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Q9BTC0

- DIDO1_HUMAN

UniProt

Q9BTC0 - DIDO1_HUMAN

Protein

Death-inducer obliterator 1

Gene

DIDO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 5 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Putative transcription factor, weakly pro-apoptotic when overexpressed By similarity. Tumor suppressor. Required for early embryonic stem cell development.By similarity1 Publication
    Isoform 2: Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri268 – 32255PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic signaling pathway Source: Ensembl
    2. transcription, DNA-templated Source: InterPro

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Death-inducer obliterator 1
    Short name:
    DIO-1
    Short name:
    hDido1
    Alternative name(s):
    Death-associated transcription factor 1
    Short name:
    DATF-1
    Gene namesi
    Name:DIDO1
    Synonyms:C20orf158, DATF1, KIAA0333
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:2680. DIDO1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus PROSITE-ProRule annotation. Cytoplasmcytoskeletonspindle 1 Publication
    Note: Translocates to the nucleus after pro-apoptotic stimuli By similarity. Translocates to the mitotic spindle upon loss of interaction with H3K4me3 during early mitosis.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi291 – 2911W → T: Abolishes binding to H3K4me3. 1 Publication

    Organism-specific databases

    PharmGKBiPA27147.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22402240Death-inducer obliterator 1PRO_0000059324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei151 – 1511Phosphothreonine2 Publications
    Modified residuei152 – 1521Phosphoserine3 Publications
    Modified residuei154 – 1541Phosphoserine3 Publications
    Modified residuei805 – 8051Phosphoserine5 Publications
    Modified residuei809 – 8091Phosphoserine4 Publications
    Modified residuei898 – 8981Phosphoserine3 Publications
    Modified residuei1019 – 10191Phosphoserine1 Publication
    Modified residuei1030 – 10301Phosphoserine2 Publications
    Modified residuei1040 – 10401Phosphoserine3 Publications
    Modified residuei1260 – 12601Phosphoserine2 Publications
    Modified residuei1312 – 13121Phosphoserine1 Publication
    Modified residuei1456 – 14561Phosphoserine5 Publications
    Modified residuei1469 – 14691Phosphothreonine1 Publication
    Modified residuei1522 – 15221Phosphoserine1 Publication
    Modified residuei1714 – 17141Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BTC0.
    PaxDbiQ9BTC0.
    PeptideAtlasiQ9BTC0.
    PRIDEiQ9BTC0.

    PTM databases

    PhosphoSiteiQ9BTC0.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    BgeeiQ9BTC0.
    GenevestigatoriQ9BTC0.

    Organism-specific databases

    HPAiCAB004374.
    HPA049904.

    Interactioni

    Subunit structurei

    Interacts specifically (via PHD-type zinc finger) with histone H3 that is trimethylated at 'Lys-4' (H3K4me3), histone phosphorylation at 'Thr-3' or 'Thr-6' disrupts this binding and promotes translocation of DIDO1 from chromatin to the mitotic spindle during mitosis.1 Publication

    Protein-protein interaction databases

    BioGridi116266. 30 interactions.
    IntActiQ9BTC0. 14 interactions.
    MINTiMINT-3061319.

    Structurei

    Secondary structure

    1
    2240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni271 – 2744
    Beta strandi277 – 2804
    Beta strandi282 – 2843
    Turni286 – 2883
    Beta strandi291 – 2933
    Helixi294 – 2974
    Helixi301 – 31010
    Turni317 – 3193

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M3HNMR-A265-322[»]
    4L7XX-ray1.35A266-325[»]
    ProteinModelPortaliQ9BTC0.
    SMRiQ9BTC0. Positions 265-355, 669-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini670 – 790121TFIIS centralPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi165 – 1739Nuclear localization signalSequence Analysis
    Motifi185 – 1939Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1257 – 128630Pro-richAdd
    BLAST
    Compositional biasi1725 – 2034310Pro-richAdd
    BLAST
    Compositional biasi2108 – 2214107Arg-richAdd
    BLAST

    Domaini

    The PHD-type zinc finger forms an aromatic cage around H3K4me3.

