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O70133

- DHX9_MOUSE

UniProt

O70133 - DHX9_MOUSE

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Protein
ATP-dependent RNA helicase A
Gene
Dhx9, Ddx9
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the CRD-mediated complex that promotes MYC mRNA stability. Unwinds double-stranded DNA and RNA in a 3' to 5' direction. Alterations of secondary structure may subsequently influence interactions with proteins or other nucleic acids. Functions as a transcriptional activator. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi413 – 4208ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. DNA binding Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular response to heat Source: MGI
  2. circadian rhythm Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Helicase, Hydrolase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase A (EC:3.6.4.13)
Short name:
RHA
Alternative name(s):
DEAH box protein 9
Short name:
mHEL-5
Nuclear DNA helicase II
Short name:
NDH II
Gene namesi
Name:Dhx9
Synonyms:Ddx9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:108177. Dhx9.

Subcellular locationi

Nucleusnucleolus. Cytoplasm By similarity
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Can shuttle between nucleus and cytoplasm By similarity.1 Publication

GO - Cellular componenti

  1. CRD-mediated mRNA stability complex Source: UniProtKB
  2. nucleolus Source: MGI
  3. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13801380ATP-dependent RNA helicase A
PRO_0000055158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481N6-acetyllysine1 Publication
Modified residuei193 – 1931N6-acetyllysine By similarity
Modified residuei201 – 2011N6-acetyllysine By similarity
Modified residuei323 – 3231Phosphoserine By similarity
Modified residuei1026 – 10261N6-acetyllysine By similarity

Post-translational modificationi

Methylated By similarity.
May be phosphorylated by PRKDC/XRCC7 By similarity. Phosphorylated by EIF2AK2/PKR and this phosphorylation perturbs its association with dsRNA.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO70133.
PaxDbiO70133.
PRIDEiO70133.

PTM databases

PhosphoSiteiO70133.

Expressioni

Gene expression databases

CleanExiMM_DHX9.
GenevestigatoriO70133.

Interactioni

Subunit structurei

Interacts with ZIC2, IGF2BP1, IGF2BP2, IGF2BP3, MBD2, HRMT1L2/PRMT1, RELA and LARP6. Can also interact with XRCC5 and with TOP2A in an RNA dependent manner; these interactions may be indirect. Interaction with TOP2A is promoted by UBC9. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts (via N-terminus) with EIF2AK2/PKR and this interaction is dependent upon the activation of the kinase. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. May act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase II complex. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active).3 Publications

Protein-protein interaction databases

BioGridi199088. 6 interactions.
IntActiO70133. 8 interactions.
MINTiMINT-1868227.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410
Beta strandi20 – 278
Beta strandi29 – 3911
Beta strandi47 – 537
Helixi54 – 7219
Turni77 – 793
Helixi172 – 1754
Helixi180 – 19314
Beta strandi201 – 2066
Beta strandi212 – 22110
Turni222 – 2254
Beta strandi226 – 2316
Helixi237 – 25519

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UILNMR-A163-262[»]
1WHQNMR-A4-89[»]
2RS6NMR-A4-89[»]
2RS7NMR-A163-262[»]
ProteinModelPortaliO70133.
SMRiO70133. Positions 4-89, 168-262, 331-1073.

Miscellaneous databases

EvolutionaryTraceiO70133.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 7169DRBM 1
Add
BLAST
Domaini182 – 25473DRBM 2
Add
BLAST
Domaini400 – 566167Helicase ATP-binding
Add
BLAST
Domaini638 – 811174Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 253253Interaction with CREBBP By similarity
Add
BLAST
Regioni233 – 32896Interaction with BRCA1 By similarity
Add
BLAST
Regioni333 – 38250MTAD By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi513 – 5164DEAH box
Motifi588 – 59710Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1171 – 1380210Arg/Gly/Ser/Tyr-rich
Add
BLAST

Domaini

The MTAD domain mediates interaction with the RNA polymerase II holoenzyme By similarity.

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1643.
HOGENOMiHOG000247063.
HOVERGENiHBG039429.
InParanoidiO70133.
KOiK13184.
PhylomeDBiO70133.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRNA-bd_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O70133-1) [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

MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN     50
STNKKDAQSN AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA 100
SAAEGLPAPM GGPLPPHLAL KAEENNSGVE SSGYGSPGPT WDRGANLKDY 150
YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL ENAKARLNQY FQKEKIQGEY 200
KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA AQSCALSLVR 250
QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV 300
PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID 350
EGPLAYASTE QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL 400
EAISSNSVVI IRGATGCGKT TQVPQYILDD FIQNDRAAEC NIVVTQPRRI 450
SAVAVAERVA YERGEEPGKS CGYSVRFESI LPRPHASIMF CTVGVLLRKL 500
EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR IVLMSATIDT 550
TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED 600
DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN 650
VPGAVLVFLP GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV 700
FDPVPDGVTK VILSTNIAET SITINDVVYV IDSCKQKVKL FTAHNNMTNY 750
ATVWASKTNL EQRKGRAGRV RPGFCFHLCS RARFDRLETH MTPEMFRTPL 800
HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE LDALDANDEL 850
TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK 900
RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA 950
TLRMTWEAKV QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG 1000
VYPNVCYHKE KRKILTTEGR NALIHKSSVN CPFSSQDMKY PSPFFVFGEK 1050
IRTRAISAKG MTLVTPLQLL LFASKKVQSD GQIVFIDDWI RLQISHEAAA 1100
CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS RPSAAGINLM 1150
IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG 1200
FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG 1250
RGGGGGGFGG SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG 1300
GEGYSISPNS YRGNYGGGGG GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG 1350
GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY 1380
Length:1,380
Mass (Da):149,475
Last modified:July 19, 2005 - v2
Checksum:i005D641CD9A4F0C9
GO
Isoform 2 (identifier: O70133-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-123: E → EA

Note: Contains a phosphoserine at position 137.

