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Protein

ATP-dependent RNA helicase DDX55

Gene

DDX55

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

Functioni

Probable ATP-binding RNA helicase.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 608ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX55 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 55
Gene namesi
Name:DDX55
Synonyms:KIAA1595
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20085. DDX55.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134984021.

Polymorphism and mutation databases

BioMutaiDDX55.
DMDMi296439376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 600600ATP-dependent RNA helicase DDX55PRO_0000252210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei544 – 5441PhosphoserineCombined sources
Modified residuei594 – 5941PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NHQ9.
MaxQBiQ8NHQ9.
PaxDbiQ8NHQ9.
PRIDEiQ8NHQ9.

PTM databases

iPTMnetiQ8NHQ9.
PhosphoSiteiQ8NHQ9.

Expressioni

Gene expression databases

BgeeiQ8NHQ9.
CleanExiHS_DDX55.
ExpressionAtlasiQ8NHQ9. baseline and differential.
GenevisibleiQ8NHQ9. HS.

Organism-specific databases

HPAiHPA044101.
HPA048180.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-5459844,EBI-741181
KRTAP10-8P604103EBI-5459844,EBI-10171774

Protein-protein interaction databases

BioGridi121721. 24 interactions.
IntActiQ8NHQ9. 6 interactions.
STRINGi9606.ENSP00000238146.

Structurei

3D structure databases

ProteinModelPortaliQ8NHQ9.
SMRiQ8NHQ9. Positions 9-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 223184Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini254 – 402149Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 3729Q motifAdd
BLAST
Motifi171 – 1744DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi487 – 56882Lys-richAdd
BLAST

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0345. Eukaryota.
ENOG410XNT7. LUCA.
GeneTreeiENSGT00550000074969.
HOGENOMiHOG000268803.
HOVERGENiHBG107796.
InParanoidiQ8NHQ9.
KOiK14809.
OMAiRANVVEK.
OrthoDBiEOG7QVM2B.
PhylomeDBiQ8NHQ9.
TreeFamiTF314573.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR025313. DUF4217.
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.
PF13959. DUF4217. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM01178. DUF4217. 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. AlignAdd to basket

Isoform 1 (identifier: Q8NHQ9-1) [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
MEHVTEGSWE SLPVPLHPQV LGALRELGFP YMTPVQSATI PLFMRNKDVA
60 70 80 90 100
AEAVTGSGKT LAFVIPILEI LLRREEKLKK SQVGAIIITP TRELAIQIDE
110 120 130 140 150
VLSHFTKHFP EFSQILWIGG RNPGEDVERF KQQGGNIIVA TPGRLEDMFR
160 170 180 190 200
RKAEGLDLAS CVRSLDVLVL DEADRLLDMG FEASINTILE FLPKQRRTGL
210 220 230 240 250
FSATQTQEVE NLVRAGLRNP VRVSVKEKGV AASSAQKTPS RLENYYMVCK
260 270 280 290 300
ADEKFNQLVH FLRNHKQEKH LVFFSTCACV EYYGKALEVL VKGVKIMCIH
310 320 330 340 350
GKMKYKRNKI FMEFRKLQSG ILVCTDVMAR GIDIPEVNWV LQYDPPSNAS
360 370 380 390 400
AFVHRCGRTA RIGHGGSALV FLLPMEESYI NFLAINQKCP LQEMKPQRNT
410 420 430 440 450
ADLLPKLKSM ALADRAVFEK GMKAFVSYVQ AYAKHECNLI FRLKDLDFAS
460 470 480 490 500
LARGFALLRM PKMPELRGKQ FPDFVPVDVN TDTIPFKDKI REKQRQKLLE
510 520 530 540 550
QQRREKTENE GRRKFIKNKA WSKQKAKKEK KKKMNEKRKR EEGSDIEDED
560 570 580 590 600
MEELLNDTRL LKKLKKGKIT EEEFEKGLLT TGKRTIKTVD LGISDLEDDC
Length:600
Mass (Da):68,547
Last modified:May 18, 2010 - v3
Checksum:iD696ABBED51B370B
GO
Isoform 2 (identifier: Q8NHQ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-393: Missing.

