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Q9BTC0 (DIDO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DIDO1
Synonyms:C20orf158, DATF1, KIAA0333
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative transcription factor, weakly pro-apoptotic when overexpressed By similarity. Tumor suppressor. Required for early embryonic stem cell development. Ref.1 Ref.19

Isoform 2:Displaces isoform 4 at the onset of differentiation, required for repression of stemness genes. Ref.1 Ref.19

Subunit structure

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. Ref.19

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Cytoplasmcytoskeletonspindle. 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. Ref.19

Tissue specificity

Ubiquitous.

Domain

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

Miscellaneous

Defects in DIDO1 may be a cause of myeloid neoplasms.

Sequence similarities

Contains 1 PHD-type zinc finger.

Contains 1 TFIIS central domain.

Sequence caution

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

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q9BTC0-4)

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.
Isoform 1 (identifier: Q9BTC0-1)

Also known as: DIDO2;

The sequence of this isoform differs from the canonical sequence as follows:
     1182-1189: LESPRPNI → KRRLSGWR
     1190-2240: Missing.
Isoform 2 (identifier: Q9BTC0-2)

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.
Isoform 3 (identifier: Q9BTC0-3)

Also known as: a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22402240Death-inducer obliterator 1
PRO_0000059324

Regions

Domain670 – 790121TFIIS central
Zinc finger268 – 32255PHD-type
Motif165 – 1739Nuclear localization signal Potential
Motif185 – 1939Nuclear localization signal Potential
Compositional bias1257 – 128630Pro-rich
Compositional bias1725 – 2034310Pro-rich
Compositional bias2108 – 2214107Arg-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.14
Modified residue1511Phosphothreonine Ref.13 Ref.16
Modified residue1521Phosphoserine Ref.13 Ref.16 Ref.18
Modified residue1541Phosphoserine Ref.13 Ref.16 Ref.18
Modified residue8051Phosphoserine Ref.11 Ref.13 Ref.15 Ref.16 Ref.18
Modified residue8091Phosphoserine Ref.11 Ref.13 Ref.15 Ref.16
Modified residue8981Phosphoserine Ref.10 Ref.13 Ref.18
Modified residue10191Phosphoserine Ref.13
Modified residue10301Phosphoserine Ref.13 Ref.16
Modified residue10401Phosphoserine Ref.12 Ref.16 Ref.18
Modified residue12601Phosphoserine Ref.13 Ref.18
Modified residue13121Phosphoserine Ref.16
Modified residue14561Phosphoserine Ref.10 Ref.12 Ref.13 Ref.16 Ref.18
Modified residue14691Phosphothreonine Ref.13
Modified residue15221Phosphoserine Ref.16
Modified residue17141Phosphoserine Ref.13

Natural variations

Alternative sequence530 – 56233STKED…GKQPA → CMYHLGVGLLDPSRSFWIAI PWACPGLGVAALC in isoform 3.
VSP_007211
Alternative sequence530 – 54415STKED…KAAAM → CSGKYSYSLHPSLIA in isoform 2.
VSP_007209
Alternative sequence545 – 22401696Missing in isoform 2.
VSP_007210
Alternative sequence563 – 22401678Missing in isoform 3.
VSP_007212
Alternative sequence1182 – 11898LESPRPNI → KRRLSGWR in isoform 1.
VSP_017225
Alternative sequence1190 – 22401051Missing in isoform 1.
VSP_017226
Natural variant131P → L.
Corresponds to variant rs6090161 [ dbSNP | Ensembl ].
VAR_028310
Natural variant2761P → L.
Corresponds to variant rs6090160 [ dbSNP | Ensembl ].
VAR_028311
Natural variant5441M → T. Ref.1
Corresponds to variant rs1883848 [ dbSNP | Ensembl ].
VAR_057093
Natural variant5561A → T. Ref.1
Corresponds to variant rs1883847 [ dbSNP | Ensembl ].
VAR_057094
Natural variant7931A → G.
Corresponds to variant rs750077 [ dbSNP | Ensembl ].
VAR_057095
Natural variant12201P → Q.
Corresponds to variant rs6011441 [ dbSNP | Ensembl ].
VAR_057096
Natural variant17081S → C.
Corresponds to variant rs41282984 [ dbSNP | Ensembl ].
VAR_061740

Experimental info

Mutagenesis2911W → T: Abolishes binding to H3K4me3. Ref.19
Sequence conflict2521G → E in BAA92094. Ref.4
Isoform 2:
Sequence conflict5351S → L in AAH00770. Ref.7

Secondary structure

................ 2240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (DIDO3) [UniParc].

Last modified October 17, 2006. Version 5.
Checksum: 9B89361A24A72C58

FASTA2,240243,873
        10         20         30         40         50         60 
MDDKGDPSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDAEADPLEP PPPQQQLGLS 

        70         80         90        100        110        120 
LRRSGRQPKR TERVEQFLTI ARRRGRRSMP VSLEDSGEPT SCPATDAETA SEGSVESASE 

       130        140        150        160        170        180 
TRSGPQSAST AVKERPASSE KVKGGDDHDD TSDSDSDGLT LKELQNRLRR KREQEPTERP 

       190        200        210        220        230        240 
LKGIQSRLRK KRREEGPAET VGSEASDTVE GVLPSKQEPE NDQGVVSQAG KDDRESKLEG 

       250        260        270        280        290        300 
KAAQDIKDEE PGDLGRPKPE CEGYDPNALY CICRQPHNNR FMICCDRCEE WFHGDCVGIS 

       310        320        330        340        350        360 
EARGRLLERN GEDYICPNCT ILQVQDETHS ETADQQEAKW RPGDADGTDC TSIGTIEQKS 

       370        380        390        400        410        420 
SEDQGIKGRI EKAANPSGKK KLKIFQPVIE APGASKCIGP GCCHVAQPDS VYCSNDCILK 

       430        440        450        460        470        480 
HAAATMKFLS SGKEQKPKPK EKMKMKPEKP SLPKCGAQAG IKISSVHKRP APEKKETTVK 

       490        500        510        520        530        540 
KAVVVPARSE ALGKEAACES STPSWASDHN YNAVKPEKTA APSPSLLYKS TKEDRRSEEK 

       550        560        570        580        590        600 
AAAMAASKKT APPGSAVGKQ PAPRNLVPKK SSFANVAAAT PAIKKPPSGF KGTIPKRPWL 

       610        620        630        640        650        660 
SATPSSGASA ARQAGPAPAA ATAASKKFPG SAALVGAVRK PVVPSVPMAS PAPGRLGAMS 

       670        680        690        700        710        720 
AAPSQPNSQI RQNIRRSLKE ILWKRVNDSD DLIMTENEVG KIALHIEKEM FNLFQVTDNR 

       730        740        750        760        770        780 
YKSKYRSIMF NLKDPKNQGL FHRVLREEIS LAKLVRLKPE ELVSKELSTW KERPARSVME 

       790        800        810        820        830        840 
SRTKLHNESK KTAPRQEAIP DLEDSPPVSD SEEQQESARA VPEKSTAPLL DVFSSMLKDT 

       850        860        870        880        890        900 
TSQHRAHLFD LNCKICTGQV PSAEDEPAPK KQKLSASVKK EDLKSKHDSS APDPAPDSAD 

       910        920        930        940        950        960 
EVMPEAVPEV ASEPGLESAS HPNVDRTYFP GPPGDGHPEP SPLEDLSPCP ASCGSGVVTT 

       970        980        990       1000       1010       1020 
VTVSGRDPRT APSSSCTAVA SAASRPDSTH MVEARQDVPK PVLTSVMVPK SILAKPSSSP 

      1030       1040       1050       1060       1070       1080 
DPRYLSVPPS PNISTSESRS PPEGDTTLFL SRLSTIWKGF INMQSVAKFV TKAYPVSGCF 

      1090       1100       1110       1120       1130       1140 
DYLSEDLPDT IHIGGRIAPK TVWDYVGKLK SSVSKELCLI RFHPATEEEE VAYISLYSYF 

      1150       1160       1170       1180       1190       1200 
SSRGRFGVVA NNNRHVKDLY LIPLSAQDPV PSKLLPFEGP GLESPRPNII LGLVICQKIK 

      1210       1220       1230       1240       1250       1260 
RPANSGELDK MDEKRTRLQP EEADVPAYPK VATVPQSEKK PSKYPLCSAD AAVSTTPPGS 

      1270       1280       1290       1300       1310       1320 
PPPPPPLPEP PVLKVLSSLK PAAPSPATAA TTAAAASTAA SSTASSASKT ASPLEHILQT 

      1330       1340       1350       1360       1370       1380 
LFGKKKSFDP SAREPPGSTA GLPQEPKTTA EDGVPAPPLL DPIVQQFGQF SKDKALEEEE 

      1390       1400       1410       1420       1430       1440 
DDRPYDPEEE YDPERAFDTQ LVERGRRHEV ERAPEAAAAE REEVAYDPED ETILEEAKVT 

      1450       1460       1470       1480       1490       1500 
VDDLPNRMCA DVRRNSVERP AEPVAGAATP SLVEQQKMLE ELNKQIEEQK RQLEEQEEAL 

      1510       1520       1530       1540       1550       1560 
RQQRAAVGVS MAHFSVSDAL MSPPPKSSLP KAELFQQEQQ SADKPASLPP ASQASNHRDP 

      1570       1580       1590       1600       1610       1620 
RQARRLATET GEGEGEPLSR LSARGAQGAL PERDASRGGL VGQAPMPVPE EKEPASSPWA 

      1630       1640       1650       1660       1670       1680 
SGEKPPAGSE QDGWKAEPGE GTRPATVGDS SARPARRVLL PTPPCGALQP GFPLQHDGER 

      1690       1700       1710       1720       1730       1740 
DPFTCPGFAS QDKALGSAQY EDPRNLHSAG RSSSPAGETE GDREPQARPG EGTAPLPPPG 

      1750       1760       1770       1780       1790       1800 
QKVGGSQPPF QGQREPGPHA LGMSGLHGPN FPGPRGPAPP FPEENIASND GPRGPPPARF 

      1810       1820       1830       1840       1850       1860 
GAQKGPIPSL FSGQHGPPPY GDSRGPSPSY LGGPRGVAPS QFEERKDPHG EKREFQDAPY 

      1870       1880       1890       1900       1910       1920 
NEVTGAPAQF EGTEQAPFLG SRGGAPFQFG GQRRPLLSQL KGPRGGPPPS QFGGQRGPPP 

      1930       1940       1950       1960       1970       1980 
GHFVGPRGPH PSQFETARGP HPNQFEGPRG QAPNFMPGPR GIQPQQFEDQ RVHSPPRFTN 

      1990       2000       2010       2020       2030       2040 
QRAPAPLQFG GLRGSAPFSE KNEQTPSRFH FQGQAPQVMK PGPRPLLELP SHPPQHRKDR 

      2050       2060       2070       2080       2090       2100 
WEEAGPPSAL SSSAPGQGPE ADGQWASADF REGKGHEYRN QTFEGRQRER FDVGPKEKPL 

      2110       2120       2130       2140       2150       2160 
EEPDAQGRAS EDRRRERERG RNWSRERDWD RPREWDRHRD KDSSRDWDRN RERSANRDRE 

      2170       2180       2190       2200       2210       2220 
READRGKEWD RSRERSRNRE RERDRRRDRD RSRSRERDRD KARDRERGRD RKDRSKSKES 

      2230       2240 
ARDPKPEASR ASDAGTASQA 

« Hide

Isoform 1 (DIDO2) [UniParc].

Checksum: 6C536EE25776C086
Show »

FASTA1,189129,181
Isoform 2 (DIDO1) [UniParc].

Checksum: 192BE2A77ED5FADA
Show »

FASTA54459,461
Isoform 3 (a) [UniParc].

