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Protein

ATP-dependent RNA helicase DDX51

Gene

DDX51

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

Functioni

ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi256 – 2638ATPPROSITE-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 - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX51 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 51
Gene namesi
Name:DDX51
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:20082. DDX51.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134974036.

Polymorphism and mutation databases

BioMutaiDDX51.
DMDMi229462978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 666665ATP-dependent RNA helicase DDX51PRO_0000228096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei103 – 1031PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8N8A6.
MaxQBiQ8N8A6.
PaxDbiQ8N8A6.
PRIDEiQ8N8A6.

PTM databases

iPTMnetiQ8N8A6.
PhosphoSiteiQ8N8A6.

Expressioni

Gene expression databases

BgeeiQ8N8A6.
CleanExiHS_DDX51.
GenevisibleiQ8N8A6. HS.

Organism-specific databases

HPAiHPA039503.

Interactioni

Protein-protein interaction databases

BioGridi130475. 30 interactions.
IntActiQ8N8A6. 9 interactions.
MINTiMINT-3038025.
STRINGi9606.ENSP00000380495.

Structurei

3D structure databases

ProteinModelPortaliQ8N8A6.
SMRiQ8N8A6. Positions 200-660.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini243 – 452210Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini494 – 640147Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi221 – 2299Q motif
Motifi371 – 3744DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 7546Arg-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

eggNOGiKOG0350. Eukaryota.
ENOG410XRWM. LUCA.
GeneTreeiENSGT00550000075141.
HOGENOMiHOG000239572.
HOVERGENiHBG081427.
InParanoidiQ8N8A6.
KOiK14807.
OMAiKLVCKSN.
OrthoDBiEOG708VZB.
PhylomeDBiQ8N8A6.
TreeFamiTF314505.

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.
[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. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8N8A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALFYVARYP GPDAAAAAGP EGAEAGAHGR ARALLERLQS RARERQQQRE
60 70 80 90 100
PAQTEAAAST EPATRRRRRP RRRRRVNDAE PGSPEAPQGK RRKADGEDAG
110 120 130 140 150
AESNEEAPGE PSAGSSEEAP GEPSAGSSEE APGERSTSAS AEAAPDGPAL
160 170 180 190 200
EEAAGPLVPG LVLGGFGKRK APKVQPFLPR WLAEPNCVRR NVTEDLVPIE
210 220 230 240 250
DIPDVHPDLQ KQLRAHGISS YFPVQAAVIP ALLESAACGF LVGRGGYRPS
260 270 280 290 300
DLCVSAPTGS GKTLAFVIPV VQALLSRVVC HIRALVVLPT KELAQQVSKV
310 320 330 340 350
FNIYTDATPL RVSLVTGQKS LAKEQESLVQ KTADGYRCLA DIVVATPGRL
360 370 380 390 400
VDHIDQTPGF SLQQLRFLII DEADRMIDSM HQSWLPRVVA AAFQSEDPAD
410 420 430 440 450
PCALLQRRQA QAVTAASTCC PQMPLQKLLF SATLTQNPEK LQQLGLHQPR
460 470 480 490 500
LFSTGLAHRG LEDTDGDGDS GKYAFPVGLT HHYVPCSLSS KPLVVLHLVL
510 520 530 540 550
EMGFSRVLCF TNSRENSHRL FLLVQAFGGV DVAEFSSRYG PGQRRMILKQ
560 570 580 590 600
FEQGKIQLLI STDATARGID VQGVELVVNY DAPQYLRTYV HRVGRTARAG
610 620 630 640 650
KTGQAFTLLL KVQERRFLRM LTEAGAPELQ RHELSSKLLQ PLVPRYEEAL
660
SQLEESVKEE RKQRAA
Length:666
Mass (Da):72,457
Last modified:May 5, 2009 - v3
Checksum:iB1A8D275918B194C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1223PGE → QGG in AAH40185 (PubMed:15489334).Curated
Sequence conflicti592 – 5921R → RR in CAI59782 (PubMed:17974005).Curated
Sequence conflicti617 – 6171F → L in CAI59782 (PubMed:17974005).Curated
Sequence conflicti654 – 6541E → G in CAI59782 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411R → Q.1 Publication
Corresponds to variant rs17857214 [ dbSNP | Ensembl ].
VAR_055299
Natural varianti134 – 1341E → V.1 Publication
Corresponds to variant rs17855642 [ dbSNP | Ensembl ].
VAR_055300
Natural varianti175 – 1751Q → K.1 Publication
Corresponds to variant rs17855639 [ dbSNP | Ensembl ].
VAR_055301
Natural varianti249 – 2491P → L.1 Publication
Corresponds to variant rs17857213 [ dbSNP | Ensembl ].
VAR_055302
Natural varianti295 – 2951Q → R.1 Publication
Corresponds to variant rs1133690 [ dbSNP | Ensembl ].
VAR_055303
Natural varianti322 – 3221A → V.1 Publication
Corresponds to variant rs60927391 [ dbSNP | Ensembl ].
VAR_061825
Natural varianti406 – 4061Q → K.1 Publication
Corresponds to variant rs17853968 [ dbSNP | Ensembl ].
VAR_055304
Natural varianti652 – 6521Q → K.1 Publication
Corresponds to variant rs17853969 [ dbSNP | Ensembl ].
VAR_055305

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097078 mRNA. Translation: BAC04942.1.
AC138466 Genomic DNA. No translation available.
BC012461 mRNA. Translation: AAH12461.2.
BC040185 mRNA. Translation: AAH40185.1.
CR936870 Transcribed RNA. Translation: CAI59782.1.
CCDSiCCDS41865.1.
RefSeqiNP_778236.2. NM_175066.3.
UniGeneiHs.445168.

Genome annotation databases

EnsembliENST00000397333; ENSP00000380495; ENSG00000185163.
GeneIDi317781.
KEGGihsa:317781.
UCSCiuc001ujy.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK097078 mRNA. Translation: BAC04942.1.
AC138466 Genomic DNA. No translation available.
BC012461 mRNA. Translation: AAH12461.2.
BC040185 mRNA. Translation: AAH40185.1.
CR936870 Transcribed RNA. Translation: CAI59782.1.
CCDSiCCDS41865.1.
RefSeqiNP_778236.2. NM_175066.3.
UniGeneiHs.445168.

3D structure databases

ProteinModelPortaliQ8N8A6.
SMRiQ8N8A6. Positions 200-660.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi130475. 30 interactions.
IntActiQ8N8A6. 9 interactions.
MINTiMINT-3038025.
STRINGi9606.ENSP00000380495.

PTM databases

iPTMnetiQ8N8A6.
PhosphoSiteiQ8N8A6.

Polymorphism and mutation databases

BioMutaiDDX51.
DMDMi229462978.

Proteomic databases

EPDiQ8N8A6.
MaxQBiQ8N8A6.
PaxDbiQ8N8A6.
PRIDEiQ8N8A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397333; ENSP00000380495; ENSG00000185163.
GeneIDi317781.
KEGGihsa:317781.
UCSCiuc001ujy.5. human.

Organism-specific databases

CTDi317781.
GeneCardsiDDX51.
H-InvDBHIX0018137.
HGNCiHGNC:20082. DDX51.
HPAiHPA039503.
neXtProtiNX_Q8N8A6.
PharmGKBiPA134974036.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0350. Eukaryota.
ENOG410XRWM. LUCA.
GeneTreeiENSGT00550000075141.
HOGENOMiHOG000239572.
HOVERGENiHBG081427.
InParanoidiQ8N8A6.
KOiK14807.
OMAiKLVCKSN.
OrthoDBiEOG708VZB.
PhylomeDBiQ8N8A6.
TreeFamiTF314505.

Miscellaneous databases

GenomeRNAii317781.
PROiQ8N8A6.

Gene expression databases

BgeeiQ8N8A6.
CleanExiHS_DDX51.
GenevisibleiQ8N8A6. HS.

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.
[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. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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], VARIANT VAL-322.
    Tissue: Small intestine.
  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. "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], VARIANTS GLN-41; VAL-134; LYS-175; LEU-249; ARG-295; LYS-406 AND LYS-652.
    Tissue: Brain and Urinary bladder.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-666.
    Tissue: Retina.
  5. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, 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-83, 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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDDX51_HUMAN
AccessioniPrimary (citable) accession number: Q8N8A6
Secondary accession number(s): A8MPT9
, Q5CZ71, Q8IXK5, Q96ED1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 121 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.