Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q06455

- MTG8_HUMAN

UniProt

Q06455 - MTG8_HUMAN

Protein

Protein CBFA2T1

Gene

RUNX1T1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transcription regulator that excerts its function by binding to histone deacetylases and transcription factors. Can repress transactivation mediated by TCF12.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei30 – 312Breakpoint for translocation to form AML1-MTG8 in AML-M2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri515 – 55137MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. fat cell differentiation Source: Ensembl
    2. generation of precursor metabolites and energy Source: ProtInc
    3. regulation of DNA binding Source: Ensembl
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein CBFA2T1
    Alternative name(s):
    Cyclin-D-related protein
    Eight twenty one protein
    Protein ETO
    Protein MTG8
    Zinc finger MYND domain-containing protein 2
    Gene namesi
    Name:RUNX1T1
    Synonyms:AML1T1, CBFA2T1, CDR, ETO, MTG8, ZMYND2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1535. RUNX1T1.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation
    Note: Colocalizes with ATN1 in discrete nuclear dots.

    GO - Cellular componenti

    1. nuclear matrix Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving RUNX1T1 is a cause of acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1/AML1.
    Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
    Note: The disease may be caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi125 – 1251K → A or D: Loss of interaction with TCF12. 1 Publication
    Mutagenesisi126 – 1261L → A: Loss of interaction with TCF12. 1 Publication
    Mutagenesisi128 – 1281R → D: Loss of interaction with TCF12. 1 Publication
    Mutagenesisi129 – 1291F → A: Loss of interaction with TCF12. 2 Publications
    Mutagenesisi129 – 1291F → K: Abolishes interaction with corepressor. 2 Publications
    Mutagenesisi136 – 1361F → A: Abolishes interaction with corepressor. 1 Publication
    Mutagenesisi170 – 1701Q → A: Abolishes interaction with corepressor. 1 Publication
    Mutagenesisi173 – 1731T → Q: Abolishes interaction with corepressor. 1 Publication
    Mutagenesisi175 – 1751F → A: Abolishes interaction with corepressor. 1 Publication
    Mutagenesisi177 – 1771L → A: Abolishes interaction with corepressor. 1 Publication
    Mutagenesisi178 – 1781R → A or D: Loss of interaction with TCF12. 1 Publication
    Mutagenesisi184 – 1841F → A: Loss of interaction with TCF12. 1 Publication
    Mutagenesisi547 – 5471H → A: Causes unfolding of the MYND-type zinc finger domain. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi114500. phenotype.
    Orphaneti102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    PharmGKBiPA26111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 604604Protein CBFA2T1PRO_0000218299Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei417 – 4171Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ06455.
    PRIDEiQ06455.

    PTM databases

    PhosphoSiteiQ06455.

    Expressioni

    Tissue specificityi

    Most abundantly expressed in brain. Lower levels in lung, heart, testis and ovary.

    Gene expression databases

    ArrayExpressiQ06455.
    BgeeiQ06455.
    GenevestigatoriQ06455.

    Interactioni

    Subunit structurei

    Homotetramer. Heterotetramer with CBFA2T2 and CBFA2T3. Interacts with TCF12, SIN3A, HDAC1, HDAC2, HDAC3, NCOR1 and NCOR2. Interacts with ATN1 (via its N-terminus); the interaction enhances the transcriptional repression.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-743342,EBI-743342
    SP1P080472EBI-743342,EBI-298336

    Protein-protein interaction databases

    BioGridi107310. 41 interactions.
    DIPiDIP-29401N.
    IntActiQ06455. 14 interactions.
    MINTiMINT-1439547.

