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Q9H0S4

- DDX47_HUMAN

UniProt

Q9H0S4 - DDX47_HUMAN

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Protein

Probable ATP-dependent RNA helicase DDX47

Gene

DDX47

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

Functioni

Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 758ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
  2. mRNA processing Source: UniProtKB-KW
  3. RNA splicing Source: UniProtKB
  4. rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX47 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 47
Gene namesi
Name:DDX47
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18682. DDX47.

Subcellular locationi

Nucleusnucleolus 2 Publications
Note: Localizes in the nucleolar-organizing region during ribosome biogenesis.

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134918403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 455454Probable ATP-dependent RNA helicase DDX47PRO_0000055050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei424 – 4241Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0S4.
PaxDbiQ9H0S4.
PRIDEiQ9H0S4.

2D gel databases

SWISS-2DPAGEQ9H0S4.

PTM databases

PhosphoSiteiQ9H0S4.

Expressioni

Gene expression databases

BgeeiQ9H0S4.
CleanExiHS_DDX47.
ExpressionAtlasiQ9H0S4. baseline.
GenevestigatoriQ9H0S4.

Organism-specific databases

HPAiHPA014855.

Interactioni

Subunit structurei

Interacts with AGO1 and AGO2. Interacts with GABARAP. Interacts with NOL8; the interaction is RNA-dependent.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951663EBI-2515241,EBI-712001

Protein-protein interaction databases

BioGridi119375. 22 interactions.
IntActiQ9H0S4. 13 interactions.
MINTiMINT-3056694.
STRINGi9606.ENSP00000350698.

Structurei

Secondary structure

1
455
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 236
Helixi27 – 293
Helixi33 – 419
Helixi49 – 5911
Beta strandi64 – 674
Helixi74 – 8815
Beta strandi95 – 984
Helixi102 – 11615
Helixi117 – 1193
Beta strandi123 – 1264
Helixi132 – 1409
Beta strandi144 – 1485
Helixi150 – 15910
Beta strandi170 – 1734
Helixi176 – 1816
Helixi185 – 1939
Beta strandi197 – 20711
Helixi210 – 21910
Beta strandi224 – 2274

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BERX-ray1.40A5-230[»]
ProteinModelPortaliQ9H0S4.
SMRiQ9H0S4. Positions 11-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0S4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 226172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini237 – 397161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi24 – 5229Q motifAdd
BLAST
Motifi174 – 1774DEAD box

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00730000110914.
HOGENOMiHOG000268802.
HOVERGENiHBG100512.
InParanoidiQ9H0S4.
KOiK14777.
OMAiNKFRAGS.
OrthoDBiEOG7GTT3T.
PhylomeDBiQ9H0S4.
TreeFamiTF105714.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0S4-1) [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
MAAPEEHDSP TEASQPIVEE EETKTFKDLG VTDVLCEACD QLGWTKPTKI
60 70 80 90 100
QIEAIPLALQ GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP
110 120 130 140 150
TRELAFQISE QFEALGSSIG VQSAVIVGGI DSMSQSLALA KKPHIIIATP
160 170 180 190 200
GRLIDHLENT KGFNLRALKY LVMDEADRIL NMDFETEVDK ILKVIPRDRK
210 220 230 240 250
TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ YYIFIPSKFK
260 270 280 290 300
DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS
310 320 330 340 350
KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR
360 370 380 390 400
VGRTARAGRS GKAITFVTQY DVELFQRIEH LIGKKLPGFP TQDDEVMMLT
410 420 430 440 450
ERVAEAQRFA RMELREHGEK KKRSREDAGD NDDTEGAIGV RNKVAGGKMK

KRKGR
Length:455
Mass (Da):50,647
Last modified:March 1, 2001 - v1
Checksum:i5F64F26AD2C11286
GO
Isoform 2 (identifier: Q9H0S4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     251-299: Missing.

Note: No experimental confirmation available.

Show »
Length:406
Mass (Da):45,169
Checksum:iE6FFADA03AFAB679
GO

Sequence cautioni

The sequence AAF23354.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551I → V in BAB70762. (PubMed:16541075)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei251 – 29949Missing in isoform 2. 1 PublicationVSP_045239Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136666 mRNA. Translation: CAB66601.1.
AK054574 mRNA. Translation: BAB70762.1.
AK127712 mRNA. Translation: BAG54556.1.
AC007215 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96277.1.
CH471094 Genomic DNA. Translation: EAW96283.1.
BC009379 mRNA. Translation: AAH09379.2.
BC068009 mRNA. Translation: AAH68009.1.
AF078843 mRNA. Translation: AAF23354.1. Different initiation.
CCDSiCCDS8655.1. [Q9H0S4-1]
CCDS8656.1. [Q9H0S4-2]
RefSeqiNP_057439.2. NM_016355.3. [Q9H0S4-1]
NP_957518.1. NM_201224.1. [Q9H0S4-2]
UniGeneiHs.719938.

Genome annotation databases

EnsembliENST00000352940; ENSP00000319578; ENSG00000213782. [Q9H0S4-2]
ENST00000358007; ENSP00000350698; ENSG00000213782. [Q9H0S4-1]
GeneIDi51202.
KEGGihsa:51202.
UCSCiuc001rav.3. human. [Q9H0S4-1]
uc001ray.3. human.

Polymorphism databases

DMDMi52782792.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136666 mRNA. Translation: CAB66601.1 .
AK054574 mRNA. Translation: BAB70762.1 .
AK127712 mRNA. Translation: BAG54556.1 .
AC007215 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96277.1 .
CH471094 Genomic DNA. Translation: EAW96283.1 .
BC009379 mRNA. Translation: AAH09379.2 .
BC068009 mRNA. Translation: AAH68009.1 .
AF078843 mRNA. Translation: AAF23354.1 . Different initiation.
CCDSi CCDS8655.1. [Q9H0S4-1 ]
CCDS8656.1. [Q9H0S4-2 ]
RefSeqi NP_057439.2. NM_016355.3. [Q9H0S4-1 ]
NP_957518.1. NM_201224.1. [Q9H0S4-2 ]
UniGenei Hs.719938.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BER X-ray 1.40 A 5-230 [» ]
ProteinModelPortali Q9H0S4.
SMRi Q9H0S4. Positions 11-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119375. 22 interactions.
IntActi Q9H0S4. 13 interactions.
MINTi MINT-3056694.
STRINGi 9606.ENSP00000350698.

PTM databases

PhosphoSitei Q9H0S4.

Polymorphism databases

DMDMi 52782792.

2D gel databases

SWISS-2DPAGE Q9H0S4.

Proteomic databases

MaxQBi Q9H0S4.
PaxDbi Q9H0S4.
PRIDEi Q9H0S4.

Protocols and materials databases

DNASUi 51202.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000352940 ; ENSP00000319578 ; ENSG00000213782 . [Q9H0S4-2 ]
ENST00000358007 ; ENSP00000350698 ; ENSG00000213782 . [Q9H0S4-1 ]
GeneIDi 51202.
KEGGi hsa:51202.
UCSCi uc001rav.3. human. [Q9H0S4-1 ]
uc001ray.3. human.

Organism-specific databases

CTDi 51202.
GeneCardsi GC12P012966.
HGNCi HGNC:18682. DDX47.
HPAi HPA014855.
MIMi 615428. gene.
neXtProti NX_Q9H0S4.
PharmGKBi PA134918403.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00730000110914.
HOGENOMi HOG000268802.
HOVERGENi HBG100512.
InParanoidi Q9H0S4.
KOi K14777.
OMAi NKFRAGS.
OrthoDBi EOG7GTT3T.
PhylomeDBi Q9H0S4.
TreeFami TF105714.

Miscellaneous databases

ChiTaRSi DDX47. human.
EvolutionaryTracei Q9H0S4.
GeneWikii DDX47.
GenomeRNAii 51202.
NextBioi 54238.
PROi Q9H0S4.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0S4.
CleanExi HS_DDX47.
ExpressionAtlasi Q9H0S4. baseline.
Genevestigatori Q9H0S4.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "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 1).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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).
    Tissue: Brain and Eye.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-24; 75-102; 142-161; 170-190; 238-248; 285-301; 315-325; 378-384 AND 424-441, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver."
    Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-455 (ISOFORM 2).
    Tissue: Liver.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "GABAA receptor-associated protein (GABARAP) induces apoptosis by interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX 47)."
    Lee J.H., Rho S.B., Chun T.
    Biotechnol. Lett. 27:623-628(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GABARAP, IDENTIFICATION BY MASS SPECTROMETRY.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47."
    Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.
    Nucleic Acids Res. 34:4593-4608(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOL8, SUBCELLULAR LOCATION.
  12. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
    Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
    EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1 AND AGO2.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, 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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-230 IN COMPLEX WITH AMP.

Entry informationi

Entry nameiDDX47_HUMAN
AccessioniPrimary (citable) accession number: Q9H0S4
Secondary accession number(s): B3KXP4
, G5E955, Q96GM0, Q96NV8, Q9UI98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 126 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3