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Protein

YTH domain-containing family protein 1

Gene

YTHDF1

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

Functioni

Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and promotes mRNA translation efficiency (PubMed:24284625, PubMed:26046440, PubMed:26318451). 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 (PubMed:24284625). Acts as a regulator of mRNA translation efficiency: promotes ribosome loading to m6A-containing mRNAs and interacts with translation initiation factors eIF3 (EIF3A or EIF3B) to facilitate translation initiation (PubMed:26046440).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei401 – 4011N6-methyladenosineCombined sources1 Publication
Binding sitei441 – 4411N6-methyladenosineBy similarity
Binding sitei465 – 4651N6-methyladenosineCombined sources1 Publication
Binding sitei470 – 4701N6-methyladenosineCombined sources1 Publication

GO - Molecular functioni

  • N6-methyladenosine-containing RNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • ribosome binding Source: UniProtKB

GO - Biological processi

  • positive regulation of translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
YTH domain-containing family protein 1Curated
Alternative name(s):
Dermatomyositis associated with cancer putative autoantigen 11 Publication
Short name:
DACA-11 Publication
Gene namesi
Name:YTHDF1Imported
Synonyms:C20orf21Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15867. YTHDF1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi397 – 3971Y → A: Strongly reduced binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi401 – 4011D → N: Increased binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi411 – 4111W → A: Abolished binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi465 – 4651W → A: Abolished binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi470 – 4701W → A: Abolished binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication
Mutagenesisi506 – 5061R → A: Reduced binding to N6-methyladenosine (m6A)-containing RNAs. 1 Publication

Organism-specific databases

PharmGKBiPA25737.

Polymorphism and mutation databases

BioMutaiYTHDF1.
DMDMi28380041.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 559558YTH domain-containing family protein 1PRO_0000223073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BYJ9.
MaxQBiQ9BYJ9.
PaxDbiQ9BYJ9.
PRIDEiQ9BYJ9.

PTM databases

iPTMnetiQ9BYJ9.
PhosphoSiteiQ9BYJ9.

Miscellaneous databases

PMAP-CutDBQ9BYJ9.

Expressioni

Gene expression databases

BgeeiQ9BYJ9.
CleanExiHS_YTHDF1.
ExpressionAtlasiQ9BYJ9. baseline and differential.
GenevisibleiQ9BYJ9. HS.

Interactioni

Subunit structurei

Interacts with ribosomes. Interacts with eIF3 (EIF3A or EIF3B).1 Publication

Protein-protein interaction databases

BioGridi120257. 59 interactions.
IntActiQ9BYJ9. 15 interactions.
MINTiMINT-7970439.
STRINGi9606.ENSP00000359364.

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi366 – 3749Combined sources
Beta strandi390 – 3978Combined sources
Helixi399 – 40810Combined sources
Helixi415 – 42814Combined sources
Beta strandi434 – 4407Combined sources
Beta strandi443 – 45210Combined sources
Beta strandi457 – 4593Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi473 – 48513Combined sources
Helixi486 – 4883Combined sources
Turni489 – 4913Combined sources
Helixi495 – 4973Combined sources
Helixi502 – 5043Combined sources
Helixi513 – 52513Combined sources
Helixi532 – 5354Combined sources
Helixi536 – 55015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RCIX-ray1.97A/B/C/D361-559[»]
4RCJX-ray1.60A365-554[»]
ProteinModelPortaliQ9BYJ9.
SMRiQ9BYJ9. Positions 365-552.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini389 – 523135YTHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni395 – 3973N6-methyladenosine bindingCombined sources1 Publication
Regioni411 – 4122N6-methyladenosine bindingCombined sources1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi241 – 33191Gln/Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 YTH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1901. Eukaryota.
ENOG410YABQ. LUCA.
GeneTreeiENSGT00390000017549.
HOVERGENiHBG060315.
InParanoidiQ9BYJ9.
OMAiGSKGPVY.
OrthoDBiEOG71VSSM.
PhylomeDBiQ9BYJ9.
TreeFamiTF323736.