    Structurei

    Secondary structure

    1
    604
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi121 – 1233
    Helixi125 – 13511
    Helixi137 – 1404
    Helixi142 – 15615
    Helixi162 – 17211
    Beta strandi173 – 1764
    Beta strandi179 – 1813
    Helixi182 – 1865
    Helixi189 – 19911
    Helixi200 – 2023
    Helixi209 – 2124
    Helixi347 – 39953
    Helixi444 – 46522
    Beta strandi512 – 5143
    Beta strandi516 – 5183
    Beta strandi524 – 5263
    Turni527 – 5293
    Beta strandi533 – 5364
    Helixi537 – 5426
    Helixi544 – 5474
    Turni548 – 5503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WQ6X-ray2.00A/B335-403[»]
    2DJ8NMR-A505-551[»]
    2H7BNMR-A120-222[»]
    2KNHNMR-A119-216[»]
    2KYGNMR-C437-467[»]
    2OD1NMR-A510-559[»]
    2ODDNMR-A510-559[»]
    2PP4NMR-A119-225[»]
    4JOLX-ray2.91A/B/C/D338-400[»]
    ProteinModelPortaliQ06455.
    SMRiQ06455. Positions 119-216, 341-400, 437-467, 510-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06455.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini120 – 21596TAFHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni337 – 38347Important for oligomerizationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi57 – 604Poly-Pro
    Compositional biasi102 – 1087Poly-Ser
    Compositional biasi290 – 2978Poly-Pro
    Compositional biasi408 – 4136Poly-Ser

    Domaini

    The TAFH domain mediates interaction with transcription regulators.1 Publication

    Sequence similaritiesi

    Belongs to the CBFA2T family.Curated
    Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
    Contains 1 TAFH (NHR1) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri515 – 55137MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG79810.
    HOVERGENiHBG000169.
    KOiK10053.
    OMAiPPNGYSN.
    OrthoDBiEOG70W3D2.
    PhylomeDBiQ06455.
    TreeFamiTF106303.

    Family and domain databases

    InterProiIPR013289. ETO.
    IPR013290. MTG8.
    IPR014896. NHR2.
    IPR003894. TAFH_NHR1.
    IPR002893. Znf_MYND.
    [Graphical view]
    PANTHERiPTHR10379:SF5. PTHR10379:SF5. 1 hit.
    PfamiPF08788. NHR2. 1 hit.
    PF07531. TAFH. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    PRINTSiPR01875. ETOFAMILY.
    PR01876. MTG8PROTEIN.
    SMARTiSM00549. TAFH. 1 hit.
    [Graphical view]
    PROSITEiPS51119. TAFH. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform MTG8B (identifier: Q06455-1) [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

    MISVKRNTWR ALSLVIGDCR KKGNFEYCQD RTEKHSTMPD SPVDVKTQSR    50
    LTPPTMPPPP TTQGAPRTSS FTPTTLTNGT SHSPTALNGA PSPPNGFSNG 100
    PSSSSSSSLA NQQLPPACGA RQLSKLKRFL TTLQQFGNDI SPEIGERVRT 150
    LVLGLVNSTL TIEEFHSKLQ EATNFPLRPF VIPFLKANLP LLQRELLHCA 200
    RLAKQNPAQY LAQHEQLLLD ASTTSPVDSS ELLLDVNENG KRRTPDRTKE 250
    NGFDREPLHS EHPSKRPCTI SPGQRYSPNN GLSYQPNGLP HPTPPPPQHY 300
    RLDDMAIAHH YRDSYRHPSH RDLRDRNRPM GLHGTRQEEM IDHRLTDREW 350
    AEEWKHLDHL LNCIMDMVEK TRRSLTVLRR CQEADREELN YWIRRYSDAE 400
    DLKKGGGSSS SHSRQQSPVN PDPVALDAHR EFLHRPASGY VPEEIWKKAE 450
    EAVNEVKRQA MTELQKAVSE AERKAHDMIT TERAKMERTV AEAKRQAAED 500
    ALAVINQQED SSESCWNCGR KASETCSGCN TARYCGSFCQ HKDWEKHHHI 550
    CGQTLQAQQQ GDTPAVSSSV TPNSGAGSPM DTPPAATPRS TTPGTPSTIE 600
    TTPR 604
    Length:604
    Mass (Da):67,566
    Last modified:November 1, 1997 - v2
    Checksum:iC3D2452F96E65679
    GO
    Isoform MTG8A (identifier: Q06455-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MISVKRNTWRALSLVIGDCRKKGNFEYCQ → MP

    Show »
    Length:577
    Mass (Da):64,396
    Checksum:i70E84F0120C11C3B
    GO
    Isoform 3 (identifier: Q06455-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MISVKRNTWRALSLVIGDCRKKGNFEYCQ → MCHPDKAFTSDKLQCVFNEYKAAVWVPPRPRPLSRAPLPE

    Show »
    Length:615
    Mass (Da):68,746
    Checksum:i4FB11B0FAEC56B07
    GO
    Isoform 4 (identifier: Q06455-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: Missing.

