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Protein

Death-inducer obliterator 1

Gene

Dido1

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

Functioni

Required for early embryonic stem cell development (By similarity). Putative transcription factor, weakly pro-apoptotic when overexpressed.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri265 – 31955PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic signaling pathway Source: MGI
  • transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.

Names & Taxonomyi

Protein namesi
Recommended name:
Death-inducer obliterator 1
Short name:
DIO-1
Alternative name(s):
Death-associated transcription factor 1
Short name:
DATF-1
Gene namesi
Name:Dido1
Synonyms:Datf1, Dio1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1344352. Dido1.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • Cytoplasmcytoskeletonspindle By similarity

  • Note: Translocates to the mitotic spindle upon loss of interaction with H3K4me3 during early mitosis (By similarity). Translocates to the nucleus after pro-apoptotic stimuli.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22562256Death-inducer obliterator 1PRO_0000059325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei58 – 581PhosphoserineBy similarity
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei149 – 1491PhosphoserineCombined sources
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineBy similarity
Modified residuei802 – 8021PhosphoserineCombined sources
Modified residuei806 – 8061PhosphoserineCombined sources
Modified residuei886 – 8861PhosphoserineCombined sources
Modified residuei1016 – 10161PhosphoserineCombined sources
Modified residuei1027 – 10271PhosphoserineBy similarity
Modified residuei1035 – 10351PhosphoserineCombined sources
Modified residuei1239 – 12391PhosphotyrosineBy similarity
Modified residuei1252 – 12521PhosphothreonineCombined sources
Modified residuei1256 – 12561PhosphoserineCombined sources
Modified residuei1307 – 13071PhosphoserineBy similarity
Modified residuei1514 – 15141PhosphoserineBy similarity
Modified residuei1726 – 17261PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C9B9.
MaxQBiQ8C9B9.
PaxDbiQ8C9B9.
PeptideAtlasiQ8C9B9.
PRIDEiQ8C9B9.

PTM databases

iPTMnetiQ8C9B9.
PhosphoSiteiQ8C9B9.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at intermediate levels.

Inductioni

Up-regulated during apoptosis.

Gene expression databases

BgeeiQ8C9B9.
CleanExiMM_DIDO1.
MM_DIO1.
GenevisibleiQ8C9B9. MM.

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.By similarity

Protein-protein interaction databases

BioGridi204761. 3 interactions.
IntActiQ8C9B9. 3 interactions.
MINTiMINT-4111472.
STRINGi10090.ENSMUSP00000084794.

Structurei

Secondary structure

1
2256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi279 – 2813Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi288 – 2903Combined sources
Helixi291 – 2944Combined sources
Helixi298 – 30710Combined sources
Helixi314 – 3196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEMNMR-A257-319[»]
ProteinModelPortaliQ8C9B9.
SMRiQ8C9B9. Positions 257-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8C9B9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini667 – 787121TFIIS centralPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi162 – 1709Nuclear localization signalSequence analysis
Motifi182 – 1909Nuclear localization signalSequence analysis

Domaini

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

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 fingeri265 – 31955PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1632. Eukaryota.
KOG1634. Eukaryota.
ENOG411031H. LUCA.
GeneTreeiENSGT00530000063844.
HOVERGENiHBG060199.
InParanoidiQ8C9B9.
OMAiPGHFVGP.
OrthoDBiEOG7NW685.
PhylomeDBiQ8C9B9.
TreeFamiTF350578.

Family and domain databases

Gene3Di1.10.472.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033082. DIDO1.
IPR012921. SPOC_C.
IPR003618. TFIIS_cen_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11477:SF13. PTHR11477:SF13. 5 hits.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C9B9-1) [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