Checksum: 91A714668F9C5C12
Show »

FASTA56261,354

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"Dido3 PHD modulates cell differentiation and division."
Gatchalian J., Futterer A., Rothbart S.B., Tong Q., Rincon-Arano H., Sanchez de Diego A., Groudine M., Strahl B.D., Martinez-A C., van Wely K.H., Kutateladze T.G.
Cell Rep. 4:148-158(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13508.2. [Q9BTC0-1]
CCDS13509.1. [Q9BTC0-3]
CCDS33506.1. [Q9BTC0-4]
RefSeqNP_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]
UniGeneHs.517172.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M3HNMR-A265-322[»]
4L7XX-ray1.35A266-325[»]
ProteinModelPortalQ9BTC0.
SMRQ9BTC0. Positions 265-355, 669-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116266. 30 interactions.
IntActQ9BTC0. 14 interactions.
MINTMINT-3061319.

PTM databases

PhosphoSiteQ9BTC0.

Polymorphism databases

DMDM116241332.

Proteomic databases

MaxQBQ9BTC0.
PaxDbQ9BTC0.
PeptideAtlasQ9BTC0.
PRIDEQ9BTC0.

Protocols and materials databases

DNASU11083.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266070; ENSP00000266070; ENSG00000101191. [Q9BTC0-4]
ENST00000266071; ENSP00000266071; ENSG00000101191. [Q9BTC0-2]
ENST00000354665; ENSP00000346692; ENSG00000101191. [Q9BTC0-3]
ENST00000370366; ENSP00000359391; ENSG00000101191. [Q9BTC0-2]
ENST00000370368; ENSP00000359394; ENSG00000101191. [Q9BTC0-3]
ENST00000370371; ENSP00000359397; ENSG00000101191. [Q9BTC0-3]
ENST00000395335; ENSP00000378744; ENSG00000101191. [Q9BTC0-1]
ENST00000395340; ENSP00000378749; ENSG00000101191. [Q9BTC0-1]
ENST00000395343; ENSP00000378752; ENSG00000101191. [Q9BTC0-4]
GeneID11083.
KEGGhsa:11083.
UCSCuc002ydr.2. human. [Q9BTC0-4]
uc002ydt.2. human. [Q9BTC0-1]
uc002ydv.2. human. [Q9BTC0-3]
uc011aao.1. human. [Q9BTC0-2]

Organism-specific databases

CTD11083.
GeneCardsGC20M061510.
HGNCHGNC:2680. DIDO1.
HPACAB004374.
HPA049904.
MIM604140. gene.
neXtProtNX_Q9BTC0.
PharmGKBPA27147.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255142.
HOVERGENHBG060199.
InParanoidQ9BTC0.
OMAGPHPNQF.
OrthoDBEOG7NW685.
PhylomeDBQ9BTC0.
TreeFamTF350578.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

BgeeQ9BTC0.
GenevestigatorQ9BTC0.

Family and domain databases

Gene3D1.10.472.30. 1 hit.
3.30.40.10. 1 hit.
InterProIPR012921. 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]
PfamPF00628. PHD. 1 hit.
PF07744. SPOC. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
SM00510. TFS2M. 1 hit.
[Graphical view]
SUPFAMSSF46942. SSF46942. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS51321. TFIIS_CENTRAL. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDIDO1. human.
GeneWikiDIDO1.
GenomeRNAi11083.
NextBio42138.
PROQ9BTC0.
SOURCESearch...

Entry information

Entry nameDIDO1_HUMAN
AccessionPrimary (citable) accession number: Q9BTC0
Secondary accession number(s): A8MY65 expand/collapse secondary AC list , B9EH82, E1P5I1, O15043, Q3ZTL7, Q3ZTL8, Q4VXS1, Q4VXS2, Q4VXV8, Q4VXV9, Q96D72, Q9BQW0, Q9BW03, Q9H4G6, Q9H4G7, Q9NTU8, Q9NUM8, Q9UFB6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 136 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM