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Q86U44

- MTA70_HUMAN

UniProt

Q86U44 - MTA70_HUMAN

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Protein
N6-adenosine-methyltransferase 70 kDa subunit
Gene
METTL3, MTA70
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

N6-methyltransferase that methylates adenosine residues of some mRNAs and acts as a regulator of the circadian clock. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing and processing. M6A regulates the length of the ciracadian clock: acts as a early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  1. RNA methylation Source: UniProtKB
  2. circadian rhythm Source: UniProtKB
  3. gene expression Source: Reactome
  4. mRNA destabilization Source: UniProtKB
  5. mRNA methylation Source: UniProtKB
  6. mRNA processing Source: UniProtKB
  7. stem cell maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
N6-adenosine-methyltransferase 70 kDa subunit (EC:2.1.1.62)
Short name:
MT-A70
Alternative name(s):
Methyltransferase-like protein 3
Gene namesi
Name:METTL3
Synonyms:MTA70
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:17563. METTL3.

Subcellular locationi

Nucleus speckle
Note: Colocalizes with speckles in interphase nuclei. Suggesting that it may be associated with nuclear pre-mRNA splicing components.1 Publication

GO - Cellular componenti

  1. MIS complex Source: UniProtKB
  2. nuclear speck Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134955499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 580579N6-adenosine-methyltransferase 70 kDa subunit
PRO_0000207630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei43 – 431Phosphoserine3 Publications
Modified residuei219 – 2191Phosphoserine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ86U44.
PaxDbiQ86U44.
PeptideAtlasiQ86U44.
PRIDEiQ86U44.

PTM databases

PhosphoSiteiQ86U44.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

ArrayExpressiQ86U44.
BgeeiQ86U44.
CleanExiHS_METTL3.
GenevestigatoriQ86U44.

Organism-specific databases

HPAiHPA001299.

Interactioni

Protein-protein interaction databases

BioGridi121139. 3 interactions.
DIPiDIP-60727N.
STRINGi9606.ENSP00000298717.

Structurei

3D structure databases

ProteinModelPortaliQ86U44.

Family & Domainsi

Sequence similaritiesi

Belongs to the MT-A70-like family.

Phylogenomic databases

eggNOGiCOG4725.
HOGENOMiHOG000012669.
HOVERGENiHBG052521.
InParanoidiQ86U44.
KOiK05925.
OMAiHTKLWAM.
OrthoDBiEOG7PZRWV.
PhylomeDBiQ86U44.
TreeFamiTF323854.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025848. MT-A70.
IPR007757. MT-A70-like.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF05063. MT-A70. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51143. MT_A70. 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. Align

Isoform 1 (identifier: Q86U44-1) [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

MSDTWSSIQA HKKQLDSLRE RLQRRRKQDS GHLDLRNPEA ALSPTFRSDS    50
PVPTAPTSGG PKPSTASAVP ELATDPELEK KLLHHLSDLA LTLPTDAVSI 100
CLAISTPDAP ATQDGVESLL QKFAAQELIE VKRGLLQDDA HPTLVTYADH 150
SKLSAMMGAV AEKKGPGEVA GTVTGQKRRA EQDSTTVAAF ASSLVSGLNS 200
SASEPAKEPA KKSRKHAASD VDLEIESLLN QQSTKEQQSK KVSQEILELL 250
NTTTAKEQSI VEKFRSRGRA QVQEFCDYGT KEECMKASDA DRPCRKLHFR 300
RIINKHTDES LGDCSFLNTC FHMDTCKYVH YEIDACMDSE APGSKDHTPS 350
QELALTQSVG GDSSADRLFP PQWICCDIRY LDVSILGKFA VVMADPPWDI 400
HMELPYGTLT DDEMRRLNIP VLQDDGFLFL WVTGRAMELG RECLNLWGYE 450
RVDEIIWVKT NQLQRIIRTG RTGHWLNHGK EHCLVGVKGN PQGFNQGLDC 500
DVIVAEVRST SHKPDEIYGM IERLSPGTRK IELFGRPHNV QPNWITLGNQ 550
LDGIHLLDPD VVARFKQRYP DGIISKPKNL 580
Length:580
Mass (Da):64,474
Last modified:July 25, 2003 - v2
Checksum:i63A7F10195A3C6AC
GO
Isoform 2 (identifier: Q86U44-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-284: Missing.
     486-505: GVKGNPQGFNQGLDCDVIVA → SSSGAQFNRWSTKKNHLISY
     506-580: Missing.