        10         20         30         40         50
MDDKGHLSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDTEVDPSEQ
60 70 80 90 100
QPQQHNLSLR RSGRQPKRTE RVEEFLTTVR RRGKKNVPVS LEDSSEPTSS
110 120 130 140 150
TVTDVETASE GSVESSSEIR SGPVSDSLGK EHPASSEKAK GGEEEEDTSD
160 170 180 190 200
SDSDGLTLKE LQNRLRRKRE QEPVERSLRG SQNRLRKKRR EEDSAETGSV
210 220 230 240 250
QIGSAEQDRP LCKQEPEASQ GPVSQSETDD IENQLEGKAT QGNTEENPRE
260 270 280 290 300
AGKPKPECEV YDPNALYCIC RQPHNNRFMI CCDRCEEWFH GDCVGISEAR
310 320 330 340 350
GRLLERNGED YICPNCTILQ VQDETNGSAT DEQDSGCRSV GADGTDCTSI
360 370 380 390 400
GTVEQKSGED QGIKGRIEKA ANPSGKKKLK IFQPVVEAPG APKCIGPGCS
410 420 430 440 450
SVAQPDSVYC SNDCILKHAA ATMRFLSSGK EQKTKPKEKV KTKPEKFSLP
460 470 480 490 500
KCSVQVGIKI SSVHKRLASE KRENPVKKVM LASRSETSGK EAACESSTPS
510 520 530 540 550
WASDHNYNAV KPEKPEKPTA LSPTLLSKSM KDDRRVEDRT MAAVTIPKKA
560 570 580 590 600
LPSASLVGRQ TSPRNLVPKK LPPYSNMAGA KPAIKKLPSG FKGTIPKRPW
610 620 630 640 650
PSATLSGTSA RQAGPTPMTA ASKKLPGSAA VVGVTRKPMS ANVPAASPAP
660 670 680 690 700
GRLGPVSPAP SQPNSQIRQN IRRSLKEILW KRVNDSDDLI MTENEVGKIA
710 720 730 740 750
LHIEKEMFNL FQVTDNRYKS KYRSIMFNLK DPKNQGLFHR VLREEISLAK
760 770 780 790 800
LVRMKPEELV SKELSMWTEK PTKSVIESRT KLLNESKKNT TKPETIPDME
810 820 830 840 850
DSPPVSDSEE QQESVRAAPE KSAAPLLDVF SSMLKDTTSQ HRAHLFDLNC
860 870 880 890 900
KICTGQVPSS EDEPAPKKQK LSASSKKEDF KPRHDSSPPN AVPNTADEGI
910 920 930 940 950
ADTLPENASE PDPESTSSLN QERKCFPESP GDSHPEPSSL GGLSPSSASG
960 970 980 990 1000
GSGVVTTVTM SGRDPRTALS GSCTVTASMA AHLDNSQASE TKLDMIKPAL
1010 1020 1030 1040 1050
TSAVVPKSIL AKPSSSPDPR YLSVPPSPSI SESRSPPEGD TTLFLSRLNT
1060 1070 1080 1090 1100
IWKGFINMQS VAKFVTKAYP VSGCLDYLSE DLPDTIHIGG RIAPKTVWDY
1110 1120 1130 1140 1150
VGKLKSSVSK ELCLIRFHPA TEEEEVAYIS LYSYFSSRGR FGVVANNNRH
1160 1170 1180 1190 1200
VKDLYLIPLS AKDPVPSKLL PFEGPGLESP RPNIILGLVI CQKVKRPSSA
1210 1220 1230 1240 1250
GELDKTDEKR TRLQQEELET SVYPKVTAAL PSEKKPPKYS VHSIDTAATS
1260 1270 1280 1290 1300
TTPPGSPPPP PPLPEPPVLK ILSSLKPGST STVTAPTTAA ITTTASPVTA
1310 1320 1330 1340 1350
ATSKTASPLE HILQTLFGKK KSFEPSGKES VGSTLSPHQD SKAKGEDTMS
1360 1370 1380 1390 1400
AAPLLDPIVQ QFGQFSKDKA LEEEEEDDRP YDPEEEYNPD RAFHTLLAEP
1410 1420 1430 1440 1450
GRPHDVQSVS ETAEREEVAY DPEDETILEE AKVTIDDLPN RMCMKVSATE
1460 1470 1480 1490 1500
RPADFTTDAS SASLVEQQKM LEELNKQIEE QKRQLEEQEE ALRQQRAAVG
1510 1520 1530 1540 1550
VSMAHFSVSD ALMSPPPKSS LGKTELFSQE QQAPDPSQGA PNTNHNLDSR
1560 1570 1580 1590 1600
QSRDPRQARR LAAENTENES LPRAPTGSTP GPQGTLPARE TPAGTAVVQG
1610 1620 1630 1640 1650
PGLAAEAKES MAVPWAPGEN AVLRPEHDIQ KCEHPGNPVS LPLDTSHLPT
1660 1670 1680 1690 1700
AGDGAARPAP PRRVLLPTPP STTFPPSFPL QPKAQNFSSG SREPFSGPTF
1710 1720 1730 1740 1750
MSQETSLGSS QYEDPRGAQS AGKNDSPVAD MEDSREPQPR PGESTTSFPQ
1760 1770 1780 1790 1800
PGQRGGGPQP QFPGQREPAP RTFGMSGHHG PSFPGPRGPV PPYSEENLVP
1810 1820 1830 1840 1850
NSDGPRGPPP ARFGAQKPPI PSLFSGQHGP PPYGDNRGLS PSYLGGPRGG
1860 1870 1880 1890 1900
APAQFEDRKD PHGEKREFQD TPYNEMTGAP AQCEGPDQAQ FMGNRAPFQF
1910 1920 1930 1940 1950
GGQRRPLLTQ MKGPRGGPPP SQFGAQRGPP PGHFVGPRGP HPSQFENSRG
1960 1970 1980 1990 2000
THPGQFEGAR GQAPGFMPGP RGIQPQQFEE QRVNSPPRFA GQRASAPLPY
2010 2020 2030 2040 2050
GGPRGPAPFP EKNEQPPSRF HFQGPSSQPV KPPPRPLLEL PSHPPQHRKD
2060 2070 2080 2090 2100
RWDEAGPATA LPSSAGPGQG HEADGQWATS EFREGKGHEY RSPAFEGRQR
2110 2120 2130 2140 2150
ERFEAGSKEK PLDEPEAQGL ESRQGRAFED RRRERERGRN WSRERDWERS
2160 2170 2180 2190 2200
RDWDRHREWD KGRDRSSNRD RERDNDRAKE WDRSRERSRN RDRDRERRRD
2210 2220 2230 2240 2250
RDRSRSRDRD RDRERARDRD RDRGRDRKDR SKSRESPRDQ KPEARTSEGG

