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Q7Z739 (YTHD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
YTH domain-containing family protein 3
Gene names
Name:YTHDF3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability. Ref.10 Ref.12

Sequence similarities

Contains 1 YTH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gagP045912EBI-2849837,EBI-6179727From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 585584YTH domain-containing family protein 3
PRO_0000230991

Regions

Domain416 – 550135YTH

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.11
Modified residue231Phosphoserine Ref.8

Experimental info

Sequence conflict1391S → R in CAH56224. Ref.2
Sequence conflict3811P → S in CAH56224. Ref.2
Sequence conflict5321S → P in CAH56480. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q7Z739 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C7021FE48DEA441E

FASTA58563,861
        10         20         30         40         50         60 
MSATSVDQRP KGQGNKVSVQ NGSIHQKDAV NDDDFEPYLS SQTNQSNSYP PMSDPYMPSY 

        70         80         90        100        110        120 
YAPSIGFPYS LGEAAWSTAG DQPMPYLTTY GQMSNGEHHY IPDGVFSQPG ALGNTPPFLG 

       130        140        150        160        170        180 
QHGFNFFPGN ADFSTWGTSG SQGQSTQSSA YSSSYGYPPS SLGRAITDGQ AGFGNDTLSK 

       190        200        210        220        230        240 
VPGISSIEQG MTGLKIGGDL TAAVTKTVGT ALSSSGMTSI ATNSVPPVSS AAPKPTSWAA 

       250        260        270        280        290        300 
IARKPAKPQP KLKPKGNVGI GGSAVPPPPI KHNMNIGTWD EKGSVVKAPP TQPVLPPQTI 

       310        320        330        340        350        360 
IQQPQPLIQP PPLVQSQLPQ QQPQPPQPQQ QQGPQPQAQP HQVQPQQQQL QNRWVAPRNR 

       370        380        390        400        410        420 
GAGFNQNNGA GSENFGLGVV PVSASPSSVE VHPVLEKLKA INNYNPKDFD WNLKNGRVFI 

       430        440        450        460        470        480 
IKSYSEDDIH RSIKYSIWCS TEHGNKRLDA AYRSLNGKGP LYLLFSVNGS GHFCGVAEMK 

       490        500        510        520        530        540 
SVVDYNAYAG VWSQDKWKGK FEVKWIFVKD VPNNQLRHIR LENNDNKPVT NSRDTQEVPL 

       550        560        570        580 
EKAKQVLKII ATFKHTTSIF DDFAHYEKRQ EEEEAMRRER NRNKQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
Tissue: Tongue.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle and Spinal cord.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Testis.
[5]Bienvenut W.V., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 256-271; 408-414 AND 534-542, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[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-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq."
Dominissini D., Moshitch-Moshkovitz S., Schwartz S., Salmon-Divon M., Ungar L., Osenberg S., Cesarkas K., Jacob-Hirsch J., Amariglio N., Kupiec M., Sorek R., Rechavi G.
Nature 485:201-206(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, FUNCTION.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-methyladenosine-dependent regulation of messenger RNA stability."
Wang X., Lu Z., Gomez A., Hon G.C., Yue Y., Han D., Fu Y., Parisien M., Dai Q., Jia G., Ren B., Pan T., He C.
Nature 505:117-120(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK127574 mRNA. Translation: BAG54526.1.
AL832005 mRNA. Translation: CAH56224.1.
BX537996 mRNA. Translation: CAH56480.1.
CH471068 Genomic DNA. Translation: EAW86867.1.
BC052970 mRNA. Translation: AAH52970.1.
RefSeqNP_001264742.1. NM_001277813.1.
NP_001264743.1. NM_001277814.1.
NP_001264744.1. NM_001277815.1.
NP_001264745.1. NM_001277816.1.
NP_001264746.1. NM_001277817.1.
NP_001264747.1. NM_001277818.1.
NP_689971.4. NM_152758.5.
UniGeneHs.491861.

3D structure databases

ProteinModelPortalQ7Z739.
SMRQ7Z739. Positions 417-549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128997. 5 interactions.
IntActQ7Z739. 2 interactions.
MINTMINT-5005374.
STRING9606.ENSP00000398476.

PTM databases

PhosphoSiteQ7Z739.

Polymorphism databases

DMDM74738853.

Proteomic databases

PaxDbQ7Z739.
PRIDEQ7Z739.

Protocols and materials databases

DNASU253943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID253943.
KEGGhsa:253943.
UCSCuc003xuy.4. human.

Organism-specific databases

CTD253943.
GeneCardsGC08P064081.
HGNCHGNC:26465. YTHDF3.
neXtProtNX_Q7Z739.
PharmGKBPA134976395.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276347.
HOVERGENHBG060315.
InParanoidQ7Z739.

Gene expression databases

CleanExHS_YTHDF3.
GenevestigatorQ7Z739.

Family and domain databases

InterProIPR007275. YTH_domain.
[Graphical view]
PfamPF04146. YTH. 1 hit.
[Graphical view]
PROSITEPS50882. YTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiYTHDF3.
GenomeRNAi253943.
NextBio92198.
PMAP-CutDBQ7Z739.
PROQ7Z739.

Entry information

Entry nameYTHD3_HUMAN
AccessionPrimary (citable) accession number: Q7Z739
Secondary accession number(s): B3KXL4, Q63Z37, Q659A3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 1, 2003
Last modified: March 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM