259112ELM2PROSITE-ProRule annotationAdd
BLAST
Domaini266 – 31853SANTPROSITE-ProRule annotationAdd
BLAST

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 fingeri379 – 40628GATA-type; atypicalAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG252834.
GeneTreeiENSGT00580000081398.
HOGENOMiHOG000045387.
HOVERGENiHBG002598.
InParanoidiQ9BTC8.
KOiK11660.
OMAiHMSRQAT.
PhylomeDBiQ9BTC8.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BTC8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTASGNVEA KVVCFYRRRD
60 70 80 90 100
ISNTLIMLAD KHAKEIEEES ETTVEADLTD KQKHQLKHRE LFLSRQYESL
110 120 130 140 150
PATHIRGKCS VALLNETESV LSYLDKEDTF FYSLVYDPSL KTLLADKGEI
160 170 180 190 200
RVGPRYQADI PEMLLEGESD EREQSKLEVK VWDPNSPLTD RQIDQFLVVA
210 220 230 240 250
RAVGTFARAL DCSSSVRQPS LHMSAAAASR DITLFHAMDT LYRHSYDLSS
260 270 280 290 300
AISVLVPLGG PVLCRDEMEE WSASEASLFE EALEKYGKDF NDIRQDFLPW
310 320 330 340 350
KSLTSIIEYY YMWKTTDRYV QQKRLKAAEA ESKLKQVYIP TYSKPNPNQI
360 370 380 390 400
STSNGKPGAV NGAVGTTFQP QNPLLGRACE SCYATQSHQW YSWGPPNMQC
410 420 430 440 450
RLCAICWLYW KKYGGLKMPT QSEEEKLSPS PTTEDPRVRS HVSRQAMQGM
460 470 480 490 500
PVRNTGSPKS AVKTRQAFFL HTTYFTKFAR QVCKNTLRLR QAARRPFVAI
510 520 530 540 550
NYAAIRAEYA DRHAELSGSP LKSKSTRKPL ACIIGYLEIH PAKKPNVIRS
560 570 580 590
TPSLQTPTTK RMLTTPNHTS LSILGKRNYS HHNGLDELTC CVSD
Length:594
Mass (Da):67,504
Last modified:February 28, 2003 - v2
Checksum:iE773603F65A16DF1
GO
Isoform 2 (identifier: Q9BTC8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     509-515: YADRHAE → CKMLLNS
     516-594: Missing.

Show »
Length:515
Mass (Da):58,814
Checksum:i55E53C5ABC30528C
GO

Sequence cautioni

The sequence BAA86580.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 99MAANMYRVG → ATGGFPRDR in BAA86580. (PubMed:10574462)Curated
Sequence conflicti343 – 3431Missing in BAA86580. (PubMed:10574462)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei509 – 5157YADRHAE → CKMLLNS in isoform 2. 2 PublicationsVSP_001603
Alternative sequencei516 – 59479Missing in isoform 2. 2 PublicationsVSP_001604Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033092 mRNA. Translation: BAA86580.1. Different initiation.
AK027304 mRNA. Translation: BAB55028.1.
BC004227 mRNA. Translation: AAH04227.1.
BC053631 mRNA. Translation: AAH53631.1.
AL161954 mRNA. Translation: CAB82305.1.
CCDSiCCDS46267.1. [Q9BTC8-2]
PIRiT47180.
RefSeqiNP_001269684.1. NM_001282755.1.
NP_001269685.1. NM_001282756.1.
NP_065795.1. NM_020744.3. [Q9BTC8-2]
XP_005264513.1. XM_005264456.2. [Q9BTC8-1]
UniGeneiHs.435413.
Hs.646800.
Hs.745162.

Genome annotation databases

EnsembliENST00000405094; ENSP00000385823; ENSG00000057935. [Q9BTC8-1]
ENST00000407270; ENSP00000385045; ENSG00000057935. [Q9BTC8-2]
GeneIDi57504.
KEGGihsa:57504.
UCSCiuc002rsq.3. human. [Q9BTC8-2]

Polymorphism databases

DMDMi29840798.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033092 mRNA. Translation: BAA86580.1 . Different initiation.
AK027304 mRNA. Translation: BAB55028.1 .
BC004227 mRNA. Translation: AAH04227.1 .
BC053631 mRNA. Translation: AAH53631.1 .
AL161954 mRNA. Translation: CAB82305.1 .
CCDSi CCDS46267.1. [Q9BTC8-2 ]
PIRi T47180.
RefSeqi NP_001269684.1. NM_001282755.1.
NP_001269685.1. NM_001282756.1.
NP_065795.1. NM_020744.3. [Q9BTC8-2 ]
XP_005264513.1. XM_005264456.2. [Q9BTC8-1 ]
UniGenei Hs.435413.
Hs.646800.
Hs.745162.

3D structure databases

ProteinModelPortali Q9BTC8.
SMRi Q9BTC8. Positions 148-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121568. 39 interactions.
DIPi DIP-47460N.
IntActi Q9BTC8. 17 interactions.
MINTi MINT-4538323.
STRINGi 9606.ENSP00000385045.

PTM databases

PhosphoSitei Q9BTC8.

Polymorphism databases

DMDMi 29840798.

Proteomic databases

MaxQBi Q9BTC8.
PaxDbi Q9BTC8.
PRIDEi Q9BTC8.

Protocols and materials databases

DNASUi 57504.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000405094 ; ENSP00000385823 ; ENSG00000057935 . [Q9BTC8-1 ]
ENST00000407270 ; ENSP00000385045 ; ENSG00000057935 . [Q9BTC8-2 ]
GeneIDi 57504.
KEGGi hsa:57504.
UCSCi uc002rsq.3. human. [Q9BTC8-2 ]

Organism-specific databases

CTDi 57504.
GeneCardsi GC02P042722.
HGNCi HGNC:23784. MTA3.
HPAi HPA039433.
MIMi 609050. gene.
neXtProti NX_Q9BTC8.
PharmGKBi PA134953540.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252834.
GeneTreei ENSGT00580000081398.
HOGENOMi HOG000045387.
HOVERGENi HBG002598.
InParanoidi Q9BTC8.
KOi K11660.
OMAi HMSRQAT.
PhylomeDBi Q9BTC8.
TreeFami TF106444.

Enzyme and pathway databases

Reactomei REACT_228222. HDACs deacetylate histones.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSi MTA3. human.
GeneWikii MTA3.
GenomeRNAii 57504.
NextBioi 63833.
PROi Q9BTC8.
SOURCEi Search...

Gene expression databases

Bgeei Q9BTC8.
CleanExi HS_MTA3.
ExpressionAtlasi Q9BTC8. baseline and differential.
Genevestigatori Q9BTC8.

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. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryo.
  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] (ISOFORM 2).
    Tissue: Lymph and Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-594.
    Tissue: Testis.
  5. "MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in breast cancer."
    Fujita N., Jaye D.L., Kajita M., Geigerman C., Moreno C.S., Wade P.A.
    Cell 113:207-219(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN NURD COMPLEX, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
  6. "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
    Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
    Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BCL6, IDENTIFICATION IN THE NURD COMPLEX.
  7. "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 THR-455; SER-457 AND SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene."
    Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z., Shang Y.
    Oncogene 32:3711-3721(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NACC2.

Entry informationi

Entry nameiMTA3_HUMAN
AccessioniPrimary (citable) accession number: Q9BTC8
Secondary accession number(s): Q9NSP2, Q9ULF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: February 28, 2003
Last modified: November 26, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3