    Show »
    Length:567
    Mass (Da):63,212
    Checksum:i44AADF2EC7032050
    GO

    Sequence cautioni

    The sequence AAH05850.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA03247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti427 – 4271D → G in AAC26143. (PubMed:9661669)Curated
    Sequence conflicti455 – 4551E → G in BAH12630. (PubMed:14702039)Curated
    Sequence conflicti506 – 5061N → S in BAH12630. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti386 – 3861R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036321
    Natural varianti395 – 3951R → W in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036322
    Natural varianti471 – 4711A → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036323

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3737Missing in isoform 4. 2 PublicationsVSP_045442Add
    BLAST
    Alternative sequencei1 – 2929MISVK…FEYCQ → MCHPDKAFTSDKLQCVFNEY KAAVWVPPRPRPLSRAPLPE in isoform 3. 1 PublicationVSP_044558Add
    BLAST
    Alternative sequencei1 – 2929MISVK…FEYCQ → MP in isoform MTG8A. 1 PublicationVSP_003327Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14821 mRNA. Translation: BAA03558.1.
    D13979 mRNA. Translation: BAA03089.1. Sequence problems.
    D14289 mRNA. Translation: BAA03247.1. Different initiation.
    AF018282
    , AF018271, AF018272, AF018273, AF018274, AF018275, AF018276, AF018277, AF018278, AF018279, AF018281 Genomic DNA. Translation: AAC28932.1.
    AF018282
    , AF018270, AF018272, AF018273, AF018274, AF018275, AF018276, AF018277, AF018278, AF018279, AF018281 Genomic DNA. Translation: AAC28931.1.
    AF018283 mRNA. Translation: AAC26143.1.
    AK297616 mRNA. Translation: BAH12630.1.
    BT009871 mRNA. Translation: AAP88873.1.
    CR456792 mRNA. Translation: CAG33073.1.
    AC103680 Genomic DNA. No translation available.
    AC104339 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91685.1.
    BC005850 mRNA. Translation: AAH05850.1. Different initiation.
    BC067078 mRNA. Translation: AAH67078.2.
    AF181450 Genomic DNA. No translation available.
    D43638 mRNA. Translation: BAA07755.1.
    X79990 mRNA. Translation: CAA56311.1.
    S74096 Genomic DNA. Translation: AAB32126.1.
    S74092 Genomic DNA. No translation available.
    S78158 mRNA. Translation: AAB34819.2. Sequence problems.
    S78159 mRNA. Translation: AAB34820.2. Sequence problems.
    D14822 mRNA. Translation: BAA03559.1. Sequence problems.
    D14823 mRNA. Translation: BAA03560.1. Sequence problems.
    S50186 Genomic DNA. No translation available.
    CCDSiCCDS47891.1. [Q06455-2]
    CCDS56544.1. [Q06455-3]
    CCDS6256.1. [Q06455-1]
    CCDS6257.1. [Q06455-4]
    PIRiA57784.
    C57784.
    RefSeqiNP_001185554.1. NM_001198625.1. [Q06455-2]
    NP_001185555.1. NM_001198626.1. [Q06455-1]
    NP_001185556.1. NM_001198627.1. [Q06455-1]
    NP_001185557.1. NM_001198628.1. [Q06455-1]
    NP_001185558.1. NM_001198629.1. [Q06455-1]
    NP_001185559.1. NM_001198630.1. [Q06455-1]
    NP_001185560.1. NM_001198631.1. [Q06455-1]
    NP_001185561.1. NM_001198632.1. [Q06455-2]
    NP_001185562.1. NM_001198633.1.
    NP_001185563.1. NM_001198634.1. [Q06455-3]
    NP_001185608.1. NM_001198679.1.
    NP_004340.1. NM_004349.3. [Q06455-2]
    NP_783552.1. NM_175634.2. [Q06455-1]
    NP_783553.1. NM_175635.2. [Q06455-4]
    NP_783554.1. NM_175636.2. [Q06455-4]
    XP_006716739.1. XM_006716676.1. [Q06455-4]
    UniGeneiHs.368431.
    Hs.739194.

