Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BTC0

- DIDO1_HUMAN

UniProt

Q9BTC0 - DIDO1_HUMAN

(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)

Protein

Death-inducer obliterator 1

Gene

DIDO1

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

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
Complete GO annotation...

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-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

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. 31 interactions.
IntActiQ9BTC0. 14 interactions.
MINTiMINT-3061319.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063844.
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

        10         20         30         40         50
MDDKGDPSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDAEADPLEP
60 70 80 90 100
PPPQQQLGLS LRRSGRQPKR TERVEQFLTI ARRRGRRSMP VSLEDSGEPT
110 120 130 140 150
SCPATDAETA SEGSVESASE TRSGPQSAST AVKERPASSE KVKGGDDHDD
160 170 180 190 200
TSDSDSDGLT LKELQNRLRR KREQEPTERP LKGIQSRLRK KRREEGPAET
210 220 230 240 250
VGSEASDTVE GVLPSKQEPE NDQGVVSQAG KDDRESKLEG KAAQDIKDEE
260 270 280 290 300
PGDLGRPKPE CEGYDPNALY CICRQPHNNR FMICCDRCEE WFHGDCVGIS
310 320 330 340 350
EARGRLLERN GEDYICPNCT ILQVQDETHS ETADQQEAKW RPGDADGTDC
360 370 380 390 400
TSIGTIEQKS SEDQGIKGRI EKAANPSGKK KLKIFQPVIE APGASKCIGP
410 420 430 440 450
GCCHVAQPDS VYCSNDCILK HAAATMKFLS SGKEQKPKPK EKMKMKPEKP
460 470 480 490 500
SLPKCGAQAG IKISSVHKRP APEKKETTVK KAVVVPARSE ALGKEAACES
510 520 530 540 550
STPSWASDHN YNAVKPEKTA APSPSLLYKS TKEDRRSEEK AAAMAASKKT
560 570 580 590 600
APPGSAVGKQ PAPRNLVPKK SSFANVAAAT PAIKKPPSGF KGTIPKRPWL
610 620 630 640 650
SATPSSGASA ARQAGPAPAA ATAASKKFPG SAALVGAVRK PVVPSVPMAS
660 670 680 690 700
PAPGRLGAMS AAPSQPNSQI RQNIRRSLKE ILWKRVNDSD DLIMTENEVG
710 720 730 740 750
KIALHIEKEM FNLFQVTDNR YKSKYRSIMF NLKDPKNQGL FHRVLREEIS
760 770 780 790 800
LAKLVRLKPE ELVSKELSTW KERPARSVME SRTKLHNESK KTAPRQEAIP
810 820 830 840 850
DLEDSPPVSD SEEQQESARA VPEKSTAPLL DVFSSMLKDT TSQHRAHLFD
860 870 880 890 900
LNCKICTGQV PSAEDEPAPK KQKLSASVKK EDLKSKHDSS APDPAPDSAD
910 920 930 940 950
EVMPEAVPEV ASEPGLESAS HPNVDRTYFP GPPGDGHPEP SPLEDLSPCP
960 970 980 990 1000
ASCGSGVVTT VTVSGRDPRT APSSSCTAVA SAASRPDSTH MVEARQDVPK
1010 1020 1030 1040 1050
PVLTSVMVPK SILAKPSSSP DPRYLSVPPS PNISTSESRS PPEGDTTLFL
1060 1070 1080 1090 1100
SRLSTIWKGF INMQSVAKFV TKAYPVSGCF DYLSEDLPDT IHIGGRIAPK
1110 1120 1130 1140 1150
TVWDYVGKLK SSVSKELCLI RFHPATEEEE VAYISLYSYF SSRGRFGVVA
1160 1170 1180 1190 1200
NNNRHVKDLY LIPLSAQDPV PSKLLPFEGP GLESPRPNII LGLVICQKIK
1210 1220 1230 1240 1250
RPANSGELDK MDEKRTRLQP EEADVPAYPK VATVPQSEKK PSKYPLCSAD
1260 1270 1280 1290 1300
AAVSTTPPGS PPPPPPLPEP PVLKVLSSLK PAAPSPATAA TTAAAASTAA
1310 1320 1330 1340 1350
SSTASSASKT ASPLEHILQT LFGKKKSFDP SAREPPGSTA GLPQEPKTTA
1360 1370 1380 1390 1400
EDGVPAPPLL DPIVQQFGQF SKDKALEEEE DDRPYDPEEE YDPERAFDTQ
1410 1420 1430 1440 1450
LVERGRRHEV ERAPEAAAAE REEVAYDPED ETILEEAKVT VDDLPNRMCA
1460 1470 1480 1490 1500
DVRRNSVERP AEPVAGAATP SLVEQQKMLE ELNKQIEEQK RQLEEQEEAL
1510 1520 1530 1540 1550
RQQRAAVGVS MAHFSVSDAL MSPPPKSSLP KAELFQQEQQ SADKPASLPP
1560 1570 1580 1590 1600
ASQASNHRDP RQARRLATET GEGEGEPLSR LSARGAQGAL PERDASRGGL
1610 1620 1630 1640 1650
VGQAPMPVPE EKEPASSPWA SGEKPPAGSE QDGWKAEPGE GTRPATVGDS
1660 1670 1680 1690 1700
SARPARRVLL PTPPCGALQP GFPLQHDGER DPFTCPGFAS QDKALGSAQY
1710 1720 1730 1740 1750
EDPRNLHSAG RSSSPAGETE GDREPQARPG EGTAPLPPPG QKVGGSQPPF
1760 1770 1780 1790 1800
QGQREPGPHA LGMSGLHGPN FPGPRGPAPP FPEENIASND GPRGPPPARF
1810 1820 1830 1840 1850
GAQKGPIPSL FSGQHGPPPY GDSRGPSPSY LGGPRGVAPS QFEERKDPHG
1860 1870 1880 1890 1900
EKREFQDAPY NEVTGAPAQF EGTEQAPFLG SRGGAPFQFG GQRRPLLSQL
1910 1920 1930 1940 1950
KGPRGGPPPS QFGGQRGPPP GHFVGPRGPH PSQFETARGP HPNQFEGPRG
1960 1970 1980 1990 2000
QAPNFMPGPR GIQPQQFEDQ RVHSPPRFTN QRAPAPLQFG GLRGSAPFSE
2010 2020 2030 2040 2050
KNEQTPSRFH FQGQAPQVMK PGPRPLLELP SHPPQHRKDR WEEAGPPSAL
2060 2070 2080 2090 2100
SSSAPGQGPE ADGQWASADF REGKGHEYRN QTFEGRQRER FDVGPKEKPL
2110 2120 2130 2140 2150
EEPDAQGRAS EDRRRERERG RNWSRERDWD RPREWDRHRD KDSSRDWDRN
2160 2170 2180 2190 2200
RERSANRDRE READRGKEWD RSRERSRNRE RERDRRRDRD RSRSRERDRD
2210 2220 2230 2240
KARDRERGRD RKDRSKSKES ARDPKPEASR ASDAGTASQA
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 31 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.
GeneTreei ENSGT00530000063844.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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