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Protein

Pre-mRNA-splicing regulator WTAP

Gene

Wtap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the WMM N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation of some adenosine residues of some mRNAs and plays a role in the efficiency of mRNA splicing, processing and mRNA stability. Required for accumulation of METTL3 and METTL14 to nuclear speckle. Acts as a mRNA splicing regulator. Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability. Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing regulator WTAP
Alternative name(s):
Female-lethal(2)D homolog
WT1-associated protein
Wilms tumor 1-associating protein
Gene namesi
Name:Wtap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1926395. Wtap.

Subcellular locationi

  • Nucleusnucleoplasm By similarity
  • Nucleus speckle By similarity

GO - Cellular componenti

  • MIS complex Source: UniProtKB
  • nuclear membrane Source: MGI
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Death at E6.5 due to defecs in cell proliferation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Pre-mRNA-splicing regulator WTAPPRO_0000065984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei297 – 2971PhosphoserineCombined sources
Modified residuei305 – 3051PhosphoserineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei341 – 3411PhosphoserineCombined sources
Modified residuei350 – 3501PhosphothreonineCombined sources
Modified residuei388 – 3881PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9ER69.
MaxQBiQ9ER69.
PaxDbiQ9ER69.
PRIDEiQ9ER69.

PTM databases

PhosphoSiteiQ9ER69.

Expressioni

Gene expression databases

BgeeiQ9ER69.
CleanExiMM_WTAP.
ExpressionAtlasiQ9ER69. baseline and differential.
GenevisibleiQ9ER69. MM.

Interactioni

Subunit structurei

Component of the WMM complex, a N6-methyltransferase complex composed of WTAP, METTL3 and METTL14. Interacts with WT1. Component of the WTAP complex composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).By similarity1 Publication

Protein-protein interaction databases

BioGridi208601. 1 interaction.
DIPiDIP-58948N.
IntActiQ9ER69. 1 interaction.
STRINGi10090.ENSMUSP00000007007.

Structurei

3D structure databases

ProteinModelPortaliQ9ER69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the fl(2)d family.Curated

Phylogenomic databases

eggNOGiKOG2991. Eukaryota.
ENOG410XNW7. LUCA.
GeneTreeiENSGT00390000013931.
HOGENOMiHOG000112606.
HOVERGENiHBG104906.
InParanoidiQ9ER69.
OrthoDBiEOG7TTQ8P.

Family and domain databases

InterProiIPR029732. WTAP.
[Graphical view]
PANTHERiPTHR15217:SF0. PTHR15217:SF0. 1 hit.
PfamiPF17098. Wtap. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9ER69-1) [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
MTNEEPLPKK VRLSETDFKV MARDELILRW KQYEAYVQAL EGKYTDLNSN
60 70 80 90 100
DVTGLRESEE KLKQQQQESA RRENILVMRL ATKEQEMQEC TTQIQYLKQV
110 120 130 140 150
QQPSVAQLRS TMVDPAINLF FLKMKGELEQ TKDKLEQAQN ELSAWKFTPD
160 170 180 190 200
SQTGKKLMAK CRMLIQENQE LGRQLSQGRI AQLEAELALQ KKYSEELKSS
210 220 230 240 250
QDELNDFIIQ LDEEVEGMQS TILVLQQQLK ETRQQLAQYQ QQQSQASAPS
260 270 280 290 300
TSRTTSSEPV DQAEVTSKDC SRLANGPSNG SSSRQRTSGS GFHREGSTPE
310 320 330 340 350
DDFPSSSGNG NKASNSSEER TGRGGSSYIN PLSAGYESVD SPTGSENSLT
360 370 380 390
HHSNDTDSSH DPQEEKAVSG KGNRTVGSRH VQNGLDSSVN VQGAVL
Length:396
Mass (Da):44,177
Last modified:October 23, 2007 - v3
Checksum:i0B190F535C97F5D2
GO
Isoform 2 (identifier: Q9ER69-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     151-151: S → R
     152-396: Missing.