Note: No experimental confirmation available.
Show »
Length:207
Mass (Da):24,294
Checksum:i9CBD990CEF6E6F60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1345FKQQG → LSFQS in BAB13421 (PubMed:10997877).Curated
Sequence conflicti148 – 1481M → L in AAH30020 (PubMed:15489334).Curated
Sequence conflicti286 – 2861A → T in AAH30020 (PubMed:15489334).Curated
Sequence conflicti445 – 4506DLDFAS → G in CAH56233 (PubMed:17974005).Curated
Sequence conflicti599 – 5991D → G in AAH30020 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011V → L.
Corresponds to variant rs17881657 [ dbSNP | Ensembl ].
VAR_027789
Natural varianti154 – 1541E → G.
Corresponds to variant rs17886035 [ dbSNP | Ensembl ].
VAR_027790
Natural varianti264 – 2641N → S.1 Publication
Corresponds to variant rs11057306 [ dbSNP | Ensembl ].
VAR_027791
Natural varianti556 – 5561N → S.
Corresponds to variant rs10773019 [ dbSNP | Ensembl ].
VAR_027792

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 393393Missing in isoform 2. 1 PublicationVSP_056155Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055713 Genomic DNA. No translation available.
AC117503 Genomic DNA. No translation available.
BC030020 mRNA. Translation: AAH30020.1.
BC035911 mRNA. Translation: AAH35911.1.
AL833756 mRNA. Translation: CAH56233.1.
AB046815 mRNA. Translation: BAB13421.1.
CCDSiCCDS9251.1. [Q8NHQ9-1]
RefSeqiNP_065987.1. NM_020936.2. [Q8NHQ9-1]
UniGeneiHs.286173.

Genome annotation databases

EnsembliENST00000238146; ENSP00000238146; ENSG00000111364. [Q8NHQ9-1]
ENST00000421670; ENSP00000442332; ENSG00000111364. [Q8NHQ9-2]
GeneIDi57696.
KEGGihsa:57696.
UCSCiuc001ufi.4. human. [Q8NHQ9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC055713 Genomic DNA. No translation available.
AC117503 Genomic DNA. No translation available.
BC030020 mRNA. Translation: AAH30020.1.
BC035911 mRNA. Translation: AAH35911.1.
AL833756 mRNA. Translation: CAH56233.1.
AB046815 mRNA. Translation: BAB13421.1.
CCDSiCCDS9251.1. [Q8NHQ9-1]
RefSeqiNP_065987.1. NM_020936.2. [Q8NHQ9-1]
UniGeneiHs.286173.

3D structure databases

ProteinModelPortaliQ8NHQ9.
SMRiQ8NHQ9. Positions 9-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121721. 24 interactions.
IntActiQ8NHQ9. 6 interactions.
STRINGi9606.ENSP00000238146.

PTM databases

iPTMnetiQ8NHQ9.
PhosphoSiteiQ8NHQ9.

Polymorphism and mutation databases

BioMutaiDDX55.
DMDMi296439376.

Proteomic databases

EPDiQ8NHQ9.
MaxQBiQ8NHQ9.
PaxDbiQ8NHQ9.
PRIDEiQ8NHQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238146; ENSP00000238146; ENSG00000111364. [Q8NHQ9-1]
ENST00000421670; ENSP00000442332; ENSG00000111364. [Q8NHQ9-2]
GeneIDi57696.
KEGGihsa:57696.
UCSCiuc001ufi.4. human. [Q8NHQ9-1]

Organism-specific databases

CTDi57696.
GeneCardsiDDX55.
HGNCiHGNC:20085. DDX55.
HPAiHPA044101.
HPA048180.
neXtProtiNX_Q8NHQ9.
PharmGKBiPA134984021.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0345. Eukaryota.
ENOG410XNT7. LUCA.
GeneTreeiENSGT00550000074969.
HOGENOMiHOG000268803.
HOVERGENiHBG107796.
InParanoidiQ8NHQ9.
KOiK14809.
OMAiRANVVEK.
OrthoDBiEOG7QVM2B.
PhylomeDBiQ8NHQ9.
TreeFamiTF314573.

Miscellaneous databases

ChiTaRSiDDX55. human.
GenomeRNAii57696.
NextBioi64547.
PROiQ8NHQ9.

Gene expression databases

BgeeiQ8NHQ9.
CleanExiHS_DDX55.
ExpressionAtlasiQ8NHQ9. baseline and differential.
GenevisibleiQ8NHQ9. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR025313. DUF4217.
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.
PF13959. DUF4217. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM01178. DUF4217. 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]
ProtoNetiSearch...

Publicationsi

  1. "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].
  2. "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 AND 2).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-532 (ISOFORM 1), VARIANT SER-264.
    Tissue: Stomach.
  4. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-600 (ISOFORM 1).
  5. "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-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-594, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDDX55_HUMAN
AccessioniPrimary (citable) accession number: Q8NHQ9
Secondary accession number(s): Q658L6, Q8IYH0, Q9HCH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 119 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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