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Q9UHI6

- DDX20_HUMAN

UniProt

Q9UHI6 - DDX20_HUMAN

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Protein

Probable ATP-dependent RNA helicase DDX20

Gene

DDX20

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

Functioni

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841ATP; via carbonyl oxygen
Binding sitei89 – 891ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1146ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: ProtInc
  3. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. gene expression Source: Reactome
  3. ncRNA metabolic process Source: Reactome
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. oogenesis Source: Ensembl
  6. positive regulation of apoptotic process Source: UniProtKB
  7. regulation of steroid biosynthetic process Source: Ensembl
  8. RNA metabolic process Source: Reactome
  9. RNA processing Source: ProtInc
  10. spliceosomal snRNP assembly Source: UniProtKB
  11. spliceosomal tri-snRNP complex assembly Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX20 (EC:3.6.4.13)
Alternative name(s):
Component of gems 3
DEAD box protein 20
DEAD box protein DP 103
Gemin-3
Gene namesi
Name:DDX20
Synonyms:DP103, GEMIN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2743. DDX20.

Subcellular locationi

Cytoplasm. Nucleusgem
Note: Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems).

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoskeleton Source: ProtInc
  3. cytosol Source: UniProtKB
  4. membrane Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
  7. SMN complex Source: UniProtKB
  8. SMN-Sm protein complex Source: UniProtKB
  9. transcriptional repressor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27209.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 824824Probable ATP-dependent RNA helicase DDX20PRO_0000055025Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei187 – 1871Phosphoserine1 Publication
Modified residuei500 – 5001Phosphoserine1 Publication
Modified residuei505 – 5051Phosphoserine1 Publication
Modified residuei532 – 5321Phosphoserine1 Publication
Modified residuei552 – 5521Phosphothreonine2 Publications
Modified residuei652 – 6521Phosphoserine1 Publication
Modified residuei654 – 6541Phosphoserine1 Publication
Modified residuei656 – 6561Phosphoserine1 Publication
Modified residuei672 – 6721Phosphoserine2 Publications
Modified residuei677 – 6771Phosphoserine3 Publications
Modified residuei678 – 6781Phosphoserine4 Publications
Modified residuei688 – 6881Phosphothreonine1 Publication
Modified residuei703 – 7031Phosphoserine2 Publications
Modified residuei705 – 7051Phosphothreonine1 Publication
Modified residuei714 – 7141Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UHI6.
PaxDbiQ9UHI6.
PeptideAtlasiQ9UHI6.
PRIDEiQ9UHI6.

PTM databases

PhosphoSiteiQ9UHI6.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9UHI6.
CleanExiHS_DDX20.
ExpressionAtlasiQ9UHI6. baseline and differential.
GenevestigatoriQ9UHI6.

Organism-specific databases

HPAiCAB015427.
HPA005516.
HPA023541.

Interactioni

Subunit structurei

Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Interacts directly with GEMIN5. Interacts directly with SNUPN. Interacts with PPP4R2. Interacts with FOXL2. Interacts with EBV EBNA2 and EBNA3C. Interacts with NANOS1 and PUM2.8 Publications

Protein-protein interaction databases

BioGridi116387. 58 interactions.
DIPiDIP-32606N.
IntActiQ9UHI6. 16 interactions.
MINTiMINT-96973.
STRINGi9606.ENSP00000358716.

