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Protein

ATP-dependent RNA helicase DDX54

Gene

DDX54

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

Functioni

Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1478ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: UniProtKB
  3. estrogen receptor binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. receptor binding Source: UniProtKB
  6. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. intracellular estrogen receptor signaling pathway Source: UniProtKB
  3. negative regulation of nucleic acid-templated transcription Source: GOC
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. RNA metabolic process Source: UniProtKB
  6. RNA processing Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX54 (EC:3.6.4.13)
Alternative name(s):
ATP-dependent RNA helicase DP97
DEAD box RNA helicase 97 kDa
DEAD box protein 54
Gene namesi
Name:DDX54
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:20084. DDX54.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992026.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881ATP-dependent RNA helicase DDX54PRO_0000055056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine2 Publications
Modified residuei39 – 391Phosphoserine2 Publications
Modified residuei41 – 411Phosphoserine2 Publications
Modified residuei75 – 751Phosphoserine1 Publication
Modified residuei644 – 6441Phosphoserine1 Publication
Modified residuei696 – 6961Phosphoserine1 Publication
Modified residuei698 – 6981Phosphoserine1 Publication
Modified residuei782 – 7821Phosphoserine5 Publications
Modified residuei788 – 7881Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8TDD1.
PaxDbiQ8TDD1.
PRIDEiQ8TDD1.

2D gel databases

SWISS-2DPAGEQ8TDD1.

PTM databases

PhosphoSiteiQ8TDD1.

Expressioni

Gene expression databases

BgeeiQ8TDD1.
CleanExiHS_DDX54.
ExpressionAtlasiQ8TDD1. baseline and differential.
GenevestigatoriQ8TDD1.

Organism-specific databases

HPAiHPA028244.

Interactioni

Subunit structurei

Interacts in a hormone-dependent manner with nuclear receptors.

Protein-protein interaction databases

BioGridi122503. 24 interactions.
IntActiQ8TDD1. 6 interactions.
MINTiMINT-3045390.
STRINGi9606.ENSP00000323858.

Structurei

3D structure databases

ProteinModelPortaliQ8TDD1.
SMRiQ8TDD1. Positions 98-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini127 – 299173Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini326 – 473148Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni605 – 64743Interaction with nuclear receptorsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 12429Q motifAdd
BLAST
Motifi247 – 2504DEAD box

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00550000075100.
HOGENOMiHOG000246455.
HOVERGENiHBG051333.
InParanoidiQ8TDD1.
KOiK14808.
OMAiENVVNYD.
OrthoDBiEOG786H2W.
PhylomeDBiQ8TDD1.
TreeFamiTF105707.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR012541. DBP10CT.
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]
PfamiPF08147. DBP10CT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
ProDomiPD024971. DBP10CT. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
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: Q8TDD1-1) [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
MAADKGPAAG PRSRAAMAQW RKKKGLRKRR GAASQARGSD SEDGEFEIQA
60 70 80 90 100
EDDARARKLG PGRPLPTFPT SECTSDVEPD TREMVRAQNK KKKKSGGFQS
110 120 130 140 150
MGLSYPVFKG IMKKGYKVPT PIQRKTIPVI LDGKDVVAMA RTGSGKTACF
160 170 180 190 200
LLPMFERLKT HSAQTGARAL ILSPTRELAL QTLKFTKELG KFTGLKTALI
210 220 230 240 250
LGGDRMEDQF AALHENPDII IATPGRLVHV AVEMSLKLQS VEYVVFDEAD
260 270 280 290 300
RLFEMGFAEQ LQEIIARLPG GHQTVLFSAT LPKLLVEFAR AGLTEPVLIR
310 320 330 340 350
LDVDTKLNEQ LKTSFFLVRE DTKAAVLLHL LHNVVRPQDQ TVVFVATKHH
360 370 380 390 400
AEYLTELLTT QRVSCAHIYS ALDPTARKIN LAKFTLGKCS TLIVTDLAAR
410 420 430 440 450
GLDIPLLDNV INYSFPAKGK LFLHRVGRVA RAGRSGTAYS LVAPDEIPYL
460 470 480 490 500
LDLHLFLGRS LTLARPLKEP SGVAGVDGML GRVPQSVVDE EDSGLQSTLE
510 520 530 540 550
ASLELRGLAR VADNAQQQYV RSRPAPSPES IKRAKEMDLV GLGLHPLFSS
560 570 580 590 600
RFEEEELQRL RLVDSIKNYR SRATIFEINA SSRDLCSQVM RAKRQKDRKA
610 620 630 640 650
IARFQQGQQG RQEQQEGPVG PAPSRPALQE KQPEKEEEEE AGESVEDIFS
660 670 680 690 700
EVVGRKRQRS GPNRGAKRRR EEARQRDQEF YIPYRPKDFD SERGLSISGE
710 720 730 740 750
GGAFEQQAAG AVLDLMGDEA QNLTRGRQQL KWDRKKKRFV GQSGQEDKKK
760 770 780 790 800
IKTESGRYIS SSYKRDLYQK WKQKQKIDDR DSDEEGASDR RGPERRGGKR
810 820 830 840 850
DRGQGASRPH APGTPAGRVR PELKTKQQIL KQRRRAQKLH FLQRGGLKQL
860 870 880
SARNRRRVQE LQQGAFGRGA RSKKGKMRKR M
Length:881
Mass (Da):98,595
Last modified:April 26, 2004 - v2
Checksum:i9823C75156D998C4
GO
Isoform 2 (identifier: Q8TDD1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     804-804: Q → QA

Show »
Length:882
Mass (Da):98,666
Checksum:i947F50470F865F96
GO

Sequence cautioni

The sequence AAN59978.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti570 – 5701R → H.
Corresponds to variant rs35519289 [ dbSNP | Ensembl ].
VAR_052171
Natural varianti693 – 6931R → Q.
Corresponds to variant rs11564 [ dbSNP | Ensembl ].
VAR_052172
Natural varianti712 – 7121V → A.
Corresponds to variant rs10354 [ dbSNP | Ensembl ].
VAR_052173
Natural varianti821 – 8211P → L.
Corresponds to variant rs1048889 [ dbSNP | Ensembl ].
VAR_033860

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei804 – 8041Q → QA in isoform 2. 1 PublicationVSP_040135

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478457 mRNA. Translation: AAL85336.1.
AC089999 Genomic DNA. No translation available.
AY148094 mRNA. Translation: AAN59978.1. Sequence problems.
BC005848 mRNA. Translation: AAH05848.2.
CCDSiCCDS31907.1. [Q8TDD1-1]
CCDS44984.1. [Q8TDD1-2]
RefSeqiNP_001104792.1. NM_001111322.1. [Q8TDD1-2]
NP_076977.3. NM_024072.3. [Q8TDD1-1]
UniGeneiHs.506861.

Genome annotation databases

EnsembliENST00000306014; ENSP00000304072; ENSG00000123064. [Q8TDD1-1]
ENST00000314045; ENSP00000323858; ENSG00000123064. [Q8TDD1-2]
GeneIDi79039.
KEGGihsa:79039.
UCSCiuc001tup.3. human. [Q8TDD1-1]
uc001tuq.4. human. [Q8TDD1-2]

Polymorphism databases

DMDMi46576615.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478457 mRNA. Translation: AAL85336.1.
AC089999 Genomic DNA. No translation available.
AY148094 mRNA. Translation: AAN59978.1. Sequence problems.
BC005848 mRNA. Translation: AAH05848.2.
CCDSiCCDS31907.1. [Q8TDD1-1]
CCDS44984.1. [Q8TDD1-2]
RefSeqiNP_001104792.1. NM_001111322.1. [Q8TDD1-2]
NP_076977.3. NM_024072.3. [Q8TDD1-1]
UniGeneiHs.506861.

3D structure databases

ProteinModelPortaliQ8TDD1.
SMRiQ8TDD1. Positions 98-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122503. 24 interactions.
IntActiQ8TDD1. 6 interactions.
MINTiMINT-3045390.
STRINGi9606.ENSP00000323858.

PTM databases

PhosphoSiteiQ8TDD1.

Polymorphism databases

DMDMi46576615.

2D gel databases

SWISS-2DPAGEQ8TDD1.

Proteomic databases

MaxQBiQ8TDD1.
PaxDbiQ8TDD1.
PRIDEiQ8TDD1.

Protocols and materials databases

DNASUi79039.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306014; ENSP00000304072; ENSG00000123064. [Q8TDD1-1]
ENST00000314045; ENSP00000323858; ENSG00000123064. [Q8TDD1-2]
GeneIDi79039.
KEGGihsa:79039.
UCSCiuc001tup.3. human. [Q8TDD1-1]
uc001tuq.4. human. [Q8TDD1-2]

Organism-specific databases

CTDi79039.
GeneCardsiGC12M113598.
HGNCiHGNC:20084. DDX54.
HPAiHPA028244.
MIMi611665. gene.
neXtProtiNX_Q8TDD1.
PharmGKBiPA134992026.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00550000075100.
HOGENOMiHOG000246455.
HOVERGENiHBG051333.
InParanoidiQ8TDD1.
KOiK14808.
OMAiENVVNYD.
OrthoDBiEOG786H2W.
PhylomeDBiQ8TDD1.
TreeFamiTF105707.

Miscellaneous databases

ChiTaRSiDDX54. human.
GenomeRNAii79039.
NextBioi67773.
PROiQ8TDD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TDD1.
CleanExiHS_DDX54.
ExpressionAtlasiQ8TDD1. baseline and differential.
GenevestigatoriQ8TDD1.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR012541. DBP10CT.
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]
PfamiPF08147. DBP10CT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
ProDomiPD024971. DBP10CT. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
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

« Hide 'large scale' publications
  1. "Positional cloning of the Flv gene."
    Perelygin A.A.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Placenta.
  2. "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].
  3. "Regulation of nuclear receptor transcriptional activity by a novel DEAD box RNA helicase (DP97)."
    Rajendran R.R., Nye A.C., Frasor J., Balsara R.D., Martini P.G., Katzenellenbogen B.S.
    J. Biol. Chem. 278:4628-4638(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-881 (ISOFORM 1), FUNCTION.
  4. "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 18-881 (ISOFORM 1).
    Tissue: Kidney.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-75; SER-644; SER-782 AND SER-788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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-34; SER-39; SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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-696; SER-698 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-39; SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDDX54_HUMAN
AccessioniPrimary (citable) accession number: Q8TDD1
Secondary accession number(s): Q86YT8, Q9BRZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: January 7, 2015
This is version 123 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

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.