Note: No experimental confirmation available.

Show »
Length:221
Mass (Da):25,479
Checksum:iD95A9087F7B99439
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 284284Missing in isoform 2.
VSP_007864Add
BLAST
Alternative sequencei486 – 50520GVKGN…DVIVA → SSSGAQFNRWSTKKNHLISY in isoform 2.
VSP_007865Add
BLAST
Alternative sequencei506 – 58075Missing in isoform 2.
VSP_007866Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511N → I in AAB71850. 1 Publication
Sequence conflicti263 – 2642KF → I in AAB71850. 1 Publication
Sequence conflicti382 – 3821D → V in AAB71850. 1 Publication
Sequence conflicti568 – 5681R → K in AAH52244. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014837 Genomic DNA. Translation: AAB71850.1.
AF283991 Genomic DNA. Translation: AAG13956.1.
AE000658 Genomic DNA. No translation available.
BX247964 mRNA. Translation: CAD62303.1.
BC003031 mRNA. Translation: AAH03031.1.
BC001650 mRNA. Translation: AAH01650.1.
BC052244 mRNA. Translation: AAH52244.1.
CCDSiCCDS32044.1. [Q86U44-1]
RefSeqiNP_062826.2. NM_019852.3. [Q86U44-1]
UniGeneiHs.168799.

Genome annotation databases

EnsembliENST00000298717; ENSP00000298717; ENSG00000165819. [Q86U44-1]
GeneIDi56339.
KEGGihsa:56339.
UCSCiuc001wbb.3. human. [Q86U44-1]

Polymorphism databases

DMDMi33301371.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014837 Genomic DNA. Translation: AAB71850.1 .
AF283991 Genomic DNA. Translation: AAG13956.1 .
AE000658 Genomic DNA. No translation available.
BX247964 mRNA. Translation: CAD62303.1 .
BC003031 mRNA. Translation: AAH03031.1 .
BC001650 mRNA. Translation: AAH01650.1 .
BC052244 mRNA. Translation: AAH52244.1 .
CCDSi CCDS32044.1. [Q86U44-1 ]
RefSeqi NP_062826.2. NM_019852.3. [Q86U44-1 ]
UniGenei Hs.168799.

3D structure databases

ProteinModelPortali Q86U44.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121139. 3 interactions.
DIPi DIP-60727N.
STRINGi 9606.ENSP00000298717.

PTM databases

PhosphoSitei Q86U44.

Polymorphism databases

DMDMi 33301371.

Proteomic databases

MaxQBi Q86U44.
PaxDbi Q86U44.
PeptideAtlasi Q86U44.
PRIDEi Q86U44.

Protocols and materials databases

DNASUi 56339.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298717 ; ENSP00000298717 ; ENSG00000165819 . [Q86U44-1 ]
GeneIDi 56339.
KEGGi hsa:56339.
UCSCi uc001wbb.3. human. [Q86U44-1 ]

Organism-specific databases

CTDi 56339.
GeneCardsi GC14M021966.
HGNCi HGNC:17563. METTL3.
HPAi HPA001299.
MIMi 612472. gene.
neXtProti NX_Q86U44.
PharmGKBi PA134955499.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4725.
HOGENOMi HOG000012669.
HOVERGENi HBG052521.
InParanoidi Q86U44.
KOi K05925.
OMAi HTKLWAM.
OrthoDBi EOG7PZRWV.
PhylomeDBi Q86U44.
TreeFami TF323854.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.

Miscellaneous databases

GeneWikii METTL3.
GenomeRNAii 56339.
NextBioi 61981.
PROi Q86U44.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86U44.
Bgeei Q86U44.
CleanExi HS_METTL3.
Genevestigatori Q86U44.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025848. MT-A70.
IPR007757. MT-A70-like.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF05063. MT-A70. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51143. MT_A70. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase."
    Bokar J.A., Shambaugh M.E., Polayes D., Matera A.G., Rottman F.M.
    RNA 3:1233-1247(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PROTEIN SEQUENCE OF 48-56; 134-149 AND 509-522, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Lung and Pancreas.
  5. "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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-219 AND SER-243, 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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: 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-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: FUNCTION.
  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: FUNCTION.

Entry informationi

Entry nameiMTA70_HUMAN
AccessioniPrimary (citable) accession number: Q86U44
Secondary accession number(s): O14736, Q86V05, Q9HB32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: September 3, 2014
This is version 101 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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