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O60231

- DHX16_HUMAN

UniProt

O60231 - DHX16_HUMAN

Protein

Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16

Gene

DHX16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (28 Nov 2002)
      Previous versions | rss
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    Functioni

    Probable ATP-binding RNA helicase involved in pre-mRNA splicing.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi422 – 4298ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. RNA splicing Source: ProtInc

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 (EC:3.6.4.13)
    Alternative name(s):
    ATP-dependent RNA helicase #3
    DEAH-box protein 16
    Gene namesi
    Name:DHX16
    Synonyms:DBP2, DDX16, KIAA0577
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2739. DHX16.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27205.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10411041Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16PRO_0000055151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031Phosphoserine7 Publications
    Modified residuei106 – 1061Phosphoserine2 Publications
    Modified residuei107 – 1071Phosphoserine3 Publications
    Modified residuei160 – 1601Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60231.
    PaxDbiO60231.
    PRIDEiO60231.

    PTM databases

    PhosphoSiteiO60231.

    Expressioni

    Gene expression databases

    ArrayExpressiO60231.
    BgeeiO60231.
    CleanExiHS_DHX16.
    GenevestigatoriO60231.

    Organism-specific databases

    HPAiHPA051455.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX38Q926202EBI-311446,EBI-1043041
    GPKOWQ929172EBI-311446,EBI-746309
    SF3B2Q134352EBI-311446,EBI-749111
    XAB2Q9HCS72EBI-311446,EBI-295232

    Protein-protein interaction databases

    BioGridi114027. 32 interactions.
    IntActiO60231. 12 interactions.
    MINTiMINT-5003862.
    STRINGi9606.ENSP00000390938.

    Structurei

    3D structure databases

    ProteinModelPortaliO60231.
    SMRiO60231. Positions 392-1033.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini409 – 573165Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini598 – 771174Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi520 – 5234DEAH box

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1643.
    HOGENOMiHOG000175261.
    HOVERGENiHBG039428.
    InParanoidiO60231.
    KOiK12813.
    OMAiIEIESKW.
    PhylomeDBiO60231.
    TreeFamiTF313473.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR011709. DUF1605.
    IPR007502. Helicase-assoc_dom.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF04408. HA2. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF07717. OB_NTP_bind. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00847. HA2. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60231-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT     50
    DTLDLSGPAR DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL 100
    EDSEESSEET VSRAGSSLQK KRKKRKHLRK KREEEEEEEA SEKGKKKTGG 150
    SKQQTEKPES EDEWERTERE RLQDLEERDA FAERVRQRDK DRTRNVLERS 200
    DKKAYEEAQK RLKMAEEDRK AMVPELRKKS RREYLAKRER EKLEDLEAEL 250
    ADEEFLFGDV ELSRHERQEL KYKRRVRDLA REYRAAGEQE KLEATNRYHM 300
    PKETRGQPAR AVDLVEEESG APGEEQRRWE EARLGAASLK FGARDAASQE 350
    PKYQLVLEEE ETIEFVRATQ LQGDEEPSAP PTSTQAQQKE SIQAVRRSLP 400
    VFPFREELLA AIANHQVLII EGETGSGKTT QIPQYLFEEG YTNKGMKIAC 450
    TQPRRVAAMS VAARVAREMG VKLGNEVGYS IRFEDCTSER TVLRYMTDGM 500
    LLREFLSEPD LASYSVVMVD EAHERTLHTD ILFGLIKDVA RFRPELKVLV 550
    ASATMDTARF STFFDDAPVF RIPGRRFPVD IFYTKAPEAD YLEACVVSVL 600
    QIHVTQPPGD ILVFLTGQEE IEAACEMLQD RCRRLGSKIR ELLVLPIYAN 650
    LPSDMQARIF QPTPPGARKV VVATNIAETS LTIEGIIYVL DPGFCKQKSY 700
    NPRTGMESLT VTPCSKASAN QRAGRAGRVA AGKCFRLYTA WAYQHELEET 750
    TVPEIQRTSL GNVVLLLKSL GIHDLMHFDF LDPPPYETLL LALEQLYALG 800
    ALNHLGELTT SGRKMAELPV DPMLSKMILA SEKYSCSEEI LTVAAMLSVN 850
    NSIFYRPKDK VVHADNARVN FFLPGGDHLV LLNVYTQWAE SGYSSQWCYE 900
    NFVQFRSMRR ARDVREQLEG LLERVEVGLS SCQGDYIRVR KAITAGYFYH 950
    TARLTRSGYR TVKQQQTVFI HPNSSLFEQQ PRWLLYHELV LTTKEFMRQV 1000
    LEIESSWLLE VAPHYYKAKE LEDPHAKKMP KKIGKTREEL G 1041
    Length:1,041
    Mass (Da):119,264
    Last modified:November 28, 2002 - v2
    Checksum:i5CAC4DBEF21A4E6D
    GO