    Sequence similaritiesi

    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 TFIIS central domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri268 – 32255PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG255142.
    HOVERGENiHBG060199.
    InParanoidiQ9BTC0.
    OMAiGPHPNQF.
    OrthoDBiEOG7NW685.
    PhylomeDBiQ9BTC0.
    TreeFamiTF350578.

    Family and domain databases

    Gene3Di1.10.472.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR012921. SPOC_C.
    IPR003618. TFIIS_cen_dom.
    IPR017890. TFS2M.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00628. PHD. 1 hit.
    PF07744. SPOC. 1 hit.
    PF07500. TFIIS_M. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    SM00510. TFS2M. 1 hit.
    [Graphical view]
    SUPFAMiSSF46942. SSF46942. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS51321. TFIIS_CENTRAL. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: Q9BTC0-4) [UniParc]FASTAAdd to Basket

    Also known as: DIDO3

    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

    MDDKGDPSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDAEADPLEP     50
    PPPQQQLGLS LRRSGRQPKR TERVEQFLTI ARRRGRRSMP VSLEDSGEPT 100
    SCPATDAETA SEGSVESASE TRSGPQSAST AVKERPASSE KVKGGDDHDD 150
    TSDSDSDGLT LKELQNRLRR KREQEPTERP LKGIQSRLRK KRREEGPAET 200
    VGSEASDTVE GVLPSKQEPE NDQGVVSQAG KDDRESKLEG KAAQDIKDEE 250
    PGDLGRPKPE CEGYDPNALY CICRQPHNNR FMICCDRCEE WFHGDCVGIS 300
    EARGRLLERN GEDYICPNCT ILQVQDETHS ETADQQEAKW RPGDADGTDC 350
    TSIGTIEQKS SEDQGIKGRI EKAANPSGKK KLKIFQPVIE APGASKCIGP 400
    GCCHVAQPDS VYCSNDCILK HAAATMKFLS SGKEQKPKPK EKMKMKPEKP 450
    SLPKCGAQAG IKISSVHKRP APEKKETTVK KAVVVPARSE ALGKEAACES 500
    STPSWASDHN YNAVKPEKTA APSPSLLYKS TKEDRRSEEK AAAMAASKKT 550
    APPGSAVGKQ PAPRNLVPKK SSFANVAAAT PAIKKPPSGF KGTIPKRPWL 600
    SATPSSGASA ARQAGPAPAA ATAASKKFPG SAALVGAVRK PVVPSVPMAS 650
    PAPGRLGAMS AAPSQPNSQI RQNIRRSLKE ILWKRVNDSD DLIMTENEVG 700
    KIALHIEKEM FNLFQVTDNR YKSKYRSIMF NLKDPKNQGL FHRVLREEIS 750
    LAKLVRLKPE ELVSKELSTW KERPARSVME SRTKLHNESK KTAPRQEAIP 800