    Genome annotation databases

    EnsembliENST00000265814; ENSP00000265814; ENSG00000079102. [Q06455-1]
    ENST00000360348; ENSP00000353504; ENSG00000079102. [Q06455-4]
    ENST00000396218; ENSP00000379520; ENSG00000079102. [Q06455-2]
    ENST00000422361; ENSP00000390137; ENSG00000079102. [Q06455-4]
    ENST00000436581; ENSP00000402257; ENSG00000079102. [Q06455-3]
    ENST00000518844; ENSP00000430728; ENSG00000079102. [Q06455-2]
    ENST00000520724; ENSP00000428742; ENSG00000079102. [Q06455-4]
    ENST00000523629; ENSP00000428543; ENSG00000079102. [Q06455-1]
    GeneIDi862.
    KEGGihsa:862.
    UCSCiuc003yfb.2. human. [Q06455-1]
    uc003yfc.2. human. [Q06455-2]

    Polymorphism databases

    DMDMi2498595.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14821 mRNA. Translation: BAA03558.1 .
    D13979 mRNA. Translation: BAA03089.1 . Sequence problems.
    D14289 mRNA. Translation: BAA03247.1 . Different initiation.
    AF018282
    , AF018271 , AF018272 , AF018273 , AF018274 , AF018275 , AF018276 , AF018277 , AF018278 , AF018279 , AF018281 Genomic DNA. Translation: AAC28932.1 .
    AF018282
    , AF018270 , AF018272 , AF018273 , AF018274 , AF018275 , AF018276 , AF018277 , AF018278 , AF018279 , AF018281 Genomic DNA. Translation: AAC28931.1 .
    AF018283 mRNA. Translation: AAC26143.1 .
    AK297616 mRNA. Translation: BAH12630.1 .
    BT009871 mRNA. Translation: AAP88873.1 .
    CR456792 mRNA. Translation: CAG33073.1 .
    AC103680 Genomic DNA. No translation available.
    AC104339 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91685.1 .
    BC005850 mRNA. Translation: AAH05850.1 . Different initiation.
    BC067078 mRNA. Translation: AAH67078.2 .
    AF181450 Genomic DNA. No translation available.
    D43638 mRNA. Translation: BAA07755.1 .
    X79990 mRNA. Translation: CAA56311.1 .
    S74096 Genomic DNA. Translation: AAB32126.1 .
    S74092 Genomic DNA. No translation available.
    S78158 mRNA. Translation: AAB34819.2 . Sequence problems.
    S78159 mRNA. Translation: AAB34820.2 . Sequence problems.
    D14822 mRNA. Translation: BAA03559.1 . Sequence problems.
    D14823 mRNA. Translation: BAA03560.1 . Sequence problems.
    S50186 Genomic DNA. No translation available.
    CCDSi CCDS47891.1. [Q06455-2 ]
    CCDS56544.1. [Q06455-3 ]
    CCDS6256.1. [Q06455-1 ]
    CCDS6257.1. [Q06455-4 ]
    PIRi A57784.
    C57784.
    RefSeqi NP_001185554.1. NM_001198625.1. [Q06455-2 ]
    NP_001185555.1. NM_001198626.1. [Q06455-1 ]
    NP_001185556.1. NM_001198627.1. [Q06455-1 ]
    NP_001185557.1. NM_001198628.1. [Q06455-1 ]
    NP_001185558.1. NM_001198629.1. [Q06455-1 ]
    NP_001185559.1. NM_001198630.1. [Q06455-1 ]
    NP_001185560.1. NM_001198631.1. [Q06455-1 ]
    NP_001185561.1. NM_001198632.1. [Q06455-2 ]
    NP_001185562.1. NM_001198633.1.
    NP_001185563.1. NM_001198634.1. [Q06455-3 ]
    NP_001185608.1. NM_001198679.1.
    NP_004340.1. NM_004349.3. [Q06455-2 ]
    NP_783552.1. NM_175634.2. [Q06455-1 ]
    NP_783553.1. NM_175635.2. [Q06455-4 ]
    NP_783554.1. NM_175636.2. [Q06455-4 ]
    XP_006716739.1. XM_006716676.1. [Q06455-4 ]
    UniGenei Hs.368431.
    Hs.739194.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WQ6 X-ray 2.00 A/B 335-403 [» ]
    2DJ8 NMR - A 505-551 [» ]
    2H7B NMR - A 120-222 [» ]
    2KNH NMR - A 119-216 [» ]
    2KYG NMR - C 437-467 [» ]
    2OD1 NMR - A 510-559 [» ]
    2ODD NMR - A 510-559 [» ]
    2PP4 NMR - A 119-225 [» ]
    4JOL X-ray 2.91 A/B/C/D 338-400 [» ]
    ProteinModelPortali Q06455.
    SMRi Q06455. Positions 119-216, 341-400, 437-467, 510-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107310. 41 interactions.
    DIPi DIP-29401N.
    IntActi Q06455. 14 interactions.
    MINTi MINT-1439547.