    Sequence cautioni

    The sequence BAA25503.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231V → I in BAA25908. (PubMed:9547260)Curated
    Sequence conflicti631 – 6311R → P in BAA25908. (PubMed:9547260)Curated
    Sequence conflicti681 – 6811L → P in BAA25908. (PubMed:9547260)Curated
    Sequence conflicti792 – 7921A → T in BAA25908. (PubMed:9547260)Curated
    Sequence conflicti899 – 8991Y → C in BAA25908. (PubMed:9547260)Curated
    Sequence conflicti1032 – 10321K → KK in AAH08825. (PubMed:15489334)Curated
    Sequence conflicti1032 – 10321K → KK in AAH09392. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti352 – 3521K → E.
    Corresponds to variant rs17189239 [ dbSNP | Ensembl ].
    VAR_057236
    Natural varianti502 – 5021L → F.
    Corresponds to variant rs17189232 [ dbSNP | Ensembl ].
    VAR_057237
    Natural varianti566 – 5661D → G.1 Publication
    Corresponds to variant rs9262138 [ dbSNP | Ensembl ].
    VAR_057238

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001601 mRNA. Translation: BAA25908.1.
    BA000025 Genomic DNA. Translation: BAB63323.1.
    AB011149 mRNA. Translation: BAA25503.2. Different initiation.
    AL845353 Genomic DNA. Translation: CAI41883.1.
    BC008825 mRNA. Translation: AAH08825.1.
    BC009392 mRNA. Translation: AAH09392.1.
    CCDSiCCDS4685.1.
    RefSeqiNP_001157711.1. NM_001164239.1.
    NP_003578.2. NM_003587.4.
    UniGeneiHs.485060.

    Genome annotation databases

    EnsembliENST00000376442; ENSP00000365625; ENSG00000204560.
    ENST00000383577; ENSP00000373071; ENSG00000206486.
    ENST00000417308; ENSP00000390938; ENSG00000233561.
    ENST00000421095; ENSP00000396193; ENSG00000226171.
    ENST00000424672; ENSP00000389862; ENSG00000233418.
    ENST00000451456; ENSP00000408956; ENSG00000233049.
    ENST00000458094; ENSP00000393958; ENSG00000231377.
    GeneIDi8449.
    KEGGihsa:8449.
    UCSCiuc003nqz.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001601 mRNA. Translation: BAA25908.1 .
    BA000025 Genomic DNA. Translation: BAB63323.1 .
    AB011149 mRNA. Translation: BAA25503.2 . Different initiation.
    AL845353 Genomic DNA. Translation: CAI41883.1 .
    BC008825 mRNA. Translation: AAH08825.1 .
    BC009392 mRNA. Translation: AAH09392.1 .
    CCDSi CCDS4685.1.
    RefSeqi NP_001157711.1. NM_001164239.1.
    NP_003578.2. NM_003587.4.
    UniGenei Hs.485060.

    3D structure databases

    ProteinModelPortali O60231.
    SMRi O60231. Positions 392-1033.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114027. 32 interactions.
    IntActi O60231. 12 interactions.
    MINTi MINT-5003862.
    STRINGi 9606.ENSP00000390938.

    PTM databases

    PhosphoSitei O60231.

    Proteomic databases

    MaxQBi O60231.
    PaxDbi O60231.
    PRIDEi O60231.

    Protocols and materials databases

    DNASUi 8449.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376442 ; ENSP00000365625 ; ENSG00000204560 .
    ENST00000383577 ; ENSP00000373071 ; ENSG00000206486 .
    ENST00000417308 ; ENSP00000390938 ; ENSG00000233561 .
    ENST00000421095 ; ENSP00000396193 ; ENSG00000226171 .
    ENST00000424672 ; ENSP00000389862 ; ENSG00000233418 .
    ENST00000451456 ; ENSP00000408956 ; ENSG00000233049 .
    ENST00000458094 ; ENSP00000393958 ; ENSG00000231377 .
    GeneIDi 8449.
    KEGGi hsa:8449.
    UCSCi uc003nqz.3. human.

    Organism-specific databases

    CTDi 8449.
    GeneCardsi GC06M030620.
    GC06Mj30610.
    GC06Mk30611.
    GC06Ml30665.
    GC06Mm30699.
    GC06Mn30610.
    GC06Mo30612.
    HGNCi HGNC:2739. DHX16.
    HPAi HPA051455.
    MIMi 603405. gene.
    neXtProti NX_O60231.
    PharmGKBi PA27205.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1643.
    HOGENOMi HOG000175261.
    HOVERGENi HBG039428.
    InParanoidi O60231.
    KOi K12813.
    OMAi IEIESKW.
    PhylomeDBi O60231.
    TreeFami TF313473.

    Miscellaneous databases

    GeneWikii DHX16.
    GenomeRNAii 8449.
    NextBioi 31614.
    PROi O60231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60231.
    Bgeei O60231.
    CleanExi HS_DHX16.
    Genevestigatori O60231.

    Family and domain databases

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

    Publicationsi

    1. "Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8."
      Imamura O., Saiki K., Tani T., Ohshima Y., Sugawara M., Furuichi Y.
      Nucleic Acids Res. 26:2063-2068(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-566.
    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].
      Tissue: Brain.
    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-103 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-106 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "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].
    11. "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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-103; SER-106; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-103; SER-107 AND SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDHX16_HUMAN
    AccessioniPrimary (citable) accession number: O60231
    Secondary accession number(s): O60322
    , Q5JP45, Q969X7, Q96QC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 28, 2002
    Last modified: October 1, 2014
    This is version 155 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 6
      Human chromosome 6: 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