    DLEDSPPVSD SEEQQESARA VPEKSTAPLL DVFSSMLKDT TSQHRAHLFD 850
    LNCKICTGQV PSAEDEPAPK KQKLSASVKK EDLKSKHDSS APDPAPDSAD 900
    EVMPEAVPEV ASEPGLESAS HPNVDRTYFP GPPGDGHPEP SPLEDLSPCP 950
    ASCGSGVVTT VTVSGRDPRT APSSSCTAVA SAASRPDSTH MVEARQDVPK 1000
    PVLTSVMVPK SILAKPSSSP DPRYLSVPPS PNISTSESRS PPEGDTTLFL 1050
    SRLSTIWKGF INMQSVAKFV TKAYPVSGCF DYLSEDLPDT IHIGGRIAPK 1100
    TVWDYVGKLK SSVSKELCLI RFHPATEEEE VAYISLYSYF SSRGRFGVVA 1150
    NNNRHVKDLY LIPLSAQDPV PSKLLPFEGP GLESPRPNII LGLVICQKIK 1200
    RPANSGELDK MDEKRTRLQP EEADVPAYPK VATVPQSEKK PSKYPLCSAD 1250
    AAVSTTPPGS PPPPPPLPEP PVLKVLSSLK PAAPSPATAA TTAAAASTAA 1300
    SSTASSASKT ASPLEHILQT LFGKKKSFDP SAREPPGSTA GLPQEPKTTA 1350
    EDGVPAPPLL DPIVQQFGQF SKDKALEEEE DDRPYDPEEE YDPERAFDTQ 1400
    LVERGRRHEV ERAPEAAAAE REEVAYDPED ETILEEAKVT VDDLPNRMCA 1450
    DVRRNSVERP AEPVAGAATP SLVEQQKMLE ELNKQIEEQK RQLEEQEEAL 1500
    RQQRAAVGVS MAHFSVSDAL MSPPPKSSLP KAELFQQEQQ SADKPASLPP 1550
    ASQASNHRDP RQARRLATET GEGEGEPLSR LSARGAQGAL PERDASRGGL 1600
    VGQAPMPVPE EKEPASSPWA SGEKPPAGSE QDGWKAEPGE GTRPATVGDS 1650
    SARPARRVLL PTPPCGALQP GFPLQHDGER DPFTCPGFAS QDKALGSAQY 1700
    EDPRNLHSAG RSSSPAGETE GDREPQARPG EGTAPLPPPG QKVGGSQPPF 1750
    QGQREPGPHA LGMSGLHGPN FPGPRGPAPP FPEENIASND GPRGPPPARF 1800
    GAQKGPIPSL FSGQHGPPPY GDSRGPSPSY LGGPRGVAPS QFEERKDPHG 1850
    EKREFQDAPY NEVTGAPAQF EGTEQAPFLG SRGGAPFQFG GQRRPLLSQL 1900
    KGPRGGPPPS QFGGQRGPPP GHFVGPRGPH PSQFETARGP HPNQFEGPRG 1950
    QAPNFMPGPR GIQPQQFEDQ RVHSPPRFTN QRAPAPLQFG GLRGSAPFSE 2000
    KNEQTPSRFH FQGQAPQVMK PGPRPLLELP SHPPQHRKDR WEEAGPPSAL 2050
    SSSAPGQGPE ADGQWASADF REGKGHEYRN QTFEGRQRER FDVGPKEKPL 2100
    EEPDAQGRAS EDRRRERERG RNWSRERDWD RPREWDRHRD KDSSRDWDRN 2150
    RERSANRDRE READRGKEWD RSRERSRNRE RERDRRRDRD RSRSRERDRD 2200
    KARDRERGRD RKDRSKSKES ARDPKPEASR ASDAGTASQA 2240
    Length:2,240
    Mass (Da):243,873
    Last modified:October 17, 2006 - v5
    Checksum:i9B89361A24A72C58
    GO
    Isoform 1 (identifier: Q9BTC0-1) [UniParc]FASTAAdd to Basket

    Also known as: DIDO2

    The sequence of this isoform differs from the canonical sequence as follows:
         1182-1189: LESPRPNI → KRRLSGWR
         1190-2240: Missing.

    Show »
    Length:1,189
    Mass (Da):129,181
    Checksum:i6C536EE25776C086
    GO
    Isoform 2 (identifier: Q9BTC0-2) [UniParc]FASTAAdd to Basket

    Also known as: DIDO1

    The sequence of this isoform differs from the canonical sequence as follows:
         530-544: STKEDRRSEEKAAAM → CSGKYSYSLHPSLIA
         545-2240: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:544
    Mass (Da):59,461
    Checksum:i192BE2A77ED5FADA
    GO
    Isoform 3 (identifier: Q9BTC0-3) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         530-562: STKEDRRSEEKAAAMAASKKTAPPGSAVGKQPA → CMYHLGVGLLDPSRSFWIAIPWACPGLGVAALC
         563-2240: Missing.

    Show »
    Length:562
    Mass (Da):61,354
    Checksum:i91A714668F9C5C12
    GO

    Sequence cautioni

    The sequence BAA20791.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521G → E in BAA92094. (PubMed:14702039)Curated
    Isoform 2 (identifier: Q9BTC0-2)
    Sequence conflicti535 – 5351S → L in AAH00770. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131P → L.
    Corresponds to variant rs6090161 [ dbSNP | Ensembl ].
    VAR_028310
    Natural varianti276 – 2761P → L.
    Corresponds to variant rs6090160 [ dbSNP | Ensembl ].
    VAR_028311
    Natural varianti544 – 5441M → T.1 Publication
    Corresponds to variant rs1883848 [ dbSNP | Ensembl ].
    VAR_057093
    Natural varianti556 – 5561A → T.1 Publication
    Corresponds to variant rs1883847 [ dbSNP | Ensembl ].
    VAR_057094
    Natural varianti793 – 7931A → G.
    Corresponds to variant rs750077 [ dbSNP | Ensembl ].
    VAR_057095
    Natural varianti1220 – 12201P → Q.
    Corresponds to variant rs6011441 [ dbSNP | Ensembl ].
    VAR_057096
    Natural varianti1708 – 17081S → C.
    Corresponds to variant rs41282984 [ dbSNP | Ensembl ].
    VAR_061740

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei530 – 56233STKED…GKQPA → CMYHLGVGLLDPSRSFWIAI PWACPGLGVAALC in isoform 3. 2 PublicationsVSP_007211Add
    BLAST
    Alternative sequencei530 – 54415STKED…KAAAM → CSGKYSYSLHPSLIA in isoform 2. 1 PublicationVSP_007209Add
    BLAST
    Alternative sequencei545 – 22401696Missing in isoform 2. 1 PublicationVSP_007210Add
    BLAST
    Alternative sequencei563 – 22401678Missing in isoform 3. 2 PublicationsVSP_007212Add
    BLAST
    Alternative sequencei1182 – 11898LESPRPNI → KRRLSGWR in isoform 1. 3 PublicationsVSP_017225
    Alternative sequencei1190 – 22401051Missing in isoform 1. 3 PublicationsVSP_017226Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY481571 mRNA. Translation: AAS49898.1.
    AY481572 mRNA. Translation: AAS49899.1.
    AB002331 mRNA. Translation: BAA20791.2. Different initiation.
    AK002127 mRNA. Translation: BAA92094.1.
    AL117379, AL035669 Genomic DNA. Translation: CAI95707.1.
    AL117379, AL035669 Genomic DNA. Translation: CAO03650.1.
    AL035669, AL117379 Genomic DNA. Translation: CAI95769.2.
    AL035669, AL117379 Genomic DNA. Translation: CAI95761.1.
    AL117379, AL035669 Genomic DNA. Translation: CAI95708.1.
    AL035669, AL117379 Genomic DNA. Translation: CAI95762.1.
    AL035669, AL117379 Genomic DNA. Translation: CAI95770.2.
    AL117379, AL035669 Genomic DNA. Translation: CAM28273.1.
    CH471077 Genomic DNA. Translation: EAW75322.1.
    CH471077 Genomic DNA. Translation: EAW75323.1.
    BC000770 mRNA. Translation: AAH00770.1.
    BC004237 mRNA. Translation: AAH04237.1.
    BC012757 mRNA. No translation available.
    BC014489 mRNA. Translation: AAH14489.1.
    BC137177 mRNA. Translation: AAI37178.1.
    AL133063 mRNA. Translation: CAB61387.1.
    CCDSiCCDS13508.2. [Q9BTC0-1]
    CCDS13509.1. [Q9BTC0-3]
    CCDS33506.1. [Q9BTC0-4]
    RefSeqiNP_001180298.1. NM_001193369.1. [Q9BTC0-4]
    NP_001180299.1. NM_001193370.1. [Q9BTC0-1]
    NP_071388.2. NM_022105.4. [Q9BTC0-3]
    NP_149072.2. NM_033081.2. [Q9BTC0-4]
    NP_542986.1. NM_080796.3. [Q9BTC0-3]
    NP_542987.2. NM_080797.3. [Q9BTC0-1]
    UniGeneiHs.517172.