Structurei

Secondary structure

1
824
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 674Combined sources
Helixi71 – 799Combined sources
Helixi87 – 9711Combined sources
Beta strandi102 – 1054Combined sources
Helixi112 – 12312Combined sources
Beta strandi133 – 1364Combined sources
Helixi140 – 15314Combined sources
Turni154 – 1563Combined sources
Beta strandi162 – 1654Combined sources
Helixi171 – 1777Combined sources
Beta strandi182 – 1865Combined sources
Helixi188 – 1969Combined sources
Helixi202 – 2043Combined sources
Beta strandi207 – 2126Combined sources
Helixi213 – 2175Combined sources
Helixi223 – 23210Combined sources
Beta strandi238 – 2447Combined sources
Helixi248 – 2547Combined sources
Turni255 – 2573Combined sources
Beta strandi262 – 2643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OXCX-ray1.30A/B41-268[»]
3B7GX-ray1.90A/B41-268[»]
ProteinModelPortaliQ9UHI6.
SMRiQ9UHI6. Positions 21-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHI6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 264172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini299 – 448150Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni456 – 54893SMN interactingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi62 – 9029Q motifAdd
BLAST
Motifi211 – 2144DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00770000120538.
HOGENOMiHOG000112184.
HOVERGENiHBG051330.
InParanoidiQ9UHI6.
KOiK13131.
OMAiQYYKIVN.
OrthoDBiEOG7PGDPX.
PhylomeDBiQ9UHI6.
TreeFamiTF352222.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHI6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAFEASGA LAAVATAMPA EHVAVQVPAP EPTPGPVRIL RTAQDLSSPR
60 70 80 90 100
TRTGDVLLAE PADFESLLLS RPVLEGLRAA GFERPSPVQL KAIPLGRCGL
110 120 130 140 150
DLIVQAKSGT GKTCVFSTIA LDSLVLENLS TQILILAPTR EIAVQIHSVI
160 170 180 190 200
TAIGIKMEGL ECHVFIGGTP LSQDKTRLKK CHIAVGSPGR IKQLIELDYL
210 220 230 240 250
NPGSIRLFIL DEADKLLEEG SFQEQINWIY SSLPASKQML AVSATYPEFL
260 270 280 290 300
ANALTKYMRD PTFVRLNSSD PSLIGLKQYY KVVNSYPLAH KVFEEKTQHL
310 320 330 340 350
QELFSRIPFN QALVFSNLHS RAQHLADILS SKGFPAECIS GNMNQNQRLD
360 370 380 390 400
AMAKLKHFHC RVLISTDLTS RGIDAEKVNL VVNLDVPLDW ETYMHRIGRA
410 420 430 440 450
GRFGTLGLTV TYCCRGEEEN MMMRIAQKCN INLLPLPDPI PSGLMEECVD
460 470 480 490 500
WDVEVKAAVH TYGIASVPNQ PLKKQIQKIE RTLQIQKAHG DHMASSRNNS
510 520 530 540 550
VSGLSVKSKN NTKQKLPVKS HSECGIIEKA TSPKELGCDR QSEEQMKNSV
560 570 580 590 600
QTPVENSTNS QHQVKEALPV SLPQIPCLSS FKIHQPYTLT FAELVEDYEH
610 620 630 640 650
YIKEGLEKPV EIIRHYTGPG DQTVNPQNGF VRNKVIEQRV PVLASSSQSG
660 670 680 690 700
DSESDSDSYS SRTSSQSKGN KSYLEGSSDN QLKDSESTPV DDRISLEQPP
710 720 730 740 750
NGSDTPNPEK YQESPGIQMK TRLKEGASQR AKQSRRNLPR RSSFRLQTEA
760 770 780 790 800
QEDDWYDCHR EIRLSFSDTY QDYEEYWRAY YRAWQEYYAA ASHSYYWNAQ
810 820
RHPSWMAAYH MNTIYLQEMM HSNQ
Length:824
Mass (Da):92,241
Last modified:December 1, 2000 - v2
Checksum:i76712F014B2A0CF2
GO
Isoform 2 (identifier: Q9UHI6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-138: ILILAP → AELSNS
     139-824: Missing.

Note: No experimental confirmation available.

Show »
Length:138
Mass (Da):14,272
Checksum:iA3075B1CEE1AF15C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51F → V in AAD42744. (PubMed:10383418)Curated
Sequence conflicti279 – 2791Y → C in BAA91727. (PubMed:14702039)Curated
Sequence conflicti639 – 6391R → K in AAF14544. (PubMed:10601333)Curated
Sequence conflicti659 – 6591Y → H in AAD42744. (PubMed:10383418)Curated
Sequence conflicti676 – 6761G → S in AAF14544. (PubMed:10601333)Curated
Sequence conflicti703 – 7031S → T in AAF14544. (PubMed:10601333)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti636 – 6361I → T.1 Publication
Corresponds to variant rs197412 [ dbSNP | Ensembl ].
VAR_057231
Natural varianti693 – 6931R → S.
Corresponds to variant rs197414 [ dbSNP | Ensembl ].
VAR_057232
Natural varianti762 – 7621I → T.
Corresponds to variant rs85276 [ dbSNP | Ensembl ].
VAR_057233

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei133 – 1386ILILAP → AELSNS in isoform 2. 1 PublicationVSP_056505
Alternative sequencei139 – 824686Missing in isoform 2. 1 PublicationVSP_056506Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171063 mRNA. Translation: AAF14544.1.
AF106019 mRNA. Translation: AAD42744.1.
AK001506 mRNA. Translation: BAA91727.1.
AK301697 mRNA. Translation: BAG63169.1.
AL049557 Genomic DNA. Translation: CAB55686.2.
BC011556 mRNA. Translation: AAH11556.1.
AL133598 mRNA. Translation: CAB63734.2.
CCDSiCCDS842.1. [Q9UHI6-1]
PIRiT43476.
RefSeqiNP_009135.4. NM_007204.4. [Q9UHI6-1]
UniGeneiHs.591405.