Family and domain databases

InterProiIPR007275. YTH_domain.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
PROSITEiPS50882. YTH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BYJ9-1) [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
MSATSVDTQR TKGQDNKVQN GSLHQKDTVH DNDFEPYLTG QSNQSNSYPS
60 70 80 90 100
MSDPYLSSYY PPSIGFPYSL NEAPWSTAGD PPIPYLTTYG QLSNGDHHFM
110 120 130 140 150
HDAVFGQPGG LGNNIYQHRF NFFPENPAFS AWGTSGSQGQ QTQSSAYGSS
160 170 180 190 200
YTYPPSSLGG TVVDGQPGFH SDTLSKAPGM NSLEQGMVGL KIGDVSSSAV
210 220 230 240 250
KTVGSVVSSV ALTGVLSGNG GTNVNMPVSK PTSWAAIASK PAKPQPKMKT
260 270 280 290 300
KSGPVMGGGL PPPPIKHNMD IGTWDNKGPV PKAPVPQQAP SPQAAPQPQQ
310 320 330 340 350
VAQPLPAQPP ALAQPQYQSP QQPPQTRWVA PRNRNAAFGQ SGGAGSDSNS
360 370 380 390 400
PGNVQPNSAP SVESHPVLEK LKAAHSYNPK EFEWNLKSGR VFIIKSYSED
410 420 430 440 450
DIHRSIKYSI WCSTEHGNKR LDSAFRCMSS KGPVYLLFSV NGSGHFCGVA
460 470 480 490 500
EMKSPVDYGT SAGVWSQDKW KGKFDVQWIF VKDVPNNQLR HIRLENNDNK
510 520 530 540 550
PVTNSRDTQE VPLEKAKQVL KIISSYKHTT SIFDDFAHYE KRQEEEEVVR

KERQSRNKQ
Length:559
Mass (Da):60,874
Last modified:June 1, 2001 - v1
Checksum:iDB8AA15636130E18
GO
Isoform 2 (identifier: Q9BYJ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-190: Missing.
     191-260: KIGDVSSSAV...KSGPVMGGGL → MLFLGSLGAW...QAFTATPSAR
     383-559: Missing.

Note: No experimental confirmation available.
Show »
Length:197
Mass (Da):20,833
Checksum:iDD50829544FE6119
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1242FP → AR in BAB62751 (Ref. 4) Curated
Sequence conflicti283 – 2842AP → PH in CAD39029 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 190190Missing in isoform 2. 1 PublicationVSP_006815Add
BLAST
Alternative sequencei191 – 26070KIGDV…MGGGL → MLFLGSLGAWGTTSISTGSI FSLKTLRSQHGGQVGLKVSR PRAPRMGAATPTPRAPWVAR WLMGSQAFTATPSAR in isoform 2. 1 PublicationVSP_006816Add
BLAST
Alternative sequencei383 – 559177Missing in isoform 2. 1 PublicationVSP_006817Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000398 mRNA. Translation: BAA91138.1.
AL096828 Genomic DNA. Translation: CAC09391.3.
BC003681 mRNA. Translation: AAH03681.1.
BC016920 mRNA. Translation: AAH16920.2.
BC025264 mRNA. Translation: AAH25264.1.
BC050284 mRNA. Translation: AAH50284.1.
AB055518 mRNA. Translation: BAB62751.1.
AL834366 mRNA. Translation: CAD39029.1.
CCDSiCCDS13511.1. [Q9BYJ9-1]
RefSeqiNP_060268.2. NM_017798.3. [Q9BYJ9-1]
UniGeneiHs.744852.

Genome annotation databases

EnsembliENST00000370339; ENSP00000359364; ENSG00000149658. [Q9BYJ9-1]
GeneIDi54915.
KEGGihsa:54915.
UCSCiuc002yeh.4. human. [Q9BYJ9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000398 mRNA. Translation: BAA91138.1.
AL096828 Genomic DNA. Translation: CAC09391.3.
BC003681 mRNA. Translation: AAH03681.1.
BC016920 mRNA. Translation: AAH16920.2.
BC025264 mRNA. Translation: AAH25264.1.
BC050284 mRNA. Translation: AAH50284.1.
AB055518 mRNA. Translation: BAB62751.1.
AL834366 mRNA. Translation: CAD39029.1.
CCDSiCCDS13511.1. [Q9BYJ9-1]
RefSeqiNP_060268.2. NM_017798.3. [Q9BYJ9-1]
UniGeneiHs.744852.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RCIX-ray1.97A/B/C/D361-559[»]
4RCJX-ray1.60A365-554[»]
ProteinModelPortaliQ9BYJ9.
SMRiQ9BYJ9. Positions 365-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120257. 59 interactions.
IntActiQ9BYJ9. 15 interactions.
MINTiMINT-7970439.
STRINGi9606.ENSP00000359364.