Show »
Length:151
Mass (Da):17,801
Checksum:i70C549E73369A233
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei151 – 1511S → R in isoform 2. 2 PublicationsVSP_010280
Alternative sequencei152 – 396245Missing in isoform 2. 2 PublicationsVSP_010281Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276707 mRNA. Translation: CAC16790.1.
AK076111 mRNA. Translation: BAC36191.1.
AK156334 mRNA. Translation: BAE33680.1.
BC046416 mRNA. Translation: AAH46416.1.
BC093504 mRNA. Translation: AAH93504.1.
CCDSiCCDS49949.1. [Q9ER69-2]
CCDS49950.1. [Q9ER69-1]
RefSeqiNP_001107004.1. NM_001113532.1. [Q9ER69-2]
NP_780603.1. NM_175394.2. [Q9ER69-2]
UniGeneiMm.275521.
Mm.491604.

Genome annotation databases

EnsembliENSMUST00000159986; ENSMUSP00000123961; ENSMUSG00000060475. [Q9ER69-2]
ENSMUST00000160781; ENSMUSP00000124138; ENSMUSG00000060475. [Q9ER69-2]
GeneIDi60532.
KEGGimmu:60532.
UCSCiuc008alt.2. mouse. [Q9ER69-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276707 mRNA. Translation: CAC16790.1.
AK076111 mRNA. Translation: BAC36191.1.
AK156334 mRNA. Translation: BAE33680.1.
BC046416 mRNA. Translation: AAH46416.1.
BC093504 mRNA. Translation: AAH93504.1.
CCDSiCCDS49949.1. [Q9ER69-2]
CCDS49950.1. [Q9ER69-1]
RefSeqiNP_001107004.1. NM_001113532.1. [Q9ER69-2]
NP_780603.1. NM_175394.2. [Q9ER69-2]
UniGeneiMm.275521.
Mm.491604.

3D structure databases

ProteinModelPortaliQ9ER69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208601. 1 interaction.
DIPiDIP-58948N.
IntActiQ9ER69. 1 interaction.
STRINGi10090.ENSMUSP00000007007.

PTM databases

PhosphoSiteiQ9ER69.

Proteomic databases

EPDiQ9ER69.
MaxQBiQ9ER69.
PaxDbiQ9ER69.
PRIDEiQ9ER69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000159986; ENSMUSP00000123961; ENSMUSG00000060475. [Q9ER69-2]
ENSMUST00000160781; ENSMUSP00000124138; ENSMUSG00000060475. [Q9ER69-2]
GeneIDi60532.
KEGGimmu:60532.
UCSCiuc008alt.2. mouse. [Q9ER69-2]

Organism-specific databases

CTDi9589.
MGIiMGI:1926395. Wtap.

Phylogenomic databases

eggNOGiKOG2991. Eukaryota.
ENOG410XNW7. LUCA.
GeneTreeiENSGT00390000013931.
HOGENOMiHOG000112606.
HOVERGENiHBG104906.
InParanoidiQ9ER69.
OrthoDBiEOG7TTQ8P.

Enzyme and pathway databases

ReactomeiR-MMU-72203. Processing of Capped Intron-Containing Pre-mRNA.

Miscellaneous databases

ChiTaRSiWtap. mouse.
NextBioi314965.
PROiQ9ER69.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ER69.
CleanExiMM_WTAP.
ExpressionAtlasiQ9ER69. baseline and differential.
GenevisibleiQ9ER69. MM.

Family and domain databases

InterProiIPR029732. WTAP.
[Graphical view]
PANTHERiPTHR15217:SF0. PTHR15217:SF0. 1 hit.
PfamiPF17098. Wtap. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of WTAP, a novel Wilms' tumour 1-associating protein."
    Little N.A., Hastie N.D., Davies R.C.
    Hum. Mol. Genet. 9:2231-2239(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-396 (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Spleen.
  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 2).
    Strain: Czech II.
    Tissue: Eye and Mammary tumor.
  4. "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif."
    Tomsig J.L., Snyder S.L., Creutz C.E.
    J. Biol. Chem. 278:10048-10054(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CPNE4.
  5. "Wilms' tumor 1-associating protein regulates G2/M transition through stabilization of cyclin A2 mRNA."
    Horiuchi K., Umetani M., Minami T., Okayama H., Takada S., Yamamoto M., Aburatani H., Reid P.C., Housman D.E., Hamakubo T., Kodama T.
    Proc. Natl. Acad. Sci. U.S.A. 103:17278-17283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-341 AND THR-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung and Spleen.

Entry informationi

Entry nameiFL2D_MOUSE
AccessioniPrimary (citable) accession number: Q9ER69
Secondary accession number(s): Q3U120, Q566J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 23, 2007
Last modified: May 11, 2016
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.