    PTM databases

    PhosphoSitei Q06455.

    Polymorphism databases

    DMDMi 2498595.

    Proteomic databases

    PaxDbi Q06455.
    PRIDEi Q06455.

    Protocols and materials databases

    DNASUi 862.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265814 ; ENSP00000265814 ; ENSG00000079102 . [Q06455-1 ]
    ENST00000360348 ; ENSP00000353504 ; ENSG00000079102 . [Q06455-4 ]
    ENST00000396218 ; ENSP00000379520 ; ENSG00000079102 . [Q06455-2 ]
    ENST00000422361 ; ENSP00000390137 ; ENSG00000079102 . [Q06455-4 ]
    ENST00000436581 ; ENSP00000402257 ; ENSG00000079102 . [Q06455-3 ]
    ENST00000518844 ; ENSP00000430728 ; ENSG00000079102 . [Q06455-2 ]
    ENST00000520724 ; ENSP00000428742 ; ENSG00000079102 . [Q06455-4 ]
    ENST00000523629 ; ENSP00000428543 ; ENSG00000079102 . [Q06455-1 ]
    GeneIDi 862.
    KEGGi hsa:862.
    UCSCi uc003yfb.2. human. [Q06455-1 ]
    uc003yfc.2. human. [Q06455-2 ]

    Organism-specific databases

    CTDi 862.
    GeneCardsi GC08M092971.
    HGNCi HGNC:1535. RUNX1T1.
    MIMi 114500. phenotype.
    133435. gene.
    neXtProti NX_Q06455.
    Orphaneti 102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    PharmGKBi PA26111.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79810.
    HOVERGENi HBG000169.
    KOi K10053.
    OMAi PPNGYSN.
    OrthoDBi EOG70W3D2.
    PhylomeDBi Q06455.
    TreeFami TF106303.

    Miscellaneous databases

    ChiTaRSi RUNX1T1. human.
    EvolutionaryTracei Q06455.
    GeneWikii RUNX1T1.
    GenomeRNAii 862.
    NextBioi 3586.
    PROi Q06455.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06455.
    Bgeei Q06455.
    Genevestigatori Q06455.