    Genome annotation databases

    EnsembliENST00000266070; ENSP00000266070; ENSG00000101191. [Q9BTC0-4]
    ENST00000354665; ENSP00000346692; ENSG00000101191. [Q9BTC0-3]
    ENST00000370366; ENSP00000359391; ENSG00000101191. [Q9BTC0-2]
    ENST00000370368; ENSP00000359394; ENSG00000101191. [Q9BTC0-3]
    ENST00000370371; ENSP00000359397; ENSG00000101191. [Q9BTC0-3]
    ENST00000395340; ENSP00000378749; ENSG00000101191. [Q9BTC0-1]
    ENST00000395343; ENSP00000378752; ENSG00000101191. [Q9BTC0-4]
    GeneIDi11083.
    KEGGihsa:11083.
    UCSCiuc002ydr.2. human. [Q9BTC0-4]
    uc002ydt.2. human. [Q9BTC0-1]
    uc002ydv.2. human. [Q9BTC0-3]
    uc011aao.1. human. [Q9BTC0-2]

    Polymorphism databases

    DMDMi116241332.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY481571 mRNA. Translation: AAS49898.1 .
    AY481572 mRNA. Translation: AAS49899.1 .
    AB002331 mRNA. Translation: BAA20791.2 . Different initiation.
    AK002127 mRNA. Translation: BAA92094.1 .
    AL117379 , AL035669 Genomic DNA. Translation: CAI95707.1 .
    AL117379 , AL035669 Genomic DNA. Translation: CAO03650.1 .
    AL035669 , AL117379 Genomic DNA. Translation: CAI95769.2 .
    AL035669 , AL117379 Genomic DNA. Translation: CAI95761.1 .
    AL117379 , AL035669 Genomic DNA. Translation: CAI95708.1 .
    AL035669 , AL117379 Genomic DNA. Translation: CAI95762.1 .
    AL035669 , AL117379 Genomic DNA. Translation: CAI95770.2 .
    AL117379 , AL035669 Genomic DNA. Translation: CAM28273.1 .
    CH471077 Genomic DNA. Translation: EAW75322.1 .
    CH471077 Genomic DNA. Translation: EAW75323.1 .
    BC000770 mRNA. Translation: AAH00770.1 .
    BC004237 mRNA. Translation: AAH04237.1 .
    BC012757 mRNA. No translation available.
    BC014489 mRNA. Translation: AAH14489.1 .
    BC137177 mRNA. Translation: AAI37178.1 .
    AL133063 mRNA. Translation: CAB61387.1 .
    CCDSi CCDS13508.2. [Q9BTC0-1 ]
    CCDS13509.1. [Q9BTC0-3 ]
    CCDS33506.1. [Q9BTC0-4 ]
    RefSeqi NP_001180298.1. NM_001193369.1. [Q9BTC0-4 ]
    NP_001180299.1. NM_001193370.1. [Q9BTC0-1 ]
    NP_071388.2. NM_022105.4. [Q9BTC0-3 ]
    NP_149072.2. NM_033081.2. [Q9BTC0-4 ]
    NP_542986.1. NM_080796.3. [Q9BTC0-3 ]
    NP_542987.2. NM_080797.3. [Q9BTC0-1 ]
    UniGenei Hs.517172.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M3H NMR - A 265-322 [» ]
    4L7X X-ray 1.35 A 266-325 [» ]
    ProteinModelPortali Q9BTC0.
    SMRi Q9BTC0. Positions 265-355, 669-777.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116266. 30 interactions.
    IntActi Q9BTC0. 14 interactions.
    MINTi MINT-3061319.

    PTM databases

    PhosphoSitei Q9BTC0.

    Polymorphism databases

    DMDMi 116241332.

    Proteomic databases

    MaxQBi Q9BTC0.
    PaxDbi Q9BTC0.
    PeptideAtlasi Q9BTC0.
    PRIDEi Q9BTC0.

