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O60231

- DHX16_HUMAN

UniProt

O60231 - DHX16_HUMAN

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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

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. RNA helicase activity Source: ProtInc

GO - Biological processi

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

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
Complete GO annotation...

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

BgeeiO60231.
CleanExiHS_DHX16.
ExpressionAtlasiO60231. baseline and differential.
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. 36 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. DEAD/DEAH_box_helicase_dom.
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

        10         20         30         40         50
MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT
60 70 80 90 100
DTLDLSGPAR DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL
110 120 130 140 150
EDSEESSEET VSRAGSSLQK KRKKRKHLRK KREEEEEEEA SEKGKKKTGG
160 170 180 190 200
SKQQTEKPES EDEWERTERE RLQDLEERDA FAERVRQRDK DRTRNVLERS
210 220 230 240 250
DKKAYEEAQK RLKMAEEDRK AMVPELRKKS RREYLAKRER EKLEDLEAEL
260 270 280 290 300
ADEEFLFGDV ELSRHERQEL KYKRRVRDLA REYRAAGEQE KLEATNRYHM
310 320 330 340 350
PKETRGQPAR AVDLVEEESG APGEEQRRWE EARLGAASLK FGARDAASQE
360 370 380 390 400
PKYQLVLEEE ETIEFVRATQ LQGDEEPSAP PTSTQAQQKE SIQAVRRSLP
410 420 430 440 450
VFPFREELLA AIANHQVLII EGETGSGKTT QIPQYLFEEG YTNKGMKIAC
460 470 480 490 500
TQPRRVAAMS VAARVAREMG VKLGNEVGYS IRFEDCTSER TVLRYMTDGM
510 520 530 540 550
LLREFLSEPD LASYSVVMVD EAHERTLHTD ILFGLIKDVA RFRPELKVLV
560 570 580 590 600
ASATMDTARF STFFDDAPVF RIPGRRFPVD IFYTKAPEAD YLEACVVSVL
610 620 630 640 650
QIHVTQPPGD ILVFLTGQEE IEAACEMLQD RCRRLGSKIR ELLVLPIYAN
660 670 680 690 700
LPSDMQARIF QPTPPGARKV VVATNIAETS LTIEGIIYVL DPGFCKQKSY
710 720 730 740 750
NPRTGMESLT VTPCSKASAN QRAGRAGRVA AGKCFRLYTA WAYQHELEET
760 770 780 790 800
TVPEIQRTSL GNVVLLLKSL GIHDLMHFDF LDPPPYETLL LALEQLYALG
810 820 830 840 850
ALNHLGELTT SGRKMAELPV DPMLSKMILA SEKYSCSEEI LTVAAMLSVN
860 870 880 890 900
NSIFYRPKDK VVHADNARVN FFLPGGDHLV LLNVYTQWAE SGYSSQWCYE
910 920 930 940 950
NFVQFRSMRR ARDVREQLEG LLERVEVGLS SCQGDYIRVR KAITAGYFYH
960 970 980 990 1000
TARLTRSGYR TVKQQQTVFI HPNSSLFEQQ PRWLLYHELV LTTKEFMRQV
1010 1020 1030 1040
LEIESSWLLE VAPHYYKAKE LEDPHAKKMP KKIGKTREEL G
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. 36 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

Bgeei O60231.
CleanExi HS_DHX16.
ExpressionAtlasi O60231. baseline and differential.
Genevestigatori O60231.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 156 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