PAAAQA
Length:2,256
Mass (Da):247,176
Last modified:July 10, 2007 - v4
Checksum:iCB4F6F6D3FE53747
GO
Isoform 2 (identifier: Q8C9B9-2) [UniParc]FASTAAdd to basket

Also known as: Dido1

The sequence of this isoform differs from the canonical sequence as follows:
     529-614: SMKDDRRVED...LSGTSARQAG → CTYHPKAGFP...AISYFSFRPW
     615-2256: Missing.

Show »
Length:614
Mass (Da):67,395
Checksum:i15A20A74BAEBC9E9
GO
Isoform 3 (identifier: Q8C9B9-3) [UniParc]FASTAAdd to basket

Also known as: Dido2

The sequence of this isoform differs from the canonical sequence as follows:
     1177-1183: LESPRPN → KHPVSGR
     1184-2256: Missing.

Show »
Length:1,183
Mass (Da):129,171
Checksum:i5D808FD9C763F72D
GO

Sequence cautioni

The sequence AAH44755.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC28053.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC97927.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451V → A in CAB48401 (PubMed:10393935).Curated
Sequence conflicti331 – 3311D → N in CAB48401 (PubMed:10393935).Curated
Sequence conflicti353 – 3531V → I in BAC31270 (PubMed:16141072).Curated
Sequence conflicti436 – 4361P → K in AAH29110 (PubMed:15489334).Curated
Sequence conflicti688 – 6881D → Y in AAR84049 (PubMed:16127461).Curated
Sequence conflicti688 – 6881D → Y in AAR84050 (PubMed:16127461).Curated
Sequence conflicti718 – 7181Y → F in AAR84049 (PubMed:16127461).Curated
Sequence conflicti718 – 7181Y → F in AAR84050 (PubMed:16127461).Curated
Sequence conflicti1739 – 17391P → L in AAR84050 (PubMed:16127461).Curated
Sequence conflicti2046 – 20461Q → H in AAR84050 (PubMed:16127461).Curated
Sequence conflicti2049 – 20491K → T in AAR84050 (PubMed:16127461).Curated
Sequence conflicti2054 – 20541E → K in AAR84050 (PubMed:16127461).Curated
Sequence conflicti2058 – 20581A → P in AAR84050 (PubMed:16127461).Curated
Sequence conflicti2118 – 21181Q → L in BAC28053 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei529 – 61486SMKDD…ARQAG → CTYHPKAGFPGPSHHLGGCL GLSRTRVLGVLVLIVASSSL PARSRYQDASGPQVFLPSLW SLSGWFLKSCVGLMLEAISY FSFRPW in isoform 2. 3 PublicationsVSP_012363Add
BLAST
Alternative sequencei615 – 22561642Missing in isoform 2. 3 PublicationsVSP_012364Add
BLAST
Alternative sequencei1177 – 11837LESPRPN → KHPVSGR in isoform 3. 3 PublicationsVSP_026606
Alternative sequencei1184 – 22561073Missing in isoform 3. 3 PublicationsVSP_026607Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238332 mRNA. Translation: CAB48401.1.
AY425951 mRNA. Translation: AAR84049.1.
AY425952 mRNA. Translation: AAR84050.1.
AK129117 mRNA. Translation: BAC97927.1. Different initiation.
AK032843 mRNA. Translation: BAC28053.1. Different initiation.
AK042474 mRNA. Translation: BAC31270.1.
AK044919 mRNA. Translation: BAC32141.1.
AL732560 Genomic DNA. Translation: CAM27684.1.
AL732560 Genomic DNA. Translation: CAM27685.1.
AL732560 Genomic DNA. Translation: CAM27686.1.
AL732560 Genomic DNA. Translation: CAM27687.1.
BC029110 mRNA. Translation: AAH29110.1.