    Protocols and materials databases

    DNASUi 11083.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266070 ; ENSP00000266070 ; ENSG00000101191 . [Q9BTC0-4 ]
    ENST00000354665 ; ENSP00000346692 ; ENSG00000101191 . [Q9BTC0-3 ]
    ENST00000370366 ; ENSP00000359391 ; ENSG00000101191 . [Q9BTC0-2 ]
    ENST00000370368 ; ENSP00000359394 ; ENSG00000101191 . [Q9BTC0-3 ]
    ENST00000370371 ; ENSP00000359397 ; ENSG00000101191 . [Q9BTC0-3 ]
    ENST00000395340 ; ENSP00000378749 ; ENSG00000101191 . [Q9BTC0-1 ]
    ENST00000395343 ; ENSP00000378752 ; ENSG00000101191 . [Q9BTC0-4 ]
    GeneIDi 11083.
    KEGGi hsa:11083.
    UCSCi uc002ydr.2. human. [Q9BTC0-4 ]
    uc002ydt.2. human. [Q9BTC0-1 ]
    uc002ydv.2. human. [Q9BTC0-3 ]
    uc011aao.1. human. [Q9BTC0-2 ]

    Organism-specific databases

    CTDi 11083.
    GeneCardsi GC20M061510.
    HGNCi HGNC:2680. DIDO1.
    HPAi CAB004374.
    HPA049904.
    MIMi 604140. gene.
    neXtProti NX_Q9BTC0.
    PharmGKBi PA27147.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255142.
    HOVERGENi HBG060199.
    InParanoidi Q9BTC0.
    OMAi GPHPNQF.
    OrthoDBi EOG7NW685.
    PhylomeDBi Q9BTC0.
    TreeFami TF350578.

    Enzyme and pathway databases

    Reactomei REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    ChiTaRSi DIDO1. human.
    GeneWikii DIDO1.
    GenomeRNAii 11083.
    NextBioi 42138.
    PROi Q9BTC0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BTC0.
    Genevestigatori Q9BTC0.

    Family and domain databases

    Gene3Di 1.10.472.30. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR012921. SPOC_C.
    IPR003618. TFIIS_cen_dom.
    IPR017890. TFS2M.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00628. PHD. 1 hit.
    PF07744. SPOC. 1 hit.
    PF07500. TFIIS_M. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    SM00510. TFS2M. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46942. SSF46942. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS51321. TFIIS_CENTRAL. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dido gene expression alterations are implicated in the induction of hematological myeloid neoplasms."
      Futterer A., Campanero M.R., Leonardo E., Criado L.M., Flores J.M., Hernandez J.M., San Miguel J.F., Martinez-A C.
      J. Clin. Invest. 115:2351-2362(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, ROLE IN MYELOID NEOPLASMS, VARIANTS THR-544 AND THR-556.
    2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "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: Placenta.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORMS 1; 3 AND 2).
      Tissue: Brain, Colon, Kidney, Muscle and Placenta.
    8. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-14; 74-82; 519-529; 613-626; 1218-1230; 1334-1347; 1439-1447 AND 1743-1754, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1623-2240 (ISOFORM 4).
      Tissue: Testis.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898 AND SER-1456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1040 AND SER-1456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; SER-152; SER-154; SER-805; SER-809; SER-898; SER-1019; SER-1030; SER-1260; SER-1456; THR-1469 AND SER-1714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-805 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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 THR-151; SER-152; SER-154; SER-805; SER-809; SER-1030; SER-1040; SER-1312; SER-1456 AND SER-1522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-152; SER-154; SER-805; SER-898; SER-1040; SER-1260 AND SER-1456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 266-325 IN COMPLEX WITH METHYLATED HISTONE H3 PEPTIDE, FUNCTION (ISOFORMS 2 AND 4), SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-291.

    Entry informationi

    Entry nameiDIDO1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BTC0
    Secondary accession number(s): A8MY65
    , B9EH82, E1P5I1, O15043, Q3ZTL7, Q3ZTL8, Q4VXS1, Q4VXS2, Q4VXV8, Q4VXV9, Q96D72, Q9BQW0, Q9BW03, Q9H4G6, Q9H4G7, Q9NTU8, Q9NUM8, Q9UFB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 138 of the entry and version 5 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

    Miscellaneous

    Defects in DIDO1 may be a cause of myeloid neoplasms.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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