Show »
Length:1,381
Mass (Da):149,546
Checksum:i0AB5502F91DEFB73
GO
Isoform 3 (identifier: O70133-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.

Show »
Length:1,164
Mass (Da):125,615
Checksum:iDA64E679A88D87C2
GO

Sequence cautioni

The sequence AAR87796.1 differs from that shown. Reason: Intron retention.
The sequence AAH89159.1 differs from that shown. Reason: Frameshift at positions 447 and 448.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 216216Missing in isoform 3.
VSP_014778Add
BLAST
Alternative sequencei123 – 1231E → EA in isoform 2.
VSP_014779

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → R in AAC05725. 1 Publication
Sequence conflicti136 – 1361S → A in AAC05725. 1 Publication
Sequence conflicti136 – 1361S → A in AAC05301. 1 Publication
Sequence conflicti187 – 1871L → V1 Publication
Sequence conflicti189 – 1891Q → H in AAC05725. 1 Publication
Sequence conflicti211 – 2111R → G in BAB28848. 1 Publication
Sequence conflicti235 – 2351S → C in AAC05725. 1 Publication
Sequence conflicti257 – 2571V → C in AAC05725. 1 Publication
Sequence conflicti281 – 2811S → P in AAC05725. 1 Publication
Sequence conflicti674 – 6741N → M in AAB72087. 1 Publication
Sequence conflicti748 – 7481T → I in AAB72087. 1 Publication
Sequence conflicti831 – 8311I → V in AAB72087. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U91922 mRNA. Translation: AAC05725.1.
AF023530 Genomic DNA. Translation: AAC05301.1.
AY512925 mRNA. Translation: AAR87796.1. Sequence problems.
BC089159 mRNA. Translation: AAH89159.1. Sequence problems.
AK013423 mRNA. Translation: BAB28848.1.
U92080 mRNA. Translation: AAB72087.1.
RefSeqiNP_031868.2. NM_007842.2.
UniGeneiMm.20000.

Genome annotation databases

GeneIDi13211.
KEGGimmu:13211.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U91922 mRNA. Translation: AAC05725.1 .
AF023530 Genomic DNA. Translation: AAC05301.1 .
AY512925 mRNA. Translation: AAR87796.1 . Sequence problems.
BC089159 mRNA. Translation: AAH89159.1 . Sequence problems.
AK013423 mRNA. Translation: BAB28848.1 .
U92080 mRNA. Translation: AAB72087.1 .
RefSeqi NP_031868.2. NM_007842.2.
UniGenei Mm.20000.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UIL NMR - A 163-262 [» ]
1WHQ NMR - A 4-89 [» ]
2RS6 NMR - A 4-89 [» ]
2RS7 NMR - A 163-262 [» ]
ProteinModelPortali O70133.
SMRi O70133. Positions 4-89, 168-262, 331-1073.
ModBasei Search...

Protein-protein interaction databases

BioGridi 199088. 6 interactions.
IntActi O70133. 8 interactions.
MINTi MINT-1868227.

PTM databases

PhosphoSitei O70133.

Proteomic databases

MaxQBi O70133.
PaxDbi O70133.
PRIDEi O70133.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 13211.
KEGGi mmu:13211.

Organism-specific databases

CTDi 1660.
MGIi MGI:108177. Dhx9.

Phylogenomic databases

eggNOGi COG1643.
HOGENOMi HOG000247063.
HOVERGENi HBG039429.
InParanoidi O70133.
KOi K13184.
PhylomeDBi O70133.

Miscellaneous databases

ChiTaRSi DHX9. mouse.
EvolutionaryTracei O70133.
NextBioi 283382.
PROi O70133.
SOURCEi Search...

Gene expression databases

CleanExi MM_DHX9.
Genevestigatori O70133.

Family and domain databases

Gene3Di 3.30.160.20. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR014720. dsRNA-bd_dom.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00035. dsrm. 2 hits.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00358. DSRM. 2 hits.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
PS50137. DS_RBD. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase A."
    Lee C.-G., Eki T., Okumura K., da Costa Soares V., Hurwitz J.
    Genomics 47:365-371(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-161.
    Strain: 129/Sv.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
    Strain: C57BL/6NCr.
  3. "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] OF 1-756 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryonic germ cell.
  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] OF 1-264 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo.
  5. "mHEL-5."
    Kisielow P., Miazek A.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
    Strain: C57BL/6.
  6. "Nucleolar localization of murine nuclear DNA helicase II (RNA helicase A)."
    Zhang S., Herrmann C., Grosse F.
    J. Cell Sci. 112:2693-2703(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "An antiviral response directed by PKR phosphorylation of the RNA helicase A."
    Sadler A.J., Latchoumanin O., Hawkes D., Mak J., Williams B.R.
    PLoS Pathog. 5:E1000311-E1000311(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
  10. "Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
    Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
    Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "Solution structure of double-stranded RNA-binding motifs from hypothetical protein BAB28848."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 4-262.
  13. "Functional role of Zic2 phosphorylation in transcriptional regulation."
    Ishiguro A., Aruga J.
    FEBS Lett. 582:154-158(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZIC2.

Entry informationi

Entry nameiDHX9_MOUSE
AccessioniPrimary (citable) accession number: O70133
Secondary accession number(s): O35931
, O54703, Q5FWY1, Q6R5F7, Q9CSA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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