    Family and domain databases

    InterProi IPR013289. ETO.
    IPR013290. MTG8.
    IPR014896. NHR2.
    IPR003894. TAFH_NHR1.
    IPR002893. Znf_MYND.
    [Graphical view ]
    PANTHERi PTHR10379:SF5. PTHR10379:SF5. 1 hit.
    Pfami PF08788. NHR2. 1 hit.
    PF07531. TAFH. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view ]
    PRINTSi PR01875. ETOFAMILY.
    PR01876. MTG8PROTEIN.
    SMARTi SM00549. TAFH. 1 hit.
    [Graphical view ]
    PROSITEi PS51119. TAFH. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript."
      Miyoshi H., Kozu T., Shimizu K., Enomoto K., Maseki N., Kaneko Y., Kamada N., Ohki M.
      EMBO J. 12:2715-2721(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MTG8B), VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
      Tissue: Fetal brain.
    2. "Structure and expression of the human MTG8/ETO gene."
      Wolford J.K., Prochazka M.
      Gene 212:103-109(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MTG8B).
    3. "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 3).
      Tissue: Brain.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MTG8A).
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 4).
      Tissue: Muscle.
    9. "The ETO portion of acute myeloid leukemia t(8;21) fusion transcript encodes a highly evolutionarily conserved putative transcription factor."
      Erickson P.F., Robinson M., Owens G., Drabkin H.A.
      Cancer Res. 54:1782-1786(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-604.
    10. "Alternative, out-of-frame runt/MTG8 transcripts are encoded by the derivative (8) chromosome in the t(8;21) of acute myeloid leukemia M2."
      Tighe J.E., Calabi F.
      Blood 84:2115-2121(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-432, VARIANT AML1-MTG8/ETO FUSION.
    11. "Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription."
      Wood J.D., Nucifora F.C. Jr., Duan K., Zhang C., Wang J., Kim Y., Schilling G., Sacchi N., Liu J.M., Ross C.A.
      J. Cell Biol. 150:939-948(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATN1, SUBCELLULAR LOCATION, FUNCTION.
    12. "The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t(16; 21)-positive myeloid malignancies."
      Hoogeveen A.T., Rossetti S., Stoyanova V., Schonkeren J., Fenaroli A., Schiaffonati L., van Unen L., Sacchi N.
      Oncogene 21:6703-6712(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBFA2T3.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-41 AND SER-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity."
      Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D., Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H.
      Cancer Cell 9:249-260(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 335-403, SUBUNIT, INTERACTION WITH HDAC1; HDAC2; HDAC3; TCF12; NCOR1; NCOR2; SIN3A; CBFA2T2 AND CBFA2T3.
    16. "The acute myeloid leukemia fusion protein AML1-ETO targets E proteins via a paired amphipathic helix-like TBP-associated factor homology domain."
      Plevin M.J., Zhang J., Guo C., Roeder R.G., Ikura M.
      Proc. Natl. Acad. Sci. U.S.A. 103:10242-10247(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 120-222, INTERACTION WITH TCF12, FUNCTION, MUTAGENESIS OF LYS-125; LEU-126; ARG-128; PHE-129; ARG-178 AND PHE-184.
    17. "Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity."
      Liu Y., Chen W., Gaudet J., Cheney M.D., Roudaia L., Cierpicki T., Klet R.C., Hartman K., Laue T.M., Speck N.A., Bushweller J.H.
      Cancer Cell 11:483-497(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 510-559 IN COMPLEX WITH ZINC IONS AND NCOR2, MUTAGENESIS OF HIS-547, INTERACTION WITH NCOR1 AND NCOR2.
    18. "A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription."
      Wei Y., Liu S., Lausen J., Woodrell C., Cho S., Biris N., Kobayashi N., Wei Y., Yokoyama S., Werner M.H.
      Nat. Struct. Mol. Biol. 14:653-661(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 119-225, INTERACTION WITH NCOR1 AND TCF12, MUTAGENESIS OF PHE-129; PHE-136; GLN-170; THR-173; PHE-175 AND LEU-177, DOMAIN.
    19. "Solution structure of ZF-MYND domain of protein CBFA2TI (protein MTG8)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 505-551.
    20. "Identification of two transcripts of AML1/ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells."
      Era T., Asou N., Kunisada T., Yamasaki H., Asou H., Kamada N., Nishikawa S., Yamaguchi K., Takatsuki K.
      Genes Chromosomes Cancer 13:25-33(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
    21. "Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction."
      Kozu T., Miyoshi H., Shimizu K., Maseki N., Kaneko Y., Asou H., Kamada N., Ohki M.
      Blood 82:1270-1276(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
    22. "Transcriptionally active chimeric gene derived from the fusion of the AML1 gene and a novel gene on chromosome 8 in t(8;21) leukemic cells."
      Nisson P.E., Watkins P.C., Sacchi N.
      Cancer Genet. Cytogenet. 63:81-88(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
    23. Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-386; TRP-395 AND VAL-471.

    Entry informationi

    Entry nameiMTG8_HUMAN
    AccessioniPrimary (citable) accession number: Q06455
    Secondary accession number(s): B7Z4P4
    , E7EPN4, O14784, Q06456, Q14873, Q16239, Q16346, Q16347, Q6IBL1, Q6NXH1, Q7Z4J5, Q92479, Q9BRZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 154 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3