BC044755 mRNA. Translation: AAH44755.1. Different initiation.
BC096662 mRNA. Translation: AAH96662.1.
BC138712 mRNA. Translation: AAI38713.1.
BC138713 mRNA. Translation: AAI38714.1.
CCDSiCCDS17182.1. [Q8C9B9-1]
CCDS17183.1. [Q8C9B9-3]
CCDS17184.1. [Q8C9B9-2]
RefSeqiNP_001278361.1. NM_001291432.1. [Q8C9B9-2]
NP_001278362.1. NM_001291433.1. [Q8C9B9-3]
NP_035935.2. NM_011805.3. [Q8C9B9-2]
NP_780760.2. NM_175551.4. [Q8C9B9-1]
NP_808520.2. NM_177852.4. [Q8C9B9-3]
XP_006500671.1. XM_006500608.2. [Q8C9B9-1]
XP_006500672.1. XM_006500609.2. [Q8C9B9-1]
XP_006500673.1. XM_006500610.2. [Q8C9B9-1]
XP_006500674.1. XM_006500611.2. [Q8C9B9-1]
XP_006500675.1. XM_006500612.2. [Q8C9B9-1]
XP_006500678.1. XM_006500615.2. [Q8C9B9-1]
XP_006500679.1. XM_006500616.2. [Q8C9B9-1]
UniGeneiMm.253836.
Mm.490825.

Genome annotation databases

EnsembliENSMUST00000087517; ENSMUSP00000084794; ENSMUSG00000038914. [Q8C9B9-1]
ENSMUST00000103055; ENSMUSP00000099344; ENSMUSG00000038914. [Q8C9B9-2]
ENSMUST00000103056; ENSMUSP00000099345; ENSMUSG00000038914. [Q8C9B9-3]
ENSMUST00000103057; ENSMUSP00000099346; ENSMUSG00000038914. [Q8C9B9-3]
ENSMUST00000130986; ENSMUSP00000119689; ENSMUSG00000038914. [Q8C9B9-2]
GeneIDi23856.
KEGGimmu:23856.
UCSCiuc008ojq.2. mouse. [Q8C9B9-1]
uc008ojr.2. mouse. [Q8C9B9-3]
uc008oju.2. mouse. [Q8C9B9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ238332 mRNA. Translation: CAB48401.1.
AY425951 mRNA. Translation: AAR84049.1.
AY425952 mRNA. Translation: AAR84050.1.
AK129117 mRNA. Translation: BAC97927.1. Different initiation.
AK032843 mRNA. Translation: BAC28053.1. Different initiation.
AK042474 mRNA. Translation: BAC31270.1.
AK044919 mRNA. Translation: BAC32141.1.
AL732560 Genomic DNA. Translation: CAM27684.1.
AL732560 Genomic DNA. Translation: CAM27685.1.
AL732560 Genomic DNA. Translation: CAM27686.1.
AL732560 Genomic DNA. Translation: CAM27687.1.
BC029110 mRNA. Translation: AAH29110.1.
BC044755 mRNA. Translation: AAH44755.1. Different initiation.
BC096662 mRNA. Translation: AAH96662.1.
BC138712 mRNA. Translation: AAI38713.1.
BC138713 mRNA. Translation: AAI38714.1.
CCDSiCCDS17182.1. [Q8C9B9-1]
CCDS17183.1. [Q8C9B9-3]
CCDS17184.1. [Q8C9B9-2]
RefSeqiNP_001278361.1. NM_001291432.1. [Q8C9B9-2]
NP_001278362.1. NM_001291433.1. [Q8C9B9-3]
NP_035935.2. NM_011805.3. [Q8C9B9-2]
NP_780760.2. NM_175551.4. [Q8C9B9-1]
NP_808520.2. NM_177852.4. [Q8C9B9-3]
XP_006500671.1. XM_006500608.2. [Q8C9B9-1]
XP_006500672.1. XM_006500609.2. [Q8C9B9-1]
XP_006500673.1. XM_006500610.2. [Q8C9B9-1]
XP_006500674.1. XM_006500611.2. [Q8C9B9-1]
XP_006500675.1. XM_006500612.2. [Q8C9B9-1]
XP_006500678.1. XM_006500615.2. [Q8C9B9-1]
XP_006500679.1. XM_006500616.2. [Q8C9B9-1]
UniGeneiMm.253836.
Mm.490825.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEMNMR-A257-319[»]
ProteinModelPortaliQ8C9B9.
SMRiQ8C9B9. Positions 257-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204761. 3 interactions.
IntActiQ8C9B9. 3 interactions.
MINTiMINT-4111472.
STRINGi10090.ENSMUSP00000084794.

PTM databases

iPTMnetiQ8C9B9.
PhosphoSiteiQ8C9B9.

Proteomic databases

EPDiQ8C9B9.
MaxQBiQ8C9B9.
PaxDbiQ8C9B9.
PeptideAtlasiQ8C9B9.
PRIDEiQ8C9B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087517; ENSMUSP00000084794; ENSMUSG00000038914. [Q8C9B9-1]
ENSMUST00000103055; ENSMUSP00000099344; ENSMUSG00000038914. [Q8C9B9-2]
ENSMUST00000103056; ENSMUSP00000099345; ENSMUSG00000038914. [Q8C9B9-3]
ENSMUST00000103057; ENSMUSP00000099346; ENSMUSG00000038914. [Q8C9B9-3]
ENSMUST00000130986; ENSMUSP00000119689; ENSMUSG00000038914. [Q8C9B9-2]
GeneIDi23856.
KEGGimmu:23856.
UCSCiuc008ojq.2. mouse. [Q8C9B9-1]
uc008ojr.2. mouse. [Q8C9B9-3]
uc008oju.2. mouse. [Q8C9B9-2]

Organism-specific databases

CTDi11083.
MGIiMGI:1344352. Dido1.

Phylogenomic databases

eggNOGiKOG1632. Eukaryota.
KOG1634. Eukaryota.
ENOG411031H. LUCA.
GeneTreeiENSGT00530000063844.
HOVERGENiHBG060199.
InParanoidiQ8C9B9.
OMAiPGHFVGP.
OrthoDBiEOG7NW685.
PhylomeDBiQ8C9B9.
TreeFamiTF350578.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.

Miscellaneous databases

ChiTaRSiDido1. mouse.
EvolutionaryTraceiQ8C9B9.
PROiQ8C9B9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C9B9.
CleanExiMM_DIDO1.
MM_DIO1.
GenevisibleiQ8C9B9. MM.

Family and domain databases

Gene3Di1.10.472.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033082. DIDO1.
IPR012921. SPOC_C.
IPR003618. TFIIS_cen_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11477:SF13. PTHR11477:SF13. 5 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DIO-1 is a novel gene involved in onset of apoptosis in vitro, whose misexpression disrupts limb development."
    Garcia-Domingo D., Leonardo E., Grandien A., Martinez P., Albar J.P., Izpisua-Belmonte J.-C., Martinez-A C.
    Proc. Natl. Acad. Sci. U.S.A. 96:7992-7997(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
    Tissue: Pre-B cell.
  2. "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 3).
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1484-2256 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo, Thymus and Wolffian duct.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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 2 AND 3).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain, Mammary gland and Mammary tumor.
  7. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 540-548 AND 699-705, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; THR-148; SER-149; SER-802; SER-806; SER-886; SER-1016; SER-1035; THR-1252 AND SER-1256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "Solution structure of PHD domain in death inducer-obliterator 1(DIO-1)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 257-319.

Entry informationi

Entry nameiDIDO1_MOUSE
AccessioniPrimary (citable) accession number: Q8C9B9
Secondary accession number(s): A2AJ47
, A2AJ48, B2RS46, Q05C59, Q3ZTP5, Q3ZTP6, Q4V9W1, Q6ZQD7, Q80V34, Q8BMD0, Q8BRG2, Q8CHR5, Q9WV00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 10, 2007
Last modified: July 6, 2016
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.