PTM databases

iPTMnetiQ9BYJ9.
PhosphoSiteiQ9BYJ9.

Polymorphism and mutation databases

BioMutaiYTHDF1.
DMDMi28380041.

Proteomic databases

EPDiQ9BYJ9.
MaxQBiQ9BYJ9.
PaxDbiQ9BYJ9.
PRIDEiQ9BYJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370339; ENSP00000359364; ENSG00000149658. [Q9BYJ9-1]
GeneIDi54915.
KEGGihsa:54915.
UCSCiuc002yeh.4. human. [Q9BYJ9-1]

Organism-specific databases

CTDi54915.
GeneCardsiYTHDF1.
HGNCiHGNC:15867. YTHDF1.
MIMi616529. gene.
neXtProtiNX_Q9BYJ9.
PharmGKBiPA25737.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1901. Eukaryota.
ENOG410YABQ. LUCA.
GeneTreeiENSGT00390000017549.
HOVERGENiHBG060315.
InParanoidiQ9BYJ9.
OMAiGSKGPVY.
OrthoDBiEOG71VSSM.
PhylomeDBiQ9BYJ9.
TreeFamiTF323736.

Miscellaneous databases

ChiTaRSiYTHDF1. human.
GenomeRNAii54915.
PMAP-CutDBQ9BYJ9.
PROiQ9BYJ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYJ9.
CleanExiHS_YTHDF1.
ExpressionAtlasiQ9BYJ9. baseline and differential.
GenevisibleiQ9BYJ9. HS.

Family and domain databases

InterProiIPR007275. YTH_domain.
[Graphical view]
PfamiPF04146. YTH. 1 hit.
[Graphical view]
PROSITEiPS50882. YTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 2).
    Tissue: Ileal mucosa.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [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] (ISOFORM 1).
    Tissue: Colon, Lymph, Placenta and Testis.
  4. "Dermatomyositis associated with cancer autoantigen."
    Onouchi H., Muro Y., Tomita Y.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-559 (ISOFORM 1).
    Tissue: Cervix carcinoma.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-559 (ISOFORM 1).
    Tissue: Melanoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. "N(6)-methyladenosine modulates messenger RNA translation efficiency."
    Wang X., Zhao B.S., Roundtree I.A., Lu Z., Han D., Ma H., Weng X., Chen K., Shi H., He C.
    Cell 161:1388-1399(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RIBOSOMES; EIF3A AND EIF3B.
  15. Cited for: ABSENCE IN CAP-INDEPENDENT MRNA TRANSLATION.
  16. "structural basis for the discriminative recognition of N6-methyladenosine RNA by the human YT521-B homology domain family of proteins."
    Xu C., Liu K., Ahmed H., Loppnau P., Schapira M., Min J.
    J. Biol. Chem. 290:24902-24913(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 361-559 IN COMPLEX WITH N6-METHYLADENOSINE (M6A)-CONTAINING RNA, FUNCTION, RNA-BINDING, MUTAGENESIS OF TYR-397; ASP-401; TRP-411; TRP-465; TRP-470 AND ARG-506.

Entry informationi

Entry nameiYTHD1_HUMAN
AccessioniPrimary (citable) accession number: Q9BYJ9
Secondary accession number(s): Q8N3G5
, Q8TBT1, Q96AN4, Q96S57, Q9BTI7, Q9NX79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 128 of the entry and version 1 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

Caution

Promotes mRNA translation efficiency (PubMed:26046440). It is however unclear whether it plays a role in cap-independent mRNA translation following heat shock stress, since it has not been identified purified eIF3 preparations that promote cap-independent mRNA translation (PubMed:26593424).2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.