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Protein

Pre-miRNA 5'-monophosphate methyltransferase

Gene

Bcdin3d

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

O-methyltransferase that specifically dimethylates the 5' monophosphate of pre-miRNAs, acting as a negative regulator of miRNA processing. The 5' monophosphate of pre-miRNAs is recognized by DICER1 and is required for pre-miRNAs processing: methylation at this position reduces the processing of pre-miRNAs by DICER1. Able to mediate methylation of pre-miR-145, as well as other pre-miRNAs (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-miRNA 5'-monophosphate methyltransferase (EC:2.1.1.-)
Alternative name(s):
BCDIN3 domain-containing protein
Gene namesi
Name:Bcdin3d
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1922534. Bcdin3d.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Pre-miRNA 5'-monophosphate methyltransferasePRO_0000289266Add
BLAST

Proteomic databases

MaxQBiQ91YP1.
PaxDbiQ91YP1.
PRIDEiQ91YP1.

PTM databases

PhosphoSiteiQ91YP1.

Expressioni

Gene expression databases

BgeeiQ91YP1.
CleanExiMM_BCDIN3D.
GenevisibleiQ91YP1. MM.

Interactioni

Subunit structurei

Interacts with DICER1; the interaction may be mediated by RNA.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041809.

Structurei

3D structure databases

ProteinModelPortaliQ91YP1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 275223Bin3-type SAMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the methyltransferase superfamily.Curated
Contains 1 Bin3-type SAM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2899. Eukaryota.
ENOG410XZ7T. LUCA.
GeneTreeiENSGT00390000014918.
HOGENOMiHOG000013152.
HOVERGENiHBG057674.
InParanoidiQ91YP1.
OMAiDVGCNCG.
OrthoDBiEOG715Q5R.
PhylomeDBiQ91YP1.
TreeFamiTF324061.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010675. Bin3_C.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91YP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAADGTLSRG GVGEAVEEEH PGALEPGAAP FGNFPHYSRF HPPEQRLRLL
60 70 80 90 100
PPELLRQLFP PEGPEKRPIL GLDVGCNSGD LSVALYKHFL SPRDGETCSG
110 120 130 140 150
ASRELRILCC DIDPVLVERA ERDCPFPEAL TFITLDIMDQ ESRKVPLSSF
160 170 180 190 200
LSQFGRSVFD MVFCMSVTMW IHLNHGDRGL CEFLAHVSSL CSYLLVEPQP
210 220 230 240 250
WKCYRAAARR LRKLGLHSFD HFRSLAIRGD MAKQIVRILT QDHGMELACC
260 270 280
FGNTSWDRSL LLFRAKHTHE TQAIPESSTK ETRTD
Length:285
Mass (Da):32,035
Last modified:December 1, 2001 - v1
Checksum:iC58CF217213A7E91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541F → Y in BAB30128 (PubMed:16141072).Curated
Sequence conflicti157 – 1571S → V in BAB30128 (PubMed:16141072).Curated
Sequence conflicti185 – 1851A → G in BAB30128 (PubMed:16141072).Curated
Sequence conflicti197 – 1971E → K in BAB30128 (PubMed:16141072).Curated
Sequence conflicti226 – 2261A → P in BAB30128 (PubMed:16141072).Curated
Sequence conflicti227 – 2271I → F in BAB30128 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016154 mRNA. Translation: BAB30128.1.
BC016225 mRNA. Translation: AAH16225.1.
CCDSiCCDS37202.1.
RefSeqiNP_083512.2. NM_029236.2.
UniGeneiMm.32826.

Genome annotation databases

EnsembliENSMUST00000040313; ENSMUSP00000041809; ENSMUSG00000037525.
GeneIDi75284.
KEGGimmu:75284.
UCSCiuc007xpo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016154 mRNA. Translation: BAB30128.1.
BC016225 mRNA. Translation: AAH16225.1.
CCDSiCCDS37202.1.
RefSeqiNP_083512.2. NM_029236.2.
UniGeneiMm.32826.

3D structure databases

ProteinModelPortaliQ91YP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041809.

PTM databases

PhosphoSiteiQ91YP1.

Proteomic databases

MaxQBiQ91YP1.
PaxDbiQ91YP1.
PRIDEiQ91YP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040313; ENSMUSP00000041809; ENSMUSG00000037525.
GeneIDi75284.
KEGGimmu:75284.
UCSCiuc007xpo.2. mouse.

Organism-specific databases

CTDi144233.
MGIiMGI:1922534. Bcdin3d.

Phylogenomic databases

eggNOGiKOG2899. Eukaryota.
ENOG410XZ7T. LUCA.
GeneTreeiENSGT00390000014918.
HOGENOMiHOG000013152.
HOVERGENiHBG057674.
InParanoidiQ91YP1.
OMAiDVGCNCG.
OrthoDBiEOG715Q5R.
PhylomeDBiQ91YP1.
TreeFamiTF324061.

Miscellaneous databases

NextBioi342634.
PROiQ91YP1.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YP1.
CleanExiMM_BCDIN3D.
GenevisibleiQ91YP1. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010675. Bin3_C.
IPR024160. BIN3_SAM-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF06859. Bin3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51515. BIN3_SAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiBN3D2_MOUSE
AccessioniPrimary (citable) accession number: Q91YP1
Secondary accession number(s): Q9D4U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 1, 2001
Last modified: February 17, 2016
This is version 85 of the entry and version 1 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.