Genome annotation databases

EnsembliENST00000369702; ENSP00000358716; ENSG00000064703. [Q9UHI6-1]
ENST00000533164; ENSP00000434085; ENSG00000064703. [Q9UHI6-2]
GeneIDi11218.
KEGGihsa:11218.
UCSCiuc001ebs.3. human. [Q9UHI6-1]

Polymorphism databases

DMDMi12643886.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF171063 mRNA. Translation: AAF14544.1 .
AF106019 mRNA. Translation: AAD42744.1 .
AK001506 mRNA. Translation: BAA91727.1 .
AK301697 mRNA. Translation: BAG63169.1 .
AL049557 Genomic DNA. Translation: CAB55686.2 .
BC011556 mRNA. Translation: AAH11556.1 .
AL133598 mRNA. Translation: CAB63734.2 .
CCDSi CCDS842.1. [Q9UHI6-1 ]
PIRi T43476.
RefSeqi NP_009135.4. NM_007204.4. [Q9UHI6-1 ]
UniGenei Hs.591405.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OXC X-ray 1.30 A/B 41-268 [» ]
3B7G X-ray 1.90 A/B 41-268 [» ]
ProteinModelPortali Q9UHI6.
SMRi Q9UHI6. Positions 21-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116387. 58 interactions.
DIPi DIP-32606N.
IntActi Q9UHI6. 16 interactions.
MINTi MINT-96973.
STRINGi 9606.ENSP00000358716.

PTM databases

PhosphoSitei Q9UHI6.

Polymorphism databases

DMDMi 12643886.

Proteomic databases

MaxQBi Q9UHI6.
PaxDbi Q9UHI6.
PeptideAtlasi Q9UHI6.
PRIDEi Q9UHI6.

Protocols and materials databases

DNASUi 11218.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369702 ; ENSP00000358716 ; ENSG00000064703 . [Q9UHI6-1 ]
ENST00000533164 ; ENSP00000434085 ; ENSG00000064703 . [Q9UHI6-2 ]
GeneIDi 11218.
KEGGi hsa:11218.
UCSCi uc001ebs.3. human. [Q9UHI6-1 ]

Organism-specific databases

CTDi 11218.
GeneCardsi GC01P112298.
HGNCi HGNC:2743. DDX20.
HPAi CAB015427.
HPA005516.
HPA023541.
MIMi 606168. gene.
neXtProti NX_Q9UHI6.
PharmGKBi PA27209.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00770000120538.
HOGENOMi HOG000112184.
HOVERGENi HBG051330.
InParanoidi Q9UHI6.
KOi K13131.
OMAi QYYKIVN.
OrthoDBi EOG7PGDPX.
PhylomeDBi Q9UHI6.
TreeFami TF352222.

Enzyme and pathway databases

Reactomei REACT_11066. snRNP Assembly.

Miscellaneous databases

EvolutionaryTracei Q9UHI6.
GeneWikii DDX20.
GenomeRNAii 11218.
NextBioi 35475826.
PROi Q9UHI6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHI6.
CleanExi HS_DDX20.
ExpressionAtlasi Q9UHI6. baseline and differential.
Genevestigatori Q9UHI6.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gemin3: a novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and a component of gems."
    Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M., Dreyfuss G.
    J. Cell Biol. 147:1181-1194(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN THE CORE SMN COMPLEX, INTERACTION WITH SNRPB; SNRPD2 AND SNRPD3, IDENTIFICATION BY MASS SPECTROMETRY.
  2. "Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C."
    Grundhoff A.T., Kremmer E., Tuereci O., Glieden A., Gindorf C., Atz J., Mueller-Lantzsch N., Schubach W.H., Grasser F.A.
    J. Biol. Chem. 274:19136-19144(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH EBV EBNA2 AND EBV EBNA3C.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Esophagus.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-636.
    Tissue: Placenta.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-275 (ISOFORM 1).
    Tissue: Testis.
  7. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
    Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
    Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNUPN; SMN1 AND SNRPB.
  8. "Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs."
    Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W.
    J. Cell Sci. 116:1905-1913(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP4R2.
  9. "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis."
    Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y., Bae J.
    Biochem. Biophys. Res. Commun. 336:876-881(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXL2.
  10. "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 THR-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; THR-552 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-500; SER-532; THR-552; SER-652; SER-654; SER-656; SER-677; SER-678; SER-703; THR-705 AND SER-714, 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: 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-677; SER-678 AND SER-703, 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 SER-672; SER-678 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "NANOS1 and PUMILIO2 bind microRNA biogenesis factor GEMIN3, within chromatoid body in human germ cells."
    Ginter-Matuszewska B., Kusz K., Spik A., Grzeszkowiak D., Rembiszewska A., Kupryjanczyk J., Jaruzelska J.
    Histochem. Cell Biol. 136:279-287(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PUM2 AND NANOS1.
  19. "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-505; SER-672; SER-677 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein."
    Schutz P., Wahlberg E., Karlberg T., Hammarstrom M., Collins R., Flores A., Schuler H.
    J. Mol. Biol. 400:768-782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 41-268 IN COMPLEX WITH ADP, ADP-BINDING.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-268.

Entry informationi

Entry nameiDDX20_HUMAN
AccessioniPrimary (citable) accession number: Q9UHI6
Secondary accession number(s): B4DWV7
, Q96F72, Q9NVM3, Q9UF59, Q9UIY0